|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
7-443 |
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: 595.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSIDDFHQG 86
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGV----EVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 87 TK-----------------------------------------------------VKEEMKILVqDKGVNSFKMFMAYKD 113
Cdd:cd01314 77 TRaaaaggtttiidfaipnkgqslleavekwrgkadgksvidygfhmiitdwtdsVIEELPELV-KKGISSFKVFMAYKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 114 LYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 193
Cdd:cd01314 156 LLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 194 VHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWnKEWHHAAHHVMGPPLRPDpSTPDFLMNLLANDDLTTTGTD 273
Cdd:cd01314 236 VHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 274 NCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIVIW 353
Cdd:cd01314 314 HCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 354 DPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVYEA 433
Cdd:cd01314 394 DPN------------------------------------AEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVED 437
|
490
....*....|
gi 2462618093 434 GVFSVTAGDG 443
Cdd:cd01314 438 GELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
7-448 |
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: 532.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSIDDFHQG 86
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAV----EVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 87 TK-----------------------------------------------------VKEEMKILVQDKGVNSFKMFMAYKD 113
Cdd:TIGR02033 77 TKaaaaggtttiidfvvpekgssltealetwhekaegksvidygfhmdithwndsVLEEHIPEVKEEGINSFKVFMAYKN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 114 LYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 193
Cdd:TIGR02033 157 LLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 194 VHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWnKEWHHAAHHVMGPPLRpDPSTPDFLMNLLANDDLTTTGTD 273
Cdd:TIGR02033 237 VHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 274 NCTFNTCQK-ALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIVI 352
Cdd:TIGR02033 315 HCTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 353 WDPKGTrgcrscvafsdngsvyktnmnlplqclanarvhmeeRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVYE 432
Cdd:TIGR02033 395 WDPNRT------------------------------------TVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVE 438
|
490
....*....|....*.
gi 2462618093 433 AGVFSVTAGDGKFIPR 448
Cdd:TIGR02033 439 DGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
6-455 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 515.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 6 RLLIRGGRVVNDDFSEVADVLVEDGVVRALGHDllppggapAGLRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSIDDFHQ 85
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN--------LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 86 GTK-----------------------------------------------------VKEEMKILVqDKGVNSFKMFMAYK 112
Cdd:PRK08323 74 GTRaaacggtttiidfalqpkgqslrealeawhgkaagkavidygfhmiitdwnevVLDEMPELV-EEGITSFKLFMAYK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 113 DLYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLY 192
Cdd:PRK08323 153 GALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 193 IVHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWNKEWHHAAHHVMGPPLRPDPSTpDFLMNLLANDDLTTTGT 272
Cdd:PRK08323 233 IVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDKEHQ-DALWRGLQDGDLQVVAT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 273 DNCTFNTCQKA-LGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIV 351
Cdd:PRK08323 312 DHCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 352 IWDPKGTrgcrscvafsdngsvyktnmnlplqclanarvhmeeRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVY 431
Cdd:PRK08323 392 IWDPNAT------------------------------------KTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVV 435
|
490 500
....*....|....*....|....
gi 2462618093 432 EAGVFSVTAGDGKFIPRKPFAEYI 455
Cdd:PRK08323 436 EDGEFRGKAGHGRFLKRKPFQAVV 459
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1-477 |
4.49e-178 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 509.00 E-value: 4.49e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 1 MAAPSRLLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLlppgGAPAGLRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSI 80
Cdd:PLN02942 1 GASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNL----KVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 81 DDFHQGT---------------------------------------------------KVKEEMKILVQDKGVNSFKMFM 109
Cdd:PLN02942 77 DDFFSGQaaalaggttmhidfvipvngnllagyeayekkaekscmdygfhmaitkwddTVSRDMETLVKEKGINSFKFFM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 110 AYKDLYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNC 189
Cdd:PLN02942 157 AYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 190 PLYIVHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWNKEWHHAAHHVMGPPLRPdPSTPDFLMNLLANDDLTT 269
