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Conserved domains on  [gi|1208968218|ref|WP_088230159|]
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MULTISPECIES: dihydroorotase [Bacillus]

Protein Classification

dihydroorotase( domain architecture ID 10793206)

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

EC:  3.5.2.3
Gene Ontology:  GO:0004151|GO:0006221|GO:0046872
PubMed:  12626710|9144792
SCOP:  4002199|4002171

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pyrC PRK09357
dihydroorotase; Validated
1-423 0e+00

dihydroorotase; Validated


:

Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 694.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   1 MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAA 80
Cdd:PRK09357    1 MMILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  81 AKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASM 160
Cdd:PRK09357   81 AAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQDARL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 161 MLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRV 240
Cdd:PRK09357  161 MRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 241 IRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERA 320
Cdd:PRK09357  241 IRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 321 PFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTP 400
Cdd:PRK09357  321 PFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTP 400
                         410       420
                  ....*....|....*....|...
gi 1208968218 401 FAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK09357  401 FIGMKLKGKVVYTIVDGKIVYQD 423
 
Name Accession Description Interval E-value
pyrC PRK09357
dihydroorotase; Validated
1-423 0e+00

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 694.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   1 MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAA 80
Cdd:PRK09357    1 MMILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  81 AKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASM 160
Cdd:PRK09357   81 AAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQDARL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 161 MLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRV 240
Cdd:PRK09357  161 MRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 241 IRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERA 320
Cdd:PRK09357  241 IRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 321 PFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTP 400
Cdd:PRK09357  321 PFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTP 400
                         410       420
                  ....*....|....*....|...
gi 1208968218 401 FAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK09357  401 FIGMKLKGKVVYTIVDGKIVYQD 423
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
4-422 0e+00

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: 605.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAK 82
Cdd:COG0044     1 LIKNGRVVDPGGLERA-DVLIEDGRIAAIGPDLAApEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  83 GGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQaGSEMTDFETLKELGAFAF-----TDDGVGVQD 157
Cdd:COG0044    80 GGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGNPVLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 158 ASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGS 237
Cdd:COG0044   159 DGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 238 VRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGI 317
Cdd:COG0044   239 VELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELPF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 318 ERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLE-AGRLKEGRTADITIIDLEQEEEIDPTTFLSKG 396
Cdd:COG0044   319 AEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLPrKGRIAVGADADLVLFDPDAEWTVTAEDLHSKS 398
                         410       420
                  ....*....|....*....|....*.
gi 1208968218 397 KNTPFAGWKCQGWPVMTIVGGKIAWQ 422
Cdd:COG0044   399 KNTPFEGRELTGRVVATIVRGRVVYE 424
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
40-413 0e+00

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: 514.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  40 NAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNV 119
Cdd:cd01317     1 DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 120 LPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKH 199
Cdd:cd01317    81 LPIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 200 GLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPP 279
Cdd:cd01317   161 GLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 280 LRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPAD 359
Cdd:cd01317   241 LRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAK 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1208968218 360 TFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMT 413
Cdd:cd01317   321 ILGLPPGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
15-420 7.77e-179

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: 505.05  E-value: 7.77e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  15 GKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNT 94
Cdd:TIGR00857   1 GKETEVDILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  95 RPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFA--FTDDGVGVQDASMMLAAMKRAAKLN 172
Cdd:TIGR00857  81 KPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGrmFTDDGSEVQDILSMRRALEYAAIAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 173 MAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVT 252
Cdd:TIGR00857 161 VPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKIT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 253 AEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFP 332
Cdd:TIGR00857 241 AEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 333 LLYtNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPV 411
Cdd:TIGR00857 321 LLL-QLLVKGLISLKDLIRMLSINPARIFGLpDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPI 399

                  ....*....
gi 1208968218 412 MTIVGGKIA 420
Cdd:TIGR00857 400 ATILRGKVV 408
DHOase pfam12890
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various ...
48-237 6.56e-37

Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various bacteria.


Pssm-ID: 315550 [Multi-domain]  Cd Length: 142  Bit Score: 131.53  E-value: 6.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  48 GKLIAPGLVDVHVHLREPGGEHKETIETgtlaaakggftTICAMPNTRPVPdcrehmedlqkriqekahvnvlpyGAITV 127
Cdd:pfam12890   1 GRLIVPGLAFLHVHLTAPSGEAQELKET-----------TWAAYGVTFKAP------------------------AGITV 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 128 RQAGSEmtdfetlkelgAFAFTDDGVGVQDASMMLAAMKRAAkLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNgIPSV 207
Cdd:pfam12890  46 EDDSEE-----------GFIFTNDTYYITIQLLEGEGMKKSE-LDQELKAIATDDEVTNQSAVQDFELPQFYGTQ-LKGN 112
                         170       180       190
                  ....*....|....*....|....*....|
gi 1208968218 208 CESVHIARDILLAEAADCHYHVCHVSTKGS 237
Cdd:pfam12890 113 CETEHCVYSYLLAKAAGCGFYVSIIYTKEN 142
 
Name Accession Description Interval E-value
pyrC PRK09357
dihydroorotase; Validated
1-423 0e+00

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 694.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   1 MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAA 80
Cdd:PRK09357    1 MMILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  81 AKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASM 160
Cdd:PRK09357   81 AAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQDARL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 161 MLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRV 240
Cdd:PRK09357  161 MRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 241 IRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERA 320
Cdd:PRK09357  241 IRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 321 PFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTP 400
Cdd:PRK09357  321 PFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTP 400
                         410       420
                  ....*....|....*....|...
gi 1208968218 401 FAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK09357  401 FIGMKLKGKVVYTIVDGKIVYQD 423
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
4-422 0e+00

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: 605.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAK 82
Cdd:COG0044     1 LIKNGRVVDPGGLERA-DVLIEDGRIAAIGPDLAApEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  83 GGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQaGSEMTDFETLKELGAFAF-----TDDGVGVQD 157
Cdd:COG0044    80 GGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGNPVLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 158 ASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGS 237
Cdd:COG0044   159 DGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 238 VRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGI 317
Cdd:COG0044   239 VELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELPF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 318 ERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLE-AGRLKEGRTADITIIDLEQEEEIDPTTFLSKG 396
Cdd:COG0044   319 AEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLPrKGRIAVGADADLVLFDPDAEWTVTAEDLHSKS 398
                         410       420
                  ....*....|....*....|....*.
gi 1208968218 397 KNTPFAGWKCQGWPVMTIVGGKIAWQ 422
Cdd:COG0044   399 KNTPFEGRELTGRVVATIVRGRVVYE 424
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
40-413 0e+00

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: 514.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  40 NAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNV 119
Cdd:cd01317     1 DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 120 LPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKH 199
Cdd:cd01317    81 LPIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 200 GLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPP 279
Cdd:cd01317   161 GLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 280 LRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPAD 359
Cdd:cd01317   241 LRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAK 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1208968218 360 TFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMT 413
Cdd:cd01317   321 ILGLPPGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
15-420 7.77e-179

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: 505.05  E-value: 7.77e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  15 GKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNT 94
Cdd:TIGR00857   1 GKETEVDILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  95 RPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFA--FTDDGVGVQDASMMLAAMKRAAKLN 172
Cdd:TIGR00857  81 KPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGrmFTDDGSEVQDILSMRRALEYAAIAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 173 MAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVT 252
Cdd:TIGR00857 161 VPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKIT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 253 AEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFP 332
Cdd:TIGR00857 241 AEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 333 LLYtNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPV 411
Cdd:TIGR00857 321 LLL-QLLVKGLISLKDLIRMLSINPARIFGLpDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPI 399

                  ....*....
gi 1208968218 412 MTIVGGKIA 420
Cdd:TIGR00857 400 ATILRGKVV 408
PRK09059 PRK09059
dihydroorotase; Validated
21-418 1.06e-110

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 332.38  E-value: 1.06e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  21 DLLVQDGKIAKVAENITA----DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRP 96
Cdd:PRK09059   24 TVLIEDGVIVAAGKGAGNqgapEGAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  97 VPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVV 176
Cdd:PRK09059  104 VIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLLRAAGAVAFTDGRRSVANTQVMRRALTYARDFDAVIV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 177 AHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVT 256
Cdd:PRK09059  184 HETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVS 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 257 PHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKaqgieRAPF-----GITGFETAF 331
Cdd:PRK09059  264 INHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTK-----RLPFseaaaGAIGLETLL 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 332 PLLYtNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPV 411
Cdd:PRK09059  339 AAAL-RLYHNGEVPLLRLIEALSTRPAEIFGLPAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVV 417

                  ....*..
gi 1208968218 412 MTIVGGK 418
Cdd:PRK09059  418 RTIVAGK 424
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
48-417 2.34e-105

