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Conserved domains on  [gi|488945473|ref|WP_002856548|]
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MULTISPECIES: metal-dependent hydrolase [Campylobacter]

Protein Classification

amidohydrolase family protein; amidohydrolase/deacetylase family metallohydrolase( domain architecture ID 10793093)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue| amidohydrolase/deacetylase family metallohydrolase similar to Bradyrhizobium diazoefficiens dihydroorotase which converts carbamoyl aspartic acid into 4,5-dihydroorotic acid in the biosynthesis of pyrimidines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08417 PRK08417
metal-dependent hydrolase;
16-391 0e+00

metal-dependent hydrolase;


:

Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 552.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  16 IEIKEGKITNIGSNLQGEEILDAKGMTLLPSFVDLCVSLKNDKFSLANLELLENECLKGGISSIVLR-DCMDFDEESFAL 94
Cdd:PRK08417   1 IRIKDGKITEIGSDLKGEEILDAKGKTLLPALVDLNVSLKNDSLSSKNLKSLENECLKGGVGSIVLYpDSTPAIDNEIAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  95 FLQNLAQRK--MQIFSSVRVKDTNGKLKNLATLLNKGACALELDSSLDANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGV 172
Cdd:PRK08417  81 ELINSAQRElpMQIFPSIRALDEDGKLSNIATLLKKGAKALELSSDLDANLLKVIAQYAKMLDVPIFCRCEDSSFDDSGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 173 MNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLD------EKDLKLVSIHHLIKDDSACED 246
Cdd:PRK08417 161 MNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDkfksegEKLLKEVSIHHLILDDSACEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 247 FNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIKEGFLNWQEL 326
Cdd:PRK08417 241 FNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTYLVKEGIITWSEL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488945473 327 CRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEEIFAPKS-SLYSEDKLFGKIKMHIIKGKNILE 391
Cdd:PRK08417 321 SRFTSYNPAQFLGLNSGEIEVGKEADLVLFDPNESTIIDDNfSLYSGDELYGKIEAVIIKGKLYLE 386
 
Name Accession Description Interval E-value
PRK08417 PRK08417
metal-dependent hydrolase;
16-391 0e+00

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 552.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  16 IEIKEGKITNIGSNLQGEEILDAKGMTLLPSFVDLCVSLKNDKFSLANLELLENECLKGGISSIVLR-DCMDFDEESFAL 94
Cdd:PRK08417   1 IRIKDGKITEIGSDLKGEEILDAKGKTLLPALVDLNVSLKNDSLSSKNLKSLENECLKGGVGSIVLYpDSTPAIDNEIAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  95 FLQNLAQRK--MQIFSSVRVKDTNGKLKNLATLLNKGACALELDSSLDANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGV 172
Cdd:PRK08417  81 ELINSAQRElpMQIFPSIRALDEDGKLSNIATLLKKGAKALELSSDLDANLLKVIAQYAKMLDVPIFCRCEDSSFDDSGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 173 MNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLD------EKDLKLVSIHHLIKDDSACED 246
Cdd:PRK08417 161 MNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDkfksegEKLLKEVSIHHLILDDSACEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 247 FNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIKEGFLNWQEL 326
Cdd:PRK08417 241 FNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTYLVKEGIITWSEL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488945473 327 CRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEEIFAPKS-SLYSEDKLFGKIKMHIIKGKNILE 391
Cdd:PRK08417 321 SRFTSYNPAQFLGLNSGEIEVGKEADLVLFDPNESTIIDDNfSLYSGDELYGKIEAVIIKGKLYLE 386
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 32-382 1.64e-132

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: 384.28  E-value: 1.64e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  32 GEEILDAKGMTLLPSFVDLCVSLKNDKFS-LANLELLENECLKGGISSIVLRDCMDFDEESFAL--FLQNLAQRKMQI-- 106
Cdd:cd01317    1 DAEVIDAEGKILAPGLVDLHVHLREPGFEyKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVveLLKNRAKDVGIVrv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 107 --FSSVRVKDTNGKLKNLATLLNKGACALELDSS--LDANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFEL 182
Cdd:cd01317   81 lpIGALTKGLKGEELTEIGELLEAGAVGFSDDGKpiQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 183 GLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLDE-KDLKL-----VSIHHLIKDDSACEDFNTAAKLMPP 256
Cdd:cd01317  161 GLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKaKAKGLpvtaeVTPHHLLLDDEALESYDTNAKVNPP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 257 LRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIKEGFLNWQELCRFTSKNPSE 336
Cdd:cd01317  241 LRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAK 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488945473 337 FLGLNSGVIEVGKEANLVLFDENEEIF--------APKSSLYSEDKLFGKIKMH 382
Cdd:cd01317  321 ILGLPPGRLEVGAPADLVLFDPDAEWIvdeetfrsKSKNTPFDGQKLKGRVLAT 374
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 2-387 2.28e-64

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: 211.87  E-value: 2.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   2 IIKNAKIYGDS---LQDIEIKEGKITNIGSNLQ---GEEILDAKGMTLLPSFVDLCVSL-------KNDkfslanlelLE 68
Cdd:COG0044    1 LIKNGRVVDPGgleRADVLIEDGRIAAIGPDLAapeAAEVIDATGLLVLPGLIDLHVHLrepglehKED---------IE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  69 NE---CLKGGISSIVlrdCM-------DfDEESFAlFLQNLAQRKmqifSSVRV-------KDTNGKLKNLATLLNKGAC 131
Cdd:COG0044   72 TGtraAAAGGVTTVV---DMpntnpvtD-TPEALE-FKLARAEEK----ALVDVgphgaltKGLGENLAELGALAEAGAV 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 132 ALEL-------DSSLDANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAK 204
Cdd:COG0044  143 AFKVfmgsddgNPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAE 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 205 FYKNKVIFDLLSLKDSLVLLDE---KDLKL---VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFL 278
Cdd:COG0044  223 ETGARLHIVHVSTAEAVELIREakaRGLPVtaeVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVI 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 279 TSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIKEGFLNWQELCRFTSKNPSEFLGL-NSGVIEVGKEANLVLFD 357
Cdd:COG0044  303 ATDHAPHTLEEKELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLpRKGRIAVGADADLVLFD 382

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 488945473 358 ENEEIFAPKSSLYS-------ED-KLFGKIKMHIIKGK 387
Cdd:COG0044  383 PDAEWTVTAEDLHSkskntpfEGrELTGRVVATIVRGR 420
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 15-391 4.52e-41

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: 149.52  E-value: 4.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   15 DIEIKEGKITNIGSN--LQGEEILDAKGMTLLPSFVDLCVSLKNDKFSLA-NLELLENECLKGGISSIVlrdCM------ 85
Cdd:TIGR00857   7 DILVEGGRIKKIGKLriPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKeDIESGSKAAAHGGFTTVA---DMpntkpp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   86 -DfDEESFalflqnlaQRKMQIFSSVRVKD-------TNG-KLKNLATL--LNKGACALELDSS-----LDANTLKVSSQ 149
Cdd:TIGR00857  84 iD-TPETL--------EWKLQRLKKVSLVDvhlyggvTQGnQGKELTEAyeLKEAGAVGRMFTDdgsevQDILSMRRALE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  150 YAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSL-VLLDEKD 228
Cdd:TIGR00857 155 YAAIAGVPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLeLIVKAKS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  229 LKL-----VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHS 303
Cdd:TIGR00857 235 QGIkitaeVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  304 VCEFISLCYTFLIKeGFLNWQELCRFTSKNPSEFLGLNS-GVIEVGKEANLVLFDENEEIFAPKSSLYSEDK-------- 374
Cdd:TIGR00857 315 LETALPLLLQLLVK-GLISLKDLIRMLSINPARIFGLPDkGTLEEGNPADITVFDLKKEWTINAETFYSKAKntpfegms 393

                         410
                  ....*....|....*..
gi 488945473  375 LFGKIKMHIIKGKNILE 391
Cdd:TIGR00857 394 LKGKPIATILRGKVVYE 410
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 222-389 5.59e-09

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: 57.13  E-value: 5.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  222 VLLDEKDLKLVSIHHLIKDDSACEDFNtaaklmppLRSKEDVLALREALKEGKISFLTSLHSAKSISLKdlAFDEAAFGI 301
Cdd:pfam01979 191 VHLSPTEANLLAEHLKGAGVAHCPFSN--------SKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLN--MLEELRLAL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  302 HsvcefislcyTFLIKEGFLNWQELCRFTSKNPSEFLGL--NSGVIEVGKEANLVLFDeneeifAPKSSLYSEDKLFGKI 379
Cdd:pfam01979 261 E----------LQFDPEGGLSPLEALRMATINPAKALGLddKVGSIEVGKDADLVVVD------LDPLAAFFGLKPDGNV 324

                         170
                  ....*....|
gi 488945473  380 KMHIIKGKNI 389
Cdd:pfam01979 325 KKVIVKGKIV 334
 
Name Accession Description Interval E-value
PRK08417 PRK08417
metal-dependent hydrolase;
16-391 0e+00

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 552.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  16 IEIKEGKITNIGSNLQGEEILDAKGMTLLPSFVDLCVSLKNDKFSLANLELLENECLKGGISSIVLR-DCMDFDEESFAL 94
Cdd:PRK08417   1 IRIKDGKITEIGSDLKGEEILDAKGKTLLPALVDLNVSLKNDSLSSKNLKSLENECLKGGVGSIVLYpDSTPAIDNEIAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  95 FLQNLAQRK--MQIFSSVRVKDTNGKLKNLATLLNKGACALELDSSLDANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGV 172
Cdd:PRK08417  81 ELINSAQRElpMQIFPSIRALDEDGKLSNIATLLKKGAKALELSSDLDANLLKVIAQYAKMLDVPIFCRCEDSSFDDSGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 173 MNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLD------EKDLKLVSIHHLIKDDSACED 246
Cdd:PRK08417 161 MNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDkfksegEKLLKEVSIHHLILDDSACEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 247 FNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIKEGFLNWQEL 326
Cdd:PRK08417 241 FNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTYLVKEGIITWSEL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488945473 327 CRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEEIFAPKS-SLYSEDKLFGKIKMHIIKGKNILE 391
Cdd:PRK08417 321 SRFTSYNPAQFLGLNSGEIEVGKEADLVLFDPNESTIIDDNfSLYSGDELYGKIEAVIIKGKLYLE 386
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 32-382 1.64e-132

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: 384.28  E-value: 1.64e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  32 GEEILDAKGMTLLPSFVDLCVSLKNDKFS-LANLELLENECLKGGISSIVLRDCMDFDEESFAL--FLQNLAQRKMQI-- 106
Cdd:cd01317    1 DAEVIDAEGKILAPGLVDLHVHLREPGFEyKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVveLLKNRAKDVGIVrv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 107 --FSSVRVKDTNGKLKNLATLLNKGACALELDSS--LDANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFEL 182
Cdd:cd01317   81 lpIGALTKGLKGEELTEIGELLEAGAVGFSDDGKpiQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 183 GLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLDE-KDLKL-----VSIHHLIKDDSACEDFNTAAKLMPP 256
Cdd:cd01317  161 GLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKaKAKGLpvtaeVTPHHLLLDDEALESYDTNAKVNPP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 257 LRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIKEGFLNWQELCRFTSKNPSE 336
Cdd:cd01317  241 LRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAK 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488945473 337 FLGLNSGVIEVGKEANLVLFDENEEIF--------APKSSLYSEDKLFGKIKMH 382
Cdd:cd01317  321 ILGLPPGRLEVGAPADLVLFDPDAEWIvdeetfrsKSKNTPFDGQKLKGRVLAT 374
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 2-387 2.28e-64