Cdd:PLN02942 237 PLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 270 TGTDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDAD 349
Cdd:PLN02942 316 VGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 350 IVIWDPKGTrgcrscvafsdngsvyktnmnlplqclanarvhmeeRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKV 429
Cdd:PLN02942 396 IIILNPNST------------------------------------FTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRV 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2462618093 430 VYEAGVFSVTAGDGKFIPRKPFAeYIYKRIKQRDRTCTPTPVERAPYK 477
Cdd:PLN02942 440 VWENGELKVVRGSGRYIEMPPFS-YLFDGIQKADAAYLSSLRAPVKRT 486
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
8-448 |
2.56e-107 |
|
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: 326.66 E-value: 2.56e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 8 LIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPFM--------GSRS 79
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAA----EVIDATGLLVLPGLIDLHVHLREPGLehkedietGTRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 80 ------------------IDD--------------------FHQG-TKVK----EEMKILVqDKGVNSFKMFMAYKD-LY 115
Cdd:COG0044 77 aaaggvttvvdmpntnpvTDTpealefklaraeekalvdvgPHGAlTKGLgenlAELGALA-EAGAVAFKVFMGSDDgNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 116 MVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKkmlALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIVH 195
Cdd:COG0044 156 VLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVM---NEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 196 VMSKSAAKVIADARRDGKVVYGE--P-----IAASLGTDGTHYwnkewhhaahhVMGPPLRpDPSTPDFLMNLLANDDLT 268
Cdd:COG0044 233 VSTAEAVELIREAKARGLPVTAEvcPhhltlTDEDLERYGTNF-----------KVNPPLR-TEEDREALWEGLADGTID 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 269 TTGTDNCTFNTCQKAlgkDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRIAVGSDA 348
Cdd:COG0044 301 VIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 349 DIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGK 428
Cdd:COG0044 377 DLVLFDPD------------------------------------AEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGR 420
|
490 500
....*....|....*....|
gi 2462618093 429 VVYEAGVFsVTAGDGKFIPR 448
Cdd:COG0044 421 VVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
7-448 |
1.84e-100 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 310.09 E-value: 1.84e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLlppggaPAGLRVLDAAGKLVLPGGIDTHTHM-QFPFMGSRSIDDFHQ 85
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL------GPGAREIDATGRLVLPGGVDSHCHIdQPSGDGIMMADDFYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 86 GTK------------------------------------------------------VKEEMKILVQDkGVNSFKMFMAY 111
Cdd:PRK13404 80 GTVsaafggtttvipfaaqhrgqslreavedyhrraagkavidyafhlivadpteevLTEELPALIAQ-GYTSFKVFMTY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 112 KDLyMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPL 191
Cdd:PRK13404 159 DDL-KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 192 YIVHVMSKSAAKVIADARRDGKVVYGEP-------IAASLGTDGTHywnkewhhAAHHVMGPPLRpDPSTPDFLMNLLAN 264
Cdd:PRK13404 238 LIVHVSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLAD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 265 DDLTTTGTDNCTFN---TCQKALGKDD--FTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRK 339
Cdd:PRK13404 309 GTFEVFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 340 GRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGV 419
Cdd:PRK13404 389 GAIAIGADADIAIWDPD------------------------------------REVTITNADLHHAADYTPYEGMRVTGW 432
|
490 500
....*....|....*....|....*....
gi 2462618093 420 PLVTISRGKVVYEAGVFSVTAGDGKFIPR 448
Cdd:PRK13404 433 PVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
7-446 |
8.27e-58 |
|
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: 198.28 E-value: 8.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQG 86
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAE----EVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 87 TK----------------------------VKEEM---KILVQ-------------------DKGVNSFKMFMA---YKD 113
Cdd:cd01315 76 TKaaaaggittiidmplnsipptttvenleAKLEAaqgKLHVDvgfwgglvpgnldqlrpldEAGVVGFKCFLCpsgVDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 114 LYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 193
Cdd:cd01315 156 FPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 194 VHVMSKSAAKVIADARRDGKVVYGEpiaaslgtDGTHYwnkeWHHAAHHV--------MGPPLRpDPSTPDFLMNLLAND 265
Cdd:cd01315 236 VHLSSAEAVPLIREARAEGVDVTVE--------TCPHY----LTFTAEDVpdggtefkCAPPIR-DAANQEQLWEALENG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 266 DLTTTGTDN--CTFNtcQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIA 343
Cdd:cd01315 303 DIDMVVSDHspCTPE--LKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 344 VGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISA---KTHHQAvnfNIFEGMVCHGVP 420
Cdd:cd01315 381 VGYDADFVVWDPE------------------------------------EEFTVDAedlYYKNKI---SPYVGRTLKGRV 421
|
490 500
....*....|....*....|....*.