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: 316.20  E-value: 2.34e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  48 GKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITv 127
Cdd:cd01318     1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVT- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 128 rqagsemtDFETLKELGAFA------FTDDGVGvqDASMMLAAMKRAAKLNMAVVA-HCEENTLINKgcvHEGKFSEKHG 200
Cdd:cd01318    80 --------GSEDLEELDKAPpagykiFMGDSTG--DLLDDEETLERIFAEGSVLVTfHAEDEDRLRE---NRKELKGESA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 201 LNGIPS-VCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKragIKVTAEVTPHHLVLCEDDIPSADPNFKMNPP 279
Cdd:cd01318   147 HPRIRDaEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAK---PGVTVEVTPHHLFLDVEDYDRLGTLGKVNPP 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 280 LRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLyTNLVKKGIITLEQLIQFLTEKPAD 359
Cdd:cd01318   224 LRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLM-LTLVNKGILSLSRVVRLTSHNPAR 302
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968218 360 TFGLE-AGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGG 417
Cdd:cd01318   303 IFGIKnKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
PRK02382 PRK02382
dihydroorotase; Provisional
1-425 4.57e-99

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 303.11  E-value: 4.57e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   1 MNYLFKNGRyMNEEGKIVATDLLVQDGKIAKVAENITADNAE-VIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA 79
Cdd:PRK02382    2 RDALLKDGR-VYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEeVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  80 AAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITvrqagSEMTDFETLKELGAFAF-------TDDG 152
Cdd:PRK02382   81 AAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVT-----GNWDPLESLWERGVFALgeifmadSTGG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 153 VGVqDASMMLAAMKRAAKLNMAVVAHCEENTLINkgcvhEGKFSEKHGLNG------IPSVCESVHIARDILLAEAADCH 226
Cdd:PRK02382  156 MGI-DEELFEEALAEAARLGVLATVHAEDEDLFD-----ELAKLLKGDADAdawsayRPAAAEAAAVERALEVASETGAR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 227 YHVCHVSTKGSVRVIRDAKragikVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHA 306
Cdd:PRK02382  230 IHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 307 PHTAEEKAQGIERAPFGITGFETAFPLLYTNlVKKGIITLEQLIQFLTEKPADTFGLEA-GRLKEGRTADITIIDLEQEE 385
Cdd:PRK02382  305 PHTREEKDADIWDAPSGVPGVETMLPLLLAA-VRKNRLPLERVRDVTAANPARIFGLDGkGRIAEGYDADLVLVDPDAAR 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1208968218 386 EIDPTTFLSKGKNTPFAGWKCQgWPVMTIVGGKIAWQKES 425
Cdd:PRK02382  384 EIRGDDLHSKAGWTPFEGMEGV-FPELTMVRGTVVWDGDD 422
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
2-428 1.32e-94

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: 291.50  E-value: 1.32e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   2 NYLFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENIT-ADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAA 80
Cdd:cd01315     1 DLVIKNGRVVTPDGVREA-DIAVKGGKIAAIGPDIAnTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  81 AKGGFTTICAMP-NTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAgsemTDFETLKELGAFAF--------TDD 151
Cdd:cd01315    80 AAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNL----DQLRPLDEAGVVGFkcflcpsgVDE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 152 GVGVQDASMMLAaMKRAAKLNMAVVAHCEeNTLINKGCVHEGKFSEKHG----LNGIPSVCESVHIARDILLAEAADCHY 227
Cdd:cd01315   156 FPAVDDEQLEEA-MKELAKTGSVLAVHAE-NPEITEALQEQAKAKGKRDyrdyLASRPVFTEVEAIQRILLLAKETGCRL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 228 HVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAP 307
Cdd:cd01315   234 HIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 308 HTAEEKAQGIE---RAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEA--GRLKEGRTADITIIDLE 382
Cdd:cd01315   314 CTPELKLLGKGdffKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHqkGRIAVGYDADFVVWDPE 393
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1208968218 383 QEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKESALV 428
Cdd:cd01315   394 EEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVG 439
PRK07369 PRK07369
dihydroorotase; Provisional
20-408 2.95e-91

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 281.87  E-value: 2.95e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  20 TDLLVQDGKIAKVAENI--TADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPV 97
Cdd:PRK07369   22 ADVLIEDGKIQAIEPHIdpIPPDTQIIDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  98 PDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDdGVGVQDASMMLAAMKRAAKLNMAVVA 177
Cdd:PRK07369  102 LDNPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAAAGVVGFTD-GQPLENLALLRRLLEYLKPLGKPVAL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 178 HCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTP 257
Cdd:PRK07369  181 WPCDRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTW 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 258 HHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTN 337
Cdd:PRK07369  261 MHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVAFAEAPPGAIGLELALPLLWQN 340
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208968218 338 LVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQG 408
Cdd:PRK07369  341 LVETGELSALQLWQALSTNPARCLGQEPPSLAPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
49-413 3.16e-91

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: 279.28  E-value: 3.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  49 KLIAPGLVDVHVHLREPG-GEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITV 127
Cdd:cd01302     1 LLVLPGFIDIHVHLRDPGgTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 128 RQAGSEMT-----DFETLKELGAFAFTDDgVGVQDASMMLAAMKrAAKLNMAVVAHCEentlinkgcvhegkfsekhgln 202
Cdd:cd01302    81 GDVTDELKklfdaGINSLKVFMNYYFGEL-FDVDDGTLMRTFLE-IASRGGPVMVHAE---------------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 203 gipsvcesvhiaRDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRG 282
Cdd:cd01302   137 ------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPPLRS 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 283 KEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQG--IERAPFGITGFETAFPLLYTNLVKKGIItLEQLIQFLTEKPADT 360
Cdd:cd01302   205 KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGkdIWKAPPGFPGLETRLPILLTEGVKRGLS-LETLVEILSENPARI 283
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1208968218 361 FGLEA-GRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMT 413
Cdd:cd01302   284 FGLYPkGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
PRK07627 PRK07627
dihydroorotase; Provisional
1-422 1.98e-89

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 277.71  E-value: 1.98e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   1 MNYLFKNGRYMNEEGKIVAT-DLLVQDGKIA---KVAENITADNaeVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETG 76
Cdd:PRK07627    1 MKIHIKGGRLIDPAAGTDRQaDLYVAAGKIAaigQAPAGFNADK--TIDASGLIVCPGLVDLSARLREPGYEYKATLESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  77 TLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQ 156
Cdd:PRK07627   79 MAAAVAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFSQANVPVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 157 DASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKG 236
Cdd:PRK07627  159 DTQVLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSSAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 237 SVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQG 316
Cdd:PRK07627  239 GVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLP 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 317 IERAPFGITGFETAFPLLYTNLVKKGiITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKG 396
Cdd:PRK07627  319 FAEATPGATGLELLLPLTLKWADEAK-VPLARALARITSAPARVLGLPAGRLAEGAPADLCVFDPDAHWRVEPRALKSQG 397
                         410       420
                  ....*....|....*....|....*.
gi 1208968218 397 KNTPFAGWKCQGWPVMTIVGGKIAWQ 422
Cdd:PRK07627  398 KNTPFLGYELPGRVRATLVAGQVAFE 423
PRK07575 PRK07575
dihydroorotase; Provisional
1-423 4.21e-89

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 277.33  E-value: 4.21e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   1 MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA 79
Cdd:PRK07575    3 MSLLIRNARILLPSGELLLGDVLVEDGKIVAIAPEISAtAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  80 AAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNvlpYGAITVRQAgsemtdfETLKELGAFAFTDdGVGVQDAS 159
Cdd:PRK07575   83 CAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVN---YGFFIGATP-------DNLPELLTANPTC-GIKIFMGS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 160 M---ML----AAMKRA-AKLNMAVVAHCEENTLINkgcvhegkfSEKHGLNGIPSVC--------ESVHIA--RDILLAE 221
Cdd:PRK07575  152 ShgpLLvdeeAALERIfAEGTRLIAVHAEDQARIR---------ARRAEFAGISDPAdhsqiqdeEAALLAtrLALKLSK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 222 AADCHYHVCHVSTKGSVRVIRDAKRAgiKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMI 301
Cdd:PRK07575  223 KYQRRLHILHLSTAIEAELLRQDKPS--WVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFI 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 302 ATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVkKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIID 380
Cdd:PRK07575  301 ATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGIpNKGRIAPGYDADLVLVD 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1208968218 381 LEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK07575  380 LNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDR 422
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
4-421 1.68e-87

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: 273.32  E-value: 1.68e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIvATDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREP--GGEHKETIETGTLAA 80
Cdd:cd01314     2 IIKNGTIVTADGSF-KADILIEDGKIVAIGPNLEApGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  81 AKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAhvnVLPYG---AIT--VRQAGSEMtdfETLKELGAFAF----TDD 151
Cdd:cd01314    81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKS---VIDYGfhmIITdwTDSVIEEL---PELVKKGISSFkvfmAYK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 152 GVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGC---VHEGKFS-EKHGLNGiPSVCESVHIARDILLAEAADCHY 227
Cdd:cd01314   155 GLLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQkklLAQGKTGpEYHALSR-PPEVEAEATARAIRLAELAGAPL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 228 HVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDI--PSADPN-FKMNPPLRGKEDHAALIEGLLDGTIDMIATD 304
Cdd:cd01314   234 YIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYwkDWFEGAkYVCSPPLRPKEDQEALWDGLSSGTLQTVGSD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 305 HAPHTAEEKAQGIE---RAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL--EAGRLKEGRTADITII 379
Cdd:cd01314   314 HCPFNFAQKARGKDdftKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLypRKGTIAVGSDADLVIW 393
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1208968218 380 DLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAW 421
Cdd:cd01314   394 DPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVV 435
allantoinase TIGR03178
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ...
4-424 1.26e-84

