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Conserved domains on  [gi|491113090|ref|WP_004971548|]
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MULTISPECIES: dihydroorotase [Acinetobacter]

Protein Classification

dihydroorotase( domain architecture ID 10101434)

dihydroorotase catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis

CATH:  3.20.20.140|2.30.40.10
EC:  3.5.2.3
Gene Ontology:  GO:0004151|GO:0008270|GO:0006221
PubMed:  9144792
SCOP:  4002199|4002171

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 40-408 4.83e-129

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: 376.58  E-value: 4.83e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  40 ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVqDNGALIHGLVEKAMLDGGIYLE 119
Cdd:cd01317    3 EVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAVVELLKNRAKDVGIVRVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 120 VIGAQTQGLNGKQPANMAGLKKGGCSAVSNANAPFEDDDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQG 199
Cdd:cd01317   82 PIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRLG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 200 LPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPL 279
Cdd:cd01317  162 LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPPL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 280 RSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFGIQ-LIQEGLFSPLEWVEKVTLAPARV 358
Cdd:cd01317  242 RSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTlLVKGGLLTLPDLIRALSTNPAKI 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491113090 359 AKMQSRWEQE---AGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRV 408
Cdd:cd01317  322 LGLPPGRLEVgapADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 6-56 1.15e-04

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.


The actual alignment was detected with superfamily member PRK09237:

Pssm-ID: 469705 [Multi-domain]  Cd Length: 380  Bit Score: 44.07  E-value: 1.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491113090   6 IENVRVLDPIQQIDRVQTVYLENGKLVAESADISES-----IDAQGQWLMPTMVDL 56
Cdd:PRK09237   3 LRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSqakkvIDLSGLYVSPGWIDL 58
 
Name Accession Description Interval E-value
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 40-408 4.83e-129

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: 376.58  E-value: 4.83e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  40 ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVqDNGALIHGLVEKAMLDGGIYLE 119
Cdd:cd01317    3 EVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAVVELLKNRAKDVGIVRVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 120 VIGAQTQGLNGKQPANMAGLKKGGCSAVSNANAPFEDDDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQG 199
Cdd:cd01317   82 PIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRLG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 200 LPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPL 279
Cdd:cd01317  162 LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPPL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 280 RSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFGIQ-LIQEGLFSPLEWVEKVTLAPARV 358
Cdd:cd01317  242 RSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTlLVKGGLLTLPDLIRALSTNPAKI 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491113090 359 AKMQSRWEQE---AGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRV 408
Cdd:cd01317  322 LGLPPGRLEVgapADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
pyrC PRK09357
dihydroorotase; Validated
 1-409 1.26e-118

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 351.42  E-value: 1.26e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   1 MAIVkIENVRVLDPiQQIDRVQTVYLENGKLVAESADISES----IDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGK 76
Cdd:PRK09357   1 MMIL-IKNGRVIDP-KGLDEVADVLIDDGKIAAIGENIEAEgaevIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  77 AARENGILHLFTPPDSKPiVQDNGALIHGLVEKAMLDGGIYLEVIGAQTQGLNGKQPANMAGLKKGGCSAVSNANAPFED 156
Cdd:PRK09357  79 AAAAGGFTTVVAMPNTKP-VIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 157 DDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGAS 236
Cdd:PRK09357 158 ARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 237 VELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPF 316
Cdd:PRK09357 238 VELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 317 ADTLSGFTAFDTYIPFGIQ-LIQEGLFSPLEWVEKVTLAPARVAKMQSRWEQE---AGWVLVDPEVEWTLNKETIVSQGK 392
Cdd:PRK09357 318 EAAPFGITGLETALSLLYTtLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEgepADLVIFDPEAEWTVDGEDFASKGK 397

                        410
                 ....*....|....*..
gi 491113090 393 NTPLINQVVKGKAVRVF 409
Cdd:PRK09357 398 NTPFIGMKLKGKVVYTI 414
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 6-409 1.87e-109

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: 328.59  E-value: 1.87e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   6 IENVRVLDP--IQQIDrvqtVYLENGKLVAESADIS-----ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAA 78
Cdd:COG0044    2 IKNGRVVDPggLERAD----VLIEDGRIAAIGPDLAapeaaEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  79 RENGILHLFTPPDSKPiVQDNGALIHGLVEKAMLDGGIYLEVIGAQTQGLnGKQPANMAGLKKGGCSAV-----SNANAP 153
Cdd:COG0044   78 AAGGVTTVVDMPNTNP-VTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGNP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 154 FEDDDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSC 233
Cdd:COG0044  156 VLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVST 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 234 GASVELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKM 313
Cdd:COG0044  236 AEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKE 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 314 APFADTLSGFTAFDTYIPFGIQ-LIQEGLFSPLEWVEKVTLAPARVAKMQSRWEQEAG----WVLVDPEVEWTLNKETIV 388
Cdd:COG0044  316 LPFAEAPNGIPGLETALPLLLTeLVHKGRLSLERLVELLSTNPARIFGLPRKGRIAVGadadLVLFDPDAEWTVTAEDLH 395

                        410       420
                 ....*....|....*....|.
gi 491113090 389 SQGKNTPLINQVVKGKAVRVF 409
Cdd:COG0044  396 SKSKNTPFEGRELTGRVVATI 416
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 23-406 1.08e-69

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: 225.40  E-value: 1.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   23 TVYLENGKLVA-ESADISES---IDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVQD 98
Cdd:TIGR00857   7 DILVEGGRIKKiGKLRIPPDaevIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   99 NGAL---IHGLVEKAMLDGGIYLEVigaqTQGLNGKQPANMAGLKKGGCSAVSNANAPFE--DDDVVIRTLEYAAGLDMT 173
Cdd:TIGR00857  87 PETLewkLQRLKKVSLVDVHLYGGV----TQGNQGKELTEAYELKEAGAVGRMFTDDGSEvqDILSMRRALEYAAIAGVP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  174 VVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCD 253
Cdd:TIGR00857 163 IALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  254 VAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFG 333
Cdd:TIGR00857 243 VTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPLL 322