gi 2462618093 421 LVTISRGKVVYEAGVFSVTAgDGKFI 446
Cdd:cd01315 422 HATILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
7-449 |
2.79e-42 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 156.35 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPFM--------GSR 78
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSE----EVIDARGMLLLPGGIDVHVHFREPGYthketwytGSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 79 ------------------------------------SIDDFHQGTKVKEEMKILVQ--DKGVNSF-KMFMAYKDLYMVTD 119
Cdd:PRK02382 80 saaaggvttvvdqpntdpptvdgesfdekaelaarkSIVDFGINGGVTGNWDPLESlwERGVFALgEIFMADSTGGMGID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 120 LELY-EAFSRCKEIGAIAQVHAENGDLIAEGAKkmLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMS 198
Cdd:PRK02382 160 EELFeEALAEAARLGVLATVHAEDEDLFDELAK--LLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAHIST 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 199 KSAAKVIADA--------------RRDgkvvygepiAASLGTDGThywnkewhhaahhvMGPPLRPDPSTpDFLMNLLAN 264
Cdd:PRK02382 238 PEGVDAARREgitcevtphhlflsRRD---------WERLGTFGK--------------MNPPLRSEKRR-EALWERLND 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 265 DDLTTTGTDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRIAV 344
Cdd:PRK02382 294 GTIDVVASDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 345 GSDADIVIWDPKGTrgcrscvafsdngsvyktnmnlplqclanarvhmeeRTISAKTHHQAVNFNIFEGMVchGV-PLVT 423
Cdd:PRK02382 369 GYDADLVLVDPDAA------------------------------------REIRGDDLHSKAGWTPFEGME--GVfPELT 410
|
490 500
....*....|....*....|....*.
gi 2462618093 424 ISRGKVVYEAGVFSVTAGDGKFIPRK 449
Cdd:PRK02382 411 MVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
57-423 |
1.21e-40 |
|
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: 149.08 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 57 KLVLPGGIDTHTHMQFPFMGSRSiDDFHQGT-----------------------------KVK---EEMKI--------- 95
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTYK-EDFESGSraaaaggvttvidmpntgpppidlpaielKIKlaeESSYVdfsfhagig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 96 ---------LVQDKGVNSFKMFMAYK--DLYMVTDLELYEAFSRCKEIGAIAQVHAEngdliaegakkmlalgitgpegh 164
Cdd:cd01302 80 pgdvtdelkKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 165 elcrpeaveaeatlRAITIASAVNCPLYIVHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDgTHYWNKEWHHAahhVM 244
Cdd:cd01302 137 --------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAWG---KV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 245 GPPLRPdPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGKDdFTKIPNGVNGVEDRMSVIWEKGVHSGkMDENRFVAV 324
Cdd:cd01302 199 NPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTEGVKRG-LSLETLVEI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 325 TSTNAAKIFNLYPrKGRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQ 404
Cdd:cd01302 276 LSENPARIFGLYP-KGTIAVGYDADLVIVDPK------------------------------------KEWKVTAEEIES 318
|
410
....*....|....*....
gi 2462618093 405 AVNFNIFEGMVCHGVPLVT 423
Cdd:cd01302 319 KADWTPFEGMEVTGKPVST 337
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
7-436 |
1.65e-35 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 137.53 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglrVLDAAGKLVLPGGIDTHTHMQFP-------F-MGSR 78
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPARE-----IIDADGLYVFPGMIDVHVHFNEPgrthwegFaTGSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 79 SI----------------------DDFHQGTKVKEEmKILVQ-------------------DKGVNSFKMFMAY---KDL 114
Cdd:PRK06189 80 ALaaggcttyfdmplnsipptvtrEALDAKAELARQ-KSAVDfalwgglvpgnlehlrelaEAGVIGFKAFMSNsgtDEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 115 YMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIV 194
Cdd:PRK06189 159 RSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 195 HVMSKSAAKVIADARRDGkvvygepIAASLGTdGTHYWnkewhHAAHHVM---------GPPLRpDPSTPDFLMNLLAND 265
Cdd:PRK06189 239 HISSGKAVALIAEAKKRG-------VDVSVET-CPHYL-----LFTEEDFerigavakcAPPLR-SRSQKEELWRGLLAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 266 DLTTTGTDNctfNTCQKALGK-DDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRIAV 344
Cdd:PRK06189 305 EIDMISSDH---SPCPPELKEgDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 345 GSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTI 424
Cdd:PRK06189 381 GADADFVLVDLD------------------------------------ETYTLTKEDLFYRHKQSPYEGRTFPGRVVATY 424
|
490
....*....|..