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: 265.79  E-value: 1.26e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKG 83
Cdd:TIGR03178   3 IIRGGRVILPNGEREA-DVGVKGGKIAAIGPDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  84 GFTTICAMP-NTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQagseMTDFETLKELGAFAF--------TDDGVG 154
Cdd:TIGR03178  82 GITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYN----LDDLRELDEAGVVGFkaflspsgDDEFPH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 155 VqDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVH---EGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCH 231
Cdd:TIGR03178 158 V-DDWQLYKGMRELARLGQLLLVHAENPAITSALGEEappQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVH 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 232 VSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAE 311
Cdd:TIGR03178 237 LSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPD 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 312 EKAQG-IERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEEEIDP 389
Cdd:TIGR03178 317 LKRAGdFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGLaQKGRIAPGKDADFVFVDPDESYTLTP 396
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1208968218 390 TTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKE 424
Cdd:TIGR03178 397 DDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDE 431
PRK06189 PRK06189
allantoinase; Provisional
4-424 2.70e-78

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 249.62  E-value: 2.70e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKG 83
Cdd:PRK06189    6 IIRGGKVVTPEGVYRA-DIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALAAG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  84 GFTTICAMP-NTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQagseMTDFETLKELGAFAF--------TDDGVG 154
Cdd:PRK06189   85 GCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGN----LEHLRELAEAGVIGFkafmsnsgTDEFRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 155 VQDASMmLAAMKRAAKLNMAVVAHCEENTLINK---GCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCH 231
Cdd:PRK06189  161 SDDLTL-YEGMKEIAALGKILALHAESDALTRHlttQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFVH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 232 VSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAE 311
Cdd:PRK06189  240 ISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCPPE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 312 EKaqgiERAPF-----GITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEE 385
Cdd:PRK06189  320 LK----EGDDFflvwgGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGLpQKGRLEVGADADFVLVDLDETY 395
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1208968218 386 EIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKE 424
Cdd:PRK06189  396 TLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDG 434
PRK09060 PRK09060
dihydroorotase; Validated
4-424 1.22e-77

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 247.53  E-value: 1.22e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKG 83
Cdd:PRK09060    8 ILKGGTVVNPDGEGRA-DIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  84 GFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGsemtDFETLKELGAFA----FTDDGVG---VQ 156
Cdd:PRK09060   87 GVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNAD----ELAELERLPGCAgikvFMGSSTGdllVE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 157 DASMMLAAMKRAAKlNMAVvaHCEENTLIN--KGCVHEGKFSekhglngipsvceSVHIARD-----------ILLAEAA 223
Cdd:PRK09060  163 DDEGLRRILRNGRR-RAAF--HSEDEYRLRerKGLRVEGDPS-------------SHPVWRDeeaallatrrlVRLARET 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 224 DCHYHVCHVSTKGSVRVIRDAKRAgikVTAEVTPHHLVLcedDIPSADPNFK----MNPPLRGKEDHAALIEGLLDGTID 299
Cdd:PRK09060  227 GRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTL---AAPECYERLGtlaqMNPPIRDARHRDGLWRGVRQGVVD 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 300 MIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNlVKKGIITLEQLIQFLTEKPADTFGLEA-GRLKEGRTADITI 378
Cdd:PRK09060  301 VLGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGIAGkGRIAVGYDADFTI 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1208968218 379 IDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIA-WQKE 424
Cdd:PRK09060  380 VDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVmWDGE 426
PRK08323 PRK08323
phenylhydantoinase; Validated
1-421 2.77e-76

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 244.70  E-value: 2.77e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   1 MNYLFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENitaDNAEVIDVNGKLIAPGLVDVHVHLREP-GGEH-KETIETGTL 78
Cdd:PRK08323    1 MSTLIKNGTVVTADDTYKA-DVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHMEMPfGGTVsSDDFETGTR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  79 AAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAIT--VRQAGSEMtdfETLKELGAFAF----TDDG 152
Cdd:PRK08323   77 AAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITdwNEVVLDEM---PELVEEGITSFklfmAYKG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 153 VGVQDASMMLAAMKRAAKLNMAVVAHCEENTLIN---KGCVHEGKFS-EKHGLNGiPSVCESVHIARDILLAEAADCHYH 228
Cdd:PRK08323  154 ALMLDDDELLRALQRAAELGALPMVHAENGDAIAylqAKLLAEGKTGpEYHALSR-PPEVEGEATNRAIMLAELAGAPLY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 229 VCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPN----FKMNPPLRGKEDHAALIEGLLDGTIDMIATD 304
Cdd:PRK08323  233 IVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFegakYVMSPPLRDKEHQDALWRGLQDGDLQVVATD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 305 HAPHTAEEKAQGiERAPF-----GITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL--EAGRLKEGRTADIT 377
Cdd:PRK08323  313 HCPFCFEQKKQL-GRGDFtkipnGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLypRKGTIAVGADADIV 391
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1208968218 378 IIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAW 421
Cdd:PRK08323  392 IWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVV 435
PRK04250 PRK04250
dihydroorotase; Provisional
15-419 1.28e-75

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 241.21  E-value: 1.28e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  15 GKIVATDLLVQDGKIAKV-AENITADnaEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPN 93
Cdd:PRK04250   10 GRIVEGGIGIENGRISKIsLRDLKGK--EVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  94 TRPVPDCREHMEDLQKRIQEKAHV----NVLPYGaiTVRQAGSEMTDFETlkelgafAFTDDGVGVQDASMMLAAMKRAA 169
Cdd:PRK04250   88 TKPPIMDEKTYEKRMRIAEKKSYAdyalNFLIAG--NCEKAEEIKADFYK-------IFMGASTGGIFSENFEVDYACAP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 170 KlnmAVVAHCEENTLINKgcvhegkFSEKhglngiPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRdaKRAGI 249
Cdd:PRK04250  159 G---IVSVHAEDPELIRE-------FPER------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLIL--KSNLP 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 250 KVTAEVTPHHLVLCEDDIpSADPNFKMNPPLRGKEDHAALIEGLldGTIDMIATDHAPHTAEEKAQGierAPfGITGFET 329
Cdd:PRK04250  221 WVSFEVTPHHLFLTRKDY-ERNPLLKVYPPLRSEEDRKALWENF--SKIPIIASDHAPHTLEDKEAG---AA-GIPGLET 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 330 AFPLLYtNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGW 409
Cdd:PRK04250  294 EVPLLL-DAANKGMISLFDIVEKMHDNPARIFGIKNYGIEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGK 372
                         410
                  ....*....|
gi 1208968218 410 PVMTIVGGKI 419
Cdd:PRK04250  373 VIMTILRGEV 382
PRK09236 PRK09236
dihydroorotase; Reviewed
1-423 8.06e-73

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 235.15  E-value: 8.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   1 MNYLFKNGRYMNEeGKIVATDLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA 79
Cdd:PRK09236    2 KRILIKNARIVNE-GKIFEGDVLIENGRIAKIASSISAKSAdTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  80 AAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNvlpYGAITvrqaGSEMTDFETLKELGAfaftDDGVGVQ--- 156
Cdd:PRK09236   81 AVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLAN---YSFYF----GATNDNLDEIKRLDP----KRVCGVKvfm 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 157 ---------DASMMLAAMKRAAKlnMAVVAHCEENTLINKgcvHEGKFSEKHGlNGIP----------SVC-ESVHIArd 216
Cdd:PRK09236  150 gastgnmlvDNPETLERIFRDAP--TLIATHCEDTPTIKA---NLAKYKEKYG-DDIPaemhplirsaEACyKSSSLA-- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 217 ILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDG 296
Cdd:PRK09236  222 VSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADD 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 297 TIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYtNLVKKGIITLEQLIQFLTEKPADTFGLEA-GRLKEGRTAD 375
Cdd:PRK09236  302 RIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALL-ELVHEGKLSLEKVVEKTSHAPAILFDIKErGFIREGYWAD 380
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1208968218 376 ITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK09236  381 LVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHN 428
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
4-423 2.01e-71

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: 231.89  E-value: 2.01e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREP--GGEHKETIETGTLAA 80
Cdd:TIGR02033   2 LIKGGTVVNADDVFQA-DVLIEGGKIVAVGDNLIPpDAVEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  81 AKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKA------HVNVLPYGAITVRQAGSEMTDfETLKELGAFAFTDDGVG 154
Cdd:TIGR02033  81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSvidygfHMDITHWNDSVLEEHIPEVKE-EGINSFKVFMAYKNLLM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 155 VQDASMmLAAMKRAAKLNMAVVAHCEENTLIN---KGCVHEGKFS-EKHGLNGiPSVCESVHIARDILLAEAADCHYHVC 230
Cdd:TIGR02033 160 VDDEEL-FEILKRLKELGALLQVHAENGDIIAelqARMLAQGITGpEYHALSR-PPELEAEAVARAITLAALADAPLYVV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 231 HVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCED--DIPSADP-NFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAP 307
Cdd:TIGR02033 238 HVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDThyDKPGFEGaKYVCSPPLREPEDQDALWSALSSGALQTVGSDHCT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 308 HTAEEKAQG----IERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL--EAGRLKEGRTADITIIDL 381
Cdd:TIGR02033 318 FNFAQKKAIgkddFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLypRKGTIAVGSDADIVIWDP 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1208968218 382 EQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:TIGR02033 398 NRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVED 439
PRK08417 PRK08417
metal-dependent hydrolase;
22-419 7.86e-66