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491113090  334 IQLIQEGLFSPLEWVEKVTLAPARVAKM--QSRWE--QEAGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAV 406
Cdd:TIGR00857 323 LQLLVKGLISLKDLIRMLSINPARIFGLpdKGTLEegNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPI 399
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
6-56 1.15e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 44.07  E-value: 1.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491113090   6 IENVRVLDPIQQIDRVQTVYLENGKLVAESADISES-----IDAQGQWLMPTMVDL 56
Cdd:PRK09237   3 LRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSqakkvIDLSGLYVSPGWIDL 58
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 109-406 1.58e-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: 40.18  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  109 KAMLDGGI--YLEVIGAQTQGLNG------KQPANMAGLKKGGCSAVSNANAPFEDDDVVIRTLEYAAGLDMTVVFYAE- 179
Cdd:pfam01979  37 TTMLKSGTttVLDMGATTSTGIEAlleaaeELPLGLRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGl 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  180 ---EPQIAKDGCVHEGF-IASRQGLPMIPTLAETVAIAKYllMIEATGVRA----HFGLLSCGASVELIQQAKAKGLPVT 251
Cdd:pfam01979 117 aphGAPTFSDDELKAALeEAKKYGLPVAIHALETKGEVED--AIAAFGGGIehgtHLEVAESGGLLDIIKLILAHGVHLS 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  252 cdvaMHQLHLTDQIIDGfNSLAHV-RPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLsgftafdtyi 330
Cdd:pfam01979 195 ----PTEANLLAEHLKG-AGVAHCpFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLA---------- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  331 pFGIQLIQEGLFSPLEWVEKVTLAPARVAKMQSRWEQ-EAGW----VLVDpevewTLNKETIVSQGKNTPLINQVVKGKA 405
Cdd:pfam01979 260 -LELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSiEVGKdadlVVVD-----LDPLAAFFGLKPDGNVKKVIVKGKI 333


                  .
gi 491113090  406 V 406
Cdd:pfam01979 334 V 334
 
Name Accession Description Interval E-value
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 40-408 4.83e-129

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: 376.58  E-value: 4.83e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  40 ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVqDNGALIHGLVEKAMLDGGIYLE 119
Cdd:cd01317    3 EVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAVVELLKNRAKDVGIVRVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 120 VIGAQTQGLNGKQPANMAGLKKGGCSAVSNANAPFEDDDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQG 199
Cdd:cd01317   82 PIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRLG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 200 LPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPL 279
Cdd:cd01317  162 LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPPL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 280 RSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFGIQ-LIQEGLFSPLEWVEKVTLAPARV 358
Cdd:cd01317  242 RSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTlLVKGGLLTLPDLIRALSTNPAKI 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491113090 359 AKMQSRWEQE---AGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRV 408
Cdd:cd01317  322 LGLPPGRLEVgapADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
pyrC PRK09357
dihydroorotase; Validated
 1-409 1.26e-118

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 351.42  E-value: 1.26e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   1 MAIVkIENVRVLDPiQQIDRVQTVYLENGKLVAESADISES----IDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGK 76
Cdd:PRK09357   1 MMIL-IKNGRVIDP-KGLDEVADVLIDDGKIAAIGENIEAEgaevIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  77 AARENGILHLFTPPDSKPiVQDNGALIHGLVEKAMLDGGIYLEVIGAQTQGLNGKQPANMAGLKKGGCSAVSNANAPFED 156
Cdd:PRK09357  79 AAAAGGFTTVVAMPNTKP-VIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 157 DDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGAS 236
Cdd:PRK09357 158 ARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 237 VELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPF 316
Cdd:PRK09357 238 VELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 317 ADTLSGFTAFDTYIPFGIQ-LIQEGLFSPLEWVEKVTLAPARVAKMQSRWEQE---AGWVLVDPEVEWTLNKETIVSQGK 392
Cdd:PRK09357 318 EAAPFGITGLETALSLLYTtLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEgepADLVIFDPEAEWTVDGEDFASKGK 397

                        410
                 ....*....|....*..
gi 491113090 393 NTPLINQVVKGKAVRVF 409
Cdd:PRK09357 398 NTPFIGMKLKGKVVYTI 414
PRK07627 PRK07627
dihydroorotase; Provisional
 4-407 3.10e-111

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 332.80  E-value: 3.10e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   4 VKIENVRVLDPIQQIDRVQTVYLENGKLVA---ESADIS--ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAA 78
Cdd:PRK07627   3 IHIKGGRLIDPAAGTDRQADLYVAAGKIAAigqAPAGFNadKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  79 RENGILHLFTPPDSKPiVQDNGALIHGLVEKAMLDGGIYLEVIGAQTQGLNGKQPANMAGLKKGGCSAVSNANAPFEDDD 158
Cdd:PRK07627  83 VAGGVTSLVCPPDTDP-VLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFSQANVPVVDTQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 159 VVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVE 238
Cdd:PRK07627 162 VLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 239 LIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFAD 318
Cdd:PRK07627 242 LVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLPFAE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 319 TLSGFTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAPARVAKMQSRwEQEAGWV----LVDPEVEWTLNKETIVSQGKNT 394
Cdd:PRK07627 322 ATPGATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGLPAG-RLAEGAPadlcVFDPDAHWRVEPRALKSQGKNT 400

                        410
                 ....*....|...
gi 491113090 395 PLINQVVKGKaVR 407
Cdd:PRK07627 401 PFLGYELPGR-VR 412
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 6-409 1.87e-109