gi 2462618093 425 SRGKVVYEAGVF 436
Cdd:PRK06189 425 LRGQCVYQDGEV 436
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-433 |
3.78e-32 |
|
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: 127.56 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 23 ADVLVEDGVVRALGHDLLPPGgapagLRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQGTK-------------- 88
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-----AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKaaahggfttvadmp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 89 -----------VKEEMKILVQDKGVNSF------------------KMFMA------YKDLY--MVTDLELYEAFSRCKE 131
Cdd:TIGR00857 79 ntkppidtpetLEWKLQRLKKVSLVDVHlyggvtqgnqgkelteayELKEAgavgrmFTDDGseVQDILSMRRALEYAAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 132 IGAIAQVHAENGDLIAEGAKKmlaLGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADARRd 211
Cdd:TIGR00857 159 AGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKS- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 212 gkvvYGEPIAASLgtdgthywnkEWHH--------AAHHVMG---PPLRPdPSTPDFLMNLLANDDLTTTGTDNCTFNTC 280
Cdd:TIGR00857 235 ----QGIKITAEV----------TPHHlllseedvARLDGNGkvnPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 281 QKALGkddFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRIAVGSDADIVIWDPKgtrg 360
Cdd:TIGR00857 300 EKTKE---FAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLK---- 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462618093 361 crscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVYEA 433
Cdd:TIGR00857 371 --------------------------------KEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-433 |
1.92e-28 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 116.83 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 5 SRLLIRGGRVVN-DDFSEVADVLVEDGVVRALGHDLlppggAPAGLRVLDAAGKLVLPGGIDTHTHMQFP--------FM 75
Cdd:PRK09357 1 MMILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENI-----EAEGAEVIDATGLVVAPGLVDLHVHLREPgqedketiET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 76 GSRS------------------IDDfhqgTKVKEEMKILVQDKGV------------------NSFKMFMAYK------D 113
Cdd:PRK09357 76 GSRAaaaggfttvvampntkpvIDT----PEVVEYVLDRAKEAGLvdvlpvgaitkglageelTEFGALKEAGvvafsdD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 114 LYMVTD-LELYEAFSRCKEIG-AIAQvHAENGDLIAEGA----KKMLALGITGpeghelcRPEAVEAEATLRAITIASAV 187
Cdd:PRK09357 152 GIPVQDaRLMRRALEYAKALDlLIAQ-HCEDPSLTEGGVmnegEVSARLGLPG-------IPAVAEEVMIARDVLLAEAT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 188 NCPLYIVHVMSKSAAKVIADARRdgkvvYGEPIAA------------SLGTDGTHYwnKewhhaahhvMGPPLRpDPSTP 255
Cdd:PRK09357 224 GARVHICHVSTAGSVELIRWAKA-----LGIKVTAevtphhllltdeDLLTYDPNY--K---------VNPPLR-TEEDR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 256 DFLMNLLANDDLTTTGTD---------NCtfntcqkalgkdDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTS 326
Cdd:PRK09357 287 EALIEGLKDGTIDAIATDhaphareekEC------------EFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 327 TNAAKIFNLYPrkGRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAV 406
Cdd:PRK09357 355 INPARILGLPA--GPLAEGEPADLVIFDPE------------------------------------AEWTVDGEDFASKG 396
|
490 500
....*....|....*....|....*..
gi 2462618093 407 NFNIFEGMVCHGVPLVTISRGKVVYEA 433
Cdd:PRK09357 397 KNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
7-355 |
1.24e-27 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 114.95 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLlppgGAPAglRVLDAAGKLVLPGGIDTHTHMQFP------------- 73
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL----GDAK--EVMDASGLVVSPGMVDAHTHISEPgrshwegyetgtr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 74 ---------FM------------------------GSRSIDDFHQGTKVKEEMKIL--VQDKGVNSFKMFMAY------- 111
Cdd:PRK08044 79 aaakggittMIemplnqlpatvdrasielkfdaakGKLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcgdrgid 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 112 KDLYMVTDLELYEAFSRCKEIGAIAQVHAENG---DLIAEGAKKMlalGITGPEGHELCRPEAVEAEATLRAITIASAVN 188
Cdd:PRK08044 159 NDFRDVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKRE---GRVTAHDYVASRPVFTEVEAIRRVLYLAKVAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 189 CPLYIVHVMSKSAAKVIADARRDGKVVYGEPIaaslgtdgTHYW---NKEWHHAAHHVM-GPPLRpDPSTPDFLMNLLAN 264
Cdd:PRK08044 236 CRLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFvldTDQFEEIGTLAKcSPPIR-DLENQKGMWEKLFN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 265 DDLTTTGTDNctfNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRIAV 344
Cdd:PRK08044 307 GEIDCLVSDH---SPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAP 382
|
410
....*....|.