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 215.34  E-value: 7.86e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  22 LLVQDGKIAKVAENItaDNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKeTIETGTLAAAKGGFTTICAMPNTRPvPDCR 101
Cdd:PRK08417    1 IRIKDGKITEIGSDL--KGEEILDAKGKTLLPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTP-AIDN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 102 EHMEDLQKRIQEKAHVNVLPygAITVRQAGSEMTDFETLKELGAFA-FTDDGVgvqDASMMLAAMKRAAKLNMAVVAHCE 180
Cdd:PRK08417   77 EIALELINSAQRELPMQIFP--SIRALDEDGKLSNIATLLKKGAKAlELSSDL---DANLLKVIAQYAKMLDVPIFCRCE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 181 ENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEaadcHYHV----CHVSTKGSVRVIRDAKRAGIKVTAEVT 256
Cdd:PRK08417  152 DSSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAK----FYKNkvlfDTLALPRSLELLDKFKSEGEKLLKEVS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 257 PHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYT 336
Cdd:PRK08417  228 IHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 337 NLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPttflskgKNTPFAGWKCQGWPVMTIVG 416
Cdd:PRK08417  308 YLVKEGIITWSELSRFTSYNPAQFLGLNSGEIEVGKEADLVLFDPNESTIIDD-------NFSLYSGDELYGKIEAVIIK 380

                  ...
gi 1208968218 417 GKI 419
Cdd:PRK08417  381 GKL 383
PLN02795 PLN02795
allantoinase
24-417 2.34e-61

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 206.94  E-value: 2.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  24 VQDGKIAKVAENITAD----NAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMP-NTRPVP 98
Cdd:PLN02795   66 VEGGRIVSVTKEEEAPksqkKPHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPST 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  99 DCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEmTDFETLKELGAFAFTD-------DGVGVQDASMMLAAMKRAAKL 171
Cdd:PLN02795  146 TSVETLELKIEAAKGKLYVDVGFWGGLVPENAHNA-SVLEELLDAGALGLKSfmcpsgiNDFPMTTATHIKAALPVLAKY 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 172 NMAVVAHCEENTLINKGCVHEG--------------KFSEkhglNGIPSVCESVHIARDILLAEAAdcHYHVCHVS-TKG 236
Cdd:PLN02795  225 GRPLLVHAEVVSPVESDSRLDAdprsystylksrppSWEQ----EAIRQLLEVAKDTRPGGVAEGA--HVHIVHLSdAES 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 237 SVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAqg 316
Cdd:PLN02795  299 SLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKL-- 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 317 IE-----RAPFGITGFETAFPLLYTNLVKKGiITLEQLIQFLTEKPADTFGLEA-GRLKEGRTADITIIDLEQEEEIDPT 390
Cdd:PLN02795  377 LEegnflRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGLDSkGAIAPGKDADIVVWDPEAEFVLDES 455
                         410       420
                  ....*....|....*....|....*....
gi 1208968218 391 -TFLSKGKN-TPFAGWKCQGWPVMTIVGG 417
Cdd:PLN02795  456 yPIYHKHKSlSPYLGTKLSGKVIATFVRG 484
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
53-420 3.78e-60

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: 199.21  E-value: 3.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  53 PGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHV-----------NVLP 121
Cdd:cd01316     6 PGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCdyafsigatstNAAT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 122 YGAITVRQAGSEMTDFETLKELgafaFTDDGVGVQDASMMLAAMKraaklnmAVVAHCEENTLinkgcvhegkfsekhgl 201
Cdd:cd01316    86 VGELASEAVGLKFYLNETFSTL----ILDKITAWASHFNAWPSTK-------PIVTHAKSQTL----------------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 202 ngipsvcesvhiARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPsaDPNFKMNPPLR 281
Cdd:cd01316   138 ------------AAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLP--RGQYEVRPFLP 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 282 GKEDHAALIEGLldGTIDMIATDHAPHTAEEKAQgiERAPFGITGFETAFPLLYTnLVKKGIITLEQLIQFLTEKPADTF 361
Cdd:cd01316   204 TREDQEALWENL--DYIDCFATDHAPHTLAEKTG--NKPPPGFPGVETSLPLLLT-AVHEGRLTIEDIVDRLHTNPKRIF 278
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 362 GLEAgrlkegrTADITI-IDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIA 420
Cdd:cd01316   279 NLPP-------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETA 331
PRK08044 PRK08044
allantoinase AllB;
4-424 9.44e-60

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 201.24  E-value: 9.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVaTDLLVQDGKIAKVAENItADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKG 83
Cdd:PRK08044    6 IIKNGTVILENEARV-VDIAVKGGKIAAIGQDL-GDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  84 GFTTICAMP-NTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITvrqaGSEMTDFETLKELGAFAFT------------D 150
Cdd:PRK08044   84 GITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLV----SYNLDRLHELDEVGVVGFKcfvatcgdrgidN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 151 DGVGVQDASMmLAAMKRAAKLNMAVVAHCEeNTLI----NKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCH 226
Cdd:PRK08044  160 DFRDVNDWQF-YKGAQKLGELGQPVLVHCE-NALIcdelGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 227 YHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHA 306
Cdd:PRK08044  238 LHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 307 PHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEE 385
Cdd:PRK08044  318 PCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLqQKGRIAPGKDADFVFIQPNSSY 397
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1208968218 386 EIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKE 424
Cdd:PRK08044  398 VLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIE 436
PRK13404 PRK13404
dihydropyrimidinase; Provisional
15-423 4.20e-54

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 186.83  E-value: 4.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  15 GKIVAT------DLLVQDGKIAKVAENITAdNAEVIDVNGKLIAPGLVDVHVHLREPGGE---HKETIETGTLAAAKGGF 85
Cdd:PRK13404   11 GTVVTAtdtfqaDIGIRGGRIAALGEGLGP-GAREIDATGRLVLPGGVDSHCHIDQPSGDgimMADDFYTGTVSAAFGGT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  86 TTI---CAMPNTRPVPDCrehMEDLQKRIQEKAHVNVlPYGAItVRQAGSEMT--DFETLKELGAFAF----TDDGVGVQ 156
Cdd:PRK13404   90 TTVipfAAQHRGQSLREA---VEDYHRRAAGKAVIDY-AFHLI-VADPTEEVLteELPALIAQGYTSFkvfmTYDDLKLD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 157 DASMM--LAAMKRAAKLNMAvvaHCEENTLI---NKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCH 231
Cdd:PRK13404  165 DRQILdvLAVARRHGAMVMV---HAENHDMIawlTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 232 VSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDD--IPSAD-PNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPH 308
Cdd:PRK13404  242 VSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDldRPGMEgAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 309 ----TAEEKAQGIERA----PFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEA--GRLKEGRTADITI 378
Cdd:PRK13404  322 rfddTDGKLAAGANPSfkaiANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPrkGAIAIGADADIAI 401
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1208968218 379 IDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK13404  402 WDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVED 446
PRK01211 PRK01211
dihydroorotase; Provisional
15-419 5.97e-54

dihydroorotase; Provisional


Pssm-ID: 179247 [Multi-domain]  Cd Length: 409  Bit Score: 185.06  E-value: 5.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  15 GKIVATDLLVQDGKIAKVAENitADNAEVIDVNGkLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNT 94
Cdd:PRK01211   11 GKFDYLEIEVEDGKIKSIKKD--AGNIGKKELKG-AILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  95 RPVPDCREHMEDLQKRIQEKAHVNVLPYGAITvrQAGSEMTDFET--LKELGAFAFTDDGVGVQDASMmlaamKRAAKLN 172
Cdd:PRK01211   88 NIPIKDYNAFSDKLGRVAPKAYVDFSLYSMET--GNNALILDERSigLKVYMGGTTNTNGTDIEGGEI-----KKINEAN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 173 MAVVAHCEENTLINKGcVHEGKFSEKHGLNGiPSVCEsvhIARDILLAEAADCHYHVCHVStkgSVRVIRDakragikVT 252
Cdd:PRK01211  161 IPVFFHAELSECLRKH-QFESKNLRDHDLAR-PIECE---IKAVKYVKNLDLKTKIIAHVS---SIDVIGR-------FL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 253 AEVTPHHLVLcEDDIPSADPNfKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQgIERAPFGITGFETAFP 332
Cdd:PRK01211  226 REVTPHHLLL-NDDMPLGSYG-KVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQE-FEYAKSGIIGVETRVP 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 333 LLYTnLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQgWPVM 412
Cdd:PRK01211  303 LFLA-LVKKKILPLDVLYKTAIERPASLFGIKKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSH 380

                  ....*..
gi 1208968218 413 TIVGGKI 419
Cdd:PRK01211  381 VIMRGEV 387
pyrC PRK00369
dihydroorotase; Provisional
47-420 3.80e-51