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: 328.59  E-value: 1.87e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   6 IENVRVLDP--IQQIDrvqtVYLENGKLVAESADIS-----ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAA 78
Cdd:COG0044    2 IKNGRVVDPggLERAD----VLIEDGRIAAIGPDLAapeaaEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  79 RENGILHLFTPPDSKPiVQDNGALIHGLVEKAMLDGGIYLEVIGAQTQGLnGKQPANMAGLKKGGCSAV-----SNANAP 153
Cdd:COG0044   78 AAGGVTTVVDMPNTNP-VTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGNP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 154 FEDDDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSC 233
Cdd:COG0044  156 VLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVST 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 234 GASVELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKM 313
Cdd:COG0044  236 AEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKE 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 314 APFADTLSGFTAFDTYIPFGIQ-LIQEGLFSPLEWVEKVTLAPARVAKMQSRWEQEAG----WVLVDPEVEWTLNKETIV 388
Cdd:COG0044  316 LPFAEAPNGIPGLETALPLLLTeLVHKGRLSLERLVELLSTNPARIFGLPRKGRIAVGadadLVLFDPDAEWTVTAEDLH 395

                        410       420
                 ....*....|....*....|.
gi 491113090 389 SQGKNTPLINQVVKGKAVRVF 409
Cdd:COG0044  396 SKSKNTPFEGRELTGRVVATI 416
PRK07369 PRK07369
dihydroorotase; Provisional
 1-409 1.50e-83

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 261.46  E-value: 1.50e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   1 MAIVKIENVRVLDPIQQIDRVQTVYLENGKLVAESADIS------ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSE 74
Cdd:PRK07369   1 MSNELLQQVRVLDPVSNTDRIADVLIEDGKIQAIEPHIDpippdtQIIDASGLILGPGLVDLYSHSGEPGFEERETLASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  75 GKAARENGILHLFTPPDSKPIVqDNGALIHGLVEKAMLDGGIYLEVIGAQTQGLNGKQPANMAGLKKGGCSAVSNaNAPF 154
Cdd:PRK07369  81 AAAAAAGGFTRVAILPDTFPPL-DNPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAAAGVVGFTD-GQPL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 155 EDDDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCG 234
Cdd:PRK07369 159 ENLALLRRLLEYLKPLGKPVALWPCDRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 235 ASVELIQQAKAKGLPVTCDVA-MHQLHLTDQIIDGFNSLaHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKM 313
Cdd:PRK07369 239 RSVELIAQAKARGLPITASTTwMHLLLDTEALASYDPNL-RLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKT 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 314 APFADTLSGFTAFDTYIPFGIQ-LIQEGLFSPLEWVEKVTLAPARV---AKMQSRWEQEAGWVLVDPEVEWTLNKETIVS 389
Cdd:PRK07369 318 VAFAEAPPGAIGLELALPLLWQnLVETGELSALQLWQALSTNPARClgqEPPSLAPGQPAELILFDPQKTWTVSAQTLHS 397

                        410       420
                 ....*....|....*....|
gi 491113090 390 QGKNTPLINQVVKGKAVRVF 409
Cdd:PRK07369 398 LSRNTPWLGQTLKGRVLQTW 417
PRK09059 PRK09059
dihydroorotase; Validated
 7-411 8.14e-70

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 226.46  E-value: 8.14e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   7 ENVRVLDPIQQIDRVQTVYLENGKLVAESADI--------SESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAA 78
Cdd:PRK09059   8 ANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAgnqgapegAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASASRAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  79 RENGILHLFTPPDSKPIVqDNGALIHGLVEKAMLDGGIYLEVIGAQTQGLNGKQPANMAGLKKGGCSAVSNANAPFEDDD 158
Cdd:PRK09059  88 AAGGVTSIIMMPDTDPVI-DDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLLRAAGAVAFTDGRRSVANTQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 159 VVIRTLEYAAGLDMTVVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVE 238
Cdd:PRK09059 167 VMRRALTYARDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAE 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 239 LIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFAD 318
Cdd:PRK09059 247 ALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTKRLPFSE 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 319 TLSGFTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAPARVAKMQS---RWEQEAGWVLVDPEVEWTLNKETIVSQGKNTP 395
Cdd:PRK09059 327 AAAGAIGLETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGLPAgtlKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTP 406

                        410
                 ....*....|....*.
gi 491113090 396 LINQVVKGKAVRVFTA 411
Cdd:PRK09059 407 FEEARFQGRVVRTIVA 422
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 23-406 1.08e-69

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: 225.40  E-value: 1.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   23 TVYLENGKLVA-ESADISES---IDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVQD 98
Cdd:TIGR00857   7 DILVEGGRIKKiGKLRIPPDaevIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   99 NGAL---IHGLVEKAMLDGGIYLEVigaqTQGLNGKQPANMAGLKKGGCSAVSNANAPFE--DDDVVIRTLEYAAGLDMT 173
Cdd:TIGR00857  87 PETLewkLQRLKKVSLVDVHLYGGV----TQGNQGKELTEAYELKEAGAVGRMFTDDGSEvqDILSMRRALEYAAIAGVP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  174 VVFYAEEPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCD 253
Cdd:TIGR00857 163 IALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  254 VAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFG 333
Cdd:TIGR00857 243 VTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPLL 322

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491113090  334 IQLIQEGLFSPLEWVEKVTLAPARVAKM--QSRWE--QEAGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAV 406
Cdd:TIGR00857 323 LQLLVKGLISLKDLIRMLSINPARIFGLpdKGTLEegNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPI 399
PRK08417 PRK08417
metal-dependent hydrolase;
26-411 1.02e-43

