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Conserved domains on  [gi|1935598052|ref|NP_113893|]
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dihydropyrimidinase [Rattus norvegicus]

Protein Classification

hydantoinase/dihydropyrimidinase family protein( domain architecture ID 10101418)

hydantoinase/dihydropyrimidinase family protein similar to Homo sapiens dihydropyrimidinase that catalyzes the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
7-460 0e+00

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: 731.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQG 86
Cdd:cd01314     1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPG----GVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYKD 166
Cdd:cd01314    77 TRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 167 LYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:cd01314   156 LLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 247 VHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWnKEWRHAAHHVMGPPLRPDpSTPGFLMNLLANGDLTTTGSD 326
Cdd:cd01314   236 VHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 327 NCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIW 406
Cdd:cd01314   314 HCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIW 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1935598052 407 DPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHG 460
Cdd:cd01314   394 DPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
 
Name Accession Description Interval E-value
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
7-460 0e+00

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: 731.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQG 86
Cdd:cd01314     1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPG----GVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYKD 166
Cdd:cd01314    77 TRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 167 LYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:cd01314   156 LLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 247 VHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWnKEWRHAAHHVMGPPLRPDpSTPGFLMNLLANGDLTTTGSD 326
Cdd:cd01314   236 VHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 327 NCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIW 406
Cdd:cd01314   314 HCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIW 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1935598052 407 DPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHG 460
Cdd:cd01314   394 DPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
7-465 0e+00

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: 640.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQG 86
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPD----AVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAQDKGVNSFKMFMAYKD 166
Cdd:TIGR02033  77 TKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 167 LYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:TIGR02033 157 LLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 247 VHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWnKEWRHAAHHVMGPPLRpDPSTPGFLMNLLANGDLTTTGSD 326
Cdd:TIGR02033 237 VHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSD 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 327 NCTFNTCQK-ALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVI 405
Cdd:TIGR02033 315 HCTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVI 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 406 WDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPR 465
Cdd:TIGR02033 395 WDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
PRK08323 PRK08323
phenylhydantoinase; Validated
6-468 0e+00

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 637.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDllppgdtsRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQ 85
Cdd:PRK08323    2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN--------LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFET 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  86 GTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYK 165
Cdd:PRK08323   74 GTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 166 DLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLY 245
Cdd:PRK08323  153 GALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 246 IVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWNKEWRHAAHHVMGPPLRPDPSTpGFLMNLLANGDLTTTGS 325
Cdd:PRK08323  233 IVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDKEHQ-DALWRGLQDGDLQVVAT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 326 DNCTFNTCQKA-LGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIV 404
Cdd:PRK08323  312 DHCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIV 391
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935598052 405 IWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPRQPF 468
Cdd:PRK08323  392 IWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPF 455
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
8-465 3.48e-145

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: 424.12  E-value: 3.48e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   8 LIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQsvDDFHQGT 87
Cdd:COG0044     1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAA----EVIDATGLLVLPGLIDLHVHLREPGLEHK--EDIETGT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  88 KAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYKDL 167
Cdd:COG0044    75 RAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 168 YMVQD-QQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKkmlALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:COG0044   154 NPVLDdGLLRRALEYAAEFGALVAVHAEDPDLIRGGVM---NEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 247 VHVMSKSAAKVIADAKREGKVVYGE--P-----IAAGLGTDGTQYwnkewrhaahhVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:COG0044   231 VHVSTAEAVELIREAKARGLPVTAEvcPhhltlTDEDLERYGTNF-----------KVNPPLR-TEEDREALWEGLADGT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 320 LTTTGSDNCTFNTCQKAlgkDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGS 399
Cdd:COG0044   299 IDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGA 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935598052 400 DADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFdVTAGHGKFIPR 465
Cdd:COG0044   375 DADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
58-447 3.53e-23

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: 100.27  E-value: 3.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  58 LVLPGGIDTHTHMQFPFM------GSQSVDDFHQGTKAALAGGTTMIIDFAI--PQKGSSLIEAFEtwRNWADPKVC--- 126
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLrgipvpPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAE--ELPLGLRFLgpg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 127 ----CDYSLHVAVTWWsDKVKEEMKTLAQDKGVNSFKMFMAYKDlYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEG 202
Cdd:pfam01979  79 csldTDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPHGA-PTFSDDELKAALEEAKKYGLPVAIHALETKGEVED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 203 AKKmlALGITGPEGHELcrpEAVEAEATLRAITIASAVNcplyiVHVMSKSAAKVIADAKREGkvVYGEPIAAGLGTDGT 282
Cdd:pfam01979 157 AIA--AFGGGIEHGTHL---EVAESGGLLDIIKLILAHG-----VHLSPTEANLLAEHLKGAG--VAHCPFSNSKLRSGR 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 283 qywnkewrhaahhvmgPPLRPdpstpgflmnLLANGDLTTTGSDNCtfntcqkaLGKDDFTKIPNGVNGVEDRmsviwek 362
Cdd:pfam01979 225 ----------------IALRK----------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 363 GVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATrtisakthhqavnfNIFEGMVCHGVPLVTIS 442
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIV 329

                  ....*
gi 1935598052 443 RGRVV 447
Cdd:pfam01979 330 KGKIV 334
 
Name Accession Description Interval E-value
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
7-460 0e+00

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: 731.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQG 86
Cdd:cd01314     1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPG----GVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYKD 166
Cdd:cd01314    77 TRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 167 LYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:cd01314   156 LLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 247 VHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWnKEWRHAAHHVMGPPLRPDpSTPGFLMNLLANGDLTTTGSD 326
Cdd:cd01314   236 VHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 327 NCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIW 406
Cdd:cd01314   314 HCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIW 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1935598052 407 DPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHG 460
Cdd:cd01314   394 DPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
7-465 0e+00

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: 640.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQG 86
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPD----AVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAQDKGVNSFKMFMAYKD 166
Cdd:TIGR02033  77 TKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 167 LYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:TIGR02033 157 LLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 247 VHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWnKEWRHAAHHVMGPPLRpDPSTPGFLMNLLANGDLTTTGSD 326
Cdd:TIGR02033 237 VHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSD 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 327 NCTFNTCQK-ALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVI 405
Cdd:TIGR02033 315 HCTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVI 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 406 WDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPR 465
Cdd:TIGR02033 395 WDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
PRK08323 PRK08323
phenylhydantoinase; Validated
6-468 0e+00

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 637.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDllppgdtsRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQ 85
Cdd:PRK08323    2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN--------LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFET 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  86 GTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYK 165
Cdd:PRK08323   74 GTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 166 DLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLY 245
Cdd:PRK08323  153 GALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 246 IVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWNKEWRHAAHHVMGPPLRPDPSTpGFLMNLLANGDLTTTGS 325
Cdd:PRK08323  233 IVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDKEHQ-DALWRGLQDGDLQVVAT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 326 DNCTFNTCQKA-LGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIV 404
Cdd:PRK08323  312 DHCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIV 391
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935598052 405 IWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPRQPF 468
Cdd:PRK08323  392 IWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPF 455
PLN02942 PLN02942
dihydropyrimidinase
1-491 0e+00

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 623.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   1 MAPQERLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLlppgDTSRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSV 80
Cdd:PLN02942    1 GASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNL----KVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  81 DDFHQGTKAALAGGTTMIIDFAIPQKGSsLIEAFETWRNWADpKVCCDYSLHVAVTWWSDKVKEEMKTLAQDKGVNSFKM 160
Cdd:PLN02942   77 DDFFSGQAAALAGGTTMHIDFVIPVNGN-LLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 161 FMAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAV 240
Cdd:PLN02942  155 FMAYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 241 NCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWNKEWRHAAHHVMGPPLRPdPSTPGFLMNLLANGDL 320
Cdd:PLN02942  235 NTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGIL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 321 TTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSD 400
Cdd:PLN02942  314 QLVGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSD 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 401 ADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPRQPFAeFIYKRVKQRD 480
Cdd:PLN02942  394 ADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKAD 472
                         490
                  ....*....|....
gi 1935598052 481 QTCTP---IPVKRA 491
Cdd:PLN02942  473 AAYLSslrAPVKRT 486
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
8-465 3.48e-145

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: 424.12  E-value: 3.48e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   8 LIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQsvDDFHQGT 87
Cdd:COG0044     1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAA----EVIDATGLLVLPGLIDLHVHLREPGLEHK--EDIETGT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  88 KAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYKDL 167
Cdd:COG0044    75 RAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 168 YMVQD-QQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKkmlALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:COG0044   154 NPVLDdGLLRRALEYAAEFGALVAVHAEDPDLIRGGVM---NEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 247 VHVMSKSAAKVIADAKREGKVVYGE--P-----IAAGLGTDGTQYwnkewrhaahhVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:COG0044   231 VHVSTAEAVELIREAKARGLPVTAEvcPhhltlTDEDLERYGTNF-----------KVNPPLR-TEEDREALWEGLADGT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 320 LTTTGSDNCTFNTCQKAlgkDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGS 399
Cdd:COG0044   299 IDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGA 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935598052 400 DADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFdVTAGHGKFIPR 465
Cdd:COG0044   375 DADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
PRK13404 PRK13404
dihydropyrimidinase; Provisional
3-465 1.43e-132