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 176.88  E-value: 3.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  47 NGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREhmedlqkRIQEKahvnvlpygait 126
Cdd:PRK00369   41 QGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPE-------AITEK------------ 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 127 vrqagsemtdfetLKELGAFAFTDDGV--GVQD-----ASMMLAAMK-------------RAAKLNMAVVAHCEentlin 186
Cdd:PRK00369  102 -------------LAELEYYSRVDYFVysGVTKdpekvDKLPIAGYKifpedlereetfrVLLKSRKLKILHPE------ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 187 kgcvhegkfsekhglngIPSVCESVHIARDILLAEAADCHY-------HVCHVSTKGSVRVirdAKRAGIkvTAEVTPHH 259
Cdd:PRK00369  163 -----------------VPLALKSNRKLRRNCWYEIAALYYvkdyqnvHITHASNPRTVRL---AKELGF--TVDITPHH 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 260 LVLcedDIPSaDPNFKMNPPLRGKEDHAALIEGLLDgtIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTnLV 339
Cdd:PRK00369  221 LLV---NGEK-DCLTKVNPPIRDINERLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYT-LV 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 340 KKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIdleQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKI 419
Cdd:PRK00369  294 SKGILSIDRAVELISTNPARILGIPYGEIKEGYRANFTVI---QFEDWRYSTKYSKVIETPLDGFELKASVYATIVQGKL 370

                  .
gi 1208968218 420 A 420
Cdd:PRK00369  371 A 371
PLN02942 PLN02942
dihydropyrimidinase
4-424 2.54e-42

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 155.39  E-value: 2.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENI-TADNAEVIDVNGKLIAPGLVDVHVHLREP--GGEHKETIETGTLAA 80
Cdd:PLN02942    8 LIKGGTVVNAHHQELA-DVYVEDGIIVAVAPNLkVPDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQAAA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  81 AKGGFTTICAMPntrpVPDCREHMEDLQKrIQEKAHVNVLPYG---AITvRQAGSEMTDFETL-KELGAFAF----TDDG 152
Cdd:PLN02942   87 LAGGTTMHIDFV----IPVNGNLLAGYEA-YEKKAEKSCMDYGfhmAIT-KWDDTVSRDMETLvKEKGINSFkffmAYKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 153 VGVQDASMMLAAMKRAAKLNMAVVAHCEentliNKGCVHEGKFS---------EKHGLNGiPSVCESVHIARDILLAEAA 223
Cdd:PLN02942  161 SLMVTDELLLEGFKRCKSLGALAMVHAE-----NGDAVFEGQKRmielgitgpEGHALSR-PPLLEGEATARAIRLAKFV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 224 DCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLceDDIPSADPNFK------MNPPLRGKEDHAALIEGLLDGT 297
Cdd:PLN02942  235 NTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVL--DDSKLWDPDFTiaskyvMSPPIRPAGHGKALQAALSSGI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 298 IDMIATDHAPHTAEEKAQGIE---RAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL--EAGRLKEGR 372
Cdd:PLN02942  313 LQLVGTDHCPFNSTQKAFGKDdfrKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIypRKGAILAGS 392
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1208968218 373 TADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKE 424
Cdd:PLN02942  393 DADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENG 444
DHOase pfam12890
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various ...
48-237 6.56e-37

Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various bacteria.


Pssm-ID: 315550 [Multi-domain]  Cd Length: 142  Bit Score: 131.53  E-value: 6.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  48 GKLIAPGLVDVHVHLREPGGEHKETIETgtlaaakggftTICAMPNTRPVPdcrehmedlqkriqekahvnvlpyGAITV 127
Cdd:pfam12890   1 GRLIVPGLAFLHVHLTAPSGEAQELKET-----------TWAAYGVTFKAP------------------------AGITV 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 128 RQAGSEmtdfetlkelgAFAFTDDGVGVQDASMMLAAMKRAAkLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNgIPSV 207
Cdd:pfam12890  46 EDDSEE-----------GFIFTNDTYYITIQLLEGEGMKKSE-LDQELKAIATDDEVTNQSAVQDFELPQFYGTQ-LKGN 112
                         170       180       190
                  ....*....|....*....|....*....|
gi 1208968218 208 CESVHIARDILLAEAADCHYHVCHVSTKGS 237
Cdd:pfam12890 113 CETEHCVYSYLLAKAAGCGFYVSIIYTKEN 142
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
50-419 1.40e-32

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: 125.69  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  50 LIAPGLVDVHVHLR--------EPGGEHKETIETGTLAAAKGGFTTICAMPNTRP--VPDCREHMEDLQKRI-------- 111
Cdd:pfam01979   1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTStgIEALLEAAEELPLGLrflgpgcs 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 112 --------QEKAHVNVLPYGAITVRQAGSEMTdFETLKELGAFAFTDDgvgvqdasMMLAAMKRAAKLNMAVVAHCEENT 183
Cdd:pfam01979  81 ldtdgeleGRKALREKLKAGAEFIKGMADGVV-FVGLAPHGAPTFSDD--------ELKAALEEAKKYGLPVAIHALETK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 184 LINKgcVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAadchyHVCHVSTKGSVRVIRDAKRAGIkvtaevtphhlvlc 263
Cdd:pfam01979 152 GEVE--DAIAAFGGGIEHGTHLEVAESGGLLDIIKLILA-----HGVHLSPTEANLLAEHLKGAGV-------------- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 264 eDDIPSADpnfkmnppLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEekAQGIERAPFgitgfetafpLLYTNLVKKGI 343
Cdd:pfam01979 211 -AHCPFSN--------SKLRSGRIALRKALEDGVKVGLGTDGAGSGNS--LNMLEELRL----------ALELQFDPEGG 269
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208968218 344 ITLEQLIQFLTEKPADTFGLE--AGRLKEGRTADITIIDLEqeeeidpttflskgKNTPFAGWKCQGWPVMTIVGGKI 419
Cdd:pfam01979 270 LSPLEALRMATINPAKALGLDdkVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKGKI 333
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
3-419 1.12e-15

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 78.08  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   3 YLFKNGRY--MNEEGKIVATDLLVQDGKIAKVAENITA---DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGT 77
Cdd:COG1228    10 LLITNATLvdGTGGGVIENGTVLVEDGKIAAVGPAADLavpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  78 LAAA---------------KGGFTTICAMPNTrPVPDCREHMEDLQKRIQE----KAHVNVLPYGAITVRQAGSEMTDFE 138
Cdd:COG1228    90 ITPTvdlvnpadkrlrralAAGVTTVRDLPGG-PLGLRDAIIAGESKLLPGprvlAAGPALSLTGGAHARGPEEARAALR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 139 TLKELGAFA---FTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEEntlinkgcvhegkfsekhglngipsvcesvhiAR 215
Cdd:COG1228   169 ELLAEGADYikvFAEGGAPDFSLEELRAILEAAHALGLPVAAHAHQ--------------------------------AD 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 216 DILLA-EA-ADCHYHVCHVSTKgsvrVIRDAKRAGikvTAEVTPHHLVLceDDIPSADPNFKMNPPLRGKEDHAALIEGL 293
Cdd:COG1228   217 DIRLAvEAgVDSIEHGTYLDDE----VADLLAEAG---TVVLVPTLSLF--LALLEGAAAPVAAKARKVREAALANARRL 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 294 LDGTIDM-IATDHaphtaeekaqGIERAPFGITGFETAFpllytnLVKKGiITLEQLIQFLTEKPADTFGLEA--GRLKE 370
Cdd:COG1228   288 HDAGVPVaLGTDA----------GVGVPPGRSLHRELAL------AVEAG-LTPEEALRAATINAAKALGLDDdvGSLEP 350
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1208968218 371 GRTADITIIDleqeeeIDPTTFLSKGKNtpfagwkcqgwPVMTIVGGKI 419
Cdd:COG1228   351 GKLADLVLLD------GDPLEDIAYLED-----------VRAVMKDGRV 382
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
55-358 6.15e-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: 68.90  E-value: 6.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  55 LVDVHVHLREPGGEH------------------KETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAH 116
Cdd:cd01292     1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 117 VNVLPYGAITVRQAGSEMTDFETLKEL----------GAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLin 186
Cdd:cd01292    81 IRVVLGLGIPGVPAAVDEDAEALLLELlrrglelgavGLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHAGELPD-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 187 kgcvhegkfsekhglngipsvcESVHIARDILLAEaADCHYHVCHVSTkGSVRVIRDAKRAGIKVtaEVTPHHlvlcedd 266
Cdd:cd01292   159 ----------------------PTRALEDLVALLR-LGGRVVIGHVSH-LDPELLELLKEAGVSL--EVCPLS------- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 267 ipsadpnfkmNPPLRGKEDHA-ALIEGLLDGTIDMIATDHAPHTaeekaqgierapfgitgFETAFPLLYTNLVKKGII- 344
Cdd:cd01292   206 ----------NYLLGRDGEGAeALRRLLELGIRVTLGTDGPPHP-----------------LGTDLLALLRLLLKVLRLg 258
                         330
                  ....*....|....*
gi 1208968218 345 -TLEQLIQFLTEKPA 358
Cdd:cd01292   259 lSLEEALRLATINPA 273
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
3-380 1.15e-12