gi 2462618093 345 GSDADIVIWDP 355
Cdd:PRK08044 383 GKDADFVFIQP 393
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
48-359 |
1.07e-23 |
|
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: 102.32 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 48 GLRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQGTK------------------------VKEEMKILVQDKGVN 103
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKaaaaggfttvvcmpntnpvidnpaVVELLKNRAKDVGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 104 ------------------SFKMFMAYK------DLYMVTDLE-LYEAFSRCKEIGAIAQVHAENGDLIAEGA----KKML 154
Cdd:cd01317 79 rvlpigaltkglkgeeltEIGELLEAGavgfsdDGKPIQDAElLRRALEYAAMLDLPIIVHPEDPSLAGGGVmnegKVAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 155 ALGITGpeghelcRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADARRDGkvvygEPIAASLGtdgthywnk 234
Cdd:cd01317 159 RLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LPVTAEVT--------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 235 eWHH------------AAHHVMgPPLRpDPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGKDDftkIPNGVNGVEDR 302
Cdd:cd01317 218 -PHHlllddealesydTNAKVN-PPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAE---APPGIIGLETA 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462618093 303 MSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPrkGRIAVGSDADIVIWDPKGTR 359
Cdd:cd01317 292 LPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEW 346
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
56-427 |
4.12e-20 |
|
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: 91.63 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 56 GKLVLPGGIDTHTHMQFP--------FMGSRS------------------IDD--------------------FHQGTKV 89
Cdd:cd01318 1 GLLILPGVIDIHVHFREPgltykedfVSGSRAaaaggvttvmdmpntkppTTTaealyeklrlaaaksvvdygLYFGVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 90 KEEMKILVQdKGVNSFKMFMAYKDLYMVTDLE-LYEAFSRCKEIGAiaqVHAENGDLIAEGAKKMLALGItgpegHELCR 168
Cdd:cd01318 81 SEDLEELDK-APPAGYKIFMGDSTGDLLDDEEtLERIFAEGSVLVT---FHAEDEDRLRENRKELKGESA-----HPRIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 169 PEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADARRDGKV-------VYGEPIAASLGTdgthyWNKewhhaah 241
Cdd:cd01318 152 DAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT-----LGK------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 242 hvMGPPLRpDPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRF 321
Cdd:cd01318 220 --VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLTL-VNKGILSLSRV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 322 VAVTSTNAAKIFNLyPRKGRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKT 401
Cdd:cd01318 293 VRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLK------------------------------------EERTIRAEE 335
|
410 420
....*....|....*....|....*.
gi 2462618093 402 HHQAVNFNIFEGMVCHGVPLVTISRG 427
Cdd:cd01318 336 FHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-359 |
5.42e-20 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 92.29 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 1 MAAPSRLLIRGGRVVNDDFSEVADVLVEDGVVRALGHdllpPGGAPAGlRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSI 80
Cdd:PRK09060 1 MTQTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGD----LSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 81 DDFHQGTKVKE--------EM---------KILVQDK---------------------------------GVNSFKMFM- 109
Cdd:PRK09060 74 EDLETGSRAAVlggvtavfEMpntnpltttAEALADKlararhrmhcdfafyvggtrdnadelaelerlpGCAGIKVFMg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 110 -AYKDLyMVTDLELYEAFSRckEIGAIAQVHAENGDLIAEgaKKMLAlgITG-PEGHELCRPEAVEAEATLRAITIASAV 187
Cdd:PRK09060 154 sSTGDL-LVEDDEGLRRILR--NGRRRAAFHSEDEYRLRE--RKGLR--VEGdPSSHPVWRDEEAALLATRRLVRLARET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 188 NCPLYIVHVMSKSAAKVIADARRDGKV--------VYGEPIAASLGTdgthywnkewhhaaHHVMGPPLRpDPSTPDFLM 259
Cdd:PRK09060 227 GRRIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT--------------LAQMNPPIR-DARHRDGLW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 260 NLLANDDLTTTGTDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