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 156.79  E-value: 1.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  26 LENGKLVAESADIS--ESIDAQGQWLMPTMVDLCARLREpGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVQDNGALI 103
Cdd:PRK08417   3 IKDGKITEIGSDLKgeEILDAKGKTLLPALVDLNVSLKN-DSLSSKNLKSLENECLKGGVGSIVLYPDSTPAIDNEIALE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 104 HGLVEKAMLDGGIYLEVIGAQTQGlngkQPANMAGLKKGGCSAV---SNANApfeddDVVIRTLEYAAGLDMTVVFYAEE 180
Cdd:PRK08417  82 LINSAQRELPMQIFPSIRALDEDG----KLSNIATLLKKGAKALelsSDLDA-----NLLKVIAQYAKMLDVPIFCRCED 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 181 PQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCDVAMHQLH 260
Cdd:PRK08417 153 SSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLI 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 261 LTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPF-GIQLIQE 339
Cdd:PRK08417 233 LDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLcYTYLVKE 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113090 340 GLFSPLEWVEKVTLAPARVAKMQSRWEQ---EAGWVLVDPevewtlNKETIVsQGKNTPLINQVVKGKAVRVFTA 411
Cdd:PRK08417 313 GIITWSELSRFTSYNPAQFLGLNSGEIEvgkEADLVLFDP------NESTII-DDNFSLYSGDELYGKIEAVIIK 380
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 49-409 4.43e-39

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: 143.63  E-value: 4.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  49 LMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVQDNGAL---IHGLVEKAMLDGGIYLevigaqt 125
Cdd:cd01318    4 ILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALyekLRLAAAKSVVDYGLYF------- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 126 qGLNGKQPANMagLKKGGCSAV-----SNANAPFEDDDVVIRTLEYAAGLdmtVVFYAEEPQIAKDgcvHEGFIASRQGL 200
Cdd:cd01318   77 -GVTGSEDLEE--LDKAPPAGYkifmgDSTGDLLDDEETLERIFAEGSVL---VTFHAEDEDRLRE---NRKELKGESAH 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 201 PMIPT-LAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKglpVTCDVAMHQLHLTDQIIDGFNSLAHVRPPL 279
Cdd:cd01318  148 PRIRDaEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLGTLGKVNPPL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 280 RSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAPARVA 359
Cdd:cd01318  225 RSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIF 304

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491113090 360 KMQSRWEQEAGW----VLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRVF 409
Cdd:cd01318  305 GIKNKGRIAEGYdadlTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTI 358
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 48-408 1.11e-36

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: 136.37  E-value: 1.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  48 WLMPTMVDLCARLREPGQQQH-GTLKSEGKAARENGIL----HLFTPPDSKPIVQDNGAlIHGLVEKAMLDGGIYLEVI- 121
Cdd:cd01302    2 LVLPGFIDIHVHLRDPGGTTYkEDFESGSRAAAAGGVTtvidMPNTGPPPIDLPAIELK-IKLAEESSYVDFSFHAGIGp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 122 GAQTQGLNGKQPANMAGLKKGGCsaVSNANAPFEDDDVVIRTLEYAAGLDMTVVFYAEepqiakdgcvhegfiasrqglp 201
Cdd:cd01302   81 GDVTDELKKLFDAGINSLKVFMN--YYFGELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 202 miptlaetvaIAKYLlmIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRS 281
Cdd:cd01302  137 ----------RAAQL--AEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPPLRS 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 282 EQDKALLRQGVKDGVIDAICTHHEPLNSSAK--MAPFADTLSGFTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAPARVA 359
Cdd:cd01302  205 KEDREALWEGVKNGKIDTIASDHAPHSKEEKesGKDIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIF 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491113090 360 KMQSRWEQEAGW----VLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRV 408
Cdd:cd01302  285 GLYPKGTIAVGYdadlVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 20-406 1.74e-29

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: 118.93  E-value: 1.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  20 RVQTVYLENGKLVAESADI-----SESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLF-TPPDSK 93
Cdd:cd01315   16 READIAVKGGKIAAIGPDIanteaEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIdMPLNSI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  94 PIVQDNGALihgLVEKAMLDGGIYLEVigAQTQGLngkQPANMAGLKK---GGCSAVSNANAPFEDDD---VVIRTLEYA 167
Cdd:cd01315   96 PPTTTVENL---EAKLEAAQGKLHVDV--GFWGGL---VPGNLDQLRPldeAGVVGFKCFLCPSGVDEfpaVDDEQLEEA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 168 ----AGLDMTVVFYAEEPQI---------AKDGCVHEGFIASRqglpmiPTLAETVAIAKYLLMIEATGVRAHFGLLSCG 234
Cdd:cd01315  168 mkelAKTGSVLAVHAENPEItealqeqakAKGKRDYRDYLASR------PVFTEVEAIQRILLLAKETGCRLHIVHLSSA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 235 ASVELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMA 314
Cdd:cd01315  242 EAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTPELKLL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 315 PFADTLS---GFTAfdtyIPFGIQLI-----QEGLFSPLEWVEKVTLAPARVAKMQSRWEQ-----EAGWVLVDPEVEWT 381
Cdd:cd01315  322 GKGDFFKawgGISG----LQLGLPVMlteavNKRGLSLEDIARLMCENPAKLFGLSHQKGRiavgyDADFVVWDPEEEFT 397

                        410       420
                 ....*....|....*....|....*
gi 491113090 382 LNKETIVSQGKNTPLINQVVKGKAV 406
Cdd:cd01315  398 VDAEDLYYKNKISPYVGRTLKGRVH 422
PRK06189 PRK06189
allantoinase; Provisional
 28-406 2.87e-27