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 68.76  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   3 YLFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITADN-AEVIDVNGKLIAPGLVDVHVHlrePGGEH------KETIET 75
Cdd:cd00854     1 LIIKNARILTPGGLEDG-AVLVEDGKIVAIGPEDELEEaDEIIDLKGQYLVPGFIDIHIH---GGGGAdfmdgtAEALKT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  76 GTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVL------PYgaITVRQAGSEmtDFETLKELGAFAFT 149
Cdd:cd00854    77 IAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILgihlegPF--ISPEKKGAH--PPEYLRAPDPEELK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 150 D-DGVGVQDASMM---------LAAMKRAAKLNMAV-VAHCE---ENTlinKGCVHEGKFSEKHGLNGIPSVcesVHiaR 215
Cdd:cd00854   153 KwLEAAGGLIKLVtlapeldgaLELIRYLVERGIIVsIGHSDatyEQA---VAAFEAGATHVTHLFNAMSPL---HH--R 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 216 DILLAEAADCHYHV--------CHVStKGSVRVIRDAKRagikvtaevtPHHLVLCEDDIPSA---DPNFKMNP-PLRGK 283
Cdd:cd00854   225 EPGVVGAALSDDDVyaeliadgIHVH-PAAVRLAYRAKG----------ADKIVLVTDAMAAAglpDGEYELGGqTVTVK 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 284 EDHAALIEGLLDG-TIDMIatdhaphtaeekaQGIErapfgitgfetafpllytNLVKKGIITLEQLIQFLTEKPADTFG 362
Cdd:cd00854   294 DGVARLADGTLAGsTLTMD-------------QAVR------------------NMVKWGGCPLEEAVRMASLNPAKLLG 342
                         410       420
                  ....*....|....*....|
gi 1208968218 363 LEA--GRLKEGRTADITIID 380
Cdd:cd00854   343 LDDrkGSLKPGKDADLVVLD 362
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
2-61 2.62e-12

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 67.88  E-value: 2.62e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208968218   2 NYLFKNGRYMNEEGKIVA-TDLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVH 61
Cdd:COG3964     1 DLLIKGGRVIDPANGIDGvMDIAIKDGKIAAVAKDIDAAEAkKVIDASGLYVTPGLIDLHTH 62
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
19-383 7.77e-12

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 66.55  E-value: 7.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  19 ATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHlrepgGEHKETIETGTLAAAKGGFTTIcAMPN----T 94
Cdd:cd01297    19 TADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTH-----YDGQVFWDPDLRPSSRQGVTTV-VLGNcgvsP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  95 RPVPDcREHMEDLQKRIQEKAHVNVLPYGAITvrqagseMTDFetlkeLGAFAFTDDGVgvqDASMML--AAMKRAAKLN 172
Cdd:cd01297    93 APANP-DDLARLIMLMEGLVALGEGLPWGWAT-------FAEY-----LDALEARPPAV---NVAALVghAALRRAVMGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 173 MAVVAHCEENT----LINKGcVHEGKFSEKHGLNGIPSVC----ESVHIARdilLAEAADCHYHVcHVSTKGS------V 238
Cdd:cd01297   157 DAREATEEELAkmreLLREA-LEAGALGISTGLAYAPRLYagtaELVALAR---VAARYGGVYQT-HVRYEGDsilealD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 239 RVIRDAKRAGIKVTAEvtphHLVLCeddipsadpnfkMNPPLRGKEDHAALIEGLLDGTIDMIAtDHAPHTA--EEKAQG 316
Cdd:cd01297   232 ELLRLGRETGRPVHIS----HLKSA------------GAPNWGKIDRLLALIEAARAEGLQVTA-DVYPYGAgsEDDVRR 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 317 IERAPFgiTGFET--------------AFPLLYTNLVK-KGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIID 380
Cdd:cd01297   295 IMAHPV--VMGGSdggalgkphprsygDFTRVLGHYVReRKLLSLEEAVRKMTGLPARVFGLaDRGRIAPGYRADIVVFD 372

                  ...
gi 1208968218 381 LEQ 383
Cdd:cd01297   373 PDT 375
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
4-61 7.93e-12

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 66.41  E-value: 7.93e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVA-TDLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVH 61
Cdd:PRK09237    2 LLRGGRVIDPANGIDGvIDIAIEDGKIAAVAGDIDGSQAkKVIDLSGLYVSPGWIDLHVH 61
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
21-397 1.74e-11

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 65.49  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  21 DLLVQDGKIAKVAENITAD---NAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA---AAKGGFTTICAMPNT 94
Cdd:cd01308    19 DILIAGGKILAIEDQLNLPgyeNVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVTlsdLTTAGVTTVVGCLGT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  95 RPVpdCReHMEDLQKriqeKAHvnVLPYGAIT--VRQAGSEM---TDFETLKElgAFAFTDDGVGVQDASMmlaAMKRAA 169
Cdd:cd01308    99 DGI--SR-SMEDLLA----KAR--ALEEEGITcfVYTGSYEVptrTITGSIRK--DLLLIDKVIGVGEIAI---SDHRSS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 170 KLNMAVVAHCEENTLI------NKGCVHEGKFSEKHGLNGIPSVCES----------VHIARDILLAEAAdchyhvchvs 233
Cdd:cd01308   165 QPTVEELARIAAEARVggllggKAGIVHIHLGDGKRALSPIFELIEEteipitqflpTHINRTAPLFEQG---------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 234 tkgsvrvIRDAKRAG-IKVTAevtphhlvlceddipSADPNFKMNPPLRGKEDHAALIE-GLLDGTIDMIATDHA--PHT 309
Cdd:cd01308   235 -------VEFAKMGGtIDLTS---------------SIDPQFRKEGEVRPSEALKRLLEqGVPLERITFSSDGNGslPKF 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 310 AEEKA-QGIerapfGITGFETAFPLLyTNLVKKGIITLEQLIQFLTEKPADTFGLEA-GRLKEGRTADITIIDleqeEEI 387
Cdd:cd01308   293 DENGNlVGL-----GVGSVDTLLREV-REAVKCGDIPLEVALRVITSNVARILKLRKkGEIQPGFDADLVILD----KDL 362
                         410
                  ....*....|
gi 1208968218 388 DPTTFLSKGK 397
Cdd:cd01308   363 DINSVIAKGQ 372
PRK09061 PRK09061
D-glutamate deacylase; Validated
4-258 1.79e-11

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 65.87  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVAT-DLLVQDGKIAKVAEN-ITADnaEVIDVNGKLIAPGLVDVHVHLREPGGEHKET--------- 72
Cdd:PRK09061   22 VIRNGRVVDPETGLDAVrDVGIKGGKIAAVGTAaIEGD--RTIDATGLVVAPGFIDLHAHGQSVAAYRMQAfdgvttale 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  73 IETGTL--------AAAKG-----GFTT------ICAMPNTRPVPDcrehMEDLQKRIQEKAHVnvlpYGAITVRQAGSE 133
Cdd:PRK09061  100 LEAGVLpvarwyaeQAGEGrplnyGASVgwtparIAVLTGPQAEGT----IADFGKALGDPRWQ----ERAATPAELAEI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 134 MTDFETLKELGAFAFtddGVGVQ-----DASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGkfsekhglngipsvc 208
Cdd:PRK09061  172 LELLEQGLDEGALGI---GIGAGyapgtGHKEYLELARLAARAGVPTYTHVRYLSNVDPRSSVDA--------------- 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1208968218 209 esvhIARDILLAEAADCHYHVCHV-STKGS-----VRVIRDAKRAGIKVTAEVTPH 258
Cdd:PRK09061  234 ----YQELIAAAAETGAHMHICHVnSTSLRdidrcLALVEKAQAQGLDVTTEAYPY 285
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
21-382 1.86e-11

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 65.58  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  21 DLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVH-----LREPGGEHKetietgtlaaAKGGFTTI----CAM 91
Cdd:COG3653    23 DVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTHydlqlLWDPRLEPS----------LRQGVTTVvmgnCGV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  92 pntRPVPDCREHMEDLQKRIqekAHVNVLPYGaitvrqagsEMTDFETLKELGAfAFTDDGVGVQDASMM---------- 161
Cdd:COG3653    93 ---SFAPVRPEDRDRLIDLM---EGVEGIPEG---------LDWDWESFGEYLD-ALERRGLGVNVASLVghgtlrayvm 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 162 -----------LAAMKRAAKLNMAvvAHC-----------------EENTLINKGCVHEGKFSEKHGLNGIPSVCESVHI 213
Cdd:COG3653   157 glddrpptpeeLARMRALLREAME--AGAlglstgliyvpgtyastDELVALAKVVAEYGGVYQSHMRDEGDGLLEAVDE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 214 ARDIllAEAADCHYHVCHVSTKG---------SVRVIRDAKRAGIKVTAEVTPH-----HLVLCeddIPS---ADPNFKM 276
Cdd:COG3653   235 LIRI--GREAGVPVHISHLKAAGkpnwgkadeVLALIEAARAEGLDVTADVYPYpagstGLGAL---LPPwaaAGGLDER 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 277 NPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAE-------EKAQGI-------ERapfGITGFETAFPLL-------- 334
Cdd:COG3653   310 LARLRDPATRARIRAEIEEGLPDNLLGRGGWDNILisdsppnEPLVGKslaeiaaER---GVDPADAALDLLleedgrvl 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 335 --YT-----NLVK-------------------------------------KGIITLEQLIQFLTEKPADTFGLE-AGRLK 369
Cdd:COG3653   387 ivYFimseeDVREllrhpwvmigsdgglggkahpraygtfprvlghyvreRGVLSLEEAVRKLTSLPADRLGLKdRGLLR 466
                         490
                  ....*....|...
gi 1208968218 370 EGRTADITIIDLE 382
Cdd:COG3653   467 PGYRADLVVFDPA 479
DHOase cd01294
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ...
49-364 2.52e-11