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: 211.87  E-value: 2.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   2 IIKNAKIYGDS---LQDIEIKEGKITNIGSNLQ---GEEILDAKGMTLLPSFVDLCVSL-------KNDkfslanlelLE 68
Cdd:COG0044    1 LIKNGRVVDPGgleRADVLIEDGRIAAIGPDLAapeAAEVIDATGLLVLPGLIDLHVHLrepglehKED---------IE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  69 NE---CLKGGISSIVlrdCM-------DfDEESFAlFLQNLAQRKmqifSSVRV-------KDTNGKLKNLATLLNKGAC 131
Cdd:COG0044   72 TGtraAAAGGVTTVV---DMpntnpvtD-TPEALE-FKLARAEEK----ALVDVgphgaltKGLGENLAELGALAEAGAV 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 132 ALEL-------DSSLDANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAK 204
Cdd:COG0044  143 AFKVfmgsddgNPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAE 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 205 FYKNKVIFDLLSLKDSLVLLDE---KDLKL---VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFL 278
Cdd:COG0044  223 ETGARLHIVHVSTAEAVELIREakaRGLPVtaeVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVI 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 279 TSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIKEGFLNWQELCRFTSKNPSEFLGL-NSGVIEVGKEANLVLFD 357
Cdd:COG0044  303 ATDHAPHTLEEKELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLpRKGRIAVGADADLVLFD 382

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 488945473 358 ENEEIFAPKSSLYS-------ED-KLFGKIKMHIIKGK 387
Cdd:COG0044  383 PDAEWTVTAEDLHSkskntpfEGrELTGRVVATIVRGR 420
pyrC PRK09357
dihydroorotase; Validated
 1-387 4.97e-62

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 205.43  E-value: 4.97e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   1 MIIKNAKIY----GDSLQDIEIKEGKITNIGSNLQGE--EILDAKGMTLLPSFVDLCVSLK----NDKfslanlELLENE 70
Cdd:PRK09357   3 ILIKNGRVIdpkgLDEVADVLIDDGKIAAIGENIEAEgaEVIDATGLVVAPGLVDLHVHLRepgqEDK------ETIETG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  71 CL---KGGISSIVlrdCM-------DfDEESFAlFLQNLAQRKmqifSSVRV-------KDTNGK-LKNLATLLNKGACA 132
Cdd:PRK09357  77 SRaaaAGGFTTVV---AMpntkpviD-TPEVVE-YVLDRAKEA----GLVDVlpvgaitKGLAGEeLTEFGALKEAGVVA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 133 LELDSS--LDANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKV 210
Cdd:PRK09357 148 FSDDGIpvQDARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARV 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 211 IFDLLSLKDSL-VLLDEKDLKL-----VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSA 284
Cdd:PRK09357 228 HICHVSTAGSVeLIRWAKALGIkvtaeVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAP 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 285 KSISLKDLAFDEAAFGIHSVcEF-ISLCYTFLIKEGFLNWQELCRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEEI- 362
Cdd:PRK09357 308 HAREEKECEFEAAPFGITGL-ETaLSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWt 386

                        410       420       430
                 ....*....|....*....|....*....|..
gi 488945473 363 -----FAPKS--SLYSEDKLFGKIKMHIIKGK 387
Cdd:PRK09357 387 vdgedFASKGknTPFIGMKLKGKVVYTIVDGK 418
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 15-391 4.52e-41

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: 149.52  E-value: 4.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   15 DIEIKEGKITNIGSN--LQGEEILDAKGMTLLPSFVDLCVSLKNDKFSLA-NLELLENECLKGGISSIVlrdCM------ 85
Cdd:TIGR00857   7 DILVEGGRIKKIGKLriPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKeDIESGSKAAAHGGFTTVA---DMpntkpp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   86 -DfDEESFalflqnlaQRKMQIFSSVRVKD-------TNG-KLKNLATL--LNKGACALELDSS-----LDANTLKVSSQ 149
Cdd:TIGR00857  84 iD-TPETL--------EWKLQRLKKVSLVDvhlyggvTQGnQGKELTEAyeLKEAGAVGRMFTDdgsevQDILSMRRALE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  150 YAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSL-VLLDEKD 228
Cdd:TIGR00857 155 YAAIAGVPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLeLIVKAKS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  229 LKL-----VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHS 303
Cdd:TIGR00857 235 QGIkitaeVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  304 VCEFISLCYTFLIKeGFLNWQELCRFTSKNPSEFLGLNS-GVIEVGKEANLVLFDENEEIFAPKSSLYSEDK-------- 374
Cdd:TIGR00857 315 LETALPLLLQLLVK-GLISLKDLIRMLSINPARIFGLPDkGTLEEGNPADITVFDLKKEWTINAETFYSKAKntpfegms 393

                         410
                  ....*....|....*..
gi 488945473  375 LFGKIKMHIIKGKNILE 391
Cdd:TIGR00857 394 LKGKPIATILRGKVVYE 410
PRK09059 PRK09059
dihydroorotase; Validated
 2-391 2.65e-30

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 120.53  E-value: 2.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   2 IIKNAKIYG-----DSLQDIEIKEGKITNIGSNLQ------GEEILDAKGMTLLPSFVDLCVSLKNDKFSlaNLELLEN- 69
Cdd:PRK09059   6 LLANARIIDpsrglDEIGTVLIEDGVIVAAGKGAGnqgapeGAEIVDCAGKAVAPGLVDARVFVGEPGAE--HRETIASa 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  70 --ECLKGGISSIVlrdCMD-----FDEESFALFLQNLAQRKmqifSSVRV-------KDTNGK-LKNLATLLNKGACAL- 133
Cdd:PRK09059  84 srAAAAGGVTSII---MMPdtdpvIDDVALVEFVKRTARDT----AIVNIhpaaaitKGLAGEeMTEFGLLRAAGAVAFt 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 134 ELDSSL-DANTLKVSSQYAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIF 212
Cdd:PRK09059 157 DGRRSVaNTQVMRRALTYARDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 213 DLLSLKDSL-VLLDEKDLKL-----VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKS 286
Cdd:PRK09059 237 AQISCAESAeALRRAKDRGLkvtagVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 287 ISLKDLAFDEAAFGIHSVCEFISLCYTfLIKEGFLNWQELCRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEEIFAPK 366
Cdd:PRK09059 317 VDTKRLPFSEAAAGAIGLETLLAAALR-LYHNGEVPLLRLIEALSTRPAEIFGLPAGTLKPGAPADIIVIDLDEPWVVDP 395

                        410       420       430
                 ....*....|....*....|....*....|...
gi 488945473 367 SSLYS--------EDKLFGKIKMHIIKGKNILE 391
Cdd:PRK09059 396 EDLKSrskntpfeEARFQGRVVRTIVAGKTVYE 428
PRK07627 PRK07627
dihydroorotase; Provisional
 11-391 5.15e-25