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 393.29  E-value: 1.43e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   3 PQERLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPpgdtsrGLRILDAAGKLVLPGGIDTHTHM-QFPFMGSQSVD 81
Cdd:PRK13404    2 MAFDLVIRGGTVVTATDTFQADIGIRGGRIAALGEGLGP------GAREIDATGRLVLPGGVDSHCHIdQPSGDGIMMAD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  82 DFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKV-KEEMKTLAQDkGVNSFKM 160
Cdd:PRK13404   76 DFYTGTVSAAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 161 FMAYKDLyMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAV 240
Cdd:PRK13404  155 FMTYDDL-KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 241 NCPLYIVHVMSKSAAKVIADAKREGKVVYGEP-------IAAGLGTDGTqywnkewrHAAHHVMGPPLRpDPSTPGFLMN 313
Cdd:PRK13404  234 DVPILIVHVSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGM--------EGAKYICSPPPR-DKANQEAIWN 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 314 LLANGDLTTTGSDNCTFN---TCQKALGKDD--FTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNL 388
Cdd:PRK13404  305 GLADGTFEVFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGL 384
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1935598052 389 YPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPR 465
Cdd:PRK13404  385 YPRKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
7-463 2.66e-76

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: 247.20  E-value: 2.66e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQG 86
Cdd:cd01315     2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTE----AEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDF---AIPQkgSSLIEAFETWRNWADPKvccdysLHVAVTWWSDKVK---EEMKTLAqDKGVNSFKM 160
Cdd:cd01315    76 TKAAAAGGITTIIDMplnSIPP--TTTVENLEAKLEAAQGK------LHVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKC 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 161 FMA---YKDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIA 237
Cdd:cd01315   147 FLCpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 238 SAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYwnkEWRHAAHHVmGPPLRpDPSTPGFLMNLLAN 317
Cdd:cd01315   227 KETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDV---PDGGTEFKC-APPIR-DAANQEQLWEALEN 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 318 GDLTTTGSDN--CTFNtcQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRI 395
Cdd:cd01315   302 GDIDMVVSDHspCTPE--LKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRI 379
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935598052 396 AVGSDADIVIWDPEATRTISA---KTHHQAvnfNIFEGMVCHGVPLVTISRGRVVYEAGVFdVTAGHGKFI 463
Cdd:cd01315   380 AVGYDADFVVWDPEEEFTVDAedlYYKNKI---SPYVGRTLKGRVHATILRGTVVYQDGEV-VGEPLGQLL 446
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
57-440 1.46e-70

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: 228.82  E-value: 1.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  57 KLVLPGGIDTHTHMQFPFMGSQSvDDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVt 136
Cdd:cd01302     1 LLVLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 137 wWSDKVKEEMKtLAQDKGVNSFKMFMAYK--DLYMVQDQQMYAAFSQCKEIGAIAQVHAEngdliaegakkmlalgitgp 214
Cdd:cd01302    79 -GPGDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 215 eghelcrpeaveaeatlRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPiaaglgtdGTQYWN---KEWRH 291
Cdd:cd01302   137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEV--------CPHHLFldeSMLRL 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 292 AAHH-VMGPPLRPdPSTPGFLMNLLANGDLTTTGSDNCTFNTCQKALGKDdFTKIPNGVNGVEDRMSVIWEKGVHSGkMD 370
Cdd:cd01302   192 NGAWgKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTEGVKRG-LS 268
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 371 ENRFVAVTSTNAAKIFNLYPKKgRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVT 440
Cdd:cd01302   269 LETLVEILSENPARIFGLYPKG-TIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
PRK02382 PRK02382
dihydroorotase; Provisional
7-464 4.58e-60

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 204.50  E-value: 4.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLlppgDTSRGLRILDAAGKLVLPGGIDTHTHmqFPFMGSQSVDDFHQG 86
Cdd:PRK02382    4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDL----DGSSSEEVIDARGMLLLPGGIDVHVH--FREPGYTHKETWYTG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDfaIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMktlaqDKGVNSF-KMFMA 163
Cdd:PRK02382   78 SRSAAAGGVTTVVD--QPNTDPPTVdgESFDEKAELAARKSIVDFGINGGVTGNWDPLESLW-----ERGVFALgEIFMA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 164 YKDLYMVQDQQMYA-AFSQCKEIGAIAQVHAENGDLIAEGAKkmLALGITGPEGHELCRPEAVEAEATLRAITIASAVNC 242
Cdd:PRK02382  151 DSTGGMGIDEELFEeALAEAARLGVLATVHAEDEDLFDELAK--LLKGDADADAWSAYRPAAAEAAAVERALEVASETGA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 243 PLYIVHVmskSAAKVIADAKREGKVVYGEPIAAGLGTDgtqywnkEW-RHAAHHVMGPPLRPDPSTPGfLMNLLANGDLT 321
Cdd:PRK02382  229 RIHIAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWeRLGTFGKMNPPLRSEKRREA-LWERLNDGTID 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 322 TTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGSDA 401
Cdd:PRK02382  298 VVASDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDA 372
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935598052 402 DIVIWDPEATRTISAKTHHQAVNFNIFEGMVchGV-PLVTISRGRVVYEAGVFDVTAGHGKFIP 464
Cdd:PRK02382  373 DLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
PRK06189 PRK06189
allantoinase; Provisional
7-467 3.27e-54

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 189.14  E-value: 3.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGDtsrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQG 86
Cdd:PRK06189    5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-----EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDFAIPQKGSSLI-EAFETWRNWADPKVCCDYSLhvavtwWSDKV---KEEMKTLAqDKGVNSFKMFM 162
Cdd:PRK06189   78 SAALAAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVpgnLEHLRELA-EAGVIGFKAFM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 163 AY---KDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASA 239
Cdd:PRK06189  151 SNsgtDEFRSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 240 VNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYwnkeWRHAAHHVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:PRK06189  231 TGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDF----ERIGAVAKCAPPLR-SRSQKEELWRGLLAGE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 320 LTTTGSDNctfNTCQKALGK-DDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVG 398
Cdd:PRK06189  306 IDMISSDH---SPCPPELKEgDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVG 381
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935598052 399 SDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAgHGKFIPRQP 467
Cdd:PRK06189  382 ADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPPP-RGQLLRPSV 449
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
23-450 1.39e-52

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: 183.80  E-value: 1.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  23 ADVLVEDGVVRALGRDLLPPGDTsrglrILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGTTMIIDFA 102
Cdd:TIGR00857   6 VDILVEGGRIKKIGKLRIPPDAE-----VIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 103 IPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWwSDKVKEEMKtlaqdkgvnSFKMFMA------YKDlYMVQDQQ-- 174
Cdd:TIGR00857  79 NTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQ-GNQGKELTE---------AYELKEAgavgrmFTD-DGSEVQDil 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 175 -MYAAFSQCKEIGAIAQVHAENGDLIAEGAKKmlaLGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSKS 253
Cdd:TIGR00857 148 sMRRALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 254 AAKVIADAKREGKVVYGE--P--------IAAGLGTdgtqyWNKewrhaahhvMGPPLRPdPSTPGFLMNLLANGDLTTT 323
Cdd:TIGR00857 225 SLELIVKAKSQGIKITAEvtPhhlllseeDVARLDG-----NGK---------VNPPLRE-KEDRLALIEGLKDGIIDII 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 324 GSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGSDADI 403
Cdd:TIGR00857 290 ATDHAPHTLEEKTKE---FAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADI 364
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1935598052 404 VIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEA 450
Cdd:TIGR00857 365 TVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
pyrC PRK09357
dihydroorotase; Validated
6-450 4.62e-41

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 152.66  E-value: 4.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVVN-DDFSQVADVLVEDGVVRALGRDLLPPGDTsrglrILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFH 84
Cdd:PRK09357    2 MILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENIEAEGAE-----VIDATGLVVAPGLVDLHVHLREP--GQEDKETIE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  85 QGTKAALAGG---------TTMIIDfaipqkgsSLIEAFETWRNWADPKVCcdyslHV----AVTWWSD-KVKEEMKTLA 150
Cdd:PRK09357   75 TGSRAAAAGGfttvvampnTKPVID--------TPEVVEYVLDRAKEAGLV-----DVlpvgAITKGLAgEELTEFGALK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 151 qDKGVnsfkmFMAYKDLYMVQDQQ-MYAAFSQCKEIG-AIAQvHAENGDLIAEGA----KKMLALGITGpeghelcRPEA 224
Cdd:PRK09357  142 -EAGV-----VAFSDDGIPVQDARlMRRALEYAKALDlLIAQ-HCEDPSLTEGGVmnegEVSARLGLPG-------IPAV 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 225 VEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGE--PiaaglgtdgtqywnkewrhaaHHV------ 296
Cdd:PRK09357  208 AEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEvtP---------------------HHLlltded 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 297 ---------MGPPLRpDPSTPGFLMNLLANGDLTTTGSD---------NCtfntcqkalgkdDFTKIPNGVNGVEDRMSV 358
Cdd:PRK09357  267 lltydpnykVNPPLR-TEEDREALIEGLKDGTIDAIATDhaphareekEC------------EFEAAPFGITGLETALSL 333
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 359 IWEKGVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPL 438
Cdd:PRK09357  334 LYTTLVKTGLLDLEQLLEKMTINPARILGL--PAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVV 411
                         490
                  ....*....|..
gi 1935598052 439 VTISRGRVVYEA 450
Cdd:PRK09357  412 YTIVDGKIVYQD 423
PRK08044 PRK08044
allantoinase AllB;
7-464 2.97e-39