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 112.49  E-value: 2.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  28 NGKLVAESADISES----IDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPP-DSKPIVQDNGAL 102
Cdd:PRK06189  27 NGKIAEIAPEISSPareiIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREAL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 103 IHGLV---EKAMLDGGIYleviGAQTQGlNGKQPANMA-----GLKkggcSAVSNANA---PFEDDDVVIRTLEYAAGLD 171
Cdd:PRK06189 107 DAKAElarQKSAVDFALW----GGLVPG-NLEHLRELAeagviGFK----AFMSNSGTdefRSSDDLTLYEGMKEIAALG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 172 MTVVFYAE--------EPQIAKDGCVH-EGFIASRqglpmiPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQ 242
Cdd:PRK06189 178 KILALHAEsdaltrhlTTQARQQGKTDvRDYLESR------PVVAELEAVQRALLYAQETGCPLHFVHISSGKAVALIAE 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 243 AKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKmapfadtlSG 322
Cdd:PRK06189 252 AKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCPPELK--------EG 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 323 FTAFDTY--IPfGIQ-----LIQEGLFS---PLEWVEKVT-LAPARVAKMQSRWEQEAG----WVLVDPEVEWTLNKETI 387
Cdd:PRK06189 324 DDFFLVWggIS-GGQstllvMLTEGYIErgiPLETIARLLaTNPAKRFGLPQKGRLEVGadadFVLVDLDETYTLTKEDL 402

                        410
                 ....*....|....*....
gi 491113090 388 VSQGKNTPLINQVVKGKAV 406
Cdd:PRK06189 403 FYRHKQSPYEGRTFPGRVV 421
PRK02382 PRK02382
dihydroorotase; Provisional
 6-377 7.16e-26

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 108.59  E-value: 7.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   6 IENVRVLDPIQQIDRvqTVYLENGKLVAESADIS-----ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARE 80
Cdd:PRK02382   6 LKDGRVYYNNSLQPR--DVRIDGGKITAVGKDLDgssseEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRSAAA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  81 NGILHLFTPPDSKPIVQDNGALIHGLV---EKAMLDGGIylevigaqtqglNGKQPAN---MAGLKKGGCSA---VSNAN 151
Cdd:PRK02382  84 GGVTTVVDQPNTDPPTVDGESFDEKAElaaRKSIVDFGI------------NGGVTGNwdpLESLWERGVFAlgeIFMAD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 152 APFE---DDDVVIRTLEYAAGLDMTVVFYAE-EPQIAKDGCVHEGFIASRQGLPMIPTLAETVAIAKYLLMIEATGVRAH 227
Cdd:PRK02382 152 STGGmgiDEELFEEALAEAARLGVLATVHAEdEDLFDELAKLLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 228 FGLLSCGASVELIQQAKakglpVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPL 307
Cdd:PRK02382 232 IAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPH 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113090 308 NSSAKMAPFADTLSGFTAFDTYIPFGIQLIQEGLFsPLEWVEKVTLA-PARVAKMQSRWEQEAGW----VLVDPE 377
Cdd:PRK02382 307 TREEKDADIWDAPSGVPGVETMLPLLLAAVRKNRL-PLERVRDVTAAnPARIFGLDGKGRIAEGYdadlVLVDPD 380
PRK07575 PRK07575
dihydroorotase; Provisional
 1-385 2.08e-23

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 101.29  E-value: 2.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   1 MAIVKIENVRVLDPIQQIDrVQTVYLENGKLVAESADISES-----IDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEG 75
Cdd:PRK07575   2 MMSLLIRNARILLPSGELL-LGDVLVEDGKIVAIAPEISATavdtvIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  76 KAARENGILHLFTPPDSKPIVQDNGALIHGL---VEKAMLDGGIYlevIGAQTQGLNGKQPANMA-GLK--KGgcsavSN 149
Cdd:PRK07575  81 RACAKGGVTSFLEMPNTKPLTTTQAALDDKLaraAEKCVVNYGFF---IGATPDNLPELLTANPTcGIKifMG-----SS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 150 ANAPFEDDDVVIRTLeYAAGLDMTVVFYAEEPQIAK---------DGCVHE-------GFIASRQGLpmipTLAEtvaia 213
Cdd:PRK07575 153 HGPLLVDEEAALERI-FAEGTRLIAVHAEDQARIRArraefagisDPADHSqiqdeeaALLATRLAL----KLSK----- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 214 KYLLmieatgvRAHFGLLSCGASVELIQQAKakGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVK 293
Cdd:PRK07575 223 KYQR-------RLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALR 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 294 DGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAPARVAKMQSRWEQEAGW-- 371
Cdd:PRK07575 294 DGVIDFIATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGIPNKGRIAPGYda 373

                        410
                 ....*....|....*.
gi 491113090 372 --VLVDPEVEWTLNKE 385
Cdd:PRK07575 374 dlVLVDLNTYRPVRRE 389
PRK04250 PRK04250
dihydroorotase; Provisional
 26-409 4.96e-22

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 96.76  E-value: 4.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  26 LENGKLVAESA-DIS--ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVQDNGAL 102
Cdd:PRK04250  19 IENGRISKISLrDLKgkEVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTY 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 103 ihgLVEKAMLDGGIYLE-VIGAQTQGLNGKQPANMAGLKKGGCSAVSNA--NAPFEDDdvvirtleYAAGLDMTVVfYAE 179
Cdd:PRK04250  99 ---EKRMRIAEKKSYADyALNFLIAGNCEKAEEIKADFYKIFMGASTGGifSENFEVD--------YACAPGIVSV-HAE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 180 EPQIAKDgcvhegfiasrqgLPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQakaKGLP-VTCDVAMHQ 258
Cdd:PRK04250 167 DPELIRE-------------FPERPPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILK---SNLPwVSFEVTPHH 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 259 LHLTDQIIDgFNSLAHVRPPLRSEQD-KALLRQGVKdgvIDAICTHHEPLNSSAKMApfadTLSGFTAFDTYIPFGIQLI 337
Cdd:PRK04250 231 LFLTRKDYE-RNPLLKVYPPLRSEEDrKALWENFSK---IPIIASDHAPHTLEDKEA----GAAGIPGLETEVPLLLDAA 302

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113090 338 QEGLFSPLEWVEKVTLAPARVAKMQSR-WE--QEAGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRVF 409
Cdd:PRK04250 303 NKGMISLFDIVEKMHDNPARIFGIKNYgIEegNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTI 377
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 50-408 4.77e-18