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: 64.61  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  49 KLIAPGlvDVHVHLREpgGEHKETIeTGTLAAakgGFTTICAMPNTRP----VPDCREHMEDLQKRIQEKahvNVLPYGA 124
Cdd:cd01294     2 TIPRPD--DMHLHLRD--GAMLKLV-LPYTAR---GFSRAIVMPNLKPpvttTADALAYRERILAADPGP---NFTPLMT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 125 ITVR--------QAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFs 196
Cdd:cd01294    71 LYLTenttpeelREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKF- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 197 ekhglngIPsVCESVHI---ARDILLAeaadchyhvcHVSTKGSVRVIrdaKRAGIKVTAEVTPHHLVLCEDDI--PSAD 271
Cdd:cd01294   150 -------IP-VLEPLAQrfpKLKIVLE----------HITTADAVEYV---KSCNENVAATITPHHLLLTRDDLlgGGLN 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 272 PNFKMNPPLRGKEDHAALIEGLLDGTID-MIATDHAPHTAEEK-----AQGIERAPFgitgfetAFPLLYTNLVKKGIit 345
Cdd:cd01294   209 PHLYCKPVAKRPEDREALRKAATSGHPKfFLGSDSAPHPKSNKesscgCAGIFSAPI-------ALPYLAEVFEEHNA-- 279
                         330
                  ....*....|....*....
gi 1208968218 346 LEQLIQFLTEKPADTFGLE 364
Cdd:cd01294   280 LDKLEAFASDNGPNFYGLP 298
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
21-387 5.05e-11

Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.


Pssm-ID: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 63.50  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  21 DLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVHLRE---PGGEHKETIetgtlaAAKGGFTTI--CAMPNT 94
Cdd:cd01307     1 DVAIENGKIAAVGAALAAPAAtQIVDAGGCYVSPGWIDLHVHVYQggtRYGDRPDMI------GVKSGVTTVvdAGSAGA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  95 RPVPDCREH-MEDLQKRIqeKAHVNVLPYGAItvrqAGSEMTDFETLkelgafaftddgvgvqDASMMLAAMKRAAKLNM 173
Cdd:cd01307    75 DNIDGFRYTvIERSATRV--YAFLNISRVGLV----AQDELPDPDNI----------------DEDAVVAAAREYPDVIV 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 174 AVVAHCEentlinKGCVhegkfsekhGLNGIpsvcESVHIARDIllAEAADCHYHVcHVstkGSVRVIRDakragikvta 253
Cdd:cd01307   133 GLKARAS------KSVV---------GEWGI----KPLELAKKI--AKEADLPLMV-HI---GSPPPILD---------- 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 254 EVTPhhlVLCEDDIPSADPNFKMNPPLRGKED-----HAALIEGL-LD---GTID--------MIATDHAPHTAEEKAQG 316
Cdd:cd01307   178 EVVP---LLRRGDVLTHCFNGKPNGIVDEEGEvlplvRRARERGViFDvghGTASfsfrvaraAIAAGLLPDTISSDIHG 254
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208968218 317 IERAPFGI-TGFETAFPLLYTNLvkkgiiTLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEEEI 387
Cdd:cd01307   255 RNRTNGPVyALATTLSKLLALGM------PLEEVIEAVTANPARMLGLaEIGTLAVGYDADLTVFDLKDGRVE 321
PRK08204 PRK08204
hypothetical protein; Provisional
3-62 8.11e-11

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 63.48  E-value: 8.11e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208968218   3 YLFKNGRYMNEE---GKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK08204    4 TLIRGGTVLTMDpaiGDLPRGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHT 66
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
4-90 1.43e-10

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 62.42  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADnAEVIDVNGKLIAPGLVDVHVHlrepGG-------EHKETIETG 76
Cdd:COG1820     1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPD-AEVIDLGGGYLAPGFIDLHVH----GGggvdfmdGTPEALRTI 75
                          90
                  ....*....|....
gi 1208968218  77 TLAAAKGGFTTICA 90
Cdd:COG1820    76 ARAHARHGTTSFLP 89
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
4-176 2.27e-10

Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 61.88  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEGKIVatDLLVQDGKIAKVAENIT-ADNAEVIDVNGKLIAPGLVDVHVHLREP--GGEHKETIETGTLAA 80
Cdd:cd01293     1 LLRNARLADGGTALV--DIAIEDGRIAAIGPALAvPPDAEEVDAKGRLVLPAFVDPHIHLDKTftGGRWPNNSGGTLLEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  81 AKGGFTTIcampNTRPVPDCREHMEDLQKRIQE------KAHVNVLPYGAITVRQAGSEMtdFETLK---ELGAFAFTDD 151
Cdd:cd01293    79 IIAWEERK----LLLTAEDVKERAERALELAIAhgttaiRTHVDVDPAAGLKALEALLEL--REEWAdliDLQIVAFPQH 152
                         170       180
                  ....*....|....*....|....*
gi 1208968218 152 GVGVQDASMMLaaMKRAAKLNMAVV 176
Cdd:cd01293   153 GLLSTPGGEEL--MREALKMGADVV 175
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
4-62 2.34e-09

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 59.04  E-value: 2.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208968218   4 LFKNGR-YMNEEGKIVATDLLVQDGKIAKV-----AENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:COG1574    11 LLTNGRiYTMDPAQPVAEAVAVRDGRIVAVgsdaeVRALAGPATEVIDLGGKTVLPGFIDAHVHL 75
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
1-61 1.18e-08

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 56.73  E-value: 1.18e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208968218   1 MNYLFKNGRYM-NEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:PRK08393    1 MSILIKNGYVIyGENLKVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTH 62
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
11-62 2.49e-08

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 55.78  E-value: 2.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1208968218  11 MNEEGKIVATDLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK07228   13 MNAKREIVDGDVLIEDDRIAAVGDRLDLEDYdDHIDATGKVVIPGLIQGHIHL 65
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
3-62 3.93e-08

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 55.22  E-value: 3.93e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208968218   3 YLFKNGR--YMNEEGKIVAT-DLLVQDGKIAKVAENITA----DNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:COG0402     2 LLIRGAWvlTMDPAGGVLEDgAVLVEDGRIAAVGPGAELparyPAAEVIDAGGKLVLPGLVNTHTHL 68
PRK06846 PRK06846
putative deaminase; Validated
2-62 1.19e-07

putative deaminase; Validated


Pssm-ID: 235873 [Multi-domain]  Cd Length: 410  Bit Score: 53.48  E-value: 1.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208968218   2 NYLFKNGR----YMNEEGKIVAT-----DLLVQDGKIAKVAENITA--DNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK06846    5 HYWLTNVRletgFDYENGVIVQTetalcTLEIQDGKIVAIRPNKQVpdATLPTYDANGLLMLPAFREMHIHL 76
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
4-61 1.26e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 53.57  E-value: 1.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968218   4 LFKNGRYMN-EEGKIVATDLLVQDGKIAKVAENItADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:COG1001     8 VIKNGRLVNvFTGEILEGDIAIAGGRIAGVGDYI-GEATEVIDAAGRYLVPGFIDGHVH 65
PRK07572 PRK07572
cytosine deaminase; Validated
21-62 3.46e-07

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 51.94  E-value: 3.46e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1208968218  21 DLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK07572   19 DIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHM 60
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
4-62 6.56e-07

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 51.05  E-value: 6.56e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208968218   4 LFKNGRY--MNEEGKIVATDLLVQDGKIAKVAENITA---DNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:cd01298     2 LIRNGTIvtTDPRRVLEDGDVLVEDGRIVAVGPALPLpayPADEVIDAKGKVVMPGLVNTHTHL 65
PRK05985 PRK05985
cytosine deaminase; Provisional
4-62 8.26e-07

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 50.70  E-value: 8.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMNEEgkivATDLLVQDGKIAKVAENITAD-NAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK05985    5 LFRNVRPAGGA----AVDILIRDGRIAAIGPALAAPpGAEVEDGGGALALPGLVDGHIHL 60
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
21-107 9.17e-07

isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 131030  Cd Length: 389  Bit Score: 50.55  E-value: 9.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  21 DLLVQDGKIAKVAENITA-----DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA---AAKGGFTTICAMP 92
Cdd:TIGR01975  19 DILIANDKIIAIADEIPStkdfvPNCVVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPELTlsdITKGGVTTVVGLL 98
                          90
                  ....*....|....*
gi 1208968218  93 NTRPVpdCReHMEDL 107
Cdd:TIGR01975  99 GTDGI--TR-HMESL 110
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
1-61 2.44e-06

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 440842  Cd Length: 554  Bit Score: 49.81  E-value: 2.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208968218   1 MNYLFKNGR-Y--MNE-EGKIVatDLLVQDGKIakVAENITADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:COG1229     1 MELIIKNGRvYdpANGiDGEVM--DIAIKDGKI--VEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
26-419 3.10e-06

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 48.85  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  26 DGKIAKVAENITAD-NAEVIDVNGKLIAPGLVDVHVHL-REPGGEHKETIETGTLAAAkggftticAMPNTRPVpDCREH 103
Cdd:cd01309     1 DGKIVAVGAEITTPaDAEVIDAKGKHVTPGLIDAHSHLgLDEEGGVRETSDANEETDP--------VTPHVRAI-DGINP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 104 MEDLQKRIQEKA--HVNVLPYGAITVRQAGSEMTDFETLkelgafafTDDGVGVQDASMMLA----------AMKRAAKL 171
Cdd:cd01309    72 DDEAFKRARAGGvtTVQVLPGSANLIGGQGVVIKTDGGT--------IEDMFIKAPAGLKMAlgenpkrvygGKGKEPAT 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 172 NMAVVAHcEENTLINKGCVHEGKFSEKHGLNGIPsvcesvhiARDI---LLAEAADCHYHV-CHVSTKGSVR-VIRDAKR 246
Cdd:cd01309   144 RMGVAAL-LRDAFIKAQEYGRKYDLGKNAKKDPP--------ERDLkleALLPVLKGEIPVrIHAHRADDILtAIRIAKE 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 247 AGIKVTAEvtpHHL-------VLCEDDIPSADP----NFKMNPPLRGKEDHAALIeglldgtidmiatdhaphtaeEKAQ 315
Cdd:cd01309   215 FGIKITIE---HGAegykladELAKHGIPVIYGptltLPKKVEEVNDAIDTNAYL---------------------LKKG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 316 GIeraPFGITGFETAFPLLYTNL-----VKKGiITLEQLIQFLTEKPADTFGLE--AGRLKEGRTADITIIDleqEEEID 388
Cdd:cd01309   271 GV---AFAISSDHPVLNIRNLNLeaakaVKYG-LSYEEALKAITINPAKILGIEdrVGSLEPGKDADLVVWN---GDPLE 343
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1208968218 389 PTTflskgkntpfagwkcqgWPVMTIVGGKI 419
Cdd:cd01309   344 PTS-----------------KPEQVYIDGRL 357
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
4-62 6.41e-06

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 48.21  E-value: 6.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218   4 LFKNGRYMN-EEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK06038    5 IIKNAYVLTmDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTHA 64
PRK09228 PRK09228
guanine deaminase; Provisional
22-61 1.29e-05

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 47.11  E-value: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1208968218  22 LLVQDGKIAKV--AENITA---DNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:PRK09228   34 LLVEDGRIVAAgpYAELRAqlpADAEVTDYRGKLILPGFIDTHIH 78
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
1-59 1.97e-05

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 46.33  E-value: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968218   1 MNYLFKNGRYMNEEGkIVATDLLVQDGKIAKVAENiTADNAEVIDVNGKLIAPGLVDVH 59
Cdd:PRK15446    2 MEMILSNARLVLPDE-VVDGSLLIEDGRIAAIDPG-ASALPGAIDAEGDYLLPGLVDLH 58
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
21-62 3.67e-05

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 45.76  E-value: 3.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1208968218  21 DLLVQDGKIAKV-----AENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:cd01300     1 AVAVRDGRIVAVgsdaeAKALKGPATEVIDLKGKTVLPGFIDSHSHL 47
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
22-62 4.34e-05

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 45.33  E-value: 4.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1208968218  22 LLVQDGKIAKV-----AENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:cd01296     1 IAIRDGRIAAVgpaasLPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
PRK07583 PRK07583
cytosine deaminase;
18-62 5.06e-05

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 45.36  E-value: 5.06e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1208968218  18 VATDLLVQDGKIAKVA-ENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK07583   39 VLVDIEIADGKIAAILpAGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
21-61 5.45e-05

Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.


Pssm-ID: 238629 [Multi-domain]  Cd Length: 541  Bit Score: 45.48  E-value: 5.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1208968218  21 DLLVQDGKIakVAENITADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:cd01304    19 DIFIRDGKI--VESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
Amidohydro_3 pfam07969
Amidohydrolase family;
344-419 1.08e-04

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 44.44  E-value: 1.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208968218 344 ITLEQLIQFLTEKPADTFGLE--AGRLKEGRTADITIIDLEqEEEIDPTTFLSKGkntpfagwkcqgwPVMTIVGGKI 419
Cdd:pfam07969 399 LSLEEALALYTSGPAKALGLEdrKGTLGVGKDADLVVLDDD-PLTVDPPAIADIR-------------VRLTVVDGRV 462
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
41-153 6.08e-04

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 41.51  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  41 AEVIDVNGKLIAPGLVDVHVHL--REPGGEHKETIETG--TLAAAK-------GGFTTicampntrpVPDC-REHMEDLQ 108
Cdd:cd01299     1 AQVIDLGGKTLMPGLIDAHTHLgsDPGDLPLDLALPVEyrTIRATRqaraalrAGFTT---------VRDAgGADYGLLR 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1208968218 109 KRIQEKAHV--NVLPYG-AITVRQAGSEMTDFETLKELGAFAFTDDGV 153
Cdd:cd01299    72 DAIDAGLIPgpRVFASGrALSQTGGHGDPRGLSGLFPAGGLAAVVDGV 119
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
13-61 8.24e-04

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 41.49  E-value: 8.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1208968218  13 EEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:cd01303    25 EDGLIVVVDGNIIAAGAAETLKRAAKPGARVIDSPNQFILPGFIDTHIH 73
PRK08418 PRK08418
metal-dependent hydrolase;
347-384 3.29e-03

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 39.57  E-value: 3.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1208968218 347 EQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQE 384
Cdd:PRK08418  342 KILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEE 379
ureC PRK13308
urease subunit alpha; Reviewed
17-85 3.40e-03

urease subunit alpha; Reviewed


Pssm-ID: 183965 [Multi-domain]  Cd Length: 569  Bit Score: 39.69  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218  17 IVATDLLVQDGKIAKV--AEN-----------ITADNAEVIDVNGKLIAPGLVDVHVHLREPgGEHKETIETGTLAAAKG 83
Cdd:PRK13308   84 IVKGDIGIRDGRIVGIgkAGNpdimdgvdprlVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-QLVDHALASGITTMLGG 162

                  ..
gi 1208968218  84 GF 85
Cdd:PRK13308  163 GL 164
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
1-62 3.48e-03

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 39.48  E-value: 3.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208968218   1 MNYLFKNGRYM--NEEGKIVATDLLVQDGKIAKVAEnITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK06380    1 MSILIKNAWIVtqNEKREILQGNVYIEGNKIVYVGD-VNEEADYIIDATGKVVMPGLINTHAHV 63
PRK12394 PRK12394
metallo-dependent hydrolase;
1-68 5.44e-03

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 38.97  E-value: 5.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968218   1 MNYLFKNGRYMN-EEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGE 68
Cdd:PRK12394    3 NDILITNGHIIDpARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHVFYDGTE 71
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
21-62 6.09e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 38.68  E-value: 6.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1208968218  21 DLLVQDGKIAKV--AENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK08203   25 GLVVEGGRIVEVgpGGALPQPADEVFDARGHVVTPGLVNTHHHF 68
PRK07203 PRK07203
putative aminohydrolase SsnA;
3-62 7.74e-03

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 38.38  E-value: 7.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208968218   3 YLFKNGRYM-NEEGKIVATD--LLVQDGKIAKV--AENITA--DNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK07203    2 LLIGNGTAItRDPAKPVIEDgaIAIEGNVIVEIgtTDELKAkyPDAEFIDAKGKLIMPGLINSHNHI 68
PRK12394 PRK12394
metallo-dependent hydrolase;
344-421 7.86e-03

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 38.20  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 344 ITLEQLIQFLTEKPADTFGLEA--GRLKEGRTADITIIDLeqeeeidpttflsKGKNTPFA---GWKCQGW----PVMTI 414
Cdd:PRK12394  301 MALEDVINACTHTPAVLMGMAAeiGTLAPGAFADIAIFKL-------------KNRHVEFAdihGETLTGThvlvPQMTI 367

                  ....*..
gi 1208968218 415 VGGKIAW 421
Cdd:PRK12394  368 KSGEILY 374
PRK09230 PRK09230
cytosine deaminase; Provisional
2-62 9.72e-03

cytosine deaminase; Provisional


Pssm-ID: 181713  Cd Length: 426  Bit Score: 38.14  E-value: 9.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208968218   2 NYLFKNGRYMNEEGkivATDLLVQDGKIAKVAENITADNA--EVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK09230    5 LMTIKNARLPGKEG---LWQITIEDGKISAIEPQSEASLEagEVLDAEGGLAIPPFIEPHIHL 64
 
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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