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 148.47  E-value: 2.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLlppgdtSRGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQG 86
Cdd:PRK08044    5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL------GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIIDFAIPQKGSSLIEA-FETWRNWADPKVCCDY-SLHVAVTWWSDKVKEemktlAQDKGVNSFKMFMAY 164
Cdd:PRK08044   77 TRAAAKGGITTMIEMPLNQLPATVDRAsIELKFDAAKGKLTIDAaQLGGLVSYNLDRLHE-----LDEVGVVGFKCFVAT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 165 -------KDLYMVQDQQMYAAFSQCKEIGAIAQVHAENG---DLIAEGAKKMlalGITGPEGHELCRPEAVEAEATLRAI 234
Cdd:PRK08044  152 cgdrgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKRE---GRVTAHDYVASRPVFTEVEAIRRVL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 235 TIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYwnKEWRHAAHhvMGPPLRpDPSTPGFLMNL 314
Cdd:PRK08044  229 YLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF--EEIGTLAK--CSPPIR-DLENQKGMWEK 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 315 LANGDLTTTGSDNctfNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGR 394
Cdd:PRK08044  304 LFNGEIDCLVSDH---SPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGR 379
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935598052 395 IAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVY--EAGVfdVTAGHGKFIP 464
Cdd:PRK08044  380 IAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYdiEQGF--PVAPKGQFIL 449
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
56-444 1.16e-38

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: 144.78  E-value: 1.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  56 GKLVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAV 135
Cdd:cd01318     1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 136 TwwSDKVKEEMKTLaqdkGVNSFKMFMA--YKDLyMVQDQQMYAAFSQCKEIGAiaqVHAENGDLIAEGAKKMLALGItg 213
Cdd:cd01318    79 T--GSEDLEELDKA----PPAGYKIFMGdsTGDL-LDDEETLERIFAEGSVLVT---FHAEDEDRLRENRKELKGESA-- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 214 pegHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKV-------VYGEPIAAGLGTdgtqyWN 286
Cdd:cd01318   147 ---HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT-----LG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 287 KewrhaahhvMGPPLRPDPSTPGfLMNLLANGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHS 366
Cdd:cd01318   219 K---------VNPPLRSREDRKA-LLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLTL-VNK 284
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935598052 367 GKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRG 444
Cdd:cd01318   285 GILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
48-440 3.24e-35

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: 135.44  E-value: 3.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  48 GLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGTTMII-----DFAIPQKgssliEAFETWRNWAD 122
Cdd:cd01317     1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVcmpntNPVIDNP-----AVVELLKNRAK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 123 PkvccdySLHVAVTWWS-----DKVKE--EMKTLAqDKGVNSFKmfmayKDLYMVQDQQ-MYAAFSQCKEIGAIAQVHAE 194
Cdd:cd01317    74 D------VGIVRVLPIGaltkgLKGEEltEIGELL-EAGAVGFS-----DDGKPIQDAElLRRALEYAAMLDLPIIVHPE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 195 NGDLIAEGA----KKMLALGITGpeghelcRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGkvvyg 270
Cdd:cd01317   142 DPSLAGGGVmnegKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG----- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 271 EPIAAG------------LGTDGTqywnkewrhaAHHVMgPPLRpDPSTPGFLMNLLANGDLTTTGSDNCTFNTCQKALG 338
Cdd:cd01317   210 LPVTAEvtphhlllddeaLESYDT----------NAKVN-PPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 339 KDDftkIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPkkGRIAVGSDADIVIWDPEATRTISAKT 418
Cdd:cd01317   278 FAE---APPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEET 352
                         410       420
                  ....*....|....*....|..
gi 1935598052 419 HHQAVNFNIFEGMVCHGVPLVT 440
Cdd:cd01317   353 FRSKSKNTPFDGQKLKGRVLAT 374
PLN02795 PLN02795
allantoinase
12-451 8.82e-35

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 136.83  E-value: 8.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  12 GRVVNDDFSQVADVLVEDGVVRALGRDLLPPGDTSRGlRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAAL 91
Cdd:PLN02795   51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKSQKKP-HVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  92 AGGTTMIIDF---AIPQKGSSliEAFETWRNWADPKvccdysLHVAVTWWSDKVKE------EMKTLAqDKGVNSFKMFM 162
Cdd:PLN02795  128 AGGITTLVDMplnSFPSTTSV--ETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGALGLKSFM 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 163 ---AYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAkkMLALGITGPEGHELCRPEAVEAEATLRAITIAS- 238
Cdd:PLN02795  199 cpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKd 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 239 ------AVNCPLYIVHVM-SKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWNKEWRHAAhhvmGPPLRpDPSTPGFL 311
Cdd:PLN02795  277 trpggvAEGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKC----APPIR-DAANRELL 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 312 MNLLANGDLTTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGkMDENRFVAVTSTNAAKIFNLyPK 391
Cdd:PLN02795  352 WKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-DS 429
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935598052 392 KGRIAVGSDADIVIWDPEATRTI--SAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAG 451
Cdd:PLN02795  430 KGAIAPGKDADIVVWDPEAEFVLdeSYPIYHKHKSLSPYLGTKLSGKVIATFVRGNLVFLEG 491
PRK09060 PRK09060
dihydroorotase; Validated
7-447 5.82e-34

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 133.51  E-value: 5.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRdllpPGDTSRGlRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQG 86
Cdd:PRK09060    7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD----LSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAGGTTMIidFAIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTwwSDKVkEEMKTLAQDKGVNSFKMFM-- 162
Cdd:PRK09060   80 SRAAVLGGVTAV--FEMPNTNPLTTtaEALADKLARARHRMHCDFAFYVGGT--RDNA-DELAELERLPGCAGIKVFMgs 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 163 AYKDLyMVQDQQMYAAFsqCKEIGAIAQVHAENGDLIAEgaKKMLAlgITG-PEGHELCRPEAVEAEATLRAITIASAVN 241
Cdd:PRK09060  155 STGDL-LVEDDEGLRRI--LRNGRRRAAFHSEDEYRLRE--RKGLR--VEGdPSSHPVWRDEEAALLATRRLVRLARETG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 242 CPLYIVHVMSKSAAKVIADAKREGKV--------VYGEPIAAGLGTdgtqywnkewrhaaHHVMGPPLRpDPSTPGFLMN 313
Cdd:PRK09060  228 RRIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT--------------LAQMNPPIR-DARHRDGLWR 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 314 LLANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPKKG 393
Cdd:PRK09060  293 GVRQGVVDVLGSDHAPHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKG 367
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1935598052 394 RIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVV 447
Cdd:PRK09060  368 RIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRV 421
PRK07575 PRK07575
dihydroorotase; Provisional
3-461 3.44e-30

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 122.48  E-value: 3.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   3 PQERLLIRGGRVVNDDFS-QVADVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVD 81
Cdd:PRK07575    1 MMMSLLIRNARILLPSGElLLGDVLVEDGKIVAIAPEISATAVD----TVIDAEGLTLLPGVIDPQVHFREP--GLEHKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  82 DFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTwwSDKVKEemktLAQDKGVNSFKMF 161
Cdd:PRK07575   75 DLFTASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT--PDNLPE----LLTANPTCGIKIF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 162 M--AYKDLYMVQDQQMYAAFSQCKEIgaIAqVHAENGDLIAEgAKKMLAlGITGPEGHELCRPEAVEAEATLRAITIASA 239
Cdd:PRK07575  149 MgsSHGPLLVDEEAALERIFAEGTRL--IA-VHAEDQARIRA-RRAEFA-GISDPADHSQIQDEEAALLATRLALKLSKK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 240 VNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQywnkewRHAAHHVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:PRK07575  224 YQRRLHILHLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTDAYE------RIGTLAQMNPPLR-SPEDNEALWQALRDGV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 320 LTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGS 399
Cdd:PRK07575  297 IDFIATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGY 371
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935598052 400 DADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDvTAGHGK 461
Cdd:PRK07575  372 DADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVN-TEVRGQ 432
PRK04250 PRK04250
dihydroorotase; Provisional
12-451 1.21e-24