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: 84.81  E-value: 4.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  50 MPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVQDNGALihGLVEKAMLDGGI--YLEVIGAQTQg 127
Cdd:cd01316    5 LPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASL--KLVQSLAQAKARcdYAFSIGATST- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 128 lNGKQPANMAGlkkggcSAVSNANAPFEDDDVVIRTleyaaglDMTVVfyaeepqiakdgcvHEGFIASRQGLPMIpTLA 207
Cdd:cd01316   82 -NAATVGELAS------EAVGLKFYLNETFSTLILD-------KITAW--------------ASHFNAWPSTKPIV-THA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 208 ETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCDVAMHQLHLTDQiiDGFNSLAHVRPPLRSEQDKAL 287
Cdd:cd01316  133 KSQTLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQD--DLPRGQYEVRPFLPTREDQEA 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 288 LRQGVKdgVIDAICTHHEPLNSSAKMApfADTLSGFTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAPARVAKMQsrwEQ 367
Cdd:cd01316  211 LWENLD--YIDCFATDHAPHTLAEKTG--NKPPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLP---PQ 283

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 491113090 368 EAGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRV 408
Cdd:cd01316  284 SDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRV 324
PRK09236 PRK09236
dihydroorotase; Reviewed
 1-409 5.69e-17

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 82.23  E-value: 5.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090   1 MAIVKIENVRVLDPIQQIDrvQTVYLENGKLVAESADIS-----ESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEG 75
Cdd:PRK09236   1 MKRILIKNARIVNEGKIFE--GDVLIENGRIAKIASSISaksadTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  76 KAARENGILHLFTPPDSKP--IVQDNgalihgLVEK-------AMLDGGIYLeviGA------QTQGLNgkqPANMAGLK 140
Cdd:PRK09236  79 RAAVAGGITSFMEMPNTNPptTTLEA------LEAKyqiaaqrSLANYSFYF---GAtndnldEIKRLD---PKRVCGVK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 141 -----KGGCSAVSN--------ANAPF------EDDDVVIRTLE-----YAAGLDMtvvfyAEEPQI-AKDGCvhegFIA 195
Cdd:PRK09236 147 vfmgaSTGNMLVDNpetlerifRDAPTliathcEDTPTIKANLAkykekYGDDIPA-----EMHPLIrSAEAC----YKS 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 196 SRqglpmiptLAetVAIAKyllmieATGVRAHFGLLSCGASVELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHV 275
Cdd:PRK09236 218 SS--------LA--VSLAK------KHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKC 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 276 RPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAP 355
Cdd:PRK09236 282 NPAIKTASDREALRQALADDRIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAP 361

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113090 356 ARVAKMQSR-------WeqeAGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRVF 409
Cdd:PRK09236 362 AILFDIKERgfiregyW---ADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTF 419
PRK08044 PRK08044
allantoinase AllB;
20-306 4.41e-15

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 76.43  E-value: 4.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  20 RVQTVYLENGKLVAESADISES---IDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPP-DSKPI 95
Cdd:PRK08044  19 RVVDIAVKGGKIAAIGQDLGDAkevMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  96 VQDNGALihglvEKAMLDGGIYLEVIGAQTQGLNGKQPANMAGLKKGG-----CSAVSNANAPFEDD--DV----VIRTL 164
Cdd:PRK08044  99 TVDRASI-----ELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGvvgfkCFVATCGDRGIDNDfrDVndwqFYKGA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 165 EYAAGLDMTVVFYAEEPQIakdgCVHEGFIASRQG-------LPMIPTLAETVAIAKYLLMIEATGVRAHFGLLSCGASV 237
Cdd:PRK08044 174 QKLGELGQPVLVHCENALI----CDELGEEAKREGrvtahdyVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGV 249

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113090 238 ELIQQAKAKGLPVTCDVAMHQLHLTDQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEP 306
Cdd:PRK08044 250 EEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSP 318
PRK09060 PRK09060
dihydroorotase; Validated
 29-406 1.17e-14

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 75.34  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  29 GKLVAESADisESIDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPI------VQDNGAL 102
Cdd:PRK09060  36 GDLSGASAG--EVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNPLtttaeaLADKLAR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 103 IHGlveKAMLDGGIYlevIGAQTQglngkQPANMAGLKK-GGCSAV------SNANAPFEDDDVVIRTLeyaAGLDMTVV 175
Cdd:PRK09060 114 ARH---RMHCDFAFY---VGGTRD-----NADELAELERlPGCAGIkvfmgsSTGDLLVEDDEGLRRIL---RNGRRRAA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 176 FYAEEpqiakdgcvhEGFIASRQGL--PMIPTL------AETVAIAKYLLMIEA--TGVRAHFGLLSCGASVELIQQAKA 245
Cdd:PRK09060 180 FHSED----------EYRLRERKGLrvEGDPSShpvwrdEEAALLATRRLVRLAreTGRRIHVLHVSTAEEIDFLADHKD 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 246 KglpVTCDVAMHqlHLT---DQIIDGFNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLSG 322
Cdd:PRK09060 250 V---ATVEVTPH--HLTlaaPECYERLGTLAQMNPPIRDARHRDGLWRGVRQGVVDVLGSDHAPHTLEEKAKPYPASPSG 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 323 FTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAPARVAKMQSRWEQEAGW----VLVDPEVEWTLNKETIVSQGKNTPLIN 398
Cdd:PRK09060 325 MTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAGKGRIAVGYdadfTIVDLKRRETITNEWIASRCGWTPYDG 404


                 ....*...
gi 491113090 399 QVVKGKAV 406
Cdd:PRK09060 405 KEVTGWPV 412
PLN02795 PLN02795
allantoinase
 20-409 1.68e-12

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 68.65  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  20 RVQTVYLENGKLVA----ESADISES----IDAQGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLF-TPP 90
Cdd:PLN02795  60 IPGAVEVEGGRIVSvtkeEEAPKSQKkphvLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVdMPL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  91 DSKPIVQDNGAL---IHGLVEKAMLDGGIYLEVIgAQTQG----LNGKQPANMAGLKKGGCSAVSNaNAPFEDDDVVIRT 163
Cdd:PLN02795 140 NSFPSTTSVETLelkIEAAKGKLYVDVGFWGGLV-PENAHnasvLEELLDAGALGLKSFMCPSGIN-DFPMTTATHIKAA 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 164 LEYAAGLDMTVVFYAE-------EPQIAKDGCVHEGFIASRqglpmiPTLAETVAIAKYLLMIE-------ATGVRAHFG 229
Cdd:PLN02795 218 LPVLAKYGRPLLVHAEvvspvesDSRLDADPRSYSTYLKSR------PPSWEQEAIRQLLEVAKdtrpggvAEGAHVHIV 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 230 LLS-CGASVELIQQAKAKGLPVTCDVAMHQLHLT-DQIIDGfNSLAHVRPPLRSEQDKALLRQGVKDGVIDAICTHHEPL 307
Cdd:PLN02795 292 HLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSaEEIPDG-DTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPS 370

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 308 NSSAKM---APFADTLSGFTAFDTYIP--------FGIQLIQEGLFspleWVEkvtlAPARVAKMQSRWEQEAGW----V 372
Cdd:PLN02795 371 PPDLKLleeGNFLRAWGGISSLQFVLPatwtagraYGLTLEQLARW----WSE----RPAKLAGLDSKGAIAPGKdadiV 442

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 491113090 373 LVDPEVEWTLNKE-TIVSQGKN-TPLINQVVKGKAVRVF 409
Cdd:PLN02795 443 VWDPEAEFVLDESyPIYHKHKSlSPYLGTKLSGKVIATF 481
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 156-386 4.72e-11

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: 64.16  E-value: 4.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 156 DDDVVIRTLEYAAGLDMTVVFYAEEPQIAKDGC---VHEGFIA------SRqglpmiPTLAETVAIAKYLLMIEATGVRA 226
Cdd:cd01314  160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQkklLAQGKTGpeyhalSR------PPEVEAEATARAIRLAELAGAPL 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 227 HFGLLSCGASVELIQQAKAKGLPV---TCdvaMHQLHLTDQII--DGFNSLAHV-RPPLRSEQDKALLRQGVKDGVIDAI 300
Cdd:cd01314  234 YIVHVSSKEAADEIARARKKGLPVygeTC---PQYLLLDDSDYwkDWFEGAKYVcSPPLRPKEDQEALWDGLSSGTLQTV 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 301 CTHHEPLNSSAKMApfadtlsGFTAFdTYIPFGI------------QLIQEGLFSPLEWVEKVTLAPARVAKMqsrWEQ- 367
Cdd:cd01314  311 GSDHCPFNFAQKAR-------GKDDF-TKIPNGVpgvetrmpllwsEGVAKGRITLEKFVELTSTNPAKIFGL---YPRk 379

                        250       260
                 ....*....|....*....|....*.
gi 491113090 368 -------EAGWVLVDPEVEWTLNKET 386
Cdd:cd01314  380 gtiavgsDADLVIWDPNAEKTISADT 405
pyrC PRK00369
dihydroorotase; Provisional
 45-409 1.27e-09

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 59.39  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  45 QGQWLMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVQDNGALIHGLVE---KAMLDGGIYLEVi 121
Cdd:PRK00369  41 QGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAEleyYSRVDYFVYSGV- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 122 gaqtqglnGKQPANMAGLKKGGCSAvsnanapFEDDDVVIRTLEYAAGLDMTVVFYAEEPQIAKdgcvhegfiaSRQGLp 201
Cdd:PRK00369 120 --------TKDPEKVDKLPIAGYKI-------FPEDLEREETFRVLLKSRKLKILHPEVPLALK----------SNRKL- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 202 MIPTLAETVAIakYLLMIEAtgvRAHFGLLSCGASVELiqqakAKGLPVTCDVAMHQLhltdqIIDGF-NSLAHVRPPLR 280
Cdd:PRK00369 174 RRNCWYEIAAL--YYVKDYQ---NVHITHASNPRTVRL-----AKELGFTVDITPHHL-----LVNGEkDCLTKVNPPIR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 281 SEQDKALLRQGVKDgvIDAICTHHEPLNSSAKMAPFADTLSGFTAFDTYIPFGIQLIQEGLFSPLEWVEKVTLAPARVAK 360
Cdd:PRK00369 239 DINERLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILG 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491113090 361 MQSRWEQE---AGWVLVDPEvEWTLNkeTIVSQGKNTPLINQVVKGKAVRVF 409
Cdd:PRK00369 317 IPYGEIKEgyrANFTVIQFE-DWRYS--TKYSKVIETPLDGFELKASVYATI 365
PRK01211 PRK01211
dihydroorotase; Provisional
 49-341 2.44e-05

dihydroorotase; Provisional


Pssm-ID: 179247 [Multi-domain]  Cd Length: 409  Bit Score: 46.00  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  49 LMPTMVDLCARLREPGQQQHGTLKSEGKAARENGILHLFTPPDSKPIVQDNGALIHGL---VEKAMLDGGIYLEVIGAQT 125
Cdd:PRK01211  44 ILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLgrvAPKAYVDFSLYSMETGNNA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 126 QGLNGKQPanmaGLK--KGGCSAVSNANAPFEDddvvIRTLEyaaGLDMTVVFYAEEPQiakdgCVHEGFIAS---RQGL 200
Cdd:PRK01211 124 LILDERSI----GLKvyMGGTTNTNGTDIEGGE----IKKIN---EANIPVFFHAELSE-----CLRKHQFESknlRDHD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 201 PMIPTLAETVAIAKYLLMIEATGVRAHFgllscgASVELIQQakakglpVTCDVAMHQLHLTDQIIDGfnSLAHVRPPLR 280
Cdd:PRK01211 188 LARPIECEIKAVKYVKNLDLKTKIIAHV------SSIDVIGR-------FLREVTPHHLLLNDDMPLG--SYGKVNPPLR 252

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113090 281 SEQDKALLRQGVKDGVIDAICTHHEPlNSSAKMAPFADTLSGFTAFDTYIPFGIQLIQEGL 341
Cdd:PRK01211 253 DRWTQERLLEEYISGRFDILSSDHAP-HTEEDKQEFEYAKSGIIGVETRVPLFLALVKKKI 312
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 204-408 5.56e-05

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 45.07  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 204 PTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELIQQAKAKGLPVTCDVAMHQLHLT--DQIIDGFNSLAHV-RPPLR 280
Cdd:PRK13404 215 PMLAEREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTaeDLDRPGMEGAKYIcSPPPR 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 281 SEQDKALLRQGVKDGVIDAICTHHEPLN---SSAKMAPFADtlsgfTAFDtYIPFGIQ--------LIQEGL----FSPL 345
Cdd:PRK13404 295 DKANQEAIWNGLADGTFEVFSSDHAPFRfddTDGKLAAGAN-----PSFK-AIANGIPgietrlplLFSEGVvkgrISLN 368

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491113090 346 EWVEKVTLAPARVAKMQSRWEQ-----EAGWVLVDPEVEWTLNKETIVSQGKNTPLINQVVKGKAVRV 408
Cdd:PRK13404 369 RFVALTSTNPAKLYGLYPRKGAiaigaDADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTV 436
PLN02942 PLN02942
dihydropyrimidinase
 24-386 6.49e-05

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 44.83  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  24 VYLENGKLVAESADISES-----IDAQGQWLMPTMVDLCARLREP--GQQQHGTLKSEGKAARENGI-LHL-FTPPDskp 94
Cdd:PLN02942  25 VYVEDGIIVAVAPNLKVPddvrvIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTtMHIdFVIPV--- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  95 ivqdNGALIHGL------VEKAMLDGGIYLEVigaqtQGLNGKQPANMAGL-KKGGCSA----VSNANAPFEDDDVVIRT 163
Cdd:PLN02942 102 ----NGNLLAGYeayekkAEKSCMDYGFHMAI-----TKWDDTVSRDMETLvKEKGINSfkffMAYKGSLMVTDELLLEG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 164 LEYAAGLDMTVVFYAEEPQIAKDGC--VHEGFIASRQGLPMI-PTLAETVAIAKYLLMIEATGVRAHFGLLSCGASVELI 240
Cdd:PLN02942 173 FKRCKSLGALAMVHAENGDAVFEGQkrMIELGITGPEGHALSrPPLLEGEATARAIRLAKFVNTPLYVVHVMSIDAMEEI 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 241 QQAKAKGLPVTCDVAMHQLHLTDQII--DGFNSLAH--VRPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPF 316
Cdd:PLN02942 253 ARARKSGQRVIGEPVVSGLVLDDSKLwdPDFTIASKyvMSPPIRPAGHGKALQAALSSGILQLVGTDHCPFNSTQKAFGK 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090 317 ADtlsgFTAfdtyIPFGIQLIQE------------GLFSPLEWVEKVTLAPARVAKMQSR-----WEQEAGWVLVDPEVE 379
Cdd:PLN02942 333 DD----FRK----IPNGVNGIEErmhlvwdtmvesGQISPTDYVRVTSTECAKIFNIYPRkgailAGSDADIIILNPNST 404


                 ....*..
gi 491113090 380 WTLNKET 386
Cdd:PLN02942 405 FTISAKT 411
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
6-56 1.15e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 44.07  E-value: 1.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491113090   6 IENVRVLDPIQQIDRVQTVYLENGKLVAESADISES-----IDAQGQWLMPTMVDL 56
Cdd:PRK09237   3 LRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSqakkvIDLSGLYVSPGWIDL 58
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 6-56 4.63e-04

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 42.09  E-value: 4.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491113090   6 IENVRVLDPiqqiDRVQ--TVYLENGKLVA---ESADISESIDAQGQWLMPTMVDL 56
Cdd:PRK15446   6 LSNARLVLP----DEVVdgSLLIEDGRIAAidpGASALPGAIDAEGDYLLPGLVDL 57
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 109-406 1.58e-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: 40.18  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  109 KAMLDGGI--YLEVIGAQTQGLNG------KQPANMAGLKKGGCSAVSNANAPFEDDDVVIRTLEYAAGLDMTVVFYAE- 179
Cdd:pfam01979  37 TTMLKSGTttVLDMGATTSTGIEAlleaaeELPLGLRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGl 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  180 ---EPQIAKDGCVHEGF-IASRQGLPMIPTLAETVAIAKYllMIEATGVRA----HFGLLSCGASVELIQQAKAKGLPVT 251
Cdd:pfam01979 117 aphGAPTFSDDELKAALeEAKKYGLPVAIHALETKGEVED--AIAAFGGGIehgtHLEVAESGGLLDIIKLILAHGVHLS 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  252 cdvaMHQLHLTDQIIDGfNSLAHV-RPPLRSEQDKALLRQGVKDGVIDAICTHHEPLNSSAKMAPFADTLsgftafdtyi 330
Cdd:pfam01979 195 ----PTEANLLAEHLKG-AGVAHCpFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLA---------- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113090  331 pFGIQLIQEGLFSPLEWVEKVTLAPARVAKMQSRWEQ-EAGW----VLVDpevewTLNKETIVSQGKNTPLINQVVKGKA 405
Cdd:pfam01979 260 -LELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSiEVGKdadlVVVD-----LDPLAAFFGLKPDGNVKKVIVKGKI 333


                  .
gi 491113090  406 V 406
Cdd:pfam01979 334 V 334
 
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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