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 105.53  E-value: 5.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  11 DSLQDIEIKEGKITNIGS---NLQGEEILDAKGMTLLPSFVDLCVSLKNDKFS-LANLELLENECLKGGISSIVLRDCMD 86
Cdd:PRK07627  18 DRQADLYVAAGKIAAIGQapaGFNADKTIDASGLIVCPGLVDLSARLREPGYEyKATLESEMAAAVAGGVTSLVCPPDTD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  87 --FDEESFALFL----QNLAQRKMQIFSSVRVKDTNGKLKNLATLLNKGACAL-ELDSSL-DANTLKVSSQYAFMKDSPI 158
Cdd:PRK07627  98 pvLDEPGLVEMLkfraRNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFsQANVPVvDTQVLLRALQYASTFGFTV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 159 FVRCYDKDFDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLDE---KDLKL---V 232
Cdd:PRK07627 178 WLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAakaEGLPVtcdV 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 233 SIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCY 312
Cdd:PRK07627 258 GVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLPFAEATPGATGLELLLPLTL 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 313 TFLIKEGFLNWQELCRFTSKnPSEFLGLNSGVIEVGKEANLVLFDENEEIFAPKSSLYSEDK--------LFGKIKMHII 384
Cdd:PRK07627 338 KWADEAKVPLARALARITSA-PARVLGLPAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKntpflgyeLPGRVRATLV 416


                 ....*..
gi 488945473 385 KGKNILE 391
Cdd:PRK07627 417 AGQVAFE 423
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 190-386 6.93e-25

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: 104.34  E-value: 6.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 190 IAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLDEKDLKL---VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLAL 266
Cdd:cd01318  154 EAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVtveVTPHHLFLDVEDYDRLGTLGKVNPPLRSREDRKAL 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 267 REALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVcEFISLCYTFLIKEGFLNWQELCRFTSKNPSEFLGL-NSGVI 345
Cdd:cd01318  234 LQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGV-ETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIkNKGRI 312

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488945473 346 EVGKEANLVLFDENEEIFAPKSSLYSEDK--------LFGKIKMHIIKG 386
Cdd:cd01318  313 AEGYDADLTVVDLKEERTIRAEEFHSKAGwtpfegfeVTGFPVMTIVRG 361
PRK02382 PRK02382
dihydroorotase; Provisional
 3-357 3.13e-21

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 94.72  E-value: 3.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   3 IKNAKI-YGDSLQ--DIEIKEGKITNIGSNLQG---EEILDAKGMTLLPSFVDLCVSLKNDKFslanlELLEN------E 70
Cdd:PRK02382   6 LKDGRVyYNNSLQprDVRIDGGKITAVGKDLDGsssEEVIDARGMLLLPGGIDVHVHFREPGY-----THKETwytgsrS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  71 CLKGGISSIVLRDCMD---FDEESFALFLqNLAQRKMQIFSSVrvkdtNG----KLKNLATLLNKGACAL-EL------- 135
Cdd:PRK02382  81 AAAGGVTTVVDQPNTDpptVDGESFDEKA-ELAARKSIVDFGI-----NGgvtgNWDPLESLWERGVFALgEIfmadstg 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 136 DSSLDANTLKVSSQYAFMKDSPIFVRCYDKD-FDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIFDL 214
Cdd:PRK02382 155 GMGIDEELFEEALAEAARLGVLATVHAEDEDlFDELAKLLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAH 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 215 LSLKDSLVLL-DEKDLKLVSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLA 293
Cdd:PRK02382 235 ISTPEGVDAArREGITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTREEKDAD 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488945473 294 FDEAAFGIHSVCEFISLcytFL--IKEGFLNWQELCRFTSKNPSEFLGLNS-GVIEVGKEANLVLFD 357
Cdd:PRK02382 315 IWDAPSGVPGVETMLPL---LLaaVRKNRLPLERVRDVTAANPARIFGLDGkGRIAEGYDADLVLVD 378
PRK07369 PRK07369
dihydroorotase; Provisional
 11-371 3.34e-21

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 94.28  E-value: 3.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  11 DSLQDIEIKEGKITNIGSNLQG----EEILDAKGMTLLPSFVDL-CVSLK---NDKFSLANLElleNECLKGGISSI-VL 81
Cdd:PRK07369  19 DRIADVLIEDGKIQAIEPHIDPippdTQIIDASGLILGPGLVDLySHSGEpgfEERETLASLA---AAAAAGGFTRVaIL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  82 RDC---MDfDEESFALFlqnlaQRKMQIFSSVRV-------KDTNGK-LKNLATLLNKGACALELDSSL-DANTLKVSSQ 149
Cdd:PRK07369  96 PDTfppLD-NPATLARL-----QQQAQQIPPVQLhfwgaltLGGQGKqLTELAELAAAGVVGFTDGQPLeNLALLRRLLE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 150 YAFMKDSPIFVRCYDKDFDDNGVMNDCEMSFELGLIGMSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLDE-KD 228
Cdd:PRK07369 170 YLKPLGKPVALWPCDRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQaKA 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 229 LKL-----VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLAFDEA---AFG 300
Cdd:PRK07369 250 RGLpitasTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVAFAEAppgAIG 329

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945473 301 IHSVcefISLCYTFLIKEGFLNWQELCRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEEIFAPKSSLYS 371
Cdd:PRK07369 330 LELA---LPLLWQNLVETGELSALQLWQALSTNPARCLGQEPPSLAPGQPAELILFDPQKTWTVSAQTLHS 397
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 1-386 4.91e-21

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: 94.28  E-value: 4.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   1 MIIKNAKI---YGDSLQDIEIKEGKITNIGS---NLQGEEILDAKGMTLLPSFVDLCVSLkND--KFSLANLELLENECL 72
Cdd:cd01315    2 LVIKNGRVvtpDGVREADIAVKGGKIAAIGPdiaNTEAEEVIDAGGLVVMPGLIDTHVHI-NEpgRTEWEGFETGTKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  73 KGGISSIVlrdcmDF---------DEESFALFLqNLAQRKMQIfssvrvkD-------TNGKLKNLATLLNKGA------ 130
Cdd:cd01315   81 AGGITTII-----DMplnsippttTVENLEAKL-EAAQGKLHV-------DvgfwgglVPGNLDQLRPLDEAGVvgfkcf 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 131 ---CALELDSSLDANTLKVSSQYAFMKDSPIFVRCYD----KDFDDNGVMNDCE--MSFelgLIGMSKIAETSQIAKMKE 201
Cdd:cd01315  148 lcpSGVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENpeitEALQEQAKAKGKRdyRDY---LASRPVFTEVEAIQRILL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 202 LAKFYKNKVIFDLLSLKDSLVLLDEKDLKLVSI------HHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKI 275
Cdd:cd01315  225 LAKETGCRLHIVHLSSAEAVPLIREARAEGVDVtvetcpHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDI 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 276 SFLTSLHSAKSISLKDLA---FDEAAFGIHSVCEFISLCYTFLIKEGFLNWQELCRFTSKNPSEFLGLNS--GVIEVGKE 350
Cdd:cd01315  305 DMVVSDHSPCTPELKLLGkgdFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHqkGRIAVGYD 384

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 488945473 351 ANLVLFDENEE--------IFAPKSSLYSEDKLFGKIKMHIIKG 386
Cdd:cd01315  385 ADFVVWDPEEEftvdaedlYYKNKISPYVGRTLKGRVHATILRG 428
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 202-361 1.39e-16

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: 80.13  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 202 LAKFYKNKVIFDLLSLKDSLVLLDEKDLKLVSI------HHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKI 275
Cdd:cd01302  141 LAEEAGANVHIAHVSSGEALELIKFAKNKGVKVtcevcpHHLFLDESMLRLNGAWGKVNPPLRSKEDREALWEGVKNGKI 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 276 SFLTSLHSAKSISLKDLAFD--EAAFGIHSVCEFISLCYTFLIKEGfLNWQELCRFTSKNPSEFLGL-NSGVIEVGKEAN 352
Cdd:cd01302  221 DTIASDHAPHSKEEKESGKDiwKAPPGFPGLETRLPILLTEGVKRG-LSLETLVEILSENPARIFGLyPKGTIAVGYDAD 299


                 ....*....
gi 488945473 353 LVLFDENEE 361
Cdd:cd01302  300 LVIVDPKKE 308
PRK04250 PRK04250
dihydroorotase; Provisional
 16-391 1.50e-16

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 80.58  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  16 IEIKEGKITNIG-SNLQGEEILDAKGMTLLPSFVDLCVSLKNdkFSLANLELLEN---ECLKGGISSIVLRDCMD---FD 88
Cdd:PRK04250  17 IGIENGRISKISlRDLKGKEVIKVKGGIILPGLIDVHVHLRD--FEESYKETIESgtkAALHGGITLVFDMPNTKppiMD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  89 EESFaLFLQNLAQRKMQI--FSSVRVKDTNGKLKNLATLLNK-------GACALELDSSLDANTLKVSSQYAfmkDSPIF 159
Cdd:PRK04250  95 EKTY-EKRMRIAEKKSYAdyALNFLIAGNCEKAEEIKADFYKifmgastGGIFSENFEVDYACAPGIVSVHA---EDPEL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 160 VRCYDKDfddngvmndcemsfelgligmSKIAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLDEKDLKLVSI----H 235
Cdd:PRK04250 171 IREFPER---------------------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILKSNLPWVSFevtpH 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 236 HLIKDDsacEDF--NTAAKLMPPLRSKEDVLALREALKegKISFLTSLHSAKSISLKDlafdEAAFGIHSVCEFISLcYT 313
Cdd:PRK04250 230 HLFLTR---KDYerNPLLKVYPPLRSEEDRKALWENFS--KIPIIASDHAPHTLEDKE----AGAAGIPGLETEVPL-LL 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 314 FLIKEGFLNWQELCRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEEIFAPKSSLYSED--------KLFGKIKMHIIK 385
Cdd:PRK04250 300 DAANKGMISLFDIVEKMHDNPARIFGIKNYGIEEGNYANFAVFDMKKEWTIKAEELYTKAgwtpyegfKLKGKVIMTILR 379


                 ....*.
gi 488945473 386 GKNILE 391
Cdd:PRK04250 380 GEVVME 385
PRK07575 PRK07575
dihydroorotase; Provisional
 1-361 6.55e-16

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 78.95  E-value: 6.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   1 MIIKNAKIYGDS----LQDIEIKEGKITNIGSNLQGEE---ILDAKGMTLLPSFVDLCVSL-------KNDKF--SLAnl 64
Cdd:PRK07575   5 LLIRNARILLPSgellLGDVLVEDGKIVAIAPEISATAvdtVIDAEGLTLLPGVIDPQVHFrepglehKEDLFtaSRA-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  65 elleneCLKGGISSivlrdcmdfdeesfalFLQNLAQRKMQIfSSVRVKDtngKLKNLAT--LLNK----GACALELDSS 138
Cdd:PRK07575  83 ------CAKGGVTS----------------FLEMPNTKPLTT-TQAALDD---KLARAAEkcVVNYgffiGATPDNLPEL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 139 LDAN--------------TLKVSSQYA----FMKDS-PIFVRCydkdfDDNGVMNDCEMSFElgliGMSKIAETSQI--- 196
Cdd:PRK07575 137 LTANptcgikifmgsshgPLLVDEEAAleriFAEGTrLIAVHA-----EDQARIRARRAEFA----GISDPADHSQIqde 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 197 -------AKMKELAKFYKNKVIFDLLSLKDSLVLLDEKDLKLVSI----HHLIKDDSACEDFNTAAKLMPPLRSKEDVLA 265
Cdd:PRK07575 208 eaallatRLALKLSKKYQRRLHILHLSTAIEAELLRQDKPSWVTAevtpQHLLLNTDAYERIGTLAQMNPPLRSPEDNEA 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 266 LREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIkEGFLNWQELCRFTSKNPSEFLGL-NSGV 344
Cdd:PRK07575 288 LWQALRDGVIDFIATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGIpNKGR 366

                        410
                 ....*....|....*..
gi 488945473 345 IEVGKEANLVLFDENEE 361
Cdd:PRK07575 367 IAPGYDADLVLVDLNTY 383
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 1-391 1.60e-13

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: 71.48  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   1 MIIKNAKI---YGDSLQDIEIKEGKITNIGSNLQGE---EILDAKGMTLLPSFVD----------LCVSlKNDKFS---- 60
Cdd:cd01314    1 LIIKNGTIvtaDGSFKADILIEDGKIVAIGPNLEAPggvEVIDATGKYVLPGGIDphthlelpfmGTVT-ADDFESgtra 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  61 -LAnlelleneclkGGISSIVlrdcmdfdeeSFALFL--QNLAQ------RKMQIFSS------VRVKDTNGKLKN-LAT 124
Cdd:cd01314   80 aAA-----------GGTTTII----------DFAIPNkgQSLLEavekwrGKADGKSVidygfhMIITDWTDSVIEeLPE 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 125 LLNKGAcaleldssldaNTLKVSSQYAFMK---DSPI---FVRCydkdfDDNG--VMNDCE---MSFEL-------GLIG 186
Cdd:cd01314  139 LVKKGI-----------SSFKVFMAYKGLLmvdDEELldvLKRA-----KELGalVMVHAEngdVIAELqkkllaqGKTG 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 187 -----MSK--IAETSQIAKMKELAKFYKNKVIFDLLSLKDSLVLLDEKDLKLVSI------HHLIKDDSACE-DFNTAAK 252
Cdd:cd01314  203 peyhaLSRppEVEAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVygetcpQYLLLDDSDYWkDWFEGAK 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 253 LM--PPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDLA---FDEAAFGIHSVCEFISLCYTFLIKEGFLNWQELC 327
Cdd:cd01314  283 YVcsPPLRPKEDQEALWDGLSSGTLQTVGSDHCPFNFAQKARGkddFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFV 362

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488945473 328 RFTSKNPSEFLGL--NSGVIEVGKEANLVLFDENEEIFAPKSSL--------YSEDKLFGKIKMHIIKGKNILE 391
Cdd:cd01314  363 ELTSTNPAKIFGLypRKGTIAVGSDADLVIWDPNAEKTISADTHhhnvdyniFEGMKVKGWPVVTISRGKVVVE 436
PRK06189 PRK06189
allantoinase; Provisional
 1-387 3.43e-12

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 67.42  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   1 MIIKNAKIY---GDSLQDIEIKEGKITNIGSNLQG--EEILDAKGMTLLPSFVDLCVSLKNDKFSlanlellENECLKGG 75
Cdd:PRK06189   5 LIIRGGKVVtpeGVYRADIGIKNGKIAEIAPEISSpaREIIDADGLYVFPGMIDVHVHFNEPGRT-------HWEGFATG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  76 ISSIVLRDCMDF------------DEESFaLFLQNLAQRKMQIFSSVRVKDTNGKLKNLATLLNKGA---------CALE 134
Cdd:PRK06189  78 SAALAAGGCTTYfdmplnsipptvTREAL-DAKAELARQKSAVDFALWGGLVPGNLEHLRELAEAGVigfkafmsnSGTD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 135 LDSSLDANTLkvssqYAFMKD-----SPIFVRCydkdfDDNGVMNDCEMSFEL-GLIGMSK-------IAETSQIAKMKE 201
Cdd:PRK06189 157 EFRSSDDLTL-----YEGMKEiaalgKILALHA-----ESDALTRHLTTQARQqGKTDVRDylesrpvVAELEAVQRALL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 202 LAKFYKNKVIFDLLSLKDSLVLLDE--KDLKLVSI----HHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKI 275
Cdd:PRK06189 227 YAQETGCPLHFVHISSGKAVALIAEakKRGVDVSVetcpHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEI 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 276 SFLTSLHSAKSISLK-DLAFDEAAFGIhSVCEFiSLcyTFLIKEGF----LNWQELCRFTSKNPSEFLGL-NSGVIEVGK 349
Cdd:PRK06189 307 DMISSDHSPCPPELKeGDDFFLVWGGI-SGGQS-TL--LVMLTEGYiergIPLETIARLLATNPAKRFGLpQKGRLEVGA 382

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 488945473 350 EANLVLFDENEEIFAPKSSLYSEDKL-------F-GKIKMHIIKGK 387
Cdd:PRK06189 383 DADFVLVDLDETYTLTKEDLFYRHKQspyegrtFpGRVVATYLRGQ 428
PLN02795 PLN02795
allantoinase
 243-391 7.64e-12

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 66.72  E-value: 7.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 243 ACEDF---NTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSISLKDlaFDEAAF-----GIHSVCEFISLCYTF 314
Cdd:PLN02795 325 SAEEIpdgDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKL--LEEGNFlrawgGISSLQFVLPATWTA 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 315 LIKEGfLNWQELCRFTSKNPSEFLGLNS-GVIEVGKEANLVLFDENEEIFA----------PKSSLYSEDKLFGKIKMHI 383
Cdd:PLN02795 403 GRAYG-LTLEQLARWWSERPAKLAGLDSkGAIAPGKDADIVVWDPEAEFVLdesypiyhkhKSLSPYLGTKLSGKVIATF 481


                 ....*...
gi 488945473 384 IKGKNILE 391
Cdd:PLN02795 482 VRGNLVFL 489
pyrC PRK00369
dihydroorotase; Provisional
 232-387 3.61e-10

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 60.93  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 232 VSIHHLIKD-DSACedfntAAKLMPPLRSKEDVLALREALKEgkISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISL 310
Cdd:PRK00369 216 ITPHHLLVNgEKDC-----LTKVNPPIRDINERLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPF 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 311 CYTfLIKEGFLNWQELCRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEEIFAPKSSLYSEDKLFG-----KIKMHIIK 385
Cdd:PRK00369 289 IYT-LVSKGILSIDRAVELISTNPARILGIPYGEIKEGYRANFTVIQFEDWRYSTKYSKVIETPLDGfelkaSVYATIVQ 367


                 ..
gi 488945473 386 GK 387
Cdd:PRK00369 368 GK 369
PRK08044 PRK08044
allantoinase AllB;
1-392 1.21e-09

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 59.48  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   1 MIIKNAKIY---GDSLQDIEIKEGKITNIGSNL-QGEEILDAKGMTLLPSFVDLCVSLKNDKFS-LANLELLENECLKGG 75
Cdd:PRK08044   5 LIIKNGTVIlenEARVVDIAVKGGKIAAIGQDLgDAKEVMDASGLVVSPGMVDAHTHISEPGRShWEGYETGTRAAAKGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  76 ISSIVLRDCMDF----DEESFALflqnlaqrkmqifssvRVKDTNGKLKNLATLLNkGACALELDSSLDANTLKVSSQYA 151
Cdd:PRK08044  85 ITTMIEMPLNQLpatvDRASIEL----------------KFDAAKGKLTIDAAQLG-GLVSYNLDRLHELDEVGVVGFKC 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 152 FMkdSPIFVRCYDKDFDDngvMNDCEMsFElgliGMSKIAETSQIA-----------KMKELAK---------FYKNKVI 211
Cdd:PRK08044 148 FV--ATCGDRGIDNDFRD---VNDWQF-YK----GAQKLGELGQPVlvhcenalicdELGEEAKregrvtahdYVASRPV 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 212 F-DLLSLKDSLVLLDEKDLKL---------------------------VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDV 263
Cdd:PRK08044 218 FtEVEAIRRVLYLAKVAGCRLhvchisspegveevtrarqegqdvtceSCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQ 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 264 LALREALKEGKISFLTSLHSAKSISLKDLAFDEAAFGIHSVCEFISLCYTFLIKEGFLNWQELCRFTSKNPSEFLGLNS- 342
Cdd:PRK08044 298 KGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQk 377

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488945473 343 GVIEVGKEANLVLFDEN-------EEI-FAPKSSLYSEDKLFGKIKMHIIKGKNILEK 392
Cdd:PRK08044 378 GRIAPGKDADFVFIQPNssyvlknEDLeYRHKVSPYVGRTIGARITKTILRGDVIYDI 435
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 222-389 5.59e-09

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: 57.13  E-value: 5.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  222 VLLDEKDLKLVSIHHLIKDDSACEDFNtaaklmppLRSKEDVLALREALKEGKISFLTSLHSAKSISLKdlAFDEAAFGI 301
Cdd:pfam01979 191 VHLSPTEANLLAEHLKGAGVAHCPFSN--------SKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLN--MLEELRLAL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473  302 HsvcefislcyTFLIKEGFLNWQELCRFTSKNPSEFLGL--NSGVIEVGKEANLVLFDeneeifAPKSSLYSEDKLFGKI 379
Cdd:pfam01979 261 E----------LQFDPEGGLSPLEALRMATINPAKALGLddKVGSIEVGKDADLVVVD------LDPLAAFFGLKPDGNV 324

                         170
                  ....*....|
gi 488945473  380 KMHIIKGKNI 389
Cdd:pfam01979 325 KKVIVKGKIV 334
PRK01211 PRK01211
dihydroorotase; Provisional
 207-361 9.57e-09

dihydroorotase; Provisional


Pssm-ID: 179247 [Multi-domain]  Cd Length: 409  Bit Score: 56.79  E-value: 9.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 207 KNKVIFDLLSLKDSLVLLDEkdlklVSIHHLIKDDSAceDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKS 286
Cdd:PRK01211 208 KTKIIAHVSSIDVIGRFLRE-----VTPHHLLLNDDM--PLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHT 280

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488945473 287 ISlKDLAFDEAAFGIHSVCEFISLcYTFLIKEGFLNWQELCRFTSKNPSEFLGLNSGVIEVGKEANLVLFDENEE 361
Cdd:PRK01211 281 EE-DKQEFEYAKSGIIGVETRVPL-FLALVKKKILPLDVLYKTAIERPASLFGIKKGKIEEGYDADFMAFDFTNI 353
PRK08323 PRK08323
phenylhydantoinase; Validated
 234-361 1.69e-07

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 52.87  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 234 IHHLIKDDS--ACEDFNTAAK-LM-PPLRSKEDVLALREALKEGKISFLTSLHSA------KSISLKDlaFDEAAFGIHS 303
Cdd:PRK08323 261 PQYLLLDESeyDGPDWFEGAKyVMsPPLRDKEHQDALWRGLQDGDLQVVATDHCPfcfeqkKQLGRGD--FTKIPNGTPG 338

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 304 VCEFISLCYTFLIKEGFLNWQELCRFTSKNPSEFLGL--NSGVIEVGKEANLVLFDENEE 361
Cdd:PRK08323 339 VEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLypRKGTIAVGADADIVIWDPNAT 398
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 2-49 9.71e-07

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: 50.32  E-value: 9.71e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488945473   2 IIKNAKIY--GDSLQDIEIKEGKITNIGSNLQ---GEEILDAKGMTLLPSFVD 49
Cdd:cd01293    1 LLRNARLAdgGTALVDIAIEDGRIAAIGPALAvppDAEEVDAKGRLVLPAFVD 53
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-49 3.20e-06

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 48.80  E-value: 3.20e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473   1 MIIKNAKIY---GDSL---QDIEIKEGKITNIGSNLQ-----GEEILDAKGMTLLPSFVD 49
Cdd:COG1228   10 LLITNATLVdgtGGGVienGTVLVEDGKIAAVGPAADlavpaGAEVIDATGKTVLPGLID 69
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 1-50 6.50e-06

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: 47.57  E-value: 6.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488945473   1 MIIKNAKIY-GDSLQD--IEIKEGKITNIGSNL---QGEEILDAKGMTLLPSFVDL 50
Cdd:cd00854    1 LIIKNARILtPGGLEDgaVLVEDGKIVAIGPEDeleEADEIIDLKGQYLVPGFIDI 56
PRK09236 PRK09236
dihydroorotase; Reviewed
 215-371 6.04e-05

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 44.86  E-value: 6.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 215 LSLKDSLVLLDEKDLKL------VSIHHLIKDDSACEDFNTAAKLMPPLRSKEDVLALREALKEGKISFLTSLHSAKSIS 288
Cdd:PRK09236 237 ISTAKELSLFENGPLAEkritaeVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADDRIDVIATDHAPHTWE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945473 289 LKDLAFDEAAFGI----HSVCEFISLCYtflikEGFLNWQELCRFTSKNPSEFLGL-NSGVIEVGKEANLVLFDENEEIF 363
Cdd:PRK09236 317 EKQGPYFQAPSGLplvqHALPALLELVH-----EGKLSLEKVVEKTSHAPAILFDIkERGFIREGYWADLVLVDLNSPWT 391


                 ....*...
gi 488945473 364 APKSSLYS 371
Cdd:PRK09236 392 VTKENILY 399
PRK05985 PRK05985
cytosine deaminase; Provisional
 1-49 1.07e-04

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 44.15  E-value: 1.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488945473   1 MIIKNAKIYGDSLQDIEIKEGKITNIGSNLQ---GEEILDAKGMTLLPSFVD 49
Cdd:PRK05985   4 LLFRNVRPAGGAAVDILIRDGRIAAIGPALAappGAEVEDGGGALALPGLVD 55
PRK09230 PRK09230
cytosine deaminase; Provisional
 1-49 1.09e-04

cytosine deaminase; Provisional


Pssm-ID: 181713  Cd Length: 426  Bit Score: 43.92  E-value: 1.09e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488945473   1 MIIKNAKIYG-DSLQDIEIKEGKITNIGSN----LQGEEILDAKGMTLLPSFVD 49
Cdd:PRK09230   6 MTIKNARLPGkEGLWQITIEDGKISAIEPQseasLEAGEVLDAEGGLAIPPFIE 59
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
1-50 1.27e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 43.69  E-value: 1.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488945473   1 MIIKNAKI-----YGDSLQDIEIKEGKITNIGSNL---QGEEILDAKGMTLLPSFVDL 50
Cdd:PRK09237   1 LLLRGGRVidpanGIDGVIDIAIEDGKIAAVAGDIdgsQAKKVIDLSGLYVSPGWIDL 58
PRK06846 PRK06846
putative deaminase; Validated
 13-58 1.57e-04

putative deaminase; Validated


Pssm-ID: 235873 [Multi-domain]  Cd Length: 410  Bit Score: 43.46  E-value: 1.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488945473  13 LQDIEIKEGKITNIGSN----LQGEEILDAKGMTLLPSFVDLCVSLknDK 58
Cdd:PRK06846  31 LCTLEIQDGKIVAIRPNkqvpDATLPTYDANGLLMLPAFREMHIHL--DK 78
PRK07572 PRK07572
cytosine deaminase; Validated
 1-49 2.01e-04

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 43.08  E-value: 2.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488945473   1 MIIKNAKIY-GDSLQDIEIKEGKITNIGSNLQGE--EILDAKGMTLLPSFVD 49
Cdd:PRK07572   4 LIVRNANLPdGRTGIDIGIAGGRIAAVEPGLQAEaaEEIDAAGRLVSPPFVD 55
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 315-359 2.86e-04

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: 42.57  E-value: 2.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488945473 315 LIKEGFLNWQELCRFTSKNPSEFLGLNS--GVIEVGKEANLVLFDEN 359
Cdd:cd00854  318 MVKWGGCPLEEAVRMASLNPAKLLGLDDrkGSLKPGKDADLVVLDDD 364
PRK08323 PRK08323
phenylhydantoinase; Validated
 1-49 3.30e-04

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 42.47  E-value: 3.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488945473   1 MIIKNAKI---YGDSLQDIEIKEGKITNIGSNlQGEEILDAKGMTLLPSFVD 49
Cdd:PRK08323   3 TLIKNGTVvtaDDTYKADVLIEDGKIAAIGAN-LGDEVIDATGKYVMPGGID 53
PRK09060 PRK09060
dihydroorotase; Validated
 1-49 3.41e-04

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 42.60  E-value: 3.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488945473   1 MIIKNAKIY---GDSLQDIEIKEGKITNIGSNLQGE--EILDAKGMTLLPSFVD 49
Cdd:PRK09060   7 LILKGGTVVnpdGEGRADIGIRDGRIAAIGDLSGASagEVIDCRGLHVLPGVID 60
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
1-49 4.67e-04

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 42.09  E-value: 4.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945473   1 MIIKNAKIY-GDSLQD----IEIKEGKITNIGSN-----LQGE--EILDAKGMTLLPSFVD 49
Cdd:COG1574   10 LLLTNGRIYtMDPAQPvaeaVAVRDGRIVAVGSDaevraLAGPatEVIDLGGKTVLPGFID 70
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 1-48 8.75e-04

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: 41.03  E-value: 8.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945473   1 MIIKNA--------KIYGDSlqDIEIKEGKITNIGSNL-----QGEEILDAKGMTLLPSFV 48
Cdd:cd01298    1 ILIRNGtivttdprRVLEDG--DVLVEDGRIVAVGPALplpayPADEVIDAKGKVVMPGLV 59
PRK09061 PRK09061
D-glutamate deacylase; Validated
 11-50 4.34e-03

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 38.91  E-value: 4.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 488945473  11 DSLQDIEIKEGKITNIGSN-LQGEEILDAKGMTLLPSFVDL 50
Cdd:PRK09061  36 DAVRDVGIKGGKIAAVGTAaIEGDRTIDATGLVVAPGFIDL 76
PRK09236 PRK09236
dihydroorotase; Reviewed
 2-49 4.89e-03

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 38.70  E-value: 4.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488945473   2 IIKNAKIYGDSLQ---DIEIKEGKITNIGSNL---QGEEILDAKGMTLLPSFVD 49
Cdd:PRK09236   5 LIKNARIVNEGKIfegDVLIENGRIAKIASSIsakSADTVIDAAGRYLLPGMID 58
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 1-50 8.68e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 37.86  E-value: 8.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488945473   1 MIIKNAK-IYGDSLQ----DIEIKEGKITNIGSNLQ--GEEILDAKGMTLLPSFVDL 50
Cdd:PRK08393   3 ILIKNGYvIYGENLKviraDVLIEGNKIVEVKRNINkpADTVIDASGSVVSPGFINA 59
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 15-50 9.68e-03

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: 37.88  E-value: 9.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488945473  15 DIEIKEGKITNIGSN------LQGEEILDAKGMTLLPSFVDL 50
Cdd:COG0402   23 AVLVEDGRIAAVGPGaelparYPAAEVIDAGGKLVLPGLVNT 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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