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 105.62  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  12 GRVVNddfsqvADVLVEDGVVRALGRDLLppgdtsRGLRILDAAGKLVLPGGIDTHTHMQfpfmgsqsvdDFHQ------ 85
Cdd:PRK04250   10 GRIVE------GGIGIENGRISKISLRDL------KGKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketi 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  86 --GTKAALAGGTTMIIDfaIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLaqdkgvnsFKMF 161
Cdd:PRK04250   68 esGTKAALHGGITLVFD--MPNTKPPIMdeKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADF--------YKIF 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 162 M--AYKDLYMVQDQQMYaafsqcKEIGAIAQVHAENGDLIAEGakkmlalgitgPEghelcRPEAVEAEATLRAITIASA 239
Cdd:PRK04250  138 MgaSTGGIFSENFEVDY------ACAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKK 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 240 VNCPLYIVHVMSKSAAKVIadAKREGKVVYGEPIAAGLgtdgtQYWNKEWRHAAHHVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:PRK04250  196 LKKPLHICHISTKDGLKLI--LKSNLPWVSFEVTPHHL-----FLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 320 LttTGSDNCTFNTCQKALGKddftkipNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLypkKGR-IAVG 398
Cdd:PRK04250  268 I--IASDHAPHTLEDKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFGI---KNYgIEEG 334
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1935598052 399 SDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAG 451
Cdd:PRK04250  335 NYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
58-447 3.53e-23

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: 100.27  E-value: 3.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  58 LVLPGGIDTHTHMQFPFM------GSQSVDDFHQGTKAALAGGTTMIIDFAI--PQKGSSLIEAFEtwRNWADPKVC--- 126
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLrgipvpPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAE--ELPLGLRFLgpg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 127 ----CDYSLHVAVTWWsDKVKEEMKTLAQDKGVNSFKMFMAYKDlYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEG 202
Cdd:pfam01979  79 csldTDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPHGA-PTFSDDELKAALEEAKKYGLPVAIHALETKGEVED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 203 AKKmlALGITGPEGHELcrpEAVEAEATLRAITIASAVNcplyiVHVMSKSAAKVIADAKREGkvVYGEPIAAGLGTDGT 282
Cdd:pfam01979 157 AIA--AFGGGIEHGTHL---EVAESGGLLDIIKLILAHG-----VHLSPTEANLLAEHLKGAG--VAHCPFSNSKLRSGR 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 283 qywnkewrhaahhvmgPPLRPdpstpgflmnLLANGDLTTTGSDNCtfntcqkaLGKDDFTKIPNGVNGVEDRmsviwek 362
Cdd:pfam01979 225 ----------------IALRK----------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 363 GVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATrtisakthhqavnfNIFEGMVCHGVPLVTIS 442
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIV 329

                  ....*
gi 1935598052 443 RGRVV 447
Cdd:pfam01979 330 KGKIV 334
PRK01211 PRK01211
dihydroorotase; Provisional
16-465 1.01e-21

dihydroorotase; Provisional


Pssm-ID: 179247 [Multi-domain]  Cd Length: 409  Bit Score: 97.24  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  16 NDDFSQVAdVLVEDGVVRALGRDLLPPGDTSrglriLDAAgklVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGT 95
Cdd:PRK01211   10 KGKFDYLE-IEVEDGKIKSIKKDAGNIGKKE-----LKGA---ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  96 TMIIDFA---IPQKGsslIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTlaqdkgvnSFKMFMA---YKDLYM 169
Cdd:PRK01211   79 TFIMDMPnnnIPIKD---YNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERSI--------GLKVYMGgttNTNGTD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 170 VQDQQMyaafSQCKEIGAIAQVHAENGDLIAEGAKKMLALgitgpEGHELCRPEAVEAEAT--LRAITIASAVncplyIV 247
Cdd:PRK01211  148 IEGGEI----KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVkyVKNLDLKTKI-----IA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 248 HVmskSAAKVIADAKREgkvvygepiaaglGTDGTQYWNKEWRHAAHHVMGPPLRpDPSTPGFLMNLLANGDLTTTGSDN 327
Cdd:PRK01211  214 HV---SSIDVIGRFLRE-------------VTPHHLLLNDDMPLGSYGKVNPPLR-DRWTQERLLEEYISGRFDILSSDH 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 328 CTFNTCQKAlgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWD 407
Cdd:PRK01211  277 APHTEEDKQ----EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFD 349
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935598052 408 PEATRTISAKTHHQAVNFNIFEGMVCHgVPLVTISRGRVV---YEagvfDVTAGHGKFIPR 465
Cdd:PRK01211  350 FTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVidnYE----LISERTGKFVPK 405
PRK09236 PRK09236
dihydroorotase; Reviewed
6-459 2.88e-15

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 77.99  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLlppgDTSRGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQ 85
Cdd:PRK09236    3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSI----SAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIAS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  86 GTKAALAGGTTMIIDF--AIPQkgSSLIEAFETWRNWADPKVCCDYSLHVAVTwwSDKVkEEMKTLaqDK----GVnsfK 159
Cdd:PRK09236   77 ESRAAVAGGITSFMEMpnTNPP--TTTLEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRL--DPkrvcGV---K 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 160 MFMAYKDLYM-VQDQQMYAA-FSQCKEIgaIAqVHAENGDLIAEGAKKMLAL---GITgPEGHELCRPEAVEAEATLRAI 234
Cdd:PRK09236  147 VFMGASTGNMlVDNPETLERiFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIRSAEACYKSSSLAV 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 235 TIASAVNCPLYIVHVmskSAAKVIA---DAKREGKVVYGEPIAAGLGTDGTQY--------WN-----KEWRHAahhvmg 298
Cdd:PRK09236  223 SLAKKHGTRLHVLHI---STAKELSlfeNGPLAEKRITAEVCVHHLWFDDSDYarlgnlikCNpaiktASDREA------ 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 299 pplrpdpstpgfLMNLLANGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVT 378
Cdd:PRK09236  294 ------------LRQALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKT 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 379 STNAAKIFNLyPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAG-VFDVTA 457
Cdd:PRK09236  358 SHAPAILFDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGqLVESCR 436

                  ..
gi 1935598052 458 GH 459
Cdd:PRK09236  437 GQ 438
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
2-432 3.52e-15

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 77.31  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   2 APQERLLIRGGRVVNDDFSQV---ADVLVEDGVVRALGR--DLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMQFPFMG 76
Cdd:COG1228     5 AQAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPaaDLAVPAGA----EVIDATGKTVLPGLIDAHTHLGLGGGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  77 SQS----------VDDFHQGTK---AALAGGTTMIIDfaipQKGSSL-----IEAFETWRNWADPKVCCDYSLHV---AV 135
Cdd:COG1228    81 AVEfeagggitptVDLVNPADKrlrRALAAGVTTVRD----LPGGPLglrdaIIAGESKLLPGPRVLAAGPALSLtggAH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 136 TWWSDKVKEEMKTLAQDkGVNSFKMFMAYKDLYMVQDqQMYAAFSQCKEIGAIAQVHAENgdliAEGAKKMLALGITGpe 215
Cdd:COG1228   157 ARGPEEARAALRELLAE-GADYIKVFAEGGAPDFSLE-ELRAILEAAHALGLPVAAHAHQ----ADDIRLAVEAGVDS-- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 216 ghelcrpeaveaeatlraitiasavncplyIVHVMSKSAAkVIADAKREGKVVYGePiAAGLGTDGTQYWNKEWRHAAHH 295
Cdd:COG1228   229 ------------------------------IEHGTYLDDE-VADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARK 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 296 VMGPPLRPdpstpgfLMNLLANGDLTTTGSDNctfntcqkalgkddftkipNGVNGVEDRMSVIWEKGVHSGkMDENR-F 374
Cdd:COG1228   276 VREAALAN-------ARRLHDAGVPVALGTDA-------------------GVGVPPGRSLHRELALAVEAG-LTPEEaL 328
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1935598052 375 VAVTStNAAKIFNLYPKKGRIAVGSDADIVIWDPEATRTISAkthHQAVNFNIFEGMV 432
Cdd:COG1228   329 RAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY---LEDVRAVMKDGRV 382
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
7-458 2.57e-14

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: 74.64  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVV----NDDFSqvADVLVEDGVVRALGRDLLPPGDtsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVdd 82
Cdd:cd01297     2 LVIRNGTVVdgtgAPPFT--ADVGIRDGRIAAIGPILSTSAR-----EVIDAAGLVVAPGFIDVHTHYDGQVFWDPDL-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  83 fhqgTKAALAGGTTMII----------DFAIPQKGSSLIEAF--------ETWRNWAD-----------PKVCCDY---S 130
Cdd:cd01297    73 ----RPSSRQGVTTVVLgncgvspapaNPDDLARLIMLMEGLvalgeglpWGWATFAEyldalearppaVNVAALVghaA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 131 LHVAVTWWSDKVK-----EEMKTLAqDKGVNS----FKMFMAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAEN-GDLIA 200
Cdd:cd01297   149 LRRAVMGLDAREAteeelAKMRELL-REALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSIL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 201 EGAKKMLALGitgpeghelcrpeaveaEATLRAITIASAVNCPLYIVHVMSKSAAkVIADAKREGKVVYGE--PIAAGLG 278
Cdd:cd01297   228 EALDELLRLG-----------------RETGRPVHISHLKSAGAPNWGKIDRLLA-LIEAARAEGLQVTADvyPYGAGSE 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 279 TDgtqywnKEWRHAAHHVM-----GPPLRPDPSTpgflmnllangdltttgsdNCTFNtcqKALGKddftkipngvnGVE 353
Cdd:cd01297   290 DD------VRRIMAHPVVMggsdgGALGKPHPRS-------------------YGDFT---RVLGH-----------YVR 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 354 DRMSVIWEKGVHsgKMdenrfvavtSTNAAKIFNLYpKKGRIAVGSDADIVIWDPEatrTISAKTHHQAVNFNifegmvC 433
Cdd:cd01297   331 ERKLLSLEEAVR--KM---------TGLPARVFGLA-DRGRIAPGYRADIVVFDPD---TLADRATFTRPNQP------A 389
                         490       500
                  ....*....|....*....|....*.
gi 1935598052 434 HGVPLVTISrGRVVYEAGVF-DVTAG 458
Cdd:cd01297   390 EGIEAVLVN-GVPVVRDGAFtGARPG 414
PRK09059 PRK09059
dihydroorotase; Validated
7-450 9.76e-12

