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Conserved domains on  [gi|193204318|ref|NP_495838|]
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Glutamine-dependent carbamoyl-phosphate synthase [Caenorhabditis elegans]

Protein Classification

trifunctional carbamoyl-phosphate synthase/dihydroorotase/aspartate carbamoyltransferase( domain architecture ID 12849551)

trifunctional carbamoyl-phosphate synthase (CPS)/dihydroorotase/aspartate carbamoyltransferase containing small and large subunits of CPS, is involved in pyrimidine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg super family cl36884
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1452 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


The actual alignment was detected with superfamily member TIGR01369:

Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1568.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   391 RKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGIL 470
Cdd:TIGR01369    7 KKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAIL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   471 CTFGGQTALNCAIDLYKDGIFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVL 550
Cdd:TIGR01369   87 PTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVI 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   551 VRAAYALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 628
Cdd:TIGR01369  167 VRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGDS 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   629 VVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 708
Cdd:TIGR01369  247 IVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAV 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   709 GQHLPVIRNSVTGTTTACFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADGF 788
Cdd:TIGR01369  327 GYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGF 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   789 S-PYTFSRPTTA--DDLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTVSAELLL 865
Cdd:TIGR01369  407 DlPDREVEPDEDlwRALKKPTDRRIFAIAEALRRG-VSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELLR 485

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   866 EAKQAGFSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGIENDVSFNMKNAVMVLGSGVY 945
Cdd:TIGR01369  486 RAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVLGSGPN 565

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   946 RIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGGQAPNNI 1025
Cdd:TIGR01369  566 RIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNL 645

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1026 AMSLSRAQVKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAHN 1105
Cdd:TIGR01369  646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1106 AEDLEVFLKQAAVVAKEHPVVVSKFINEAKELDVDAVALDGKLVVMAVSEHIENAGVHSGDATLVTPAQDMNKLTLDRIK 1185
Cdd:TIGR01369  726 EEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIK 805

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1186 DITFRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAMMASDSPAIRATIKPTATLlkg 1265
Cdd:TIGR01369  806 DIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGKEKEPKY--- 882

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1266 kgrVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPKQNIFISIGGYHAKAEMLKSVEAL 1345
Cdd:TIGR01369  883 ---VAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKL 959

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1346 LKLGYELYGSKGTADYFQSNKINVKPVDWPFEegssdektasGTRSVVEFLENKEFHLVINLPIRGSGayrvsaFRTHGY 1425
Cdd:TIGR01369  960 AEKGYKLYATEGTAKFLGEAGIKPELVLKVSE----------GRPNILDLIKNGEIELVINTTSKGAG------TATDGY 1023

                         1050      1060
                   ....*....|....*....|....*..
gi 193204318  1426 KTRRMAIDNGIPLITDIKCAKTFIQAL 1452
Cdd:TIGR01369 1024 KIRREALDYGVPLITTLNTAEAFAEAL 1050
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1472-1817 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


:

Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 627.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1472 SLKRLPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATP 1551
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1552 NNSKFAAEFADKAAGLKMYLNETFSTLKMDNISDWAKHLSAFPANRPIVCHAEKQTLAAILCMAQMANRAVHIAHVATAD 1631
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1632 EINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVRPRLVKPEDRQALWDNMEYIDCFATDHAPHTWAEKTGKdgKI 1711
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGN--KP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1712 PPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQDDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVF 1791
Cdd:cd01316   239 PPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVK 318

                         330       340
                  ....*....|....*....|....*.
gi 193204318 1792 GKVHNVIIRGEEAVIDGRIVAIPGFG 1817
Cdd:cd01316   319 GKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-358 5.55e-157

carbamoyl-phosphate synthase small subunit;


:

Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 488.43  E-value: 5.55e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    1 MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFES 80
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVN----------REDFES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   81 DRIWPAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDNAQNF-----DYV 155
Cdd:PRK12564   73 DRPHAKGLIVRELSD--IPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELlekarAFP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  156 DVNAENLVDFVSRKEPVVY----GSGDQTILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDT--ESDYDGLFLSNGPGD 229
Cdd:PRK12564  151 GLLGLDLVKEVSTKEPYPWpgpgGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEilALNPDGVFLSNGPGD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  230 PEICAPLVDRLAKVIARGdKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLPA 309
Cdd:PRK12564  231 PAALDYAIEMIRELLEKK-IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 193204318  310 DWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFAD 358
Cdd:PRK12564  310 NLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1877-2196 7.71e-119

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


:

Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 378.24  E-value: 7.71e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKhDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQ 1956
Cdd:COG0540     6 RHLLSIEDLSREEIEELLDTAEEFK-EVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTSSVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1957 KGETLEDTVQVLGSYG-DILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:COG0540    85 KGESLADTIRTLEAYGaDAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIVGDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2036 KNGRTVHSLAKLLCLYkDITLHYVAPSTeLeMPQEVldyvssKSNFVqKKFTSLAEGINHVDVVYVTRIQKERFSSPD-- 2113
Cdd:COG0540   165 KHSRVARSNIKALSKL-GAEVTLVAPPT-L-LPEEI------EELGV-EVTTDLDEALPDADVVYMLRIQKERFTDGLfp 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2114 EYNKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLP--RVDEIAVELDHDERAAYFRQAKNGVFVRMSILSL 2191
Cdd:COG0540   235 SYREYKRSYGLTAERLALAKPDA--------------IVMHPGPrnRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYL 300


                  ....*
gi 193204318 2192 LLGRG 2196
Cdd:COG0540   301 LLGGE 305
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1452 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1568.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   391 RKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGIL 470
Cdd:TIGR01369    7 KKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAIL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   471 CTFGGQTALNCAIDLYKDGIFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVL 550
Cdd:TIGR01369   87 PTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVI 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   551 VRAAYALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 628
Cdd:TIGR01369  167 VRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGDS 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   629 VVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 708
Cdd:TIGR01369  247 IVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAV 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   709 GQHLPVIRNSVTGTTTACFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADGF 788
Cdd:TIGR01369  327 GYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGF 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   789 S-PYTFSRPTTA--DDLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTVSAELLL 865
Cdd:TIGR01369  407 DlPDREVEPDEDlwRALKKPTDRRIFAIAEALRRG-VSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELLR 485

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   866 EAKQAGFSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGIENDVSFNMKNAVMVLGSGVY 945
Cdd:TIGR01369  486 RAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVLGSGPN 565

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   946 RIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGGQAPNNI 1025
Cdd:TIGR01369  566 RIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNL 645

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1026 AMSLSRAQVKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAHN 1105
Cdd:TIGR01369  646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1106 AEDLEVFLKQAAVVAKEHPVVVSKFINEAKELDVDAVALDGKLVVMAVSEHIENAGVHSGDATLVTPAQDMNKLTLDRIK 1185
Cdd:TIGR01369  726 EEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIK 805

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1186 DITFRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAMMASDSPAIRATIKPTATLlkg 1265
Cdd:TIGR01369  806 DIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGKEKEPKY--- 882

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1266 kgrVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPKQNIFISIGGYHAKAEMLKSVEAL 1345
Cdd:TIGR01369  883 ---VAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKL 959

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1346 LKLGYELYGSKGTADYFQSNKINVKPVDWPFEegssdektasGTRSVVEFLENKEFHLVINLPIRGSGayrvsaFRTHGY 1425
Cdd:TIGR01369  960 AEKGYKLYATEGTAKFLGEAGIKPELVLKVSE----------GRPNILDLIKNGEIELVINTTSKGAG------TATDGY 1023

                         1050      1060
                   ....*....|....*....|....*..
gi 193204318  1426 KTRRMAIDNGIPLITDIKCAKTFIQAL 1452
Cdd:TIGR01369 1024 KIRREALDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
391-1453 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1421.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  391 RKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGIL 470
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  471 CTFGGQTALNCAIDLYKDGIFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVL 550
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  551 VRAAYALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 628
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  629 VVVAPSQTLSDREYNALRTCAIKVIRHLGII-GECNIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLA 707
Cdd:PRK05294  248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  708 LGQHLPVIRNSVTGTTTACFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADG 787
Cdd:PRK05294  328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  788 FSPYTFSRPTTAD---DLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDvNTVSAELL 864
Cdd:PRK05294  408 LDEDLFEEESLEElreELKEPTPERLFYIAEAFRRG-ASVEEIHELTKIDPWFLEQIEEIVELEEELKENG-LPLDAELL 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  865 LEAKQAGFSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGiENDVSFNMKNAVMVLGSGV 944
Cdd:PRK05294  486 REAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEE-ECESNPSDRKKVLVLGSGP 564

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  945 YRIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGGQAPNN 1024
Cdd:PRK05294  565 NRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLK 644

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1025 IAMSLSRAQVKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAH 1104
Cdd:PRK05294  645 LAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVY 724

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1105 NAEDLEVFLKQAAVVAKEHPVVVSKFINEAKELDVDAVAlDGKLVVMA-VSEHIENAGVHSGDATLVTPAQDMNKLTLDR 1183
Cdd:PRK05294  725 DEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIC-DGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEE 803

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1184 IKDITFRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAMMA---SDSPAIRATIKPta 1260
Cdd:PRK05294  804 IREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGkklAELGYTKGLIPP-- 881

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1261 tllkgkgRVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPKQ-NIFISIGGyHAKAEML 1339
Cdd:PRK05294  882 -------YVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSVRD-RDKEEVV 953

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1340 KSVEALLKLGYELYGSKGTADYFQSNKINVKPVDwpfeegssdeKTASGTRSVVEFLENKEFHLVINLPiRGSGAyrvsa 1419
Cdd:PRK05294  954 ELAKRLLELGFKILATSGTAKFLREAGIPVELVN----------KVHEGRPHIVDLIKNGEIDLVINTP-TGRQA----- 1017

                        1050      1060      1070
                  ....*....|....*....|....*....|....
gi 193204318 1420 fRTHGYKTRRMAIDNGIPLITDIKCAKTFIQALE 1453
Cdd:PRK05294 1018 -IRDGFSIRRAALEYKVPYITTLAGARAAVKAIE 1050
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 396-942 0e+00

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 646.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  396 LGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGILCTFGG 475
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  476 QTALNCAIDLYKDGIFEqyDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVLVRAAY 555
Cdd:COG0458    81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  556 ALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGESVVVAP 633
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  634 SQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDpySLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGQHLP 713
Cdd:COG0458   239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  714 VIRNSvTGtttacFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADG--FSPY 791
Cdd:COG0458   317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  792 TFSRPTTADDLSKPTDKRMFALARGMyYGDFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTvsaELLLEAKQAG 871
Cdd:COG0458   391 VADDDKEEALLLARRLARLGFLIEAT-RGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVI---NTLLGAKSLG 466

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193204318  872 FSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGIENDVSFNmKNAVMVLGS 942
Cdd:COG0458   467 DSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETE-EPKVVVIGS 536
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1472-1817 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 627.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1472 SLKRLPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATP 1551
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1552 NNSKFAAEFADKAAGLKMYLNETFSTLKMDNISDWAKHLSAFPANRPIVCHAEKQTLAAILCMAQMANRAVHIAHVATAD 1631
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1632 EINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVRPRLVKPEDRQALWDNMEYIDCFATDHAPHTWAEKTGKdgKI 1711
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGN--KP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1712 PPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQDDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVF 1791
Cdd:cd01316   239 PPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVK 318

                         330       340
                  ....*....|....*....|....*.
gi 193204318 1792 GKVHNVIIRGEEAVIDGRIVAIPGFG 1817
Cdd:cd01316   319 GKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-358 5.55e-157

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 488.43  E-value: 5.55e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    1 MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFES 80
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVN----------REDFES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   81 DRIWPAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDNAQNF-----DYV 155
Cdd:PRK12564   73 DRPHAKGLIVRELSD--IPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELlekarAFP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  156 DVNAENLVDFVSRKEPVVY----GSGDQTILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDT--ESDYDGLFLSNGPGD 229
Cdd:PRK12564  151 GLLGLDLVKEVSTKEPYPWpgpgGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEilALNPDGVFLSNGPGD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  230 PEICAPLVDRLAKVIARGdKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLPA 309
Cdd:PRK12564  231 PAALDYAIEMIRELLEKK-IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 193204318  310 DWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFAD 358
Cdd:PRK12564  310 NLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-362 9.63e-157

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 487.90  E-value: 9.63e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318     3 ATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFESDR 82
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVN----------DEDAESKG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    83 IWPAALIVEKICvdGEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDNAQnfDYV------- 155
Cdd:TIGR01368   71 IHVSGLVVRELS--DRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDE--ELVekarvsp 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   156 DVNAENLVDFVSRKEPVVYGSGDQ---TILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDTESDY--DGLFLSNGPGDP 230
Cdd:TIGR01368  147 DITGINLVAEVSTKEPYTWGQRGGkgkRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYnpDGIFLSNGPGDP 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   231 EICAPLVDRLAKVIarGDKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLPA- 309
Cdd:TIGR01368  227 AAVEPAIETIRKLL--EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAg 304

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193204318   310 DWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFADSVRQ 362
Cdd:TIGR01368  305 DLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-361 4.10e-153

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 477.98  E-value: 4.10e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    1 MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFES 80
Cdd:COG0505     3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVN----------DEDFES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   81 DRIWPAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDN-------AQNFd 153
Cdd:COG0505    73 DRPWVAGLVVRELSR--RPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDieellekARAA- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  154 yVDVNAENLVDFVSRKEPVVYGSGDQ---TILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDT--ESDYDGLFLSNGPG 228
Cdd:COG0505   150 -PGMEGLDLVKEVSTKEPYEWTEAPGagfHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEilALNPDGVFLSNGPG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  229 DPEICAPLVDRLAKVIARGdKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLP 308
Cdd:COG0505   229 DPAALDYAIETIRELLGKG-IPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLP 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 193204318  309 A-DWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFADSVR 361
Cdd:COG0505   308 AtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1877-2196 7.71e-119

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 378.24  E-value: 7.71e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKhDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQ 1956
Cdd:COG0540     6 RHLLSIEDLSREEIEELLDTAEEFK-EVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTSSVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1957 KGETLEDTVQVLGSYG-DILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:COG0540    85 KGESLADTIRTLEAYGaDAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIVGDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2036 KNGRTVHSLAKLLCLYkDITLHYVAPSTeLeMPQEVldyvssKSNFVqKKFTSLAEGINHVDVVYVTRIQKERFSSPD-- 2113
Cdd:COG0540   165 KHSRVARSNIKALSKL-GAEVTLVAPPT-L-LPEEI------EELGV-EVTTDLDEALPDADVVYMLRIQKERFTDGLfp 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2114 EYNKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLP--RVDEIAVELDHDERAAYFRQAKNGVFVRMSILSL 2191
Cdd:COG0540   235 SYREYKRSYGLTAERLALAKPDA--------------IVMHPGPrnRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYL 300


                  ....*
gi 193204318 2192 LLGRG 2196
Cdd:COG0540   301 LLGGE 305
PLN02527 PLN02527
aspartate carbamoyltransferase
 1877-2194 1.23e-113

aspartate carbamoyltransferase


Pssm-ID: 178142 [Multi-domain]  Cd Length: 306  Bit Score: 363.30  E-value: 1.23e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKhDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQ--SSS 1954
Cdd:PLN02527    1 SDVIEAQQFDREMLELLFEVAREME-KVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAgeFSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1955 VQKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGD 2034
Cdd:PLN02527   80 AAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2035 LKNGRTVHSLAKLLCLYKDITLHYVAPSTeLEMPQEVLDYVSSKsNFVQKKFTSLAEGINHVDVVYVTRIQKERFS-SPD 2113
Cdd:PLN02527  160 LANGRTVRSLAYLLAKYEDVKIYFVAPDV-VKMKDDIKDYLTSK-GVEWEESSDLMEVASKCDVLYQTRIQRERFGeRID 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2114 EYNKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLPRVDEIAVELDHDERAAYFRQAKNGVFVRMSILSLLL 2193
Cdd:PLN02527  238 LYEAARGKYIVDKKVMDVLPKHA--------------VVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLL 303


                  .
gi 193204318 2194 G 2194
Cdd:PLN02527  304 G 304
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 181-356 4.84e-105

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 333.31  E-value: 4.84e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  181 ILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPID--TESDYDGLFLSNGPGDPEICAPLVDRLAKVIARgDKPIFGICLGH 258
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGK-KIPIFGICLGH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  259 QILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLPADWKALFTNENDKTNEGIVHSSKPFFSVQF 338
Cdd:cd01744    80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*...
gi 193204318  339 HPEHTAGPTDCEFLFDVF 356
Cdd:cd01744   160 HPEASPGPHDTEYLFDEF 177
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1877-2194 1.29e-102

aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273209 [Multi-domain]  Cd Length: 301  Bit Score: 331.63  E-value: 1.29e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1877 KNCISVKHLDKGQINRIFELADRYKHDVEKGHPLThILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVIS-VDSQSSSV 1955
Cdd:TIGR00670    1 RHLISISDLSREEIELLLETARELEQVLNGKEPLK-LLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNfSDSETSSV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1956 QKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:TIGR00670   80 AKGETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  2036 KNGRTVHSLAKLLCLYkDITLHYVAPStELEMPQEVLDYVSSKsNFVQKKFTSLAEGINHVDVVYVTRIQKERFSSPDEY 2115
Cdd:TIGR00670  160 KYGRTVHSLAEALTRF-GVEVYLISPE-ELRMPKEILEELKAK-GIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEY 236

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193204318  2116 NKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLPRVDEIAVELDHDERAAYFRQAKNGVFVRMSILSLLLG 2194
Cdd:TIGR00670  237 EKVKGSYGITLERLEAAKKGV--------------IIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1476-1821 7.42e-100

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 329.36  E-value: 7.42e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNSK 1555
Cdd:COG0044    49 LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGE 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 FAAEFAD----KAAGLKMYLNETFSTLKMDnisdwAKHL-----SAFPANRPIVCHAEKQTLAAILCM------------ 1614
Cdd:COG0044   129 NLAELGAlaeaGAVAFKVFMGSDDGNPVLD-----DGLLrraleYAAEFGALVAVHAEDPDLIRGGVMnegktsprlglk 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1615 -----------------AQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDG---------IRE 1668
Cdd:COG0044   204 grpaeaeeeavardialAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYgtnfkvnppLRT 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1669 vrprlvkPEDRQALW----DNMeyIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLT-AVHDGKLTMKELTDRM 1743
Cdd:COG0044   284 -------EEDREALWeglaDGT--IDVIATDHAPHTLEEKELPFAEAPNGIPGLETALPLLLTeLVHKGRLSLERLVELL 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1744 STNPRRIFNLPPQddTYIE---------VDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIP 1814
Cdd:COG0044   355 STNPARIFGLPRK--GRIAvgadadlvlFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP 432


                  ....*..
gi 193204318 1815 gFGKNVR 1821
Cdd:COG0044   433 -RGRFLR 438
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 511-713 3.76e-97

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 311.93  E-value: 3.76e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   511 DRDLFNQEISAIGEKVAPSKAAT--TMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELIAIAQQALAHS------ 582
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   583 NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLgiHTGESVVVAPSQTLSDREYNALRTCAIKVIRHLGIIGEC 662
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 193204318   663 NIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGQHLP 713
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 1476-1804 7.12e-84

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 282.02  E-value: 7.12e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNN-- 1553
Cdd:TIGR00857   38 LPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNqg 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1554 ---SKFAAEFADKAAGlKMYLNETFSTLKMDNI---------------------------------SDWAKHLSAFPanr 1597
Cdd:TIGR00857  118 kelTEAYELKEAGAVG-RMFTDDGSEVQDILSMrraleyaaiagvpialhaedpdliyggvmhegpSAAQLGLPARP--- 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1598 pivCHAEKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLP--DGIREVRPRLVK 1675
Cdd:TIGR00857  194 ---PEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVArlDGNGKVNPPLRE 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1676 PEDRQALWDNM--EYIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNL 1753
Cdd:TIGR00857  271 KEDRLALIEGLkdGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGL 350

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318  1754 PPQ-------DDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEA 1804
Cdd:TIGR00857  351 PDKgtleegnPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVV 408
pyrC PRK09357
dihydroorotase; Validated
 1476-1807 6.00e-79

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 268.22  E-value: 6.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDyALYIGATPNNSK 1555
Cdd:PRK09357   52 APGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVD-VLPVGAITKGLA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 FA--AEF-ADKAAGLKMYLN---ETFSTLKMDNISDWAKHLsafpaNRPIVCHAEKQTLAAILCM--------------- 1614
Cdd:PRK09357  131 GEelTEFgALKEAGVVAFSDdgiPVQDARLMRRALEYAKAL-----DLLIAQHCEDPSLTEGGVMnegevsarlglpgip 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1615 -----AQMA----------NRaVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLP--DGIREVRPRLVKPE 1677
Cdd:PRK09357  206 avaeeVMIArdvllaeatgAR-VHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLtyDPNYKVNPPLRTEE 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1678 DRQALWDNME--YIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTA-VHDGKLTMKELTDRMSTNPRRIFNLP 1754
Cdd:PRK09357  285 DREALIEGLKdgTIDAIATDHAPHAREEKECEFEAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTINPARILGLP 364

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318 1755 PqddTYIEV---------DLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVID 1807
Cdd:PRK09357  365 A---GPLAEgepadlvifDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-142 4.53e-65

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 216.86  E-value: 4.53e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318      1 MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFES 80
Cdd:smart01097    1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVN----------DEDFES 70

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318     81 DRIWPAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKL 142
Cdd:smart01097   71 DKIQVKGLVVRELSD--EPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-142 1.75e-64

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.


Pssm-ID: 460017 [Multi-domain]  Cd Length: 126  Bit Score: 214.88  E-value: 1.75e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318     5 LHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFESDRIW 84
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVN----------PEDFESDKIH 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318    85 PAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKL 142
Cdd:pfam00988   71 VAGLVVREYSD--EPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 800-922 3.62e-49

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 171.09  E-value: 3.62e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    800 DDLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTVSAELLLEAKQAGFSDRQIAK 879
Cdd:smart01096    3 EELRTPTDERLFYIAEALRRG-YSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 193204318    880 KIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTF 922
Cdd:smart01096   82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1878-2019 3.45e-47

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 166.06  E-value: 3.45e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1878 NCISVKHLDKGQINRIFELADRYKHDVEKGHPlTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQK 1957
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKK-LPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318  1958 GETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGdGTGEHPTQALLDVYTIRQ 2019
Cdd:pfam02729   80 GESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1323-1450 1.67e-40

Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.


Pssm-ID: 238711 [Multi-domain]  Cd Length: 116  Bit Score: 145.91  E-value: 1.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1323 QNIFISIGGYhAKAEMLKSVEALLKLGYELYGSKGTADYFQSNKINVKPVDWPFEEGSSDEktasgtRSVVEFLENKEFH 1402
Cdd:cd01423     1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK------PSLRELLAEGKID 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 193204318 1403 LVINLPIRGSGAYRVSafrthGYKTRRMAIDNGIPLITDIKCAKTFIQ 1450
Cdd:cd01423    74 LVINLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1476-1756 1.45e-03

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 43.26  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1476 LPGMVDIHVH--------VREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDT---------------------D 1526
Cdd:pfam01979    3 LPGLIDAHVHlemgllrgIPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEAlleaaeelplglrflgpgcslD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1527 SFYQTEQ-LASAKSVVDYALYIGATpNNSKFAAEFADKAAGlkmylneTFSTLKMDNISDWAKHlsafpANRPIVCHAEK 1605
Cdd:pfam01979   83 TDGELEGrKALREKLKAGAEFIKGM-ADGVVFVGLAPHGAP-------TFSDDELKAALEEAKK-----YGLPVAIHALE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1606 QTLAAILCMAQMANRAVHIAHVATADEINL---VKEAKQRGWNVTcevcPHHLFLIEEDLP-DGIREV-RPRLVKPEDRQ 1680
Cdd:pfam01979  150 TKGEVEDAIAAFGGGIEHGTHLEVAESGGLldiIKLILAHGVHLS----PTEANLLAEHLKgAGVAHCpFSNSKLRSGRI 225

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318  1681 ALWDNMEY--IDCFATDHAPHtwaektgkdGKIPPGFPGVEYMlpLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQ 1756
Cdd:pfam01979  226 ALRKALEDgvKVGLGTDGAGS---------GNSLNMLEELRLA--LELQFDPEGGLSPLEALRMATINPAKALGLDDK 292
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1452 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1568.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   391 RKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGIL 470
Cdd:TIGR01369    7 KKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAIL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   471 CTFGGQTALNCAIDLYKDGIFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVL 550
Cdd:TIGR01369   87 PTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVI 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   551 VRAAYALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 628
Cdd:TIGR01369  167 VRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGDS 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   629 VVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 708
Cdd:TIGR01369  247 IVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAV 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   709 GQHLPVIRNSVTGTTTACFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADGF 788
Cdd:TIGR01369  327 GYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGF 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   789 S-PYTFSRPTTA--DDLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTVSAELLL 865
Cdd:TIGR01369  407 DlPDREVEPDEDlwRALKKPTDRRIFAIAEALRRG-VSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELLR 485

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   866 EAKQAGFSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGIENDVSFNMKNAVMVLGSGVY 945
Cdd:TIGR01369  486 RAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVLGSGPN 565

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   946 RIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGGQAPNNI 1025
Cdd:TIGR01369  566 RIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNL 645

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1026 AMSLSRAQVKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAHN 1105
Cdd:TIGR01369  646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1106 AEDLEVFLKQAAVVAKEHPVVVSKFINEAKELDVDAVALDGKLVVMAVSEHIENAGVHSGDATLVTPAQDMNKLTLDRIK 1185
Cdd:TIGR01369  726 EEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIK 805

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1186 DITFRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAMMASDSPAIRATIKPTATLlkg 1265
Cdd:TIGR01369  806 DIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGKEKEPKY--- 882

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1266 kgrVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPKQNIFISIGGYHAKAEMLKSVEAL 1345
Cdd:TIGR01369  883 ---VAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKL 959

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1346 LKLGYELYGSKGTADYFQSNKINVKPVDWPFEegssdektasGTRSVVEFLENKEFHLVINLPIRGSGayrvsaFRTHGY 1425
Cdd:TIGR01369  960 AEKGYKLYATEGTAKFLGEAGIKPELVLKVSE----------GRPNILDLIKNGEIELVINTTSKGAG------TATDGY 1023

                         1050      1060
                   ....*....|....*....|....*..
gi 193204318  1426 KTRRMAIDNGIPLITDIKCAKTFIQAL 1452
Cdd:TIGR01369 1024 KIRREALDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
391-1453 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1421.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  391 RKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGIL 470
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  471 CTFGGQTALNCAIDLYKDGIFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVL 550
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  551 VRAAYALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 628
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  629 VVVAPSQTLSDREYNALRTCAIKVIRHLGII-GECNIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLA 707
Cdd:PRK05294  248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  708 LGQHLPVIRNSVTGTTTACFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADG 787
Cdd:PRK05294  328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  788 FSPYTFSRPTTAD---DLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDvNTVSAELL 864
Cdd:PRK05294  408 LDEDLFEEESLEElreELKEPTPERLFYIAEAFRRG-ASVEEIHELTKIDPWFLEQIEEIVELEEELKENG-LPLDAELL 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  865 LEAKQAGFSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGiENDVSFNMKNAVMVLGSGV 944
Cdd:PRK05294  486 REAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEE-ECESNPSDRKKVLVLGSGP 564

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  945 YRIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGGQAPNN 1024
Cdd:PRK05294  565 NRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLK 644

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1025 IAMSLSRAQVKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAH 1104
Cdd:PRK05294  645 LAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVY 724

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1105 NAEDLEVFLKQAAVVAKEHPVVVSKFINEAKELDVDAVAlDGKLVVMA-VSEHIENAGVHSGDATLVTPAQDMNKLTLDR 1183
Cdd:PRK05294  725 DEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIC-DGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEE 803

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1184 IKDITFRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAMMA---SDSPAIRATIKPta 1260
Cdd:PRK05294  804 IREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGkklAELGYTKGLIPP-- 881

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1261 tllkgkgRVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPKQ-NIFISIGGyHAKAEML 1339
Cdd:PRK05294  882 -------YVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSVRD-RDKEEVV 953

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1340 KSVEALLKLGYELYGSKGTADYFQSNKINVKPVDwpfeegssdeKTASGTRSVVEFLENKEFHLVINLPiRGSGAyrvsa 1419
Cdd:PRK05294  954 ELAKRLLELGFKILATSGTAKFLREAGIPVELVN----------KVHEGRPHIVDLIKNGEIDLVINTP-TGRQA----- 1017

                        1050      1060      1070
                  ....*....|....*....|....*....|....
gi 193204318 1420 fRTHGYKTRRMAIDNGIPLITDIKCAKTFIQALE 1453
Cdd:PRK05294 1018 -IRDGFSIRRAALEYKVPYITTLAGARAAVKAIE 1050
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 391-1453 0e+00

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 1079.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  391 RKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGIL 470
Cdd:PRK12815    8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  471 CTFGGQTALNCAIDLYKDGIFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVL 550
Cdd:PRK12815   88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  551 VRAAYALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGES 628
Cdd:PRK12815  168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  629 VVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 708
Cdd:PRK12815  248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  709 GQHLPVIRNSVTGTTTACFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADGF 788
Cdd:PRK12815  328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  789 S-PYTFSRPTTAD---DLSKPTDKRMF----ALARGMyygdfDVEKAHELTRIDRWFLFRMQNIVDIYHRLeKTDVNTVS 860
Cdd:PRK12815  408 SlPIELSGKSDEEllqDLRHPDDRRLFalleALRRGI-----TYEEIHELTKIDPFFLQKFEHIVALEKKL-AEDGLDLS 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  861 AELLLEAKQAGFSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGiENDVSF-NMKNAVMV 939
Cdd:PRK12815  482 ADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFG-ESEAEPsSEKKKVLI 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  940 LGSGVYRIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGG 1019
Cdd:PRK12815  561 LGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGG 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1020 QAPNNIAMSLSRAQVKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAA 1099
Cdd:PRK12815  641 QTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQG 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1100 MNVAHNAEDLEVFLKQAAvvAKEHPVVVSKFInEAKELDVDAVAlDGKLVVMA-VSEHIENAGVHSGDATLVTPAQDMNK 1178
Cdd:PRK12815  721 MAVVYDEPALEAYLAENA--SQLYPILIDQFI-DGKEYEVDAIS-DGEDVTIPgIIEHIEQAGVHSGDSIAVLPPQSLSE 796

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1179 LTLDRIKDITFRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAMMASDspaiRATIKP 1258
Cdd:PRK12815  797 EQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKS----LAELGY 872

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1259 TATLLKGKGRVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPKQN-IFISIGGYHaKAE 1337
Cdd:PRK12815  873 PNGLWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGtIFISVRDED-KPE 951

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1338 MLKSVEALLKLGYELYGSKGTADYFQSNKINVKPVdwpfeegssdEKTASGTRSVVEFLENKEFHLVINLPIRGSGayrv 1417
Cdd:PRK12815  952 VTKLARRFAQLGFKLLATEGTANWLAEEGITTGVV----------EKVQEGSPSLLERIKQHRIVLVVNTSLSDSA---- 1017

                        1050      1060      1070
                  ....*....|....*....|....*....|....*.
gi 193204318 1418 safRTHGYKTRRMAIDNGIPLITDIKCAKTFIQALE 1453
Cdd:PRK12815 1018 ---SEDAIKIRDEALSTHIPVFTELETAQAFLQVLE 1050
PLN02735 PLN02735
carbamoyl-phosphate synthase
 391-1466 0e+00

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 882.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  391 RKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGIL 470
Cdd:PLN02735   24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  471 CTFGGQTALNCAIDLYKDGIFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELG-YPV 549
Cdd:PLN02735  104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  550 LVRAAYALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGE 627
Cdd:PLN02735  184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  628 SVVVAPSQTLSDREYNALRTCAIKVIRHLGIigEC---NIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAA 704
Cdd:PLN02735  264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  705 KLALGQHLPVIRNSVTGTTTACFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDH 784
Cdd:PLN02735  342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  785 ADGFSPYTFSR-----PTTADDLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTV 859
Cdd:PLN02735  422 FSGWGCAKVKEldwdwEQLKYKLRVPNPDRIHAIYAAMKKG-MTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSEL 500

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  860 SAELLLEAKQAGFSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGiENDVSFNMKNAVMV 939
Cdd:PLN02735  501 SKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDG-ECESAPTNKKKVLI 579

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  940 LGSGVYRIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGG 1019
Cdd:PLN02735  580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1020 QAPNNIAMSLSRA-------------QVKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYP 1086
Cdd:PLN02735  660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1087 CLIRPSYVLSGAAMNVAHNAEDLEVFLKQAAVVAKEHPVVVSKFINEAKELDVDAVA-LDGKLVVMAVSEHIENAGVHSG 1165
Cdd:PLN02735  740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1166 DATLVTPAQDMNKLTLDRIKDITFRIAEAFNVNGPFNMQL-IAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAM 1244
Cdd:PLN02735  820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1245 MASDSPAIRAT--IKPTatllkgkgRVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPK 1322
Cdd:PLN02735  900 SGKSLKDLGFTeeVIPA--------HVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPL 971

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1323 Q-NIFISIGGYhAKAEMLKSVEALLKLGYELYGSKGTADYFQSNKINVKPVdwpfeegssdEKTASGTRSVVEFLENKEF 1401
Cdd:PLN02735  972 SgTVFISLNDL-TKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERV----------LKLHEGRPHAGDMLANGQI 1040

                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193204318 1402 HLVInlpIRGSGAyrvSAFRTHGYKTRRMAIDNGIPLITDIKCAKTFIQALEMVGKRP-TMNSLVD 1466
Cdd:PLN02735 1041 QLMV---ITSSGD---ALDQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECPiEMIALQD 1100
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 396-942 0e+00

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 646.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  396 LGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGILCTFGG 475
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  476 QTALNCAIDLYKDGIFEqyDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVLVRAAY 555
Cdd:COG0458    81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  556 ALGGLGSGFADNREELIAIAQQALAHS--NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGESVVVAP 633
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  634 SQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDpySLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGQHLP 713
Cdd:COG0458   239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  714 VIRNSvTGtttacFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALRMVSDHADG--FSPY 791
Cdd:COG0458   317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  792 TFSRPTTADDLSKPTDKRMFALARGMyYGDFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTvsaELLLEAKQAG 871
Cdd:COG0458   391 VADDDKEEALLLARRLARLGFLIEAT-RGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVI---NTLLGAKSLG 466

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193204318  872 FSDRQIAKKIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTFNGIENDVSFNmKNAVMVLGS 942
Cdd:COG0458   467 DSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETE-EPKVVVIGS 536
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1472-1817 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 627.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1472 SLKRLPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATP 1551
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1552 NNSKFAAEFADKAAGLKMYLNETFSTLKMDNISDWAKHLSAFPANRPIVCHAEKQTLAAILCMAQMANRAVHIAHVATAD 1631
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1632 EINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVRPRLVKPEDRQALWDNMEYIDCFATDHAPHTWAEKTGKdgKI 1711
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGN--KP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1712 PPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQDDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVF 1791
Cdd:cd01316   239 PPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVK 318

                         330       340
                  ....*....|....*....|....*.
gi 193204318 1792 GKVHNVIIRGEEAVIDGRIVAIPGFG 1817
Cdd:cd01316   319 GKVQRVVLRGETAFIDGEIVAPPGFG 344
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 940-1436 2.05e-163

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 513.66  E-value: 2.05e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  940 LGSGVYRIGSSVEFDSSCVGCIRELKALGYSTITVNCNPETVSTDYDICDRLYFEEISFETVLDVYHLEKPKGVILAFGG 1019
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1020 QAPNNIAMSLSRAQ----VKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVL 1095
Cdd:COG0458    81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1096 SGAAMNVAHNAEDLEVFLKQAAVVAKEHPVVVSKFINEAKELDVDAVAlDGKL--VVMAVSEHIENAGVHSGDATLVTPA 1173
Cdd:COG0458   161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVR-DGEDnvIIVGIMEHIEPAGVHSGDSICVAPP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1174 QDMNKLTLDRIKDITFRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPFVSKTLDYDFVALATRAMMASDSPAIR 1253
Cdd:COG0458   240 QTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1254 ATIKPTATLlkgkGRVGVKVPQFSFSRLAGADVMLGVEMASTGEVACFGTSRCDAYLKALLSTGFVVPKqNIFISIGGYH 1333
Cdd:COG0458   320 NDTGFEPTL----DYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPG-TVLLSLVADD 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1334 AKAEMLKSVEALLKLGYELYGSKGTADYFQSNKINVKPVDWPFEEGssdektasgtRSVVEFLENKEFHLVINLP----- 1408
Cdd:COG0458   395 DKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGR----------PIIVDEIELEEIILVINTLlgaks 464

                         490       500
                  ....*....|....*....|....*...
gi 193204318 1409 IRGSGAYRVSAFRTHGYKTRRMAIDNGI 1436
Cdd:COG0458   465 LGDSDGIIRRALAAKVPYVTTLAAAAAA 492
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-358 5.55e-157

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 488.43  E-value: 5.55e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    1 MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFES 80
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVN----------REDFES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   81 DRIWPAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDNAQNF-----DYV 155
Cdd:PRK12564   73 DRPHAKGLIVRELSD--IPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELlekarAFP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  156 DVNAENLVDFVSRKEPVVY----GSGDQTILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDT--ESDYDGLFLSNGPGD 229
Cdd:PRK12564  151 GLLGLDLVKEVSTKEPYPWpgpgGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEilALNPDGVFLSNGPGD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  230 PEICAPLVDRLAKVIARGdKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLPA 309
Cdd:PRK12564  231 PAALDYAIEMIRELLEKK-IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 193204318  310 DWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFAD 358
Cdd:PRK12564  310 NLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-362 9.63e-157

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 487.90  E-value: 9.63e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318     3 ATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFESDR 82
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVN----------DEDAESKG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    83 IWPAALIVEKICvdGEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDNAQnfDYV------- 155
Cdd:TIGR01368   71 IHVSGLVVRELS--DRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDE--ELVekarvsp 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   156 DVNAENLVDFVSRKEPVVYGSGDQ---TILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDTESDY--DGLFLSNGPGDP 230
Cdd:TIGR01368  147 DITGINLVAEVSTKEPYTWGQRGGkgkRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYnpDGIFLSNGPGDP 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   231 EICAPLVDRLAKVIarGDKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLPA- 309
Cdd:TIGR01368  227 AAVEPAIETIRKLL--EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAg 304

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193204318   310 DWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFADSVRQ 362
Cdd:TIGR01368  305 DLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-361 4.10e-153

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 477.98  E-value: 4.10e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    1 MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFES 80
Cdd:COG0505     3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVN----------DEDFES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   81 DRIWPAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDN-------AQNFd 153
Cdd:COG0505    73 DRPWVAGLVVRELSR--RPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDieellekARAA- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  154 yVDVNAENLVDFVSRKEPVVYGSGDQ---TILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDT--ESDYDGLFLSNGPG 228
Cdd:COG0505   150 -PGMEGLDLVKEVSTKEPYEWTEAPGagfHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEilALNPDGVFLSNGPG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  229 DPEICAPLVDRLAKVIARGdKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLP 308
Cdd:COG0505   229 DPAALDYAIETIRELLGKG-IPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLP 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 193204318  309 A-DWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFADSVR 361
Cdd:COG0505   308 AtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-364 3.76e-133

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 421.22  E-value: 3.76e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    1 MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFES 80
Cdd:PRK12838    1 MKAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGIN----------ADDYES 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   81 DRIWPAALIVEKICVDGehSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLViESDNAQNFDYVD--VN 158
Cdd:PRK12838   71 KQPQVKGVIVYELSREG--SHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASIT-TTDDAHAFDQIKalVL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  159 AENLVDFVSRKEPVVYGSGDQTILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDT--ESDYDGLFLSNGPGDPEICAPL 236
Cdd:PRK12838  148 PKNVVAQVSTKEPYTYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEikNLNPDGIVLSNGPGDPKELQPY 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  237 VDRLAKVIARgdKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSL-PADWKALF 315
Cdd:PRK12838  228 LPEIKKLISS--YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRF 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 193204318  316 TNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFADSVRQAK 364
Cdd:PRK12838  306 FNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1877-2196 7.71e-119

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 378.24  E-value: 7.71e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKhDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQ 1956
Cdd:COG0540     6 RHLLSIEDLSREEIEELLDTAEEFK-EVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTSSVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1957 KGETLEDTVQVLGSYG-DILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:COG0540    85 KGESLADTIRTLEAYGaDAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIVGDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2036 KNGRTVHSLAKLLCLYkDITLHYVAPSTeLeMPQEVldyvssKSNFVqKKFTSLAEGINHVDVVYVTRIQKERFSSPD-- 2113
Cdd:COG0540   165 KHSRVARSNIKALSKL-GAEVTLVAPPT-L-LPEEI------EELGV-EVTTDLDEALPDADVVYMLRIQKERFTDGLfp 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2114 EYNKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLP--RVDEIAVELDHDERAAYFRQAKNGVFVRMSILSL 2191
Cdd:COG0540   235 SYREYKRSYGLTAERLALAKPDA--------------IVMHPGPrnRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYL 300


                  ....*
gi 193204318 2192 LLGRG 2196
Cdd:COG0540   301 LLGGE 305
PLN02527 PLN02527
aspartate carbamoyltransferase
 1877-2194 1.23e-113

aspartate carbamoyltransferase


Pssm-ID: 178142 [Multi-domain]  Cd Length: 306  Bit Score: 363.30  E-value: 1.23e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKhDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQ--SSS 1954
Cdd:PLN02527    1 SDVIEAQQFDREMLELLFEVAREME-KVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAgeFSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1955 VQKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGD 2034
Cdd:PLN02527   80 AAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2035 LKNGRTVHSLAKLLCLYKDITLHYVAPSTeLEMPQEVLDYVSSKsNFVQKKFTSLAEGINHVDVVYVTRIQKERFS-SPD 2113
Cdd:PLN02527  160 LANGRTVRSLAYLLAKYEDVKIYFVAPDV-VKMKDDIKDYLTSK-GVEWEESSDLMEVASKCDVLYQTRIQRERFGeRID 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2114 EYNKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLPRVDEIAVELDHDERAAYFRQAKNGVFVRMSILSLLL 2193
Cdd:PLN02527  238 LYEAARGKYIVDKKVMDVLPKHA--------------VVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLL 303


                  .
gi 193204318 2194 G 2194
Cdd:PLN02527  304 G 304
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
1877-2195 2.31e-109

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 350.91  E-value: 2.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKHDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQ 1956
Cdd:PRK00856    6 KHLLSIEDLSREEIELLLDTAEEFKEVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTSSVS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1957 KGETLEDTVQVLGSYG-DILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:PRK00856   86 KGETLADTIRTLSAMGaDAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAIVGDI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2036 KNGRTVHSLAKLLCLYkDITLHYVAPSTeLeMPQEVLDYvssksnfvqKKFTSLAEGINHVDVVYVTRIQKERFSSPD-- 2113
Cdd:PRK00856  166 KHSRVARSNIQALTRL-GAEVRLIAPPT-L-LPEGMPEY---------GVHTDLDEVIEDADVVMMLRVQKERMDGGLlp 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2114 EYNKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLP--RVDEIAVELDHDERAAYFRQAKNGVFVRMSILSL 2191
Cdd:PRK00856  234 SYEEYKRSYGLTAERLALAKPDA--------------IVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLEL 299


                  ....
gi 193204318 2192 LLGR 2195
Cdd:PRK00856  300 LLGG 303
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 181-356 4.84e-105

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 333.31  E-value: 4.84e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  181 ILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPID--TESDYDGLFLSNGPGDPEICAPLVDRLAKVIARgDKPIFGICLGH 258
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGK-KIPIFGICLGH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  259 QILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITSQNHGYAVDPDSLPADWKALFTNENDKTNEGIVHSSKPFFSVQF 338
Cdd:cd01744    80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*...
gi 193204318  339 HPEHTAGPTDCEFLFDVF 356
Cdd:cd01744   160 HPEASPGPHDTEYLFDEF 177
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1877-2194 1.29e-102

aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273209 [Multi-domain]  Cd Length: 301  Bit Score: 331.63  E-value: 1.29e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1877 KNCISVKHLDKGQINRIFELADRYKHDVEKGHPLThILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVIS-VDSQSSSV 1955
Cdd:TIGR00670    1 RHLISISDLSREEIELLLETARELEQVLNGKEPLK-LLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNfSDSETSSV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1956 QKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:TIGR00670   80 AKGETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  2036 KNGRTVHSLAKLLCLYkDITLHYVAPStELEMPQEVLDYVSSKsNFVQKKFTSLAEGINHVDVVYVTRIQKERFSSPDEY 2115
Cdd:TIGR00670  160 KYGRTVHSLAEALTRF-GVEVYLISPE-ELRMPKEILEELKAK-GIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEY 236

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193204318  2116 NKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLPRVDEIAVELDHDERAAYFRQAKNGVFVRMSILSLLLG 2194
Cdd:TIGR00670  237 EKVKGSYGITLERLEAAKKGV--------------IIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1476-1821 7.42e-100

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 329.36  E-value: 7.42e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNSK 1555
Cdd:COG0044    49 LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGE 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 FAAEFAD----KAAGLKMYLNETFSTLKMDnisdwAKHL-----SAFPANRPIVCHAEKQTLAAILCM------------ 1614
Cdd:COG0044   129 NLAELGAlaeaGAVAFKVFMGSDDGNPVLD-----DGLLrraleYAAEFGALVAVHAEDPDLIRGGVMnegktsprlglk 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1615 -----------------AQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDG---------IRE 1668
Cdd:COG0044   204 grpaeaeeeavardialAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYgtnfkvnppLRT 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1669 vrprlvkPEDRQALW----DNMeyIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLT-AVHDGKLTMKELTDRM 1743
Cdd:COG0044   284 -------EEDREALWeglaDGT--IDVIATDHAPHTLEEKELPFAEAPNGIPGLETALPLLLTeLVHKGRLSLERLVELL 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1744 STNPRRIFNLPPQddTYIE---------VDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIP 1814
Cdd:COG0044   355 STNPARIFGLPRK--GRIAvgadadlvlFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP 432


                  ....*..
gi 193204318 1815 gFGKNVR 1821
Cdd:COG0044   433 -RGRFLR 438
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 511-713 3.76e-97

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 311.93  E-value: 3.76e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   511 DRDLFNQEISAIGEKVAPSKAAT--TMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELIAIAQQALAHS------ 582
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   583 NQVLVDKSLKGWKEVEYEVVRDAYDNCITVCNMENVDPLgiHTGESVVVAPSQTLSDREYNALRTCAIKVIRHLGIIGEC 662
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 193204318   663 NIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGQHLP 713
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 1476-1801 6.35e-90

Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.


Pssm-ID: 238643 [Multi-domain]  Cd Length: 361  Bit Score: 297.71  E-value: 6.35e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNsk 1555
Cdd:cd01318     5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTGSE-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 fAAEFADKA--AGLKMYLNETFSTLkmdnISDWAKHLSAFPANRPIVC-HAEKQTL------------------------ 1608
Cdd:cd01318    83 -DLEELDKAppAGYKIFMGDSTGDL----LDDEETLERIFAEGSVLVTfHAEDEDRlrenrkelkgesahprirdaeaaa 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1609 ---AAILCMAQMANRAVHIAHVATADEINLVKEAKQRgwnVTCEVCPHHLFLIEEDL-PDGIR-EVRPRLVKPEDRQALW 1683
Cdd:cd01318   158 vatARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYdRLGTLgKVNPPLRSREDRKALL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1684 DNMEY--IDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPpqDDTYI 1761
Cdd:cd01318   235 QALADgrIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIK--NKGRI 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 193204318 1762 E---------VDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRG 1801
Cdd:cd01318   313 AegydadltvVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 1473-1794 1.64e-88

Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.


Pssm-ID: 238627 [Multi-domain]  Cd Length: 337  Bit Score: 292.76  E-value: 1.64e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1473 LKRLPGMVDIHVHVREPGAT-HKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATP 1551
Cdd:cd01302     1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1552 ----NNSKFAAEFAdkAAGLKMYLNETFSTLKMDNISDWAKHLSAFPANR-PIVCHAEKqtlaaILCMAQMANRAVHIAH 1626
Cdd:cd01302    81 gdvtDELKKLFDAG--INSLKVFMNYYFGELFDVDDGTLMRTFLEIASRGgPVMVHAER-----AAQLAEEAGANVHIAH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1627 VATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDL-PDGIR-EVRPRLVKPEDRQALWDNME--YIDCFATDHAPHTWA 1702
Cdd:cd01302   154 VSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLrLNGAWgKVNPPLRSKEDREALWEGVKngKIDTIASDHAPHSKE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1703 EK-TGKDG-KIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQ---------DDTYieVDLNEEWTI 1771
Cdd:cd01302   234 EKeSGKDIwKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKgtiavgydaDLVI--VDPKKEWKV 311

                         330       340
                  ....*....|....*....|...
gi 193204318 1772 PENGGQSKAGWTPFAGRKVFGKV 1794
Cdd:cd01302   312 TAEEIESKADWTPFEGMEVTGKP 334
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 388-779 2.83e-88

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 313.47  E-value: 2.83e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   388 KEQRKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPT 467
Cdd:TIGR01369  552 TDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPE 631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   468 GILCTFGGQTALNCAIDLYKDGifeqydVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGY 547
Cdd:TIGR01369  632 GVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGY 705

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   548 PVLVRAAYALGGLGSGFADNREELIAIAQQALAHSNQ--VLVDKSLKGWKEVEYEVVrdAYDNCITVCN-MENVDPLGIH 624
Cdd:TIGR01369  706 PVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAV--SDGEEVLIPGiMEHIEEAGVH 783

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   625 TGESVVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSLtyYIIEVNARLSRSSALASKATGYPLAYVAA 704
Cdd:TIGR01369  784 SGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEV--YVIEVNPRASRTVPFVSKATGVPLAKLAV 861

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193204318   705 KLALGQHLpviRNSVTGtttacFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKALR 779
Cdd:TIGR01369  862 RVMLGKKL---EELGVG-----KEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQL 928
PRK11891 PRK11891
aspartate carbamoyltransferase; Provisional
 1868-2198 3.22e-84

aspartate carbamoyltransferase; Provisional


Pssm-ID: 183362 [Multi-domain]  Cd Length: 429  Bit Score: 283.68  E-value: 3.22e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1868 IAFPGEllaKNCISVKHLDKGQINRIFELADRYKhDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSV-I 1946
Cdd:PRK11891   82 FAFEGK---PQLLSVDQFSRDSVEALFRVADVMQ-PIARRQKISRVLEGAVLGNLFFEASTRTRVSFGAAFCRLGGSVcD 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1947 SVDSQSSSVQKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQE---MG- 2022
Cdd:PRK11891  158 TTGFTFSSMAKGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGDGPGEHPSQALLDLYTIQREfsrLGk 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2023 TVNGLTIALVGDLKNGRTVHSLAKLLCLYKDITLHYVAPsTELEMPQEVLDYVSSKSNFVQKKfTSLAEGINHVDVVYVT 2102
Cdd:PRK11891  238 IVDGAHIALVGDLKYGRTVHSLVKLLALYRGLKFTLVSP-PTLEMPAYIVEQISRNGHVIEQT-DDLAAGLRGADVVYAT 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2103 RIQKERFSSpDEYNKVKGSYVINAKLLNEA-ARDVeepssllvparslpIVMHPLPR-----VDEIAVELDHDERAAYFR 2176
Cdd:PRK11891  316 RIQKERFAD-ESFEGYTPDFQINQALVDAVcKPDT--------------LIMHPLPRdsrpgANDLSTDLNRDPRLAIFR 380

                         330       340
                  ....*....|....*....|..
gi 193204318 2177 QAKNGVFVRMSILSLLLGRGHL 2198
Cdd:PRK11891  381 QTDNGIPVRMAIFAVLLGVENL 402
carB PRK05294
carbamoyl-phosphate synthase large subunit;
389-777 5.74e-84

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 300.86  E-value: 5.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  389 EQRKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTG 468
Cdd:PRK05294  553 DRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKG 632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  469 ILCTFGGQTALNCAIDLykdgifEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYP 548
Cdd:PRK05294  633 VIVQFGGQTPLKLAKAL------EAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYP 706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  549 VLVRAAYALGGLGSGFADNREELIAIAQQALAHSNQ--VLVDKSLKGWKEVeyEVvrDAydncitVCN---------MEN 617
Cdd:PRK05294  707 VLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDhpVLIDKFLEGAIEV--DV--DA------ICDgedvliggiMEH 776

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  618 VDPLGIHTGESVVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALdpYSLTYYIIEVNARLSRSSALASKATGY 697
Cdd:PRK05294  777 IEEAGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAV--KDDEVYVIEVNPRASRTVPFVSKATGV 854

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  698 PLAYVAAKLALGQHLPVIrnsvtGTTTacfEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKA 777
Cdd:PRK05294  855 PLAKIAARVMLGKKLAEL-----GYTK---GLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 1476-1804 7.12e-84

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 282.02  E-value: 7.12e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNN-- 1553
Cdd:TIGR00857   38 LPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNqg 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1554 ---SKFAAEFADKAAGlKMYLNETFSTLKMDNI---------------------------------SDWAKHLSAFPanr 1597
Cdd:TIGR00857  118 kelTEAYELKEAGAVG-RMFTDDGSEVQDILSMrraleyaaiagvpialhaedpdliyggvmhegpSAAQLGLPARP--- 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1598 pivCHAEKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLP--DGIREVRPRLVK 1675
Cdd:TIGR00857  194 ---PEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVArlDGNGKVNPPLRE 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1676 PEDRQALWDNM--EYIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNL 1753
Cdd:TIGR00857  271 KEDRLALIEGLkdGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGL 350

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318  1754 PPQ-------DDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEA 1804
Cdd:TIGR00857  351 PDKgtleegnPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVV 408
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 386-777 7.39e-83

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 297.27  E-value: 7.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  386 HAKEQRKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKER 465
Cdd:PRK12815  551 PSSEKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAEN 630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  466 PTGILCTFGGQTALNCAIDLYKDGifeqydVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEEL 545
Cdd:PRK12815  631 IKGVIVQFGGQTAINLAKGLEEAG------LTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRI 704

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  546 GYPVLVRAAYALGGLGSGFADNREELIAIAQQALAHSNQVLVDKSLKGwKEVEYEVVRDAYDncITVCN-MENVDPLGIH 624
Cdd:PRK12815  705 GYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDG-KEYEVDAISDGED--VTIPGiIEHIEQAGVH 781

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  625 TGESVVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSLtyYIIEVNARLSRSSALASKATGYPLAYVAA 704
Cdd:PRK12815  782 SGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEI--YVLEVNPRASRTVPFVSKATGVPLAKLAT 859

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193204318  705 KLALGQHLPVIRNSVTgtttacFEPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEEALQKA 777
Cdd:PRK12815  860 KVLLGKSLAELGYPNG------LWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKG 926
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 3-365 3.86e-82

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 275.91  E-value: 3.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    3 ATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPSAEIldqfklpaefESDR 82
Cdd:CHL00197    7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDI----------ESVK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   83 IWPAALIVEKICvdGEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAklVIESDN-------------- 148
Cdd:CHL00197   77 IQVKGIIAKNIC--KSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNG--CISNQNlnlsylrakikesp 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  149 -AQNFDYV-DVNAENLVDFVSRKEPVVYgSGDQT---------ILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDTESD 217
Cdd:CHL00197  153 hMPSSDLIpRVTTSSYYEWDEKSHPSFY-LADNKrphssyqlkIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILS 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  218 Y--DGLFLSNGPGDPEICAPLVDRLAKVIARgDKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPcthyaTG---RCY 292
Cdd:CHL00197  232 YqpDGILLSNGPGDPSAIHYGIKTVKKLLKY-NIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHP-----SGlnqQVE 305

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193204318  293 ITSQNHGYAVDPDSLPAD-WKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLFDVFADSVRQAKS 365
Cdd:CHL00197  306 ITSQNHGFAVNLESLAKNkFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKS 379
PRK08192 PRK08192
aspartate carbamoyltransferase; Provisional
 1870-2194 6.40e-81

aspartate carbamoyltransferase; Provisional


Pssm-ID: 169269 [Multi-domain]  Cd Length: 338  Bit Score: 270.83  E-value: 6.40e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1870 FPGEllakNCISVKHLDKGQINRIFELADRYkHDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVD 1949
Cdd:PRK08192    3 FQGS----HILSVNQLDRDAIQRIFNVADRM-EPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVRETT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1950 -SQSSSVQKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGDGTGEHPTQALLDVYTIRQEM----GTV 2024
Cdd:PRK08192   78 gMASSSLSKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2025 NGLTIALVGDLKNGRTVHSLAKLLCLYKDITLHYVAPStELEMPQEVLDYVSSKSNFVQKKfTSLAEGINHVDVVYVTRI 2104
Cdd:PRK08192  158 DGMHIAMVGDLKFGRTVHSLSRLLCMYKNVSFTLVSPK-ELAMPDYVISDIENAGHKITIT-DQLEGNLDKADILYLTRI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2105 QKERFSSPDEYNKVKGSYVINAKLLNEAArdveEPSSllvparslpIVMHPLPR-VDEIAVELDHDERA----AYFRQAK 2179
Cdd:PRK08192  236 QEERFPSQEEANKYRGKFRLNQSIYTQHC----KSNT---------VIMHPLPRdSRAQANELDNDLNShpnlAIFRQAD 302

                         330
                  ....*....|....*
gi 193204318 2180 NGVFVRMSILSLLLG 2194
Cdd:PRK08192  303 NGLLIRMALFALTLG 317
pyrC PRK09357
dihydroorotase; Validated
 1476-1807 6.00e-79

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 268.22  E-value: 6.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDyALYIGATPNNSK 1555
Cdd:PRK09357   52 APGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVD-VLPVGAITKGLA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 FA--AEF-ADKAAGLKMYLN---ETFSTLKMDNISDWAKHLsafpaNRPIVCHAEKQTLAAILCM--------------- 1614
Cdd:PRK09357  131 GEelTEFgALKEAGVVAFSDdgiPVQDARLMRRALEYAKAL-----DLLIAQHCEDPSLTEGGVMnegevsarlglpgip 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1615 -----AQMA----------NRaVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLP--DGIREVRPRLVKPE 1677
Cdd:PRK09357  206 avaeeVMIArdvllaeatgAR-VHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLtyDPNYKVNPPLRTEE 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1678 DRQALWDNME--YIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTA-VHDGKLTMKELTDRMSTNPRRIFNLP 1754
Cdd:PRK09357  285 DREALIEGLKdgTIDAIATDHAPHAREEKECEFEAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTINPARILGLP 364

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318 1755 PqddTYIEV---------DLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVID 1807
Cdd:PRK09357  365 A---GPLAEgepadlvifDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
PRK02382 PRK02382
dihydroorotase; Provisional
 1476-1821 2.06e-77

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 264.59  E-value: 2.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNSK 1555
Cdd:PRK02382   53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGNWDP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 FAAEFADKAAGLkmylNETF---STLKMdNIS--DWAKHLSAFPANRPIVC-HAEKQTL--------------------- 1608
Cdd:PRK02382  133 LESLWERGVFAL----GEIFmadSTGGM-GIDeeLFEEALAEAARLGVLATvHAEDEDLfdelakllkgdadadawsayr 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1609 ------AAILCMAQMANR---AVHIAHVATADEINLVKEAKqrgwnVTCEVCPHHLFLIEEDLPD----GirEVRPRLVK 1675
Cdd:PRK02382  208 paaaeaAAVERALEVASEtgaRIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERlgtfG--KMNPPLRS 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1676 PEDRQALWD--NMEYIDCFATDHAPHTWAEKtgkDGKI---PPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRI 1750
Cdd:PRK02382  281 EKRREALWErlNDGTIDVVASDHAPHTREEK---DADIwdaPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARI 357

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193204318 1751 FNLPPQ-------DDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRK-VFGKVhnVIIRGEEAVIDGRIVAIPGFGKNVR 1821
Cdd:PRK02382  358 FGLDGKgriaegyDADLVLVDPDAAREIRGDDLHSKAGWTPFEGMEgVFPEL--TMVRGTVVWDGDDINAKRGRGEFLR 434
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 1476-1795 1.34e-71

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 245.22  E-value: 1.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLvDTDS--FYQTEQLASAKSVVDYAlyIGA-TP- 1551
Cdd:cd01317    13 APGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAvvELLKNRAKDVGIVRVLP--IGAlTKg 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1552 NNSKFAAEFAD-KAAGLKMYLNETFsTLKMDNISDWAKHLsAFPANRPIVCHAEKQTLAA-------------------- 1610
Cdd:cd01317    90 LKGEELTEIGElLEAGAVGFSDDGK-PIQDAELLRRALEY-AAMLDLPIIVHPEDPSLAGggvmnegkvasrlglpgipp 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1611 ---------ILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPD---GIReVRPRLVKPED 1678
Cdd:cd01317   168 eaetimvarDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESydtNAK-VNPPLRSEED 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1679 RQALWDNME--YIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTAVHD-GKLTMKELTDRMSTNPRRIFNLPP 1755
Cdd:cd01317   247 REALIEALKdgTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKgGLLTLPDLIRALSTNPAKILGLPP 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 193204318 1756 QddtYIEV---------DLNEEWTIPENGGQSKAGWTPFAGRKVFGKVH 1795
Cdd:cd01317   327 G---RLEVgapadlvlfDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVL 372
PRK07575 PRK07575
dihydroorotase; Provisional
 1429-1810 3.23e-71

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 246.51  E-value: 3.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1429 RMAIDNGIPLITDIKCAKTFIQALEMVGKRPTMNSLVDcvtSKSLKRLPGMVDIHVHVREPGATHKEDWATCSKAALAGG 1508
Cdd:PRK07575   11 RILLPSGELLLGDVLVEDGKIVAIAPEISATAVDTVID---AEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1509 VTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNskfAAEF--ADKAAGLKMYLNETFSTLKMDnisDW 1586
Cdd:PRK07575   88 VTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDN---LPELltANPTCGIKIFMGSSHGPLLVD---EE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1587 AKHLSAFPA-NRPIVCHAEKQT--------LAAI----------------------LCMAQMANRAVHIAHVATADEINL 1635
Cdd:PRK07575  162 AALERIFAEgTRLIAVHAEDQArirarraeFAGIsdpadhsqiqdeeaallatrlaLKLSKKYQRRLHILHLSTAIEAEL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1636 VKEAKqRGWnVTCEVCPHHLFLIEEDLpDGI---REVRPRLVKPEDRQALWDNME--YIDCFATDHAPHTWAEKTGKDGK 1710
Cdd:PRK07575  242 LRQDK-PSW-VTAEVTPQHLLLNTDAY-ERIgtlAQMNPPLRSPEDNEALWQALRdgVIDFIATDHAPHTLEEKAQPYPN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1711 IPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQ-------DDTYIEVDLNEEWTIPENGGQSKAGWT 1783
Cdd:PRK07575  319 SPSGMPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGIPNKgriapgyDADLVLVDLNTYRPVRREELLTKCGWS 398

                         410       420
                  ....*....|....*....|....*..
gi 193204318 1784 PFAGRKVFGKVHNVIIRGEEAVIDGRI 1810
Cdd:PRK07575  399 PFEGWNLTGWPVTTIVGGQIVFDRGQV 425
PRK04250 PRK04250
dihydroorotase; Provisional
 1476-1820 1.55e-66

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 231.58  E-value: 1.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNSK 1555
Cdd:PRK04250   46 LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 FAAEFAD-KAAGLKMYLNETFSTlkmDNISDWAKHLSA-------------FPANRPIvchAEKQTLAAILCMAQMANRA 1621
Cdd:PRK04250  126 AEEIKADfYKIFMGASTGGIFSE---NFEVDYACAPGIvsvhaedpelireFPERPPE---AEVVAIERALEAGKKLKKP 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1622 VHIAHVATADEINLVKEaKQRGWnVTCEVCPHHLFLIEEDLPDGIR-EVRPRLVKPEDRQALWDNMEYIDCFATDHAPHT 1700
Cdd:PRK04250  200 LHICHISTKDGLKLILK-SNLPW-VSFEVTPHHLFLTRKDYERNPLlKVYPPLRSEEDRKALWENFSKIPIIASDHAPHT 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1701 WAEKtgKDGKipPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPP------QDDTYIEVDLNEEWTIPEN 1774
Cdd:PRK04250  278 LEDK--EAGA--AGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNygieegNYANFAVFDMKKEWTIKAE 353

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 193204318 1775 GGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIPgFGKNV 1820
Cdd:PRK04250  354 ELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP-RGVRI 398
PRK09060 PRK09060
dihydroorotase; Validated
 1423-1821 3.08e-66

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 232.12  E-value: 3.08e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1423 HGYKTRRMAIDNG-IPLITDIKCAktfiQALEmvgkrptmnsLVDCvtsKSLKRLPGMVDIHVHVREPGATHKEDWATCS 1501
Cdd:PRK09060   18 DGEGRADIGIRDGrIAAIGDLSGA----SAGE----------VIDC---RGLHVLPGVIDSQVHFREPGLEHKEDLETGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1502 KAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNSKFAAEF--ADKAAGLKMYLNETFSTLK 1579
Cdd:PRK09060   81 RAAVLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELerLPGCAGIKVFMGSSTGDLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1580 MDNISDWAKHLSAfpANRPIVCHAEKQTL-----------------------AAILC------MAQMANRAVHIAHVATA 1630
Cdd:PRK09060  161 VEDDEGLRRILRN--GRRRAAFHSEDEYRlrerkglrvegdpsshpvwrdeeAALLAtrrlvrLARETGRRIHVLHVSTA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1631 DEINLVKEAKQRgwnVTCEVCPHHLFLIEEDLPD---GIREVRPRLVKPEDRQALWDNME--YIDCFATDHAPHTWAEKT 1705
Cdd:PRK09060  239 EEIDFLADHKDV---ATVEVTPHHLTLAAPECYErlgTLAQMNPPIRDARHRDGLWRGVRqgVVDVLGSDHAPHTLEEKA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1706 GKDGKIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQ-------DDTYIEVDLNEEWTIPENGGQS 1778
Cdd:PRK09060  316 KPYPASPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAGKgriavgyDADFTIVDLKRRETITNEWIAS 395

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 193204318 1779 KAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAiPGFGKNVR 1821
Cdd:PRK09060  396 RCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVG-PPTGEPVR 437
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-142 4.53e-65

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 216.86  E-value: 4.53e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318      1 MRATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFES 80
Cdd:smart01097    1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVN----------DEDFES 70

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318     81 DRIWPAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKL 142
Cdd:smart01097   71 DKIQVKGLVVRELSD--EPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-142 1.75e-64

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.


Pssm-ID: 460017 [Multi-domain]  Cd Length: 126  Bit Score: 214.88  E-value: 1.75e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318     5 LHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFESDRIW 84
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVN----------PEDFESDKIH 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318    85 PAALIVEKICVdgEHSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKL 142
Cdd:pfam00988   71 VAGLVVREYSD--EPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
PRK09236 PRK09236
dihydroorotase; Reviewed
 1476-1811 6.60e-64

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 225.52  E-value: 6.60e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNN-S 1554
Cdd:PRK09236   53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNlD 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1555 KFAAEFADKAAGLKMYLNEtfSTLKM--DNIsdwaKHLSAFPANRP--IVCHAE-----KQTLAAIL------------- 1612
Cdd:PRK09236  133 EIKRLDPKRVCGVKVFMGA--STGNMlvDNP----ETLERIFRDAPtlIATHCEdtptiKANLAKYKekygddipaemhp 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1613 -------C---------MAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPD-GIR-EVRPRLV 1674
Cdd:PRK09236  207 lirsaeaCykssslavsLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARlGNLiKCNPAIK 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1675 KPEDRQALW----DNMeyIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRI 1750
Cdd:PRK09236  287 TASDREALRqalaDDR--IDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAIL 364

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1751 FNLppQDDTYIE---------VDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIV 1811
Cdd:PRK09236  365 FDI--KERGFIRegywadlvlVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 3-353 9.18e-64

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 224.09  E-value: 9.18e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    3 ATLHLEDGSTFVGSIYGATKSVVGEIVFQTGMVGYVESLTDPSYAKQLLTLTYPLIGNYGVPsaeildqfklPAEFESDR 82
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVN----------FDDEESRQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   83 IWPAALIVEKICVDGehSHWQAVQSLSEWLRKADVPCLSGIDVRQLVKKIRETGTMKAKLVIESDN--------AQNFDY 154
Cdd:PLN02771  127 CFLAGLVIRSLSIST--SNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKtdeellkmSRSWDI 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  155 VDVNaenLVDFVSRKEPvvYGSGDQT-----------------ILAVDCGLKNNQIRCLAKRGFRVKVVPWNHPIDT--E 215
Cdd:PLN02771  205 VGID---LISGVSCKSP--YEWVDKTnpewdfntnsrdgesyhVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEalK 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  216 SDYDGLFLSNGPGDPEICAPLVDRLAKVIarGDKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATGRCYITS 295
Cdd:PLN02771  280 MKPDGVLFSNGPGDPSAVPYAVETVKELL--GKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISA 357

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318  296 QNHGYAVDPDSLPADWKALFTNENDKTNEGIVHSSKPFFSVQFHPEHTAGPTDCEFLF 353
Cdd:PLN02771  358 QNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
GATase pfam00117
Glutamine amidotransferase class-I;
182-356 1.42e-63

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 214.79  E-value: 1.42e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   182 LAVDCGL--KNNQIRCLAKRGFRVKVVPWNHPIDT--ESDYDGLFLSNGPGDPEICAPLVDRLAKVIARGdKPIFGICLG 257
Cdd:pfam00117    1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEilEENPDGIILSGGPGSPGAAGGAIEAIREARELK-IPILGICLG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   258 HQILSRAIGAKTYKLK-YGNRGHNQPCTH------YATGRCYITSQNHGYAVDPDSLPADWKALFTNENDKTNEGIVHSS 330
Cdd:pfam00117   80 HQLLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKK 159

                          170       180
                   ....*....|....*....|....*.
gi 193204318   331 KPFFSVQFHPEHTAGPTDCEFLFDVF 356
Cdd:pfam00117  160 LPIFGVQFHPESILTPHGPEILFNFF 185
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 1476-1821 4.72e-62

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 220.24  E-value: 4.72e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMP-NTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNS 1554
Cdd:cd01315    51 MPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1555 KFAAEFADKAA-GLK----------------MYLNETFSTLK-----------MDNISDWA---------KHLSAFPANR 1597
Cdd:cd01315   131 DQLRPLDEAGVvGFKcflcpsgvdefpavddEQLEEAMKELAktgsvlavhaeNPEITEALqeqakakgkRDYRDYLASR 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1598 PIVchAEKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVR--PRLVK 1675
Cdd:cd01315   211 PVF--TEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKcaPPIRD 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1676 PEDRQALWDNME--YIDCFATDHAPHTWAEKTGKDG---KIPPGFPGVEYMLPLLLT-AVHDGKLTMKELTDRMSTNPRR 1749
Cdd:cd01315   289 AANQEQLWEALEngDIDMVVSDHSPCTPELKLLGKGdffKAWGGISGLQLGLPVMLTeAVNKRGLSLEDIARLMCENPAK 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1750 IFNLPPQ--------DDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIPgFGKNVR 1821
Cdd:cd01315   369 LFGLSHQkgriavgyDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP-LGQLLL 447
PLN02735 PLN02735
carbamoyl-phosphate synthase
 390-777 7.69e-62

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 233.13  E-value: 7.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  390 QRKVLVLGSGGLTIGQAGEFDYSGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLPITKEYVTDVIKKERPTGI 469
Cdd:PLN02735  574 KKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGI 653

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  470 LCTFGGQTALNCAIDLykdgifEQY-------------DVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTME 536
Cdd:PLN02735  654 IVQFGGQTPLKLALPI------QKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEA 727

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  537 GAIEAAEELGYPVLVRAAYALGGLGSGFADNREELIAIAQQALAHSNQ--VLVDKSLKGWKEVEYEVVRDAYDNCITVCN 614
Cdd:PLN02735  728 DALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPErpVLVDKYLSDATEIDVDALADSEGNVVIGGI 807

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  615 MENVDPLGIHTGESVVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPySLTYYIIEVNARLSRSSALASKA 694
Cdd:PLN02735  808 MEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITP-SGEVYIIEANPRASRTVPFVSKA 886

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  695 TGYPLAYVAAKLALGQHLPVIrnsvtgtttaCF--EPSLDYCVVKIPRWDLGKFARVSTQIGSSMKSVGEVMGIGRCFEE 772
Cdd:PLN02735  887 IGHPLAKYASLVMSGKSLKDL----------GFteEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSK 956


                  ....*
gi 193204318  773 ALQKA 777
Cdd:PLN02735  957 AFAKA 961
allantoinase TIGR03178
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ...
 1476-1814 5.27e-56

allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.


Pssm-ID: 163175 [Multi-domain]  Cd Length: 443  Bit Score: 202.61  E-value: 5.27e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMP-NTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNS 1554
Cdd:TIGR03178   50 FPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNL 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1555 KFAAEFADKAA-GLKMYLnetfSTLKMD---NISDW----------------------AKHLS---------------AF 1593
Cdd:TIGR03178  130 DDLRELDEAGVvGFKAFL----SPSGDDefpHVDDWqlykgmrelarlgqlllvhaenPAITSalgeeappqggvgadAY 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1594 PANRPIVchAEKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVR--P 1671
Cdd:TIGR03178  206 LASRPVF--AEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKcaP 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1672 RLVKPEDRQALWDNME--YIDCFATDHAPHTWAEKTGKD-GKIPPGFPGVEYMLPLLLT-AVHDGKLTMKELTDRMSTNP 1747
Cdd:TIGR03178  284 PIRDLANQEGLWEALLngLIDCVVSDHSPCTPDLKRAGDfFKAWGGIAGLQSTLDVMFDeAVQKRGLPLEDIARLMATNP 363

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193204318  1748 RRIFNL-------PPQDDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIP 1814
Cdd:TIGR03178  364 AKRFGLaqkgriaPGKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
PRK06189 PRK06189
allantoinase; Provisional
 1476-1826 9.36e-52

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 190.30  E-value: 9.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMP-NTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNS 1554
Cdd:PRK06189   53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1555 KFAAEFADKAA-GLKMYLNET----------FSTLK-MDNISDWAK-------------HLS------------AFPANR 1597
Cdd:PRK06189  133 EHLRELAEAGViGFKAFMSNSgtdefrssddLTLYEgMKEIAALGKilalhaesdaltrHLTtqarqqgktdvrDYLESR 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1598 PIVchAEKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPD--GIREVRPRLVK 1675
Cdd:PRK06189  213 PVV--AELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERigAVAKCAPPLRS 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1676 PEDRQALWDNM--EYIDCFATDHAPHTWAEKTGKD-----GkippGFPGVEYMLPLLLT-AVHDGKLTMKELTDRMSTNP 1747
Cdd:PRK06189  291 RSQKEELWRGLlaGEIDMISSDHSPCPPELKEGDDfflvwG----GISGGQSTLLVMLTeGYIERGIPLETIARLLATNP 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1748 RRIFNLPP-------QDDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIPgFGKNV 1820
Cdd:PRK06189  367 AKRFGLPQkgrlevgADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPPP-RGQLL 445


                  ....*.
gi 193204318 1821 RLYPHS 1826
Cdd:PRK06189  446 RPSVVK 451
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 800-922 3.62e-49

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 171.09  E-value: 3.62e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318    800 DDLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVNTVSAELLLEAKQAGFSDRQIAK 879
Cdd:smart01096    3 EELRTPTDERLFYIAEALRRG-YSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 193204318    880 KIGSNEYTVREARFVKGITPCVKQIDTVAGEWPAQTNYLYTTF 922
Cdd:smart01096   82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 1476-1817 1.01e-47

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 178.18  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREP--GATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNN 1553
Cdd:cd01314    50 LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWT 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1554 SKFAAE----FADKAAGLKMY-------------LNETFSTLK------M------DNISDWAKHLSA--------FPAN 1596
Cdd:cd01314   130 DSVIEElpelVKKGISSFKVFmaykgllmvddeeLLDVLKRAKelgalvMvhaengDVIAELQKKLLAqgktgpeyHALS 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1597 RPIVCHAEKQTLAAILcmAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDL----PDGIREV-RP 1671
Cdd:cd01314   210 RPPEVEAEATARAIRL--AELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYwkdwFEGAKYVcSP 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1672 RLVKPEDRQALWDNMEY--IDCFATDHAPHTWAEKT-GKDG--KIPPGFPGVEYMLPLLLTA-VHDGKLTMKELTDRMST 1745
Cdd:cd01314   288 PLRPKEDQEALWDGLSSgtLQTVGSDHCPFNFAQKArGKDDftKIPNGVPGVETRMPLLWSEgVAKGRITLEKFVELTST 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1746 NPRRIFNLPPQDDTyIEV---------DLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIPGF 1816
Cdd:cd01314   368 NPAKIFGLYPRKGT-IAVgsdadlviwDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGS 446


                  .
gi 193204318 1817 G 1817
Cdd:cd01314   447 G 447
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1878-2019 3.45e-47

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 166.06  E-value: 3.45e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1878 NCISVKHLDKGQINRIFELADRYKHDVEKGHPlTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQK 1957
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKK-LPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318  1958 GETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGdGTGEHPTQALLDVYTIRQ 2019
Cdd:pfam02729   80 GESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 1476-1821 5.77e-47

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937 [Multi-domain]  Cd Length: 454  Bit Score: 176.42  E-value: 5.77e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1476 LPGMVDIHVHVREP--GATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNN 1553
Cdd:TIGR02033   50 LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWN 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1554 SKFAAEF--ADKAAGL---KMYL----------NETFSTLKM--------------DNISDW--AKHLSA-------FPA 1595
Cdd:TIGR02033  130 DSVLEEHipEVKEEGInsfKVFMayknllmvddEELFEILKRlkelgallqvhaenGDIIAElqARMLAQgitgpeyHAL 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1596 NRPIVCHAEkqTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLP----DGIREV-R 1670
Cdd:TIGR02033  210 SRPPELEAE--AVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDkpgfEGAKYVcS 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1671 PRLVKPEDRQALWDNMEY--IDCFATDHAPHTWAEKT--GKDG--KIPPGFPGVEYMLPLLLTA-VHDGKLTMKELTDRM 1743
Cdd:TIGR02033  288 PPLREPEDQDALWSALSSgaLQTVGSDHCTFNFAQKKaiGKDDftKIPNGGPGVEERMSLLFDEgVAKGRITLEKFVEVT 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1744 STNPRRIFNLPPQ--------DDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIPG 1815
Cdd:TIGR02033  368 STNPAKIFNLYPRkgtiavgsDADIVIWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAG 447


                   ....*.
gi 193204318  1816 FGKNVR 1821
Cdd:TIGR02033  448 AGRFVK 453
pyrC PRK00369
dihydroorotase; Provisional
 1476-1821 2.41e-45

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 169.94  E-value: 2.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFyqTEQLAS--AKSVVDYALYIGATPNN 1553
Cdd:PRK00369   46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAI--TEKLAEleYYSRVDYFVYSGVTKDP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1554 SKFaAEFAdkAAGLKMYLN--ETFSTLKmdNISDWAK-------HLSAFPANRPIV--CHAEkqtLAAILCMAQMANraV 1622
Cdd:PRK00369  124 EKV-DKLP--IAGYKIFPEdlEREETFR--VLLKSRKlkilhpeVPLALKSNRKLRrnCWYE---IAALYYVKDYQN--V 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1623 HIAHVATadeINLVKEAKQRGWNVtcEVCPHHLFLIEEDlpDGIREVRPRLVKPEDRQALWDNMEYIDCFATDHAPHTWA 1702
Cdd:PRK00369  194 HITHASN---PRTVRLAKELGFTV--DITPHHLLVNGEK--DCLTKVNPPIRDINERLWLLQALSEVDAIASDHAPHSSF 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1703 EKTGKDGKIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPpqdDTYIEVDLNEEWTIPE------NGG 1776
Cdd:PRK00369  267 EKLQPYEVCPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIP---YGEIKEGYRANFTVIQfedwrySTK 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 193204318 1777 QSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIPG---FGKNVR 1821
Cdd:PRK00369  344 YSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGinpFGERKR 391
PRK01211 PRK01211
dihydroorotase; Provisional
 1476-1809 5.91e-44

dihydroorotase; Provisional


Pssm-ID: 179247 [Multi-domain]  Cd Length: 409  Bit Score: 166.19  E-value: 5.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNSK 1555
Cdd:PRK01211   45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 FAAEfadKAAGLKMYLNETFSTLKMD------------NISDW---------------AKHLSAFPANRPIVCHaekqtL 1608
Cdd:PRK01211  125 ILDE---RSIGLKVYMGGTTNTNGTDieggeikkineaNIPVFfhaelseclrkhqfeSKNLRDHDLARPIECE-----I 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1609 AAILCMAQMANRAVHIAHVATADEINlvkeakqrgwNVTCEVCPHHLFLiEEDLPDG-IREVRPRLVKPEDRQALWDnmE 1687
Cdd:PRK01211  197 KAVKYVKNLDLKTKIIAHVSSIDVIG----------RFLREVTPHHLLL-NDDMPLGsYGKVNPPLRDRWTQERLLE--E 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1688 YI----DCFATDHAPHTWAEKTGKDGKiPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPP------QD 1757
Cdd:PRK01211  264 YIsgrfDILSSDHAPHTEEDKQEFEYA-KSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKgkieegYD 342

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 193204318 1758 DTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKvHNVIIRGeEAVIDGR 1809
Cdd:PRK01211  343 ADFMAFDFTNIKKINDKRLHSKCPVSPFNGFDAIFP-SHVIMRG-EVVIDNY 392
PRK08323 PRK08323
phenylhydantoinase; Validated
 1476-1821 8.48e-42

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 161.11  E-value: 8.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREP--GATHKEDWATCSKAALAGGVTTIL--AMPNTSPVLVDTDSFYQteQLASAKSVVDYALYIGATP 1551
Cdd:PRK08323   48 MPGGIDPHTHMEMPfgGTVSSDDFETGTRAAACGGTTTIIdfALQPKGQSLREALEAWH--GKAAGKAVIDYGFHMIITD 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1552 NNSKFAAEfadkaagLKMYLNETFSTLKM----DN---ISDW--------AKHLSAFPAnrpivCHAE---------KQT 1607
Cdd:PRK08323  126 WNEVVLDE-------MPELVEEGITSFKLfmayKGalmLDDDellralqrAAELGALPM-----VHAEngdaiaylqAKL 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1608 LAA-------------ILCMAQMANRAVHIA----------HVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDL-- 1662
Cdd:PRK08323  194 LAEgktgpeyhalsrpPEVEGEATNRAIMLAelagaplyivHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYdg 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1663 PDGIREVR----PRLVKPEDRQALWDNME--YIDCFATDHAPHTWAEK--TGKD--GKIPPGFPGVEYMLPLLLTA-VHD 1731
Cdd:PRK08323  274 PDWFEGAKyvmsPPLRDKEHQDALWRGLQdgDLQVVATDHCPFCFEQKkqLGRGdfTKIPNGTPGVEDRMPLLFSEgVMT 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1732 GKLTMKELTDRMSTNPRRIFNLPPQDDTyIEV---------DLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGE 1802
Cdd:PRK08323  354 GRITLNRFVELTSTNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGE 432

                         410
                  ....*....|....*....
gi 193204318 1803 EAVIDGRIVAIPGFGKNVR 1821
Cdd:PRK08323  433 VVVEDGEFRGKAGHGRFLK 451
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1323-1450 1.67e-40

Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.


Pssm-ID: 238711 [Multi-domain]  Cd Length: 116  Bit Score: 145.91  E-value: 1.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1323 QNIFISIGGYhAKAEMLKSVEALLKLGYELYGSKGTADYFQSNKINVKPVDWPFEEGSSDEktasgtRSVVEFLENKEFH 1402
Cdd:cd01423     1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK------PSLRELLAEGKID 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 193204318 1403 LVINLPIRGSGAYRVSafrthGYKTRRMAIDNGIPLITDIKCAKTFIQ 1450
Cdd:cd01423    74 LVINLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
ArgF COG0078
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ...
 1877-2195 5.02e-40

Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439848 [Multi-domain]  Cd Length: 310  Bit Score: 151.74  E-value: 5.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKHDVEKGHPlTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQ 1956
Cdd:COG0078     6 RHFLSLLDLTPEELRALLDLAAELKAKRKAGIP-HRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYLDPGDSQLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1957 KGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVING-GDgtGEHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:COG0078    85 RGESIKDTARVLSRYVDGIMIRTFGHETLEELAKYAGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLKVAYVGDG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2036 KNgrTVHSLAKLLCLYkDITLHYVAPStELEMPQEVLD-----YVSSKSNFVQkkFTSLAEGINHVDVVYvTRI------ 2104
Cdd:COG0078   163 NN--VANSLLLAAAKL-GMDVRIATPE-GYEPDPEIVAkakeiAAESGGSITI--THDPAEAVKGADVVY-TDVwvsmgq 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2105 QKERfsspDEYNKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLP--RVDEIAVE-LDHdERAAYFRQAKNG 2181
Cdd:COG0078   236 EEEA----EERIKAFKPYQVNEELMALAKPDA--------------IFMHCLPahRGEEVTDEvIDG-PQSVVFDEAENR 296

                         330
                  ....*....|....
gi 193204318 2182 VFVRMSILSLLLGR 2195
Cdd:COG0078   297 LHAQKALLAWLLGG 310
pyrB PRK13814
aspartate carbamoyltransferase;
1880-2195 3.33e-39

aspartate carbamoyltransferase;


Pssm-ID: 139876 [Multi-domain]  Cd Length: 310  Bit Score: 149.48  E-value: 3.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1880 ISVKHLDKGQINRIFELADRYKHDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQKGE 1959
Cdd:PRK13814    9 LNMRSLTRDHIEKLIQRANYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISKGE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1960 TLEDTVQVLGSYG-DILVLRSNENGAADRAAR-VCDQPVINGGDGTGEHPTQALLDVYTIRQEMGTVNGLTIALVGDLKN 2037
Cdd:PRK13814   89 TLFDTIKTLEAMGvYFFIVRHSENETPEQIAKqLSSGVVINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDIRH 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2038 GRTVHSLAKLLCLYKDITLHYVAPSTELemPQEVldyvsskSNFVQKKFTSLAEGINHVDVVYVTRIQKERFSSPDEYNK 2117
Cdd:PRK13814  169 SRVANSLMDGLVTMGVPEIRLVGPSSLL--PDKV-------GNDSIKKFTELKPSLLNSDVIVTLRLQKERHDNSVDIDA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2118 VKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLP--RVDEIAVELDHDERAAYFRQAKNGVFVRMSILSLLLGR 2195
Cdd:PRK13814  240 FRGSFRLTPEKLYSAKPDA--------------IVMHPGPvnREVEINSDVADNQQSVILQQVRNGVAMRMAVLELFLLR 305
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 1476-1821 3.28e-37

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 147.92  E-value: 3.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREP---GATHKEDWATCSKAALAGGVTTIL--AMPNTSPVLVDTDSFYQteQLASAKSVVDYALY-IGA 1549
Cdd:PRK13404   53 LPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSLREAVEDYH--RRAAGKAVIDYAFHlIVA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1550 TPN----NSKFAAEFADKAAGLKMYLneTFSTLKMDN-------------------------ISDW--AKHLSA------ 1592
Cdd:PRK13404  131 DPTeevlTEELPALIAQGYTSFKVFM--TYDDLKLDDrqildvlavarrhgamvmvhaenhdMIAWltKRLLAAgltapk 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1593 -FPANRPIVCHAEKQTLAaiLCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLP-DGIREVR 1670
Cdd:PRK13404  209 yHAISRPMLAEREATHRA--IALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDrPGMEGAK 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1671 ----PRLVKPEDRQALWDNME--YIDCFATDHAPHTWAEKTGKDG--------KIPPGFPGVEYMLPLLLTA-VHDGKLT 1735
Cdd:PRK13404  287 yicsPPPRDKANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAaganpsfkAIANGIPGIETRLPLLFSEgVVKGRIS 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1736 MKELTDRMSTNPRRIFNLPPQD-------DTYIEV-DLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVID 1807
Cdd:PRK13404  367 LNRFVALTSTNPAKLYGLYPRKgaiaigaDADIAIwDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVED 446

                         410
                  ....*....|....
gi 193204318 1808 GRIVAIPGFGKNVR 1821
Cdd:PRK13404  447 GELVAERGSGQFLA 460
PLN02795 PLN02795
allantoinase
 1476-1814 7.48e-36

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 144.53  E-value: 7.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMP-NTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNS 1554
Cdd:PLN02795   98 MPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPENA 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1555 KFAAEFAD----KAAGLKMYL-NETFSTLKMDNISDWAKHLSAFPA-NRPIVCHAEKQTLAAI---------LCMAQMAN 1619
Cdd:PLN02795  178 HNASVLEElldaGALGLKSFMcPSGINDFPMTTATHIKAALPVLAKyGRPLLVHAEVVSPVESdsrldadprSYSTYLKS 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1620 R----------------------------AVHIAHVATADE-INLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVR 1670
Cdd:PLN02795  258 RppsweqeairqllevakdtrpggvaegaHVHIVHLSDAESsLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYK 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1671 --PRLVKPEDRQALWDNME--YIDCFATDHAPHTWAEKTGKDG---KIPPGFPGVEYMLPLLLTAVHDGKLTMKELTDRM 1743
Cdd:PLN02795  338 caPPIRDAANRELLWKALLdgDIDMLSSDHSPSPPDLKLLEEGnflRAWGGISSLQFVLPATWTAGRAYGLTLEQLARWW 417

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1744 STNPRRIFNLP------PQDDTYI-------EVDLNEEWTIpengGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRI 1810
Cdd:PLN02795  418 SERPAKLAGLDskgaiaPGKDADIvvwdpeaEFVLDESYPI----YHKHKSLSPYLGTKLSGKVIATFVRGNLVFLEGKH 493


                  ....
gi 193204318 1811 VAIP 1814
Cdd:PLN02795  494 AKQA 497
PRK07369 PRK07369
dihydroorotase; Provisional
 1477-1794 2.27e-35

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 141.28  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1477 PGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVdYALYIGATPNNSKF 1556
Cdd:PRK07369   57 PGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPV-QLHFWGALTLGGQG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1557 AA--EFADKAAG-------------------LKMYLN---------ETFSTLKMDNI---SDWAKHLsAFPANRPIvchA 1603
Cdd:PRK07369  136 KQltELAELAAAgvvgftdgqplenlallrrLLEYLKplgkpvalwPCDRSLAGNGVmreGLLALRL-GLPGDPAS---A 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1604 EKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVR--PRLVKPEDRQA 1681
Cdd:PRK07369  212 ETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRldPPLGNPSDRQA 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1682 LWDNME--YIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLL-TAVHDGKLTMKELTDRMSTNPRRIFNLPP--- 1755
Cdd:PRK07369  292 LIEGVRtgVIDAIAIDHAPYTYEEKTVAFAEAPPGAIGLELALPLLWqNLVETGELSALQLWQALSTNPARCLGQEPpsl 371

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 193204318 1756 ---QDDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKV 1794
Cdd:PRK07369  372 apgQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
PRK09059 PRK09059
dihydroorotase; Validated
 1464-1802 2.68e-35

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 141.33  E-value: 2.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1464 LVDCvtsKSLKRLPGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVVDY 1543
Cdd:PRK09059   50 IVDC---AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTARDTAIVNI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1544 ----ALYIGAtpnNSKFAAEFAD-KAAGLKMYLNETFS---TLKMDNISDWAKHLSAfpanrPIVCHAEKQTLAAILCM- 1614
Cdd:PRK09059  127 hpaaAITKGL---AGEEMTEFGLlRAAGAVAFTDGRRSvanTQVMRRALTYARDFDA-----VIVHETRDPDLGGNGVMn 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1615 ----------------------------AQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDlpdgI 1666
Cdd:PRK09059  199 eglfaswlglsgipreaeviplerdlrlAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNEND----I 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1667 REVR------PRLVKPEDRQALWDNME--YIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTAVHDGKLTMKE 1738
Cdd:PRK09059  275 GEYRtffklsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTKRLPFSEAAAGAIGLETLLAAALRLYHNGEVPLLR 354

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318 1739 LTDRMSTNPRRIFNLP--------PQDdtYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGE 1802
Cdd:PRK09059  355 LIEALSTRPAEIFGLPagtlkpgaPAD--IIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGK 424
PRK08044 PRK08044
allantoinase AllB;
1477-1803 2.87e-32

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 132.67  E-value: 2.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1477 PGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMP-NTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNNSK 1555
Cdd:PRK08044   53 PGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLD 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1556 ---------------FAAEFADKA--------------AGLKMyLNETFSTLKM--------DNISDWAKH-----LSAF 1593
Cdd:PRK08044  133 rlheldevgvvgfkcFVATCGDRGidndfrdvndwqfyKGAQK-LGELGQPVLVhcenalicDELGEEAKRegrvtAHDY 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1594 PANRPIVchAEKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLpDGIREV---R 1670
Cdd:PRK08044  212 VASRPVF--TEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF-EEIGTLakcS 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1671 PRLVKPEDRQALWDNMEY--IDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLL-TAVHDGKLTMKELTDRMSTNP 1747
Cdd:PRK08044  289 PPIRDLENQKGMWEKLFNgeIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFdEAVQKRGMSLPMFGKLMATNA 368

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193204318 1748 RRIFNL-------PPQDDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEE 1803
Cdd:PRK08044  369 ADIFGLqqkgriaPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDV 431
PRK00779 PRK00779
ornithine carbamoyltransferase; Provisional
 1880-2193 2.39e-31

ornithine carbamoyltransferase; Provisional


Pssm-ID: 234835 [Multi-domain]  Cd Length: 304  Bit Score: 126.36  E-value: 2.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1880 ISVKHLDKGQINRIFELADRYKHDVEKGHPlTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQKGE 1959
Cdd:PRK00779    8 LSLDDLSPEELEELLDLAAELKKKRKAGEP-HPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFLSPRDTQLGRGE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1960 TLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVING-GDgtGEHPTQALLDVYTIRQEMGTVNGLTIALVGDlknG 2038
Cdd:PRK00779   87 PIEDTARVLSRYVDAIMIRTFEHETLEELAEYSTVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGLKVAWVGD---G 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2039 RTV-HSLAkLLCLYKDITLHYVAPStELEMPQEVLDYVSSKSNFVQKKFTSLAEGINHVDVVYvT-----------RIQK 2106
Cdd:PRK00779  162 NNVaNSLL-LAAALLGFDLRVATPK-GYEPDPEIVEKIAKETGASIEVTHDPKEAVKGADVVY-TdvwvsmgqeaeAEER 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2107 ERFSSPdeynkvkgsYVINAKLLNEAARDVeepssllvparslpIVMHPLP--RVDEIAVELDHDERAAYFRQAKNGVFV 2184
Cdd:PRK00779  239 LKAFAP---------YQVNEELMALAKPDA--------------IFMHCLPahRGEEVTDEVIDGPQSVVWDEAENRLHA 295


                  ....*....
gi 193204318 2185 RMSILSLLL 2193
Cdd:PRK00779  296 QKALLAWLL 304
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 800-879 4.94e-29

Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 460695  Cd Length: 79  Bit Score: 111.70  E-value: 4.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   800 DDLSKPTDKRMFALARGMYYGdFDVEKAHELTRIDRWFLFRMQNIVDIYHRLEKTDVnTVSAELLLEAKQAGFSDRQIAK 879
Cdd:pfam02787    1 EELRTPTDERLFAIAEALRRG-YSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGL-DLDAELLREAKRLGFSDRQIAK 78
pyrB PRK13376
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ...
 1922-2194 1.79e-27

bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional


Pssm-ID: 237369 [Multi-domain]  Cd Length: 525  Bit Score: 119.48  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1922 LFYEVSTRTSCSF-SAAMQRLGGSVISVDSQSSSVQKGETLEDTVQVLGSYGD--ILVLRSNENGAAdraaRVCDQPV-- 1996
Cdd:PRK13376   56 VFVEPSTRTKESFiNAAKFHKNVKVNIFDSEHSSFNKQESYTDTFNMLTGYSDysIFIVRTRLEGVC----RLLEEKVse 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1997 ------------INGGDGTGEHPTQALLDVYTIRQEMGTVNG-LTIALVGDLKNGRTVHSLAKLLCLYKDITLHYVAPSt 2063
Cdd:PRK13376  132 fasrngievpafINAGDGKHEHPTQELLDEFTFLEQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFKNVKVDLIAPE- 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2064 ELEMPQEvldYVS--SKSNFVQKKFTSLAEGINHVDVV---YVTRIQKERFSSP--DEYNKVKGSYVINAKLLNEAARDV 2136
Cdd:PRK13376  211 ELAMPEH---YVEkmKKNGFEVRIFSSIEEYLSQKDVAkiwYFTRLQLERMGEDilEKEHILRKAVTFRKEFLDKLPEGV 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193204318 2137 EepssllvparslpiVMHPLPR---VDEIAVELDHDERAAYFRQAKNGVFVRMSILSLLLG 2194
Cdd:PRK13376  288 K--------------FYHPLPRhkvYPTIPTFLDTLPLNGWETQAINGYWVRIVLLSMLGG 334
OTCace pfam00185
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
2028-2192 1.48e-25

Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;


Pssm-ID: 425511 [Multi-domain]  Cd Length: 154  Bit Score: 104.61  E-value: 1.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  2028 TIALVGDlKNGRTVHSLAKLLCLYKdITLHYVAPsTELEMPQEVLDYVSSKSNFVQKKFT---SLAEGINHVDVVYVTRI 2104
Cdd:pfam00185    1 KIAYVGD-GHNNVAHSLIIAAAKLG-MDVRLATP-KGYPPDPEVLDKAKKIAEKSGGSIEitdDPAEAVKGADVVYTDVW 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  2105 Q-----KERFsspDEYNKVKGsYVINAKLLNEAARDVeepssllvparslpIVMHPLP--RVDEIAVELDHDERAAYFRQ 2177
Cdd:pfam00185   78 QsmgqeKERE---ERLKAFKP-YQVNEELMKLAKKDA--------------IFMHCLPahRGEEVTDDVFDGPRSVVFDQ 139

                          170
                   ....*....|....*
gi 193204318  2178 AKNGVFVRMSILSLL 2192
Cdd:pfam00185  140 AENRLHAQKALLALL 154
PRK07627 PRK07627
dihydroorotase; Provisional
 1477-1801 5.09e-25

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 110.54  E-value: 5.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1477 PGMVDIHVHVREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVL-----VDTDSFYQ--------------------- 1530
Cdd:PRK07627   55 PGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPVLdepglVEMLKFRArnlnqahvyplgaltvglkge 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1531 --TE--QLASA---------KSVVDYALYIGATpnnsKFAAEFadkaaGLKMYLNETFSTLKMDNISdwakHLSAFpANR 1597
Cdd:PRK07627  135 vlTEmvELTEAgcvgfsqanVPVVDTQVLLRAL----QYASTF-----GFTVWLRPLDAFLGRGGVA----ASGAV-ASR 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1598 ----PIVCHAEKQTLAAILCMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLpdGIREVRPRL 1673
Cdd:PRK07627  201 lglsGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDI--GYFDSQFRL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1674 VKP----EDRQALWDNME--YIDCFATDHAPhtwaekTGKDGK-IP-----PGFPGVEYMLPLLLTAVHDGKLTMKELTD 1741
Cdd:PRK07627  279 DPPlrsqRDREAIRAALAdgTIDAICSDHTP------VDDDEKlLPfaeatPGATGLELLLPLTLKWADEAKVPLARALA 352

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193204318 1742 RMSTNPRRIFNLPPQD-------DTYIeVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRG 1801
Cdd:PRK07627  353 RITSAPARVLGLPAGRlaegapaDLCV-FDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAG 418
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 196-341 1.36e-23

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 99.92  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  196 LAKRGFRVKVVPWNHPIDTE---SDYDGLFLSNGPGDPE---ICAPLVDRLAkviarGDKPIFGICLGHQILSRAIGAKT 269
Cdd:cd01743    18 LRELGAEVVVVRNDEITLEElelLNPDAIVISPGPGHPEdagISLEIIRALA-----GKVPILGVCLGHQAIAEAFGGKV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  270 YKLKYGNRGHNQPCTHYATGRCYITSQN------HGYAVDPDSLPADWKALftnenDKTNEGIV----HSSKPFFSVQFH 339
Cdd:cd01743    93 VRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLEVT-----ASTEDGVImalrHRDLPIYGVQFH 167


                  ..
gi 193204318  340 PE 341
Cdd:cd01743   168 PE 169
PRK08417 PRK08417
metal-dependent hydrolase;
1464-1802 2.54e-22

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 101.70  E-value: 2.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1464 LVDCvTSKSLkrLPGMVDIHVHVREPGATHKeDWATCSKAALAGGVTTILAMPNTSPVLVDTDS--FYQTEQLASAKSVV 1541
Cdd:PRK08417   20 ILDA-KGKTL--LPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNEIAleLINSAQRELPMQIF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1542 DYALYIGATPNNSKFAAEFADKAAGLkmylnETFSTLKMDN---ISDWAKHLSAfpanrPIVCHAEKQTLAAILCM---- 1614
Cdd:PRK08417   96 PSIRALDEDGKLSNIATLLKKGAKAL-----ELSSDLDANLlkvIAQYAKMLDV-----PIFCRCEDSSFDDSGVMndge 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1615 -------------------AQMANRAVH------IAHVATADEINLVKEAKQRGWNVTCEVCPHHLfLIEEDLPDGIR-- 1667
Cdd:PRK08417  166 lsfelglpgipsiaetkevAKMKELAKFyknkvlFDTLALPRSLELLDKFKSEGEKLLKEVSIHHL-ILDDSACENFNta 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1668 -EVRPRLVKPEDRQALWDNME--YIDCFATDHAPHTWAEKTGKDGKIPPGFPGVEYMLPLLLTAVH-DGKLTMKELTDRM 1743
Cdd:PRK08417  245 aKLNPPLRSKEDRLALLEALKegKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTYLVkEGIITWSELSRFT 324

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318 1744 STNPRRIFNLPpqdDTYIEV---------DLNEEWTIPENGGqskagwtPFAGRKVFGKVHNVIIRGE 1802
Cdd:PRK08417  325 SYNPAQFLGLN---SGEIEVgkeadlvlfDPNESTIIDDNFS-------LYSGDELYGKIEAVIIKGK 382
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1337-1440 8.87e-22

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 460462 [Multi-domain]  Cd Length: 93  Bit Score: 91.40  E-value: 8.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1337 EMLKSVEALLKLGYELYGSKGTADYFQSNKINVKPVDWPFEEGSSDektasGTRSVVEFLENKEFHLVINLPirgsgaYR 1416
Cdd:pfam02142    1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGRPG-----GRVQIGDLIKNGEIDLVINTL------YP 69

                           90       100
                   ....*....|....*....|....
gi 193204318  1417 VSAFRTHGYKTRRMAIDNGIPLIT 1440
Cdd:pfam02142   70 FKATVHDGYAIRRAAENIDIPGPT 93
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 1038-1222 8.87e-20

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 91.47  E-value: 8.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1038 GTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAHNAEDLEVFLKQAA 1117
Cdd:COG0439    43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1118 VVAK----EHPVVVSKFInEAKELDVDAVALDGKLVVMAVSEHIeNAGVHSGDATLVTPAqDMNKLTLDRIKDITFRIAE 1193
Cdd:COG0439   123 AEAKagspNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRKH-QKPPYFVELGHEAPS-PLPEELRAEIGELVARALR 199

                         170       180       190
                  ....*....|....*....|....*....|.
gi 193204318 1194 AFNV-NGPFNMQ-LIAKNNELKVIECNLRVS 1222
Cdd:COG0439   200 ALGYrRGAFHTEfLLTPDGEPYLIEINARLG 230
PLN02342 PLN02342
ornithine carbamoyltransferase
 1877-2194 1.02e-19

ornithine carbamoyltransferase


Pssm-ID: 177976 [Multi-domain]  Cd Length: 348  Bit Score: 92.93  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKHDVEKGHPLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQ 1956
Cdd:PLN02342   46 KHFLHIDDFDKEEILGLLDRAKEVKALLKSGDRSFQPFKGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQLG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1957 KGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVING-GDgtGEHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:PLN02342  126 KREETRDIARVLSRYNDIIMARVFAHQDVLDLAEYSSVPVINGlTD--YNHPCQIMADALTIIEHIGRLEGTKVVYVGDG 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2036 KNgrTVHSLAKLLCLYkdiTLHYV-APSTELEMPQEVLDyvSSKSNFVQKKFTS--LAEGINHVDVVY----VTRIQKER 2108
Cdd:PLN02342  204 NN--IVHSWLLLAAVL---PFHFVcACPKGYEPDAKTVE--KARAAGISKIEITndPAEAVKGADVVYtdvwASMGQKEE 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2109 FsspDEYNKVKGSYVINAKLLNEAARDVeepssllvparslpIVMHPLPRVDEIAV--ELDHDERAAYFRQAKNGVFVRM 2186
Cdd:PLN02342  277 A---EKRKKAFQGFQVNEALMKLAGPQA--------------YFMHCLPAERGVEVtdGVMEAPNSIVFPQAENRMHAQN 339


                  ....*...
gi 193204318 2187 SILSLLLG 2194
Cdd:PLN02342  340 AIMLHQLG 347
PRK02102 PRK02102
ornithine carbamoyltransferase; Validated
 1877-2157 3.87e-19

ornithine carbamoyltransferase; Validated


Pssm-ID: 179366 [Multi-domain]  Cd Length: 331  Bit Score: 91.10  E-value: 3.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKHDVEKGHPlTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQ 1956
Cdd:PRK02102    8 RSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIE-HQYLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1957 KGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGGDGTgEHPTQALLDVYTIRQEMGTVNGLTIALVGDLK 2036
Cdd:PRK02102   87 KKESIEDTARVLGRMYDGIEYRGFKQEIVEELAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKLAYVGDGR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2037 NgRTVHSL----AKLlclykDITLHYVAPStELEMPQEVLDYVS--SKSNFVQKKFTS-LAEGINHVDVVY----VTRIQ 2105
Cdd:PRK02102  166 N-NMANSLmvggAKL-----GMDVRICAPK-ELWPEEELVALAReiAKETGAKITITEdPEEAVKGADVIYtdvwVSMGE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 193204318 2106 KERFsspDEYNKVKGSYVINAKLLNEAA-RDVeepssllvparslpIVMHPLP 2157
Cdd:PRK02102  239 EDEW---EERIKLLKPYQVNMDLMKATGnPDV--------------IFMHCLP 274
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1071-1242 1.90e-18

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 85.82  E-value: 1.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1071 ENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAHNAEDLEVFLKQA---AVVAKEHP-VVVSKFINEAKELDVDAVAlDG 1146
Cdd:pfam02786   25 ETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALAlaeAPAAFGNPqVLVEKSLKGPKHIEYQVLR-DA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1147 KLVVMAVSEhIENA-GVHSGDATLVTPAQDMNKLTLDRIKDITFRIAEAFNVNGPFNMQLI--AKNNELKVIECNLRVSR 1223
Cdd:pfam02786  104 HGNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQV 182

                          170
                   ....*....|....*....
gi 193204318  1224 SFPFVSKTLDYDFVALATR 1242
Cdd:pfam02786  183 EHALAEKATGYDLAKEAAK 201
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 200-341 2.09e-18

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 85.09  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  200 GFRVKVVPwNHPIDTE----SDYDGLFLSNGPGDPE---ICAPLVDRLAkviarGDKPIFGICLGHQILSRAIGAKTYKL 272
Cdd:COG0512    22 GAEVVVVR-NDEITLEeieaLAPDGIVLSPGPGTPEeagISLEVIRAFA-----GKIPILGVCLGHQAIGEAFGGKVVRA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  273 KY------------GN---RGHNQPCThyaTGRcYitsqnHGYAVDPDSLPADWKALFTNEnDKTNEGIVHSSKPFFSVQ 337
Cdd:COG0512    96 PEpmhgktspithdGSglfAGLPNPFT---ATR-Y-----HSLVVDRETLPDELEVTAWTE-DGEIMGIRHRELPIEGVQ 165


                  ....
gi 193204318  338 FHPE 341
Cdd:COG0512   166 FHPE 169
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 194-363 3.03e-18

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 85.77  E-value: 3.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  194 RCLAKRGFRVKVV--------PWNHPIDtesDYDGLFLSNGPGDP-EICAPLVD--RLAKVIARGDKPIFGICLGHQILS 262
Cdd:COG0518    20 RRLREAGIELDVLrvyageilPYDPDLE---DPDGLILSGGPMSVyDEDPWLEDepALIREAFELGKPVLGICYGAQLLA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  263 RAIGAKTYKlkygNRGHNqpcthYATGRCYITSQN---------------HGYAVdpDSLPADWKALFTNENDKtNEGIV 327
Cdd:COG0518    97 HALGGKVEP----GPGRE-----IGWAPVELTEADplfaglpdeftvwmsHGDTV--TELPEGAEVLASSDNCP-NQAFR 164

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 193204318  328 HsSKPFFSVQFHPEHTagPTDCEFLFDVFADSVRQA 363
Cdd:COG0518   165 Y-GRRVYGVQFHPEVT--HTMMEAWLEERADELAAE 197
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 505-710 9.16e-18

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 85.31  E-value: 9.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  505 TIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELIAIAQQALAHSN- 583
Cdd:COG0439    48 AIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKa 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  584 -----QVLVDKSLKGwKEVEYEVVrdAYDNCITVCNM---ENVDPLGIHTGEsvvVAPSQtLSDREYNALRTCAIKVIRH 655
Cdd:COG0439   128 gspngEVLVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRA 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318  656 LGII-GECNIQYALDPYSlTYYIIEVNARLS--RSSALASKATGYPLAYVAAKLALGQ 710
Cdd:COG0439   201 LGYRrGAFHTEFLLTPDG-EPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGE 257
MGS_CPS_II cd01424
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ...
 1324-1450 6.68e-17

Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.


Pssm-ID: 238712 [Multi-domain]  Cd Length: 110  Bit Score: 78.29  E-value: 6.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1324 NIFISIggyhA---KAEMLKSVEALLKLGYELYGSKGTADYFQSNKINVKPVDwpfeegssdeKTASGTRSVVEFLENKE 1400
Cdd:cd01424     2 TVFISV----AdrdKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVN----------KVSEGRPNIVDLIKNGE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 193204318 1401 FHLVINLPirgSGayrvSAFRTHGYKTRRMAIDNGIPLITDIKCAKTFIQ 1450
Cdd:cd01424    68 IQLVINTP---SG----KRAIRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 192-341 3.19e-16

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 79.02  E-value: 3.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  192 QIRCLakrGFRVKVVPwNHPIDTE----SDYDGLFLSNGPGDPE---ICAPLVDRLAkviarGDKPIFGICLGHQILSRA 264
Cdd:PRK05670   18 YLGEL---GAEVVVYR-NDEITLEeieaLNPDAIVLSPGPGTPAeagISLELIREFA-----GKVPILGVCLGHQAIGEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  265 IGA-----------KTYKLKYGNRG------HNQPCTHYatgrcyitsqnHGYAVDPDSLPADWKALFTNEnDKTNEGIV 327
Cdd:PRK05670   89 FGGkvvrakeimhgKTSPIEHDGSGifaglpNPFTVTRY-----------HSLVVDRESLPDCLEVTAWTD-DGEIMGVR 156

                         170
                  ....*....|....
gi 193204318  328 HSSKPFFSVQFHPE 341
Cdd:PRK05670  157 HKELPIYGVQFHPE 170
PLN02942 PLN02942
dihydropyrimidinase
 1476-1826 2.36e-15

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 81.43  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREP--GATHKEDWATCSKAALAGGVTTILAMpnTSPVLVDTDSFYQTEQLASAKSVVDYALYIGATPNN 1553
Cdd:PLN02942   56 MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTMHIDF--VIPVNGNLLAGYEAYEKKAEKSCMDYGFHMAITKWD 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1554 SKFAA--EFADKAAGLKMY----------------LNETFSTLKM------------DNISDWAKHL--------SAFPA 1595
Cdd:PLN02942  134 DTVSRdmETLVKEKGINSFkffmaykgslmvtdelLLEGFKRCKSlgalamvhaengDAVFEGQKRMielgitgpEGHAL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1596 NRPIVCHAEKqTLAAILcMAQMANRAVHIAHVATADEINLVKEAKQRGWNVTCEVCPHHLFLIEEDLPDGIREVRPRLV- 1674
Cdd:PLN02942  214 SRPPLLEGEA-TARAIR-LAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVm 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1675 KPEDR-----QALWDNME--YIDCFATDHAPHTWAEKT-GKDG--KIPPGFPGVEYMLPLLL-TAVHDGKLTMKELTDRM 1743
Cdd:PLN02942  292 SPPIRpaghgKALQAALSsgILQLVGTDHCPFNSTQKAfGKDDfrKIPNGVNGIEERMHLVWdTMVESGQISPTDYVRVT 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1744 STNPRRIFNLPPQ--------DDTYIEVDLNEEWTIPENGGQSKAGWTPFAGRKVFGKVHNVIIRGEEAVIDGRIVAIPG 1815
Cdd:PLN02942  372 STECAKIFNIYPRkgailagsDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRG 451

                         410
                  ....*....|.
gi 193204318 1816 FGKNVRLYPHS 1826
Cdd:PLN02942  452 SGRYIEMPPFS 462
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 193-342 2.91e-15

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 76.13  E-value: 2.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  193 IRCLAKRGFRVKVVPWNHPIDTES--DYDGLFLSNGPGDPEIC-----APLVDRLAKVIARGdKPIFGICLGHQILSRAI 265
Cdd:cd01741    20 LREAGAETIEIDVVDVYAGELLPDldDYDGLVILGGPMSVDEDdypwlKKLKELIRQALAAG-KPVLGICLGHQLLARAL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  266 GAKTYKLKYGNRGHNQPCTHYATGRCYITSQN----------HGYAVdpDSLPADWKALFTNENDKtNEGIVhSSKPFFS 335
Cdd:cd01741    99 GGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGlpdefpvfhwHGDTV--VELPPGAVLLASSEACP-NQAFR-YGDRALG 174


                  ....*..
gi 193204318  336 VQFHPEH 342
Cdd:cd01741   175 LQFHPEE 181
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 181-343 4.55e-15

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 75.26  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  181 ILAVDCGLKNNQIrcLAKR----GFRVKVVPWNHPIDTESDY--DGLFLSNGPG-DPEICAPLVDRLakvIARGDKPIFG 253
Cdd:cd01742     1 ILILDFGSQYTHL--IARRvrelGVYSEILPNTTPLEEIKLKnpKGIILSGGPSsVYEEDAPRVDPE---IFELGVPVLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  254 ICLGHQILSRAIGAKTyklkygNRGHNQpctHYATGRCYITSQ---------------NHGYAVdpDSLPADWKALFTNE 318
Cdd:cd01742    76 ICYGMQLIAKALGGKV------ERGDKR---EYGKAEIEIDDSsplfeglpdeqtvwmSHGDEV--VKLPEGFKVIASSD 144

                         170       180
                  ....*....|....*....|....*..
gi 193204318  319 NDKtNEGIVHSSKPFFSVQFHPE--HT 343
Cdd:cd01742   145 NCP-VAAIANEEKKIYGVQFHPEvtHT 170
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
210-341 1.36e-14

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 75.09  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  210 HPIDTESDYDGLFLSNGPGDPE---ICAPLVdrlaKVIARGDKPIFGICLGHQILSRAIGA-----------KTYKLKYG 275
Cdd:PRK07765   39 DEAAVAAQFDGVLLSPGPGTPEragASIDMV----RACAAAGTPLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHT 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318  276 NRGHNQ--PCTHYATgrcyitsQNHGYAVDPDSLPADWKALftnenDKTNEGIV----HSSKPFFSVQFHPE 341
Cdd:PRK07765  115 GVGVLAglPDPFTAT-------RYHSLTILPETLPAELEVT-----ARTDSGVImavrHRELPIHGVQFHPE 174
PRK14805 PRK14805
ornithine carbamoyltransferase; Provisional
 1877-2194 1.38e-14

ornithine carbamoyltransferase; Provisional


Pssm-ID: 237819 [Multi-domain]  Cd Length: 302  Bit Score: 77.04  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKHDVEKghpLTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQ 1956
Cdd:PRK14805    2 KHLLSIKELTQQQLLDLLALAKTIKANPAE---YRQALAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGALG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1957 KGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVING-GDGTgeHPTQALLDVYTIRQEMGTVNGLTIALVGDL 2035
Cdd:PRK14805   79 KRESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINAlCDLY--HPCQALADFLTLAEQFGDVSKVKLAYVGDG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2036 KNgrTVHSLakLLC---LYKDITLhyVAPSTELEMPQEVLDYVS-SKSNFVQKKFTSLAEGINHVDVVYV-TRIQKERFS 2110
Cdd:PRK14805  157 NN--VTHSL--MYGaaiLGATMTV--ICPPGHFPDGQIVAEAQElAAKSGGKLVLTSDIEAIEGHDAIYTdTWISMGDDT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2111 SPDEYNKVKGSYVINAKLLNEAArdveepssllvpARSlpiVMHPLP--RVDEIAVELDHDERAAYFRQAKNGVFVRMSI 2188
Cdd:PRK14805  231 PLAEIKAKFAPYQVNKALMEKAG------------ATF---VMHCQPahRGVEITSEVMDGEGSLILQQAENRMHAQNAV 295


                  ....*.
gi 193204318 2189 LSLLLG 2194
Cdd:PRK14805  296 LVTLLS 301
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 181-343 9.56e-14

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 71.96  E-value: 9.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   181 ILAVDCGLKNNQI--RCLAKRGFRVKVVPWNHPIDT--ESDYDGLFLSNGP-----GDPEICAPLVDRLakviargDKPI 251
Cdd:TIGR00888    1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTTPLEEirEKNPKGIILSGGPssvyaENAPRADEKIFEL-------GVPV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   252 FGICLGHQILSRAIGAKTYKlkyGNRGhnqpctHYATGRCYITSQN---------------HGYAVdpDSLPADWKALFT 316
Cdd:TIGR00888   74 LGICYGMQLMAKQLGGEVGR---AEKR------EYGKAELEILDEDdlfrglpdestvwmsHGDKV--KELPEGFKVLAT 142

                          170       180
                   ....*....|....*....|....*....
gi 193204318   317 NENDKtNEGIVHSSKPFFSVQFHPE--HT 343
Cdd:TIGR00888  143 SDNCP-VAAMAHEEKPIYGVQFHPEvtHT 170
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 1034-1227 1.04e-13

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 74.54  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1034 VKIFGTSPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCA--QVGYPCLIRPSYVLSGAAMNVAHNAEDLEV 1111
Cdd:PRK12767   96 VKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAkgELQFPLFVKPRDGSASIGVFKVNDKEELEF 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1112 FLKQAAvvakehPVVVSKFINEaKELDVDA-VALDGKLVVMAVSEHIEnagVHSG--DATLVTPAQDMNKLTLdrikdit 1188
Cdd:PRK12767  176 LLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGetSKGVTVKDPELFKLAE------- 238

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 193204318 1189 fRIAEAFNVNGPFNMQLIAKNNELKVIECNLRVSRSFPF 1227
Cdd:PRK12767  239 -RLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 1480-1750 2.72e-13

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 72.37  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1480 VDIHVHVREPGATHKEDWATC------------------SKAALAGGVTTILAMPNTSPVLVDTDSFYQTEQLASAKSVV 1541
Cdd:cd01292     2 IDTHVHLDGSALRGTRLNLELkeaeelspedlyedtlraLEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1542 DYALYIGATPNNSK------------FAAEFADKAAGLKMYLNETFSTLKMDNISDWAKHLSAfpANRPIVCHAEKQTLA 1609
Cdd:cd01292    82 RVVLGLGIPGVPAAvdedaealllelLRRGLELGAVGLKLAGPYTATGLSDESLRRVLEEARK--LGLPVVIHAGELPDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1610 AI----LCMAQMANRAVHIAHVA--TADEINLVKEAkqrgwNVTCEVCPHHLFLIEEDlPDGIREVRpRLVKPEDRqalw 1683
Cdd:cd01292   160 TRaledLVALLRLGGRVVIGHVShlDPELLELLKEA-----GVSLEVCPLSNYLLGRD-GEGAEALR-RLLELGIR---- 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193204318 1684 dnmeyiDCFATDHAPHtwaektgkdgkippgfPGVEYMLPLLLTAVHDGKL--TMKELTDRMSTNPRRI 1750
Cdd:cd01292   229 ------VTLGTDGPPH----------------PLGTDLLALLRLLLKVLRLglSLEEALRLATINPARA 275
DHOase cd01294
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ...
 1476-1790 3.75e-13

Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.


Pssm-ID: 238619  Cd Length: 335  Bit Score: 73.09  E-value: 3.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1476 LPGMVDIHVHVREpGATHKedwATCSKAALAGGVTTIlaMPNTSPVLVDTD--SFYQTEQLASAK-SVVDY--ALYIgaT 1550
Cdd:cd01294     3 IPRPDDMHLHLRD-GAMLK---LVLPYTARGFSRAIV--MPNLKPPVTTTAdaLAYRERILAADPgPNFTPlmTLYL--T 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1551 PNNSK---FAAEFADKAAGLKMY-LNETfsTLKMDNISDWAKHLSAFPA----NRPIVCHAEKQTLAA---------ILC 1613
Cdd:cd01294    75 ENTTPeelREAKKKGGIRGVKLYpAGAT--TNSQGGVTDLEKIYPVLEAmqklGMPLLVHGEVPDFKIdvldreakfIPV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1614 MAQMANR----AVHIAHVATADEINLVKEAKQrgwNVTCEVCPHHLFLIEEDLPDGIREV----RPRLVKPEDRQAL--- 1682
Cdd:cd01294   153 LEPLAQRfpklKIVLEHITTADAVEYVKSCNE---NVAATITPHHLLLTRDDLLGGGLNPhlycKPVAKRPEDREALrka 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1683 -WDNMEYIdCFATDHAPHTWAEKtgkdgKIPPGFPGV---EYMLPLLLTAVHD-GKLtmKELTDRMSTNPRRIFNLPPQD 1757
Cdd:cd01294   230 aTSGHPKF-FLGSDSAPHPKSNK-----ESSCGCAGIfsaPIALPYLAEVFEEhNAL--DKLEAFASDNGPNFYGLPPNK 301

                         330       340       350
                  ....*....|....*....|....*....|....
gi 193204318 1758 DTyIEVdLNEEWTIPENGGQSKAGWTPF-AGRKV 1790
Cdd:cd01294   302 KT-ITL-VKEPWKVPEKIPFGNNGVVPFrAGETL 333
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1337-1440 9.80e-13

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 214855 [Multi-domain]  Cd Length: 91  Bit Score: 65.57  E-value: 9.80e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   1337 EMLKSVEALLKLGYELYGSKGTADYFQSNKINV--KPVDWPFEegssdektasGTRSVVEFLENKEFHLVINLPirgSGA 1414
Cdd:smart00851    1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHG----------GIPQILDLIKNGEIDLVINTL---YPF 67

                            90       100
                    ....*....|....*....|....*.
gi 193204318   1415 YRVSafRTHGYKTRRMAIDNGIPLIT 1440
Cdd:smart00851   68 EAQA--HEDGYSIRRAAENIDIPGPT 91
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 205-341 1.39e-12

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 68.28  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   205 VVPWNHPiDTESDYDGLF-----LSNGPGDPE---ICAPLVDRLAkviarGDKPIFGICLGHQILSRAIGAKTYKLKYGN 276
Cdd:TIGR00566   27 VVKRNDS-LTLQEIEALLpllivISPGPCTPNeagISLEAIRHFA-----GKLPILGVCLGHQAMGQAFGGDVVRANTVM 100

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193204318   277 RGHNQPCTHYATGRC------YITSQNHGYAVDPDSLPADWKALFTNENDKTNEGIVHSSKPFFSVQFHPE 341
Cdd:TIGR00566  101 HGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPE 171
PRK00758 PRK00758
GMP synthase subunit A; Validated
 203-343 4.34e-12

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 66.80  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  203 VKVVPWNHPI-DTESDYDGLFLSNGPgdpEIcaplvDRL---AKVIARGDKPIFGICLGHQILSRAIGAKTYKLKYGNrg 278
Cdd:PRK00758   26 AKIIPNTTPVeEIKAFEDGLILSGGP---DI-----ERAgncPEYLKELDVPILGICLGHQLIAKAFGGEVGRGEYGE-- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  279 hnqpcthYATGRCYITSQN---------------HGYAVdpDSLPADWKALFTNENDKTnEGIVHSSKPFFSVQFHPE-- 341
Cdd:PRK00758   96 -------YALVEVEILDEDdilkglppeirvwasHADEV--KELPDGFEILARSDICEV-EAMKHKEKPIYGVQFHPEva 165


                  ..
gi 193204318  342 HT 343
Cdd:PRK00758  166 HT 167
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
387-721 7.09e-12

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 69.57  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  387 AKEQRKVLVLGSggltigqagefDYSGAQALKALREEGIRTVLINPN-IATVQTSKgFADFTYFLPITK-------EYVT 458
Cdd:COG3919     2 MTMRFRVVVLGG-----------DINALAVARSLGEAGVRVIVVDRDpLGPAARSR-YVDEVVVVPDPGddpeafvDALL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  459 DVIKKERPTGILCTFGGQTALncaIDLYKDgIFEQYDVqVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGA 538
Cdd:COG3919    70 ELAERHGPDVLIPTGDEYVEL---LSRHRD-ELEEHYR-LPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  539 IEAAEELGYPVLVRAAYALGGLGSGF--------ADNREELIAIAQQALAHSNQVLVDkslkgwkevEYEVVRDAYDNCI 610
Cdd:COG3919   145 DALAEDLGFPVVVKPADSVGYDELSFpgkkkvfyVDDREELLALLRRIAAAGYELIVQ---------EYIPGDDGEMRGL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  611 TVCNMENVDPLGIHTGESVVVAPSQ----TLSDREYN-ALRTCAIKVIRHLGIIGECNIQYALDPYSLTYYIIEVNARLS 685
Cdd:COG3919   216 TAYVDRDGEVVATFTGRKLRHYPPAggnsAARESVDDpELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFW 295

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 193204318  686 RSSALASKAtGYPLAYVAAKLALGQHLPVIRNSVTG 721
Cdd:COG3919   296 RSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREG 330
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 181-261 1.36e-11

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 63.39  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  181 ILAVDCGLKNNQ-----IRCLAKRGFRVKVVPWNHPIDTE----SDYDGLFLSNGPGDP---EICAPLVDRLAKVIARGd 248
Cdd:cd01653     1 VAVLLFPGFEELelaspLDALREAGAEVDVVSPDGGPVESdvdlDDYDGLILPGGPGTPddlARDEALLALLREAAAAG- 79

                          90
                  ....*....|...
gi 193204318  249 KPIFGICLGHQIL 261
Cdd:cd01653    80 KPILGICLGAQLL 92
PRK03515 PRK03515
ornithine carbamoyltransferase subunit I; Provisional
 1889-2100 2.28e-11

ornithine carbamoyltransferase subunit I; Provisional


Pssm-ID: 179587 [Multi-domain]  Cd Length: 336  Bit Score: 67.43  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1889 QINRIFELADRYKHDVEKGHPLTHiLNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQKGETLEDTVQVL 1968
Cdd:PRK03515   19 ELNSLLQLAAKLKADKKNGKEEQK-LTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGHKESIKDTARVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1969 GSYGDILVLRSNENGAADRAARVCDQPVINGgdGTGE-HPTQALLDVYTIRQEM--GTVNGLTIALVGDLKN--GRTVHS 2043
Cdd:PRK03515   98 GRMYDGIQYRGYGQEIVETLAEYAGVPVWNG--LTNEfHPTQLLADLLTMQEHLpgKAFNEMTLAYAGDARNnmGNSLLE 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193204318 2044 LAKLLCLykDITLhyVAPstELEMPQEVLdyVSSKSNFVQK---KFT---SLAEGINHVDVVY 2100
Cdd:PRK03515  176 AAALTGL--DLRL--VAP--KACWPEAAL--VTECRALAQKnggNITlteDIAEGVKGADFIY 230
PRK12562 PRK12562
ornithine carbamoyltransferase subunit F; Provisional
 1873-2100 2.60e-11

ornithine carbamoyltransferase subunit F; Provisional


Pssm-ID: 105755  Cd Length: 334  Bit Score: 67.39  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1873 ELLAKNCISVKHLDKGQINRIFELADRYKHDVEKGHPLTHiLNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQS 1952
Cdd:PRK12562    3 GFYKKHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVAR-LTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1953 SSVQKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGgdGTGE-HPTQALLDVYTIRQEM--GTVNGLTI 2029
Cdd:PRK12562   82 SQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWNG--LTNEfHPTQLLADLLTMQEHLpgKAFNEMTL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193204318 2030 ALVGDLKN--GRTVHSLAKLLCLykdiTLHYVAPstELEMPQEVLdyVSSKSNFVQK---KFT---SLAEGINHVDVVY 2100
Cdd:PRK12562  160 VYAGDARNnmGNSMLEAAALTGL----DLRLVAP--QACWPEASL--VAECSALAQKhggKITlteDIAAGVKGADFIY 230
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 181-261 4.72e-11

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 61.06  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  181 ILAVDCGLKNNQ-----IRCLAKRGFRVKVVPWNHPIDTE----SDYDGLFLSNGPGDPE---ICAPLVDRLAKVIARGd 248
Cdd:cd03128     1 VAVLLFGGSEELelaspLDALREAGAEVDVVSPDGGPVESdvdlDDYDGLILPGGPGTPDdlaWDEALLALLREAAAAG- 79

                          90
                  ....*....|...
gi 193204318  249 KPIFGICLGHQIL 261
Cdd:cd03128    80 KPVLGICLGAQLL 92
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
221-341 7.09e-11

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 67.43  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  221 LFLSNGPGDPE---ICAPLVDRLAKVIargdkPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATG------RC 291
Cdd:PRK14607   48 IVISPGPGRPEeagISVEVIRHFSGKV-----PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGlfrgipNP 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 193204318  292 YITSQNHGYAVDPDSLPADWKALFTNEnDKTNEGIVHSSKPFFSVQFHPE 341
Cdd:PRK14607  123 TVATRYHSLVVEEASLPECLEVTAKSD-DGEIMGIRHKEHPIFGVQFHPE 171
PRK04284 PRK04284
ornithine carbamoyltransferase; Provisional
 1914-2100 2.91e-10

ornithine carbamoyltransferase; Provisional


Pssm-ID: 235269 [Multi-domain]  Cd Length: 332  Bit Score: 63.99  E-value: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1914 LNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDSQSSSVQKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCD 1993
Cdd:PRK04284   43 LKGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGSQMGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1994 QPVINGGDGTgEHPTQALLDVYTIRQEM-GTVNGLTIALVGDlknGRTVHSLAKLL-CLYKDITLHYVAPsTELEMPQEV 2071
Cdd:PRK04284  123 VPVWNGLTDE-DHPTQVLADFLTAKEHLkKPYKDIKFTYVGD---GRNNVANALMQgAAIMGMDFHLVCP-KELNPDDEL 197

                         170       180       190
                  ....*....|....*....|....*....|..
gi 193204318 2072 LDYVSSKSNFVQKKFT---SLAEGINHVDVVY 2100
Cdd:PRK04284  198 LNKCKEIAAETGGKITitdDIDEGVKGSDVIY 229
PRK13566 PRK13566
anthranilate synthase component I;
191-341 3.92e-10

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 65.32  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  191 NQIRCLakrGFRVKVVPWNHPID--TESDYDGLFLSNGPGDPE--ICAPLVDrlaKVIARGdKPIFGICLGHQILSRAIG 266
Cdd:PRK13566  544 NYFRQT---GAEVTTVRYGFAEEmlDRVNPDLVVLSPGPGRPSdfDCKATID---AALARN-LPIFGVCLGLQAIVEAFG 616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  267 AKTYKLKYgnRGHNQPCTHYATG---------RCYITSQNHGYAVDPDSLPADWKALFTNEnDKTNEGIVHSSKPFFSVQ 337
Cdd:PRK13566  617 GELGQLAY--PMHGKPSRIRVRGpgrlfsglpEEFTVGRYHSLFADPETLPDELLVTAETE-DGVIMAIEHKTLPVAAVQ 693


                  ....
gi 193204318  338 FHPE 341
Cdd:PRK13566  694 FHPE 697
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 1058-1205 4.77e-10

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 60.35  E-value: 4.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1058 ESLKISQPQWKKSENMEDAKNFCAQVGYPCLI---RPSYvlSGAAMNVAHNAEDLEvflkQAAVVAKEHPVVVSKFINEA 1134
Cdd:pfam02222    1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFD 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318  1135 KELDVDAV-ALDGKLVVMAVSEHIEnagvHSGDATLVTPAQDMNKLTLDRIKDITFRIAEAFNVNGPFNMQL 1205
Cdd:pfam02222   75 RELSVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 519-787 5.73e-10

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 63.89  E-value: 5.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  519 ISAIGEKVA---------------PSKAATTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELiaiaQQALAhSN 583
Cdd:PRK06111  110 IAKMGSKIEarramqaagvpvvpgITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL----TKAFE-SN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  584 Q-----------VLVDKSLKGWKEVEYEVVRDAYDNCitvcnmenvdplgIHTGE---SV------VV--APSQTLSDRE 641
Cdd:PRK06111  185 KkraanffgngeMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPFLDEET 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  642 YNALRTCAIKVIRHLGIIGECNIQYALDPYSlTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGQHLPVIRNSVTG 721
Cdd:PRK06111  252 RKAMGERAVQAAKAIGYTNAGTIEFLVDEQK-NFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKR 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  722 TTTA-----------CFEPSLDycvvKIPRWDL--GKFARVSTQIGSSMK-------SVGEVMGIGRCFEEALQKALRMV 781
Cdd:PRK06111  331 SGHAievriyaedpkTFFPSPG----KITDLTLpgGEGVRHDHAVENGVTvtpfydpMIAKLIAHGETREEAISRLHDAL 406


                  ....*..
gi 193204318  782 SD-HADG 787
Cdd:PRK06111  407 EElKVEG 413
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
221-341 1.07e-09

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 60.26  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  221 LFLSNGPGDPE---ICAPLVDRLAkviarGDKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATG------RC 291
Cdd:PRK06774   47 LVISPGPCTPNeagISLAVIRHFA-----DKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGvfrglnQP 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 193204318  292 YITSQNHGYAVDPDSLPADWKALFTNEND-KTNE--GIVHSSKPFFSVQFHPE 341
Cdd:PRK06774  122 LTVTRYHSLVIAADSLPGCFELTAWSERGgEMDEimGIRHRTLPLEGVQFHPE 174
PRK14804 PRK14804
ornithine carbamoyltransferase; Provisional
 1877-2193 3.08e-09

ornithine carbamoyltransferase; Provisional


Pssm-ID: 173265 [Multi-domain]  Cd Length: 311  Bit Score: 60.81  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1877 KNCISVKHLDKGQINRIFELADRYKHD--VEKGHplthiLNGKVLVNLFYEVSTRTSCSFSAAMQRLGGS------VISV 1948
Cdd:PRK14804    7 KHLISWEDWSDSEILDLLDFAVHVKKNrvNYAGH-----MSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHgiyldwMASN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1949 DSQSSSVQKGETLEDTVQV----LGSYGDILVLRSNENgaadraarvcdQPVINGGDGTGeHPTQALLDVYTIRQEMGTV 2024
Cdd:PRK14804   82 FQLSDIDLEARYLSRNVSVimarLKKHEDLLVMKNGSQ-----------VPVINGCDNMF-HPCQSLADIMTIALDSPEI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2025 --NGLTIALVGDLKNgrTVHSLAKLLCLYkDITLHYVAPSTELE-MPQEVLDYVSSKSNFVQKKftSLAEGINHVDVVYV 2101
Cdd:PRK14804  150 plNQKQLTYIGVHNN--VVNSLIGITAAL-GIHLTLVTPIAAKEnIHAQTVERAKKKGTLSWEM--NLHKAVSHADYVYT 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 2102 -TRIQKERFSSPDEYNKVKGS------YVINAKLLNeaardveepssllvpaRSLPIVMHPLP--RVDEIAVELDHDERA 2172
Cdd:PRK14804  225 dTWLDMEFFNDPSYADKKKQRmelmmpYQINSSLME----------------KTNAKVMHDMPihAGYEITREVVLSDRS 288

                         330       340
                  ....*....|....*....|.
gi 193204318 2173 AYFRQAKNGVFVRMSILSLLL 2193
Cdd:PRK14804  289 IIFQQAENRLDAQKAVILKLL 309
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 392-703 5.97e-09

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 59.90  E-value: 5.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  392 KVLVLGSGGltigqagefdysGAQALKALREEGIRTVLINPNIATVQTSKGFADFTYFLP-IT-KEY---VTDVIKKERP 466
Cdd:PRK12767    3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkVTdPNYidrLLDICKKEKI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  467 TGILCTFGGQTALNCAidlYKDGiFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSKAATTMEGAIEA--AEE 544
Cdd:PRK12767   71 DLLIPLIDPELPLLAQ---NRDR-FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAlaKGE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  545 LGYPVLVRAAYALGGLGSGFADNREELiaiaQQALAHSNQVLVDKSLKGwKEVEYEVVRDAYDNCITVCNMENVDPLGih 624
Cdd:PRK12767  147 LQFPLFVKPRDGSASIGVFKVNDKEEL----EFLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIEVRA-- 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193204318  625 tGESvvvapSQTLSdREYNALRTCAIKVIRHLGIIGECNIQYALDPYslTYYIIEVNARLSrssalaskaTGYPLAYVA 703
Cdd:PRK12767  220 -GET-----SKGVT-VKDPELFKLAERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG---------GGYPLSYMA 280
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
221-341 6.39e-09

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 57.62  E-value: 6.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  221 LFLSNGPGDPE---ICAPLVDRLAkviarGDKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATG------RC 291
Cdd:PRK08007   47 IVISPGPCTPDeagISLDVIRHYA-----GRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGvfrglaNP 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 193204318  292 YITSQNHGYAVDPDSLPADWKALFTNENDKTnEGIVHSSKPFFSVQFHPE 341
Cdd:PRK08007  122 LTVTRYHSLVVEPDSLPACFEVTAWSETREI-MGIRHRQWDLEGVQFHPE 170
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 500-714 6.46e-09

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 60.92  E-value: 6.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  500 GTQINTIMKTEDRDLFNQEISAIGEKVAPSKAA--TTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELIA---I 574
Cdd:PRK12833  107 GPDAQTIRTMGDKARARRTARRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  575 AQ---QALAHSNQVLVDKSLKGWKEVEYEVVRDAYDnciTVCNMENVDPLGIHTGESVVVAPSQTLSDREYNALRTCAIK 651
Cdd:PRK12833  187 AQreaQAAFGDGGVYLERFIARARHIEVQILGDGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVR 263

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193204318  652 VIRHLGIIGECNIQYALDPYSLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGQHLPV 714
Cdd:PRK12833  264 LARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRF 326
PRK06895 PRK06895
anthranilate synthase component II;
212-341 6.57e-09

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 57.82  E-value: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  212 IDTESDYDGLFLSNGPGDPEICAPLVDRLAKVIARgdKPIFGICLGHQILSRAIGAKTYKLkygnrghNQPcTHYATGRC 291
Cdd:PRK06895   38 LDEVENFSHILISPGPDVPRAYPQLFAMLERYHQH--KSILGVCLGHQTLCEFFGGELYNL-------NNV-RHGQQRPL 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193204318  292 YITSQN---------------HGYAVDPDSLPADWKAlfTNENDktnEGIV----HSSKPFFSVQFHPE 341
Cdd:PRK06895  108 KVRSNSplfdglpeefniglyHSWAVSEENFPTPLEI--TAVCD---ENVVmamqHKTLPIYGVQFHPE 171
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
200-341 8.05e-09

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 57.58  E-value: 8.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  200 GFRVKVVPwnhpiDTESDYDG--------LFLSNGPGDPE---ICAPLVDRLAkviarGDKPIFGICLGHQILSRAIGAK 268
Cdd:PRK08857   23 GAQVKVVR-----NDEIDIDGiealnpthLVISPGPCTPNeagISLQAIEHFA-----GKLPILGVCLGHQAIAQVFGGQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  269 TYKLKYGNRGHNQPCTHyaTGRCYITSQN--------HGYAVDPDSLPA--DWKALFTNENDKTNE--GIVHSSKPFFSV 336
Cdd:PRK08857   93 VVRARQVMHGKTSPIRH--TGRSVFKGLNnpltvtryHSLVVKNDTLPEcfELTAWTELEDGSMDEimGFQHKTLPIEAV 170


                  ....*
gi 193204318  337 QFHPE 341
Cdd:PRK08857  171 QFHPE 175
PRK01713 PRK01713
ornithine carbamoyltransferase; Provisional
 1871-2037 1.60e-08

ornithine carbamoyltransferase; Provisional


Pssm-ID: 167263 [Multi-domain]  Cd Length: 334  Bit Score: 58.84  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1871 PGELLAKNCISVKHLDKGQINRIFELADRYKHDVEKGHPlTHILNGKVLVNLFYEVSTRTSCSFSAAMQRLGGSVISVDS 1950
Cdd:PRK01713    2 AFNLKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTE-QQRLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1951 QSSSVQKGETLEDTVQVLGSYGDILVLRSNENGAADRAARVCDQPVINGgdGTGE-HPTQALLDVYT-IRQEMGTVNGLT 2028
Cdd:PRK01713   81 NSSQIGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFNG--LTDEfHPTQMLADVLTmIENCDKPLSEIS 158


                  ....*....
gi 193204318 2029 IALVGDLKN 2037
Cdd:PRK01713  159 YVYIGDARN 167
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 534-719 3.04e-08

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 58.67  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  534 TMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELI----AIAQQALAHSN--QVLVDKSLKGWKEVEYEVVRDAYD 607
Cdd:PRK08463  140 SMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLEnafeSCKREALAYFNndEVFMEKYVVNPRHIEFQILGDNYG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  608 NCITVCnmENVDPLGIHTGESVVVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSlTYYIIEVNARLSRS 687
Cdd:PRK08463  220 NIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYN-RFYFMEMNTRIQVE 296

                         170       180       190
                  ....*....|....*....|....*....|..
gi 193204318  688 SALASKATGYPLAYVAAKLALGQHLPVIRNSV 719
Cdd:PRK08463  297 HGVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
490-713 4.74e-08

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 57.83  E-value: 4.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  490 IFEQYDVQVLGTQINTIMKTEDRDLFNQEISAIGEKVAPSK--AATTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADN 567
Cdd:PRK08462   96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  568 REEL----IAIAQQALAH--SNQVLVDKSLKGWKEVEYEVVRDAYDNCITV----CNMENVDPLGIHtgESvvvaPSQTL 637
Cdd:PRK08462  176 ESDLenlyLAAESEALSAfgDGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQRRHQKLIE--ES----PAVVL 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193204318  638 SDREYNALRTCAIKVIRHLGIIGECNIQYALDPySLTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGQHLP 713
Cdd:PRK08462  250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLDS-NLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP 324
trpG CHL00101
anthranilate synthase component 2
 220-341 7.64e-08

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 54.74  E-value: 7.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  220 GLFLSNGPGDPE---ICAPLVDRLAKVIargdkPIFGICLGHQILSRAIGAKTYKLKYGNRG------HNQPCTHYATGR 290
Cdd:CHL00101   46 HIIISPGPGHPRdsgISLDVISSYAPYI-----PILGVCLGHQSIGYLFGGKIIKAPKPMHGktskiyHNHDDLFQGLPN 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 193204318  291 CYITSQNHGYAVDPDSLPADWKALftnenDKTNEGIV----HSSKPF-FSVQFHPE 341
Cdd:CHL00101  121 PFTATRYHSLIIDPLNLPSPLEIT-----AWTEDGLImacrHKKYKMlRGIQFHPE 171
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
530-712 1.22e-07

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 56.64  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  530 KAATTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELIAIAQQALAHS------NQVLVDKSLKGWKEVEYEVVR 603
Cdd:PRK05586  136 GEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAkaafgdDSMYIEKFIENPKHIEFQILG 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  604 DAYDNCITVCNMEnvdpLGIHTGESVVV--APSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSlTYYIIEVN 681
Cdd:PRK05586  216 DNYGNVVHLGERD----CSLQRRNQKVLeeAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDG-NFYFMEMN 290

                         170       180       190
                  ....*....|....*....|....*....|.
gi 193204318  682 ARLSRSSALASKATGYPLAYVAAKLALGQHL 712
Cdd:PRK05586  291 TRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 196-356 1.30e-07

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 53.73  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  196 LAKRGFRVKVVPWNHPIDTESDY----DGLFLSNGP--------GDPEICAPLVDR---------LAKVIARGdKPIFGI 254
Cdd:cd01745    28 VRKAGGLPVLLPPVDDEEDLEQYlellDGLLLTGGGdvdpplygEEPHPELGPIDPerdafelalLRAALERG-KPILGI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  255 CLGHQILSRAIGAKTYKLKYGNRGHNQpcthyatgrcyitsqnhgyAVDPdsLPADWKALFTnENDKTNEGIVHSSKPF- 333
Cdd:cd01745   107 CRGMQLLNVALGGTLYQDIRVNSLHHQ-------------------AIKR--LADGLRVEAR-APDGVIEAIESPDRPFv 164

                         170       180
                  ....*....|....*....|....
gi 193204318  334 FSVQFHPE-HTAGPTDCEFLFDVF 356
Cdd:cd01745   165 LGVQWHPEwLADTDPDSLKLFEAF 188
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
530-616 1.74e-07

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 56.15  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  530 KAATTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREELI-------AIAQQALAHSNqVLVDKSLKGWKEVEYEVV 602
Cdd:PRK08654  136 EGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEdaiestqSIAQSAFGDST-VFIEKYLEKPRHIEIQIL 214

                          90
                  ....*....|....
gi 193204318  603 RDAYDNCITVCNME 616
Cdd:PRK08654  215 ADKHGNVIHLGDRE 228
guaA PRK00074
GMP synthase; Reviewed
 205-343 7.13e-07

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 54.28  E-value: 7.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  205 VVPWNHPIDTESDYD--GLFLSNGPG---DPEicAPLVDrlaKVIARGDKPIFGICLGHQILSRAIGAKTyklkygNRGH 279
Cdd:PRK00074   32 IVPYDISAEEIRAFNpkGIILSGGPAsvyEEG--APRAD---PEIFELGVPVLGICYGMQLMAHQLGGKV------ERAG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  280 NQpctHYatGRCYITSQN-----------------HGYAVdpDSLPADWKALFTNENdKTNEGIVHSSKPFFSVQFHPE- 341
Cdd:PRK00074  101 KR---EY--GRAELEVDNdsplfkglpeeqdvwmsHGDKV--TELPEGFKVIASTEN-CPIAAIANEERKFYGVQFHPEv 172


                  ...
gi 193204318  342 -HT 343
Cdd:PRK00074  173 tHT 175
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
534-714 1.39e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 53.18  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  534 TMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREEL-------IAIAQQALAhSNQVLVDKSLKGWKEVEYEVVRDAY 606
Cdd:PRK07178  139 DLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELeqnfprvISEATKAFG-SAEVFLEKCIVNPKHIEVQILADSH 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  607 DNCITV----CNMENVDPLGIHtgesvvVAPSQTLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPYSlTYYIIEVNA 682
Cdd:PRK07178  218 GNVVHLferdCSIQRRNQKLIE------IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADG-EVYFMEMNT 290

                         170       180       190
                  ....*....|....*....|....*....|..
gi 193204318  683 RLSRSSALASKATGYPLAYVAAKLALGQHLPV 714
Cdd:PRK07178  291 RVQVEHTITEEITGIDIVREQIRIASGLPLSY 322
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
219-341 2.33e-06

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 50.19  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  219 DGLFLSNGPGDPE---ICAPLVDRLAkviarGDKPIFGICLGHQILSRAIGAKTYKLKYGNRGHNQPCTHYATG------ 289
Cdd:PRK07649   45 DFLMISPGPCSPNeagISMEVIRYFA-----GKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTifsdip 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 193204318  290 RCYITSQNHGYAVDPDSLPADWKAlftneNDKTNEG----IVHSSKPFFSVQFHPE 341
Cdd:PRK07649  120 NPFTATRYHSLIVKKETLPDCLEV-----TSWTEEGeimaIRHKTLPIEGVQFHPE 170
PLN02335 PLN02335
anthranilate synthase
 220-341 3.30e-06

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 50.57  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  220 GLFLSNGPGDPE---ICAPLVDRLAKVIargdkPIFGICLGHQILSRAIGAKTYKLKYG-NRGHNQPCTHYATG------ 289
Cdd:PLN02335   65 GVLISPGPGTPQdsgISLQTVLELGPLV-----PLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYDEKGeeglfs 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 193204318  290 ---RCYITSQNHGYAVDPDSLPADWKALFTNENDKTNEGIVHSSKPFFS-VQFHPE 341
Cdd:PLN02335  140 glpNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 543-681 7.62e-06

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 48.85  E-value: 7.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   543 EELGYPVLVRAAYalggLGSGF----ADNREELIAIAQQALAHSNQVLVDKSLKGwKEVEyevvrdaydncITVCNMENV 618
Cdd:pfam07478   33 EALGYPVFVKPAR----LGSSVgvskVESREELQAAIEEAFQYDEKVLVEEGIEG-REIE-----------CAVLGNEDP 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   619 DPLGIH------------------TGESVVVAPsqtLSDREYNALRTCAIKVIRHLGIIGECNIQYALDPySLTYYIIEV 680
Cdd:pfam07478   97 EVSPVGeivpsggfydyeakyiddSAQIVVPAD---LEEEQEEQIQELALKAYKALGCRGLARVDFFLTE-DGEIVLNEV 172


                   .
gi 193204318   681 N 681
Cdd:pfam07478  173 N 173
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 519-684 1.29e-05

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 50.19  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  519 ISAIGEKVAPSKAA---------------TTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNREEL---IAIAQQ--A 578
Cdd:PRK08591  110 IRLMGDKVTAKATMkkagvpvvpgsdgpvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELekaFSMARAeaK 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  579 LAHSN-QVLVDKSLKGWKEVEYEVVRDAYDNcitvcnmenvdplGIHTGE---SV------VV--APSQTLSDREYNALR 646
Cdd:PRK08591  190 AAFGNpGVYMEKYLENPRHIEIQVLADGHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIG 256

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 193204318  647 TCAIKVIRHLGIIGECNIQYALDpYSLTYYIIEVNARL 684
Cdd:PRK08591  257 EAAVKAAKAIGYRGAGTIEFLYE-KNGEFYFIEMNTRI 293
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 240-341 2.72e-05

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 47.64  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   240 LAKVIARGdKPIFGICLGHQILSRAIGAKTY---KLKYGNRGHNQPC-------THY---ATGRCY--ITSQN------- 297
Cdd:pfam07722   98 IRAALARG-KPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapSHAvnvEPGSLLasLLGSEefrvnsl 176

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 193204318   298 HGYAVdpDSLPADWKALFTNEnDKTNEGIVH--SSKPFFSVQFHPE 341
Cdd:pfam07722  177 HHQAI--DRLAPGLRVEAVAP-DGTIEAIESpnAKGFALGVQWHPE 219
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1040-1218 1.16e-04

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 46.47  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1040 SPNDIDNAEDRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQVGYPCLIRPSYVLSGAAMNVAHNAEDLEVFLKQAAVV 1119
Cdd:COG0189    87 DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTEL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1120 AKEhPVVVSKFINEAKELDVDAVALDGKLV-----VMAVSEHIENagVHSGDAtlVTPAqdmnKLTlDRIKDITFRIAEA 1194
Cdd:COG0189   167 GSE-PVLVQEFIPEEDGRDIRVLVVGGEPVaairrIPAEGEFRTN--LARGGR--AEPV----ELT-DEERELALRAAPA 236

                         170       180
                  ....*....|....*....|....*.
gi 193204318 1195 F--NVNGpfnMQLIAKNNELKVIECN 1218
Cdd:COG0189   237 LglDFAG---VDLIEDDDGPLVLEVN 259
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 234-270 2.15e-04

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 44.94  E-value: 2.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 193204318  234 APLVDRLAKVIArGDKPIFGICLGHQILSRAIGAKTY 270
Cdd:PRK07053   70 APEIALLRQRLA-AGLPTLGICLGAQLIARALGARVY 105
ddl PRK01966
D-alanine--D-alanine ligase;
520-598 2.80e-04

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 45.50  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  520 SAIGEKVAPSKAAT----TMEGAIEAAEELGYPVLVRAAyalgGLGSGF----ADNREELIAIAQQALAHSNQVLVDKSL 591
Cdd:PRK01966  132 AAAGIPVAPYVVLTrgdwEEASLAEIEAKLGLPVFVKPA----NLGSSVgiskVKNEEELAAALDLAFEYDRKVLVEQGI 207


                  ....*..
gi 193204318  592 KGwKEVE 598
Cdd:PRK01966  208 KG-REIE 213
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 1057-1194 2.87e-04

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 44.23  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1057 LESLKISQPQWK------KSENMEDAK-NFCAQVGYPCLIRPSYVLSGAAMNVAHNAEDLEVFLKQAAvvAKEHPVVVSK 1129
Cdd:pfam07478    2 LKAAGLPVVPFVtftradWKLNPKEWCaQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAF--QYDEKVLVEE 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204318  1130 FInEAKELDVdAVALDGKLVVMAVSEHIENAGVH-------SGDATLVTPAqDMNKLTLDRIKDITFRIAEA 1194
Cdd:pfam07478   80 GI-EGREIEC-AVLGNEDPEVSPVGEIVPSGGFYdyeakyiDDSAQIVVPA-DLEEEQEEQIQELALKAYKA 148
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 181-345 8.68e-04

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 42.87  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  181 ILAVDCGLKN--NQIRCLAKRGFRVKVVPWNHPIDtesDYDGLFLsngPG----DPEICA----PLVDRLAKVIARGdKP 250
Cdd:cd01748     1 IAIIDYGMGNlrSVANALERLGAEVIITSDPEEIL---SADKLIL---PGvgafGDAMANlrerGLIEALKEAIASG-KP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  251 IFGICLGHQILSRA------------IGAKTYKLKYGNR------GHNQpcthyatgrCYITSQN--------------- 297
Cdd:cd01748    74 FLGICLGMQLLFESseegggtkglglIPGKVVRFPASEGlkvphmGWNQ---------LEITKESplfkgipdgsyfyfv 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 193204318  298 HGYAVDPDslPADWKALftnendKTNEGI----VHSSKPFFSVQFHPE--HTAG 345
Cdd:cd01748   145 HSYYAPPD--DPDYILA------TTDYGGkfpaAVEKDNIFGTQFHPEksGKAG 190
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1476-1756 1.45e-03

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 43.26  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1476 LPGMVDIHVH--------VREPGATHKEDWATCSKAALAGGVTTILAMPNTSPVLVDT---------------------D 1526
Cdd:pfam01979    3 LPGLIDAHVHlemgllrgIPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEAlleaaeelplglrflgpgcslD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1527 SFYQTEQ-LASAKSVVDYALYIGATpNNSKFAAEFADKAAGlkmylneTFSTLKMDNISDWAKHlsafpANRPIVCHAEK 1605
Cdd:pfam01979   83 TDGELEGrKALREKLKAGAEFIKGM-ADGVVFVGLAPHGAP-------TFSDDELKAALEEAKK-----YGLPVAIHALE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  1606 QTLAAILCMAQMANRAVHIAHVATADEINL---VKEAKQRGWNVTcevcPHHLFLIEEDLP-DGIREV-RPRLVKPEDRQ 1680
Cdd:pfam01979  150 TKGEVEDAIAAFGGGIEHGTHLEVAESGGLldiIKLILAHGVHLS----PTEANLLAEHLKgAGVAHCpFSNSKLRSGRI 225

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193204318  1681 ALWDNMEY--IDCFATDHAPHtwaektgkdGKIPPGFPGVEYMlpLLLTAVHDGKLTMKELTDRMSTNPRRIFNLPPQ 1756
Cdd:pfam01979  226 ALRKALEDgvKVGLGTDGAGS---------GNSLNMLEELRLA--LELQFDPEGGLSPLEALRMATINPAKALGLDDK 292
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 187-264 1.53e-03

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 41.47  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318   187 GLKNNQIRClaKRGFRVKVvpwNHPID--TESDYDGLFLSNGPGDPE---ICAPLVDrLAKVIARGDKPIFGICLGHQIL 261
Cdd:pfam01965   34 SVDGGEVKG--SRGVKVTV---DASLDdvKPDDYDALVLPGGRAGPErlrDNEKLVE-FVKDFYEKGKPVAAICHGPQVL 107


                   ...
gi 193204318   262 SRA 264
Cdd:pfam01965  108 AAA 110
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 221-266 2.19e-03

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 43.09  E-value: 2.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193204318  221 LFLSNGPGDPEI--CAP-LVDRLakviaRGDKPIFGICLGHQILSRAIG 266
Cdd:PRK09522   52 LMLSPGPGVPSEagCMPeLLTRL-----RGKLPIIGICLGHQAIVEAYG 95
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 511-593 2.44e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 43.22  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  511 DRDLFNQEISAIGEKVAPSKAATTMEGAIEAAEELGYPVLVRAAYalGGLGSG-FAD--NREELIAIAQQALAHSNQVLV 587
Cdd:PRK14016  214 DKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLD--GNHGRGvTVNitTREEIEAAYAVASKESSDVIV 291


                  ....*.
gi 193204318  588 DKSLKG 593
Cdd:PRK14016  292 ERYIPG 297
PRK14569 PRK14569
D-alanyl-alanine synthetase A; Provisional
 489-682 2.80e-03

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173033 [Multi-domain]  Cd Length: 296  Bit Score: 41.97  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  489 GIFEQYDVQVLGTQINTIMKTEDRdLFNQEIsaIGEKVAPSKAATTMEGAIEAAEELGYPVLVRAAYALGGLGSGFADNR 568
Cdd:PRK14569   76 ALLEMLEIKHTSSSMKSSVITMDK-MISKEI--LMHHRMPTPMAKFLTDKLVAEDEISFPVAVKPSSGGSSIATFKVKSI 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  569 EELIAIAQQALAHSnQVLVDKSLKGwKEVEYEVVR-DAYDNCITVCNMENVDPLGIHTGESVVVAPSQTLSDREYNaLRT 647
Cdd:PRK14569  153 QELKHAYEEASKYG-EVMIEQWVTG-KEITVAIVNdEVYSSVWIEPQNEFYDYESKYSGKSIYHSPSGLCEQKELE-VRQ 229

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 193204318  648 CAIKVIRHLGIIGECNIQYALDPYSlTYYIIEVNA 682
Cdd:PRK14569  230 LAKKAYDLLGCSGHARVDFIYDDRG-NFYIMEINS 263
PRK06849 PRK06849
hypothetical protein; Provisional
 1049-1221 2.98e-03

hypothetical protein; Provisional


Pssm-ID: 235876 [Multi-domain]  Cd Length: 389  Bit Score: 42.34  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1049 DRFKFSRKLESLKISQPQWKKSENMEDAKNFCAQ-VGYPCLIRPSYVLSGAamnvahnaeDLEVFLKQAAV----VAKEH 1123
Cdd:PRK06849  116 NKWEFAEQARSLGLSVPKTYLITDPEAIRNFMFKtPHTPYVLKPIYSRFVR---------RVDLLPKEAALkelpISKDN 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318 1124 PVVVSKFInEAKELDVDAVALDGKLVVMAVSEHIENAGVHSGDATlvtpaQDMNKltlDRIKDITFRIAEAFNVNGPFNM 1203
Cdd:PRK06849  187 PWVMQEFI-QGKEYCSYSIVRSGELRAHSCYKPEYCAGSGAQIAF-----QPINH---PRIEEFVTHFVKELNYTGQISF 257

                         170
                  ....*....|....*....
gi 193204318 1204 QLI-AKNNELKVIECNLRV 1221
Cdd:PRK06849  258 DFIeTENGDAYPIECNPRT 276
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 194-343 3.59e-03

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 41.48  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  194 RCLAKRGFRVKVvpwNHPI------DTESDYDGLFLSNGP---GDPE--ICAPlVDRLAkVIARGDKPIFGICLGHQILS 262
Cdd:PRK06490   26 QLLQERGYPLDI---RRPRlgdplpDTLEDHAGAVIFGGPmsaNDPDdfIRRE-IDWIS-VPLKENKPFLGICLGAQMLA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  263 RAIGAKTYklkygnrGHNQpcthyatGRCYI-------TSQNHGYAVDPD----------SLPADWKALFTNEnDKTNEG 325
Cdd:PRK06490  101 RHLGARVA-------PHPD-------GRVEIgyyplrpTEAGRALMHWPEmvyhwhregfDLPAGAELLATGD-DFPNQA 165

                         170
                  ....*....|....*...
gi 193204318  326 IVHSSKPfFSVQFHPEHT 343
Cdd:PRK06490  166 FRYGDNA-WGLQFHPEVT 182
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 526-593 6.03e-03

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 41.25  E-value: 6.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204318  526 VAPSKAATTMEGAIEAAEELGYPVLVRAayALGG--LGSGFADNREELIAIAQQALAHSNQVLVDKSLKG 593
Cdd:PRK01372  113 TPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGssVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG 180
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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