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 66.98  E-value: 9.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVND--DFSQVADVLVEDGVVRALGRDLLPPGdTSRGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFH 84
Cdd:PRK09059    5 ILLANARIIDPsrGLDEIGTVLIEDGVIVAAGKGAGNQG-APEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  85 QGTKAALAGGTTMII-----DFAIPQkgSSLIE-AFETWRNWADPKVccdyslHVAVTWWSDKVKEEMKT--LAQDKGVN 156
Cdd:PRK09059   82 SASRAAAAGGVTSIImmpdtDPVIDD--VALVEfVKRTARDTAIVNI------HPAAAITKGLAGEEMTEfgLLRAAGAV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 157 SFkmfmaYKDLYMVQDQQ-MYAAFSQCKEIGAIAQVHAENGDLIAEGA--KKMLA--LGITG-PeghelCRPEAVEAEAT 230
Cdd:PRK09059  154 AF-----TDGRRSVANTQvMRRALTYARDFDAVIVHETRDPDLGGNGVmnEGLFAswLGLSGiP-----REAEVIPLERD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 231 LR--AITI----ASAVNCPLyivhvmsksAAKVIADAKREgkvvyGEPIAAGLGTDGTQYwNK----EWRhaAHHVMGPP 300
Cdd:PRK09059  224 LRlaALTRgryhAAQISCAE---------SAEALRRAKDR-----GLKVTAGVSINHLSL-NEndigEYR--TFFKLSPP 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 301 LRPDPSTPGfLMNLLANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWeKGVHSGKMDENRFVAVTST 380
Cdd:PRK09059  287 LRTEDDRVA-MVEAVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIEALST 361
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 381 NAAKIFNLypKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEA 450
Cdd:PRK09059  362 RPAEIFGL--PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYEL 429
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
7-69 2.00e-11

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 65.64  E-value: 2.00e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1935598052   7 LLIRGGRVVN--DDFSQVADVLVEDGVVRALGRDLlppgDTSRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK09237    1 LLLRGGRVIDpaNGIDGVIDIAIEDGKIAAVAGDI----DGSQAKKVIDLSGLYVSPGWIDLHVH 61
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
6-115 3.76e-11

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: 64.85  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVVNDDFSQV----ADVLVEDGVVRALGRDLlPPGDTSRGLRILDAAGKLVLPGGIDTHTHM----------- 70
Cdd:COG0402     1 DLLIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGA-ELPARYPAAEVIDAGGKLVLPGLVNTHTHLpqtllrgladd 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935598052  71 ----------QFPFMGSQSVDDFHQGTKAA----LAGGTTMIIDFAIPQKGSS--LIEAFE 115
Cdd:COG0402    80 lplldwleeyIWPLEARLDPEDVYAGALLAlaemLRSGTTTVADFYYVHPESAdaLAEAAA 140
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
60-460 4.34e-11

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: 64.39  E-value: 4.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  60 LPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGTTMIIdfAIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTw 137
Cdd:cd01316     5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGAT- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 138 wsdkvKEEMKTLAQ--DKGVNS----FKMFMAYKDLYMVQDQQMYAAFSQCKEIGAiaqvHAENGDLIAegakkmlalgi 211
Cdd:cd01316    80 -----STNAATVGElaSEAVGLkfylNETFSTLILDKITAWASHFNAWPSTKPIVT----HAKSQTLAA----------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 212 tgpeghelcrpeaveaeatlrAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGE--PIAAGLGTDGTQYWNKEW 289
Cdd:cd01316   140 ---------------------VLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEvsPHHLFLSQDDLPRGQYEV 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 290 RhaahhvmgpPLRPDPSTPGFLMNLLANGDLTTTGSdnctfntCQKALGKDDFTKIPNGVNGVEDRMSVIWeKGVHSGKM 369
Cdd:cd01316   199 R---------PFLPTREDQEALWENLDYIDCFATDH-------APHTLAEKTGNKPPPGFPGVETSLPLLL-TAVHEGRL 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 370 DENRFVAVTSTNAAKIFNLYPKkgriavgSDADIVIwDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYE 449
Cdd:cd01316   262 TIEDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFI 333
                         410
                  ....*....|.
gi 1935598052 450 AGVFDVTAGHG 460
Cdd:cd01316   334 DGEIVAPPGFG 344
PRK07369 PRK07369
dihydroorotase; Provisional
4-420 5.29e-11

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 64.62  E-value: 5.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   4 QERLLIRGGRVVnDDFSQ---VADVLVEDGVVRALGRDLLP-PGDTsrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQS 79
Cdd:PRK07369    1 MSNELLQQVRVL-DPVSNtdrIADVLIEDGKIQAIEPHIDPiPPDT----QIIDASGLILGPGLVDLYSHSGEP--GFEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  80 VDDFHQGTKAALAGGTT---MIIDFAIPQKGSSLIEAFETWRNWADPkvccdyslhVAVTWW---SDKVKEEMKT----L 149
Cdd:PRK07369   74 RETLASLAAAAAAGGFTrvaILPDTFPPLDNPATLARLQQQAQQIPP---------VQLHFWgalTLGGQGKQLTelaeL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 150 AQdKGVNSFKMFMAYKDLYMVQDQQMYA-------AFSQCKeigaiAQVHAeNGdLIAEGAKKmLALGITGpeghelcRP 222
Cdd:PRK07369  145 AA-AGVVGFTDGQPLENLALLRRLLEYLkplgkpvALWPCD-----RSLAG-NG-VMREGLLA-LRLGLPG-------DP 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 223 EAVEAEATLRAITIASAVNCPlyiVHVMSKSAAK---VIADAKREGKvvygePIAAG-------LGTDGTQYWNKEWRha 292
Cdd:PRK07369  209 ASAETTALAALLELVAAIGTP---VHLMRISTARsveLIAQAKARGL-----PITASttwmhllLDTEALASYDPNLR-- 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 293 ahhvMGPPLrPDPSTPGFLMNLLANGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKGVHSGKMDEN 372
Cdd:PRK07369  279 ----LDPPL-GNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSAL 350
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1935598052 373 RFVAVTSTNAAKIFNLYPKkgRIAVGSDADIVIWDPEATRTISAKTHH 420
Cdd:PRK07369  351 QLWQALSTNPARCLGQEPP--SLAPGQPAELILFDPQKTWTVSAQTLH 396
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
7-100 6.29e-10

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: 61.06  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQV---ADVLVEDGVVRALGRDLLPPGDTsrGLRILDAAGKLVLPGGIDTHTHMQ------------ 71
Cdd:cd01298     1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALPLPAYP--ADEVIDAKGKVVMPGLVNTHTHLAmtllrgladdlp 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1935598052  72 ---------FPFMGSQSVDDFHQGTKAALA----GGTTMIID 100
Cdd:cd01298    79 lmewlkdliWPLERLLTEEDVYLGALLALAemirSGTTTFAD 120
pyrC PRK00369
dihydroorotase; Provisional
56-457 5.51e-09

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 58.23  E-value: 5.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  56 GKLVLPGGIDTHTHMQfpfmGSQSV--DDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHV 133
Cdd:PRK00369   42 GTLILPGAIDLHVHLR----GLKLSykEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 134 AVTwwsdKVKEEMKTLaqdkGVNSFKMFMAykdlymvqdqqmyaafsqckeigaiaqvhaengDLIAEGAKKMLA----L 209
Cdd:PRK00369  118 GVT----KDPEKVDKL----PIAGYKIFPE---------------------------------DLEREETFRVLLksrkL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 210 GITGPEGHELCRPEaveaEATLRAI--TIASavncpLYIVHvmskSAAKV-IADAKREGKVVygepIAAGLG--TDGTqy 284
Cdd:PRK00369  157 KILHPEVPLALKSN----RKLRRNCwyEIAA-----LYYVK----DYQNVhITHASNPRTVR----LAKELGftVDIT-- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 285 wnkewrhaAHHVM-----------GPPLRpDPSTPGFLMNLLANGDltTTGSDNCTFNTCQKalgKDDFTKIPNGVNGVE 353
Cdd:PRK00369  218 --------PHHLLvngekdcltkvNPPIR-DINERLWLLQALSEVD--AIASDHAPHSSFEK---LQPYEVCPPGIAALS 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 354 DRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEATR--TISAKTHHQAVnfNIFEGM 431
Cdd:PRK00369  284 FTPPFIYTL-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRysTKYSKVIETPL--DGFELK 358
                         410       420
                  ....*....|....*....|....*..
gi 1935598052 432 VChgvPLVTISRGRVVYEAG-VFDVTA 457
Cdd:PRK00369  359 AS---VYATIVQGKLAYLEGeVFPVKG 382
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
24-407 8.15e-09

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: 57.34  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  24 DVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMqFPFMGSQSVDDFHQGTKAalagGTTMIIDfai 103
Cdd:cd01307     1 DVAIENGKIAAVGAALAAPAAT----QIVDAGGCYVSPGWIDLHVHV-YQGGTRYGDRPDMIGVKS----GVTTVVD--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 104 pqKGSSLIEAFETWRnwadpkvccdyslhvavtwwsdkvkeemKTLAQDKGVNSFkmfmAYKDLYMV-QDQQMYAAFSQC 182
Cdd:cd01307    69 --AGSAGADNIDGFR----------------------------YTVIERSATRVY----AFLNISRVgLVAQDELPDPDN 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 183 KEIGAIAQVHAENGDLIAeGAKKMLALGITGPEGHELCRpeaveaeatlRAITIASAVNCPLYiVHVMSKSAA-KVIADA 261
Cdd:cd01307   115 IDEDAVVAAAREYPDVIV-GLKARASKSVVGEWGIKPLE----------LAKKIAKEADLPLM-VHIGSPPPIlDEVVPL 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 262 KREGKVVygepiaaglgtdgtqywnkewRHAAHHVMGPPLRPDPSTPGFLMNLLANG---DLtTTGSDNCTFNTCQKA-- 336
Cdd:cd01307   183 LRRGDVL---------------------THCFNGKPNGIVDEEGEVLPLVRRARERGvifDV-GHGTASFSFRVARAAia 240
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935598052 337 -------LGKDDFTKipNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTsTNAAKIFNLyPKKGRIAVGSDADIVIWD 407
Cdd:cd01307   241 agllpdtISSDIHGR--NRTNGPVYALATTLSKLLALGMPLEEVIEAVT-ANPARMLGL-AEIGTLAVGYDADLTVFD 314
PRK08204 PRK08204
hypothetical protein; Provisional
5-69 1.96e-08

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 56.55  E-value: 1.96e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935598052   5 ERLLIRGGRVVNDD----FSQVADVLVEDGVVRALGRDLLPPGDtsrglRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK08204    2 KRTLIRGGTVLTMDpaigDLPRGDILIEGDRIAAVAPSIEAPDA-----EVVDARGMIVMPGLVDTHRH 65
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
8-96 3.03e-08

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 55.49  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   8 LIRGGRVVNDD-FSQVADVLVEDGVVRALGRDLLPPGDtsrglrILDAAGKLVLPGGIDTHTH--MQFPFMgSQSVDDFH 84
Cdd:COG1820     1 AITNARIFTGDgVLEDGALLIEDGRIAAIGPGAEPDAE------VIDLGGGYLAPGFIDLHVHggGGVDFM-DGTPEALR 73
                          90
                  ....*....|..
gi 1935598052  85 QGTKAALAGGTT 96
Cdd:COG1820    74 TIARAHARHGTT 85
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
64-214 3.92e-08

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: 54.65  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  64 IDTHTHMQFP----------------FMGSQSVDDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADP---- 123
Cdd:cd01292     2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsagi 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 124 -KVCCDYSLHVAVTWWSDKVKEEMKTLAQ--DKGVNSFKMFMAYKDlYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIA 200
Cdd:cd01292    82 rVVLGLGIPGVPAAVDEDAEALLLELLRRglELGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDPT 160
                         170
                  ....*....|....
gi 1935598052 201 EGAKKMLALGITGP 214
Cdd:cd01292   161 RALEDLVALLRLGG 174
PRK09061 PRK09061
D-glutamate deacylase; Validated
6-468 5.63e-08

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 55.09  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVVNDD--FSQVADVLVEDGVVRALGRDLLppgdtsRGLRILDAAGKLVLPGGIDTHTHMQfpfmgSQSVDDF 83
Cdd:PRK09061   20 DLVIRNGRVVDPEtgLDAVRDVGIKGGKIAAVGTAAI------EGDRTIDATGLVVAPGFIDLHAHGQ-----SVAAYRM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  84 HqgtkaALAGGTTMiIDFAIpqkGSSLIEAFetWRNWADPKVCCDYSlhVAVTWWSDKVKeEMKTLAQDKGVNSFKMFMA 163
Cdd:PRK09061   89 Q-----AFDGVTTA-LELEA---GVLPVARW--YAEQAGEGRPLNYG--ASVGWTPARIA-VLTGPQAEGTIADFGKALG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 164 YKdlymvqDQQMYAAFSQckEIGAIAQVhAENGdlIAEGAkkmLALGI-------TGP-EGHELCRPEA----------- 224
Cdd:PRK09061  155 DP------RWQERAATPA--ELAEILEL-LEQG--LDEGA---LGIGIgagyapgTGHkEYLELARLAAragvptythvr 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 225 --------VEAEATLRAITIASAVNCPLYIVHVMSKS------AAKVIADAKREGKVVYGE--PIAAG---LGTD----- 280
Cdd:PRK09061  221 ylsnvdprSSVDAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVTTEayPYGAGstvVGAAffdpg 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 281 -----GTQYWNKEWRHAAHHVM--------------GPPL-----RPDPSTPGFLMNLLANGD-------LTTTGSDNCT 329
Cdd:PRK09061  301 wlermGLGYGSLQWVETGERLLtreelaklrandpgGLVLihfldEDNPRDRALLDRSVLFPGaaiasdaMPWTWSDGTV 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 330 FNTCQKALGKDDFTKiPNGvNG---------VEDRMSVIWEKGVHsgKMdenrfvavtSTNAAKIFNLY----PKKGRIA 396
Cdd:PRK09061  381 YEGDAWPLPEDAVSH-PRS-AGtfarflreyVRERKALSLLEAIR--KC---------TLMPAQILEDSvpamRRKGRLQ 447
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935598052 397 VGSDADIVIWDPEatrTISAKTHHQAVNfnifegMVCHGVPLVTISrGRVVYEAGVFDVTAGHGKFIpRQPF 468
Cdd:PRK09061  448 AGADADIVVFDPE---TITDRATFEDPN------RPSEGVRHVLVN-GVPVVSNGELVRDARPGRPV-RRPV 508
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
7-70 7.58e-08

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 54.80  E-value: 7.58e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935598052   7 LLIRGGRV--VNDDFSQVADVLVEDGVVRALG-----RDLLPPGDtsrglRILDAAGKLVLPGGIDTHTHM 70
Cdd:COG1574    10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGsdaevRALAGPAT-----EVIDLGGKTVLPGFIDAHVHL 75
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
7-408 1.10e-07

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: 54.12  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGrdllPPGDTSRGLRILDAAGKLVLPGGIDTHTHmqfpfmGSQSVdDFHQG 86
Cdd:cd00854     1 LIIKNARILTPGGLEDGAVLVEDGKIVAIG----PEDELEEADEIIDLKGQYLVPGFIDIHIH------GGGGA-DFMDG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  87 TKAALAG--------GTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDY-SLHVAVTWWSdkvkEEMKTlAQDKGVns 157
Cdd:cd00854    70 TAEALKTiaealakhGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEIlGIHLEGPFIS----PEKKG-AHPPEY-- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 158 fkMFMAYKDLYmvqdQQMYAAFSQCKEIGAIAQVHAENGDLIaegaKKMLALGITGPEGH-----ELCRpEAVEAEATL- 231
Cdd:cd00854   143 --LRAPDPEEL----KKWLEAAGGLIKLVTLAPELDGALELI----RYLVERGIIVSIGHsdatyEQAV-AAFEAGATHv 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 232 ------------RAITIASAVNCPLYI--------VHVmSKSAAKVIADAKREGKVVYgepI-----AAGLGtDGtqywn 286
Cdd:cd00854   212 thlfnamsplhhREPGVVGAALSDDDVyaeliadgIHV-HPAAVRLAYRAKGADKIVL---VtdamaAAGLP-DG----- 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 287 kewrhaaHHVMGPplRPDPSTPGflMNLLANGdlTTTGSDnCTFNTCQKALGKddFTKIPngvngVED--RMSviwekgv 364
Cdd:cd00854   282 -------EYELGG--QTVTVKDG--VARLADG--TLAGST-LTMDQAVRNMVK--WGGCP-----LEEavRMA------- 333
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1935598052 365 hsgkmdenrfvavtSTNAAKIFNLYPKKGRIAVGSDADIVIWDP 408
Cdd:cd00854   334 --------------SLNPAKLLGLDDRKGSLKPGKDADLVVLDD 363
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
7-69 1.17e-07

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 54.04  E-value: 1.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1935598052   7 LLIRGGRVV-NDDFSQV-ADVLVEDGVVRALGRDLLPPGDTsrglrILDAAGKLVLPGGIDTHTH 69
Cdd:PRK08393    3 ILIKNGYVIyGENLKVIrADVLIEGNKIVEVKRNINKPADT-----VIDASGSVVSPGFINAHTH 62
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
7-69 2.79e-07

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 440842  Cd Length: 554  Bit Score: 53.27  E-value: 2.79e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935598052   7 LLIRGGRV------VNDDfsqVADVLVEDGVVRAlgrdllPPGDtSRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:COG1229     3 LIIKNGRVydpangIDGE---VMDIAIKDGKIVE------EPSD-PKDAKVIDASGKVVMAGGVDIHTH 61
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
25-99 3.19e-07

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: 52.65  E-value: 3.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1935598052  25 VLVEDGVVRALGRDLLPPGDTSRGLRILDAAGKLVLPGGIDTHTHMQFpfmGSQSVDDFhqgtKAALAGGTTMII 99
Cdd:cd01296     1 IAIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVF---AGDRVDEF----AARLAGASYEEI 68
PRK08417 PRK08417
metal-dependent hydrolase;
299-449 9.19e-07

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 51.24  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 299 PPLRpDPSTPGFLMNLLANGDLTTTGSDNC-TFNTcqkalgKDD--FTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFV 375
Cdd:PRK08417  249 PPLR-SKEDRLALLEALKEGKIDFLTSLHSaKSNS------KKDlaFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELS 321
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935598052 376 AVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEaTRTISAKthhqavNFNIFEGMVCHGVPLVTISRGRVVYE 449
Cdd:PRK08417  322 RFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPN-ESTIIDD------NFSLYSGDELYGKIEAVIIKGKLYLE 386
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
6-97 1.81e-06

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 50.18  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVVNDDFSQVADVLVEDGVVRALGrdllppGDTSRGLRILDAAGKLVLPGGIDTHT-----HMQ------FPF 74
Cdd:PRK15446    3 EMILSNARLVLPDEVVDGSLLIEDGRIAAID------PGASALPGAIDAEGDYLLPGLVDLHTdnlekHLAprpgvdWPA 76
                          90       100
                  ....*....|....*....|....
gi 1935598052  75 MGS-QSVDdfhqgTKAALAGGTTM 97
Cdd:PRK15446   77 DAAlAAHD-----AQLAAAGITTV 95
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
375-409 4.02e-06

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 48.94  E-value: 4.02e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1935598052 375 VAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPE 409
Cdd:COG1820   328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
6-70 4.62e-06

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 49.08  E-value: 4.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVV---NDDFSQVAD--VLVEDGVVRALGRDLLPPGDTSRglrILDAAGKLVLPGGIDTHTHM 70
Cdd:PRK08203    2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQPADE---VFDARGHVVTPGLVNTHHHF 68
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
7-458 5.50e-06

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


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 49.02  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVndDFS----QVADVLVEDGVVRALGRDLLPPGDtsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDD 82
Cdd:COG3653     4 LLIRGGTVV--DGTgappFRADVAIKGGRIVAVGDLAAAEAA-----RVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  83 F-HQGTkaalaggTTMII-------DFAIPQKGSSLIEAFETWRnwadpkvccDYSLHVAVTWWSdkVKEEMKTL-AQDK 153
Cdd:COG3653    77 SlRQGV-------TTVVMgncgvsfAPVRPEDRDRLIDLMEGVE---------GIPEGLDWDWES--FGEYLDALeRRGL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 154 GVNsFKMFMAYKDL--Y----------------MVQ--DQQM------------YA--AFSQCKEIGAIAQVHAENGDLI 199
Cdd:COG3653   139 GVN-VASLVGHGTLraYvmglddrpptpeelarMRAllREAMeagalglstgliYVpgTYASTDELVALAKVVAEYGGVY 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 200 AegakkmlalGITGPEGHELCrpEAVEAeatlrAITIASAVNCPLYIVHV---------MSKSAAKVIADAKREG-KV-- 267
Cdd:COG3653   218 Q---------SHMRDEGDGLL--EAVDE-----LIRIGREAGVPVHISHLkaagkpnwgKADEVLALIEAARAEGlDVta 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 268 -VYGEPI------------AAGLGTDGT--------------------QYWNKEWRHAAHHVMGPPLRPDPSTPG----- 309
Cdd:COG3653   282 dVYPYPAgstglgallppwAAAGGLDERlarlrdpatrariraeieegLPDNLLGRGGWDNILISDSPPNEPLVGkslae 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 310 -----------FLMNLLANGDL----------------------TTTGSDNC--------TFNTCQKALGKddftkipng 348
Cdd:COG3653   362 iaaergvdpadAALDLLLEEDGrvlivyfimseedvrellrhpwVMIGSDGGlggkahprAYGTFPRVLGH--------- 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 349 vnGVEDR--MSViwEKGVHsgKMdenrfvavTStNAAKIFNLyPKKGRIAVGSDADIVIWDPEatrTISAK-THHQAVNF 425
Cdd:COG3653   433 --YVRERgvLSL--EEAVR--KL--------TS-LPADRLGL-KDRGLLRPGYRADLVVFDPA---TLADRaTFDLPAQR 493
                         570       580       590
                  ....*....|....*....|....*....|....
gi 1935598052 426 NifEGMVChgvplvTISRGRVVYEAGVF-DVTAG 458
Cdd:COG3653   494 A--DGIRA------VIVNGVVVVEDGKPtGARPG 519
Amidohydro_3 pfam07969
Amidohydrolase family;
50-448 1.00e-05

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 47.91  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  50 RILDAAGKLVLPGGIDTHTHM--QFPFMGSQSVDDFHQGTKAALAGGTTMIID-----------FAIPQKGSSL------ 110
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLdgGGLNLRELRLPDVLPNAVVKGQAGRTPKGRwlvgegwdeaqFAETRFPYALadldev 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 111 ----------IEAFETWRN------WADPKVCCD-----------------YSLHVAVTWWSDKVKEEMKTLAQD--KGV 155
Cdd:pfam07969  81 apdgpvllraLHTHAAVANsaaldlAGITKATEDppggeiardangegltgLLREGAYALPPLLAREAEAAAVAAalAAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 156 NSFKMFMAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAE--------NGDLIAEGAKKMLALGITG--------PEGHEL 219
Cdd:pfam07969 161 PGFGITSVDGGGGNVHSLDDYEPLRELTAAEKLKELLDAperlglphSIYELRIGAMKLFADGVLGsrtaaltePYFDAP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 220 CRPEAVEAEATL-RAITIASAVNCPLYIvH------VMS--KSAAKVIADAKREGKVV-------------YGEPIAAGL 277
Cdd:pfam07969 241 GTGWPDFEDEALaELVAAARERGLDVAI-HaigdatIDTalDAFEAVAEKLGNQGRVRiehaqgvvpytysQIERVAALG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 278 GTDGTQY-WNKEWRHAAHHVMGPPlRPDPSTPgfLMNLLANGDLTTTGSDN--CTFntcqkalgkDDFTKIPNGVNG-VE 353
Cdd:pfam07969 320 GAAGVQPvFDPLWGDWLQDRLGAE-RARGLTP--VKELLNAGVKVALGSDApvGPF---------DPWPRIGAAVMRqTA 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 354 DRMSVIWEkgvhSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVnfnifegmvc 433
Cdd:pfam07969 388 GGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRV---------- 453
                         490
                  ....*....|....*
gi 1935598052 434 hgvpLVTISRGRVVY 448
Cdd:pfam07969 454 ----RLTVVDGRVVY 464
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
8-122 1.54e-05

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: 47.24  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   8 LIRGGRVVNDDFSQVaDVLVEDGVVRALGRDLLPPGDTSRglriLDAAGKLVLPGGIDTHTHMQFPFMG----------- 76
Cdd:cd01293     1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAEE----VDAKGRLVLPAFVDPHIHLDKTFTGgrwpnnsggtl 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935598052  77 ------------SQSVDDFHQ----GTKAALAGGTTMI-----IDFAIPQKG-SSLIEAFETWRNWAD 122
Cdd:cd01293    76 leaiiaweerklLLTAEDVKEraerALELAIAHGTTAIrthvdVDPAAGLKAlEALLELREEWADLID 143
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
7-100 1.55e-05

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 47.40  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRVVNddfsqV-------ADVLVEDGVVRALGRDLLPpgdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMgsqS 79
Cdd:COG1001     7 LVIKNGRLVN-----VftgeileGDIAIAGGRIAGVGDYIGE------ATEVIDAAGRYLVPGFIDGHVHIESSMV---T 72
                          90       100
                  ....*....|....*....|..
gi 1935598052  80 VDDFhqgTKAALAGGTT-MIID 100
Cdd:COG1001    73 PAEF---ARAVLPHGTTtVIAD 91
PRK07627 PRK07627
dihydroorotase; Provisional
6-450 1.60e-05

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 47.36  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   6 RLLIRGGRVVN--DDFSQVADVLVEDGVVRALGRDllPPGDTSRglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDF 83
Cdd:PRK07627    2 KIHIKGGRLIDpaAGTDRQADLYVAAGKIAAIGQA--PAGFNAD--KTIDASGLIVCPGLVDLSARLREP--GYEYKATL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  84 HQGTKAALAGGTTMII---DFAIPQKGSSLIEAFE-TWRNWADPKVccdYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFk 159
Cdd:PRK07627   76 ESEMAAAVAGGVTSLVcppDTDPVLDEPGLVEMLKfRARNLNQAHV---YPLGALTVGLKGEVLTEMVELT-EAGCVGF- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 160 mfmAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAE-----NGDLIAEGAkkmLA--LGITGPeghelcrPEAVEAEATLR 232
Cdd:PRK07627  151 ---SQANVPVVDTQVLLRALQYASTFGFTVWLRPLdaflgRGGVAASGA---VAsrLGLSGV-------PVAAETIALHT 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 233 AITIASAVNCPLYIVHVMSKSAAKVIADAKREGKvvygePIAAGLGTDGTQ-------YWNKEWRhaahhvMGPPLRPDP 305
Cdd:PRK07627  218 IFELMRVTGARVHLARLSSAAGVALVRAAKAEGL-----PVTCDVGVNHVHlidvdigYFDSQFR------LDPPLRSQR 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052 306 STPGfLMNLLANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWeKGVHSGKMDENRFVAVTSTNAAKI 385
Cdd:PRK07627  287 DREA-IRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPLTL-KWADEAKVPLARALARITSAPARV 361
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935598052 386 FNLypKKGRIAVGSDADIVIWDPEATRTISAKT-HHQAVNfNIFEGMVCHGVPLVTISRGRVVYEA 450
Cdd:PRK07627  362 LGL--PAGRLAEGAPADLCVFDPDAHWRVEPRAlKSQGKN-TPFLGYELPGRVRATLVAGQVAFER 424
PRK07583 PRK07583
cytosine deaminase;
23-122 1.87e-05

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 47.29  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  23 ADVLVEDGVVRALgrdlLPPGDTSRGLRILDAAGKLVLPGGIDTHTHM-------QFP-----FMGSQ-----------S 79
Cdd:PRK07583   41 VDIEIADGKIAAI----LPAGGAPDELPAVDLKGRMVWPCFVDMHTHLdkghiwpRSPnpdgtFPGALdavtadreahwS 116
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1935598052  80 VDDFHQ----GTKAALAGGTTMI---IDFAIPQKGSSLiEAFETWRN-WAD 122
Cdd:PRK07583  117 AEDLYRrmefGLRCAYAHGTSAIrthLDSFAPQAAISW-EVFAELREaWAG 166
PRK05985 PRK05985
cytosine deaminase; Provisional
7-76 2.55e-05

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 46.46  E-value: 2.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052   7 LLIRGGRvvnDDFSQVADVLVEDGVVRALGRDLLPPgdtsRGLRILDAAGKLVLPGGIDTHTHMQFPFMG 76
Cdd:PRK05985    4 LLFRNVR---PAGGAAVDILIRDGRIAAIGPALAAP----PGAEVEDGGGALALPGLVDGHIHLDKTFWG 66
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
6-69 2.67e-05

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 46.53  E-value: 2.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1935598052   6 RLLIRGGRVVNDDFSQV---ADVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK07228    2 TILIKNAGIVTMNAKREivdGDVLIEDDRIAAVGDRLDLEDYD----DHIDATGKVVIPGLIQGHIH 64
PRK09228 PRK09228
guanine deaminase; Provisional
25-73 2.80e-05

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 46.34  E-value: 2.80e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1935598052  25 VLVEDGVVRALG-----RDLLPPGdtsrgLRILDAAGKLVLPGGIDTHTHmqFP 73
Cdd:PRK09228   34 LLVEDGRIVAAGpyaelRAQLPAD-----AEVTDYRGKLILPGFIDTHIH--YP 80
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
24-70 3.32e-04

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: 43.07  E-value: 3.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1935598052  24 DVLVEDGVVRALGRD----LLPPGDTsrglRILDAAGKLVLPGGIDTHTHM 70
Cdd:cd01300     1 AVAVRDGRIVAVGSDaeakALKGPAT----EVIDLKGKTVLPGFIDSHSHL 47
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
9-69 7.94e-04

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: 42.02  E-value: 7.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935598052   9 IRGGRVV---NDDFSQVADVLVEDGVVRAlgrdllPPGDTSRGlRILDAAGKLVLPGGIDTHTH 69
Cdd:cd01304     1 IKNGTVYdplNGINGEKMDIFIRDGKIVE------SSSGAKPA-KVIDASGKVVMAGGVDMHSH 57
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
27-77 9.01e-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: 41.88  E-value: 9.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1935598052  27 VEDGVVRALGRDLLPPGDTSR-------GLRILDAAGKLVLPGGIDTHTHM-QFPFMGS 77
Cdd:cd01303    24 VEDGLIVVVDGNIIAAGAAETlkraakpGARVIDSPNQFILPGFIDTHIHApQYANIGS 82
PRK07572 PRK07572
cytosine deaminase; Validated
7-70 1.45e-03

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 41.16  E-value: 1.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935598052   7 LLIRGGRVvnDDFSQVADVLVEDGVVRALGrdllpPGDTSRGLRILDAAGKLVLPGGIDTHTHM 70
Cdd:PRK07572    4 LIVRNANL--PDGRTGIDIGIAGGRIAAVE-----PGLQAEAAEEIDAAGRLVSPPFVDPHFHM 60
PRK07203 PRK07203
putative aminohydrolase SsnA;
7-69 1.75e-03

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 40.69  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935598052   7 LLIRGGRVVNDD----FSQVADVLVEDGVVRALG-RDLLppGDTSRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK07203    2 LLIGNGTAITRDpakpVIEDGAIAIEGNVIVEIGtTDEL--KAKYPDAEFIDAKGKLIMPGLINSHNH 67
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
5-69 1.87e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 40.89  E-value: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1935598052   5 ERLLIRGGRVVNDDFSQV--ADVLVEDGVVRALGRDLLPPGDTsrglrILDAAGKLVLPGGIDTHTH 69
Cdd:PRK06038    2 ADIIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSESTPGDADT-----VIDAKGSVVMPGLVNTHTH 63
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
377-409 1.91e-03

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: 40.45  E-value: 1.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1935598052 377 VTSTNAAKIFNLYpKKGRIAVGSDADIVIWDPE 409
Cdd:cd01308   330 VITSNVARILKLR-KKGEIQPGFDADLVILDKD 361
ureC PRK13206
urease subunit alpha; Reviewed
12-99 2.04e-03

urease subunit alpha; Reviewed


Pssm-ID: 237304 [Multi-domain]  Cd Length: 573  Bit Score: 40.85  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  12 GRVVNDDFSQV-ADVLVEDGVVRALGRDLLPpgDTSRGL----------RILDAAGKLVLPGGIDTHTHmqfpFMGSQSV 80
Cdd:PRK13206   77 GAVILDHWGIVkADVGIRDGRIVAIGKAGNP--DIMDGVhpdlvigpstEIIAGNGRILTAGAIDCHVH----FICPQIV 150
                          90
                  ....*....|....*....
gi 1935598052  81 DDfhqgtkaALAGGTTMII 99
Cdd:PRK13206  151 DE-------ALAAGITTLI 162
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
29-69 2.33e-03

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: 40.37  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1935598052  29 DGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTH 69
Cdd:cd01309     1 DGKIVAVGAEITTPADA----EVIDAKGKHVTPGLIDAHSH 37
Urease_alpha cd00375
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
23-99 4.09e-03

Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.


Pssm-ID: 238221 [Multi-domain]  Cd Length: 567  Bit Score: 39.62  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  23 ADVLVEDGVVRALGR----DLLPpGDTSR-----GLRILDAAGKLVLPGGIDTHTHMQFPfmgsqsvddfhQGTKAALAG 93
Cdd:cd00375    83 ADIGIKDGRIVAIGKagnpDIMD-GVTPNmivgpSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALAS 150

                  ....*.
gi 1935598052  94 GTTMII 99
Cdd:cd00375   151 GITTMI 156
ureC PRK13207
urease subunit alpha; Reviewed
23-98 4.26e-03

urease subunit alpha; Reviewed


Pssm-ID: 237305 [Multi-domain]  Cd Length: 568  Bit Score: 39.78  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598052  23 ADVLVEDGVVRALGR----DLLPPGD--TSRGLRILDAAGKLVLPGGIDTHTHmqfpFMGSQSVDdfhqgtkAALAGG-T 95
Cdd:PRK13207   85 ADIGIKDGRIVAIGKagnpDIQDGVDiiIGPGTEVIAGEGLIVTAGGIDTHIH----FICPQQIE-------EALASGvT 153

                  ...
gi 1935598052  96 TMI 98
Cdd:PRK13207  154 TMI 156
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
376-407 5.90e-03

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: 38.83  E-value: 5.90e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1935598052 376 AVTStNAAKIFNLYPKKGRIAVGSDADIVIWD 407
Cdd:cd01309   308 AITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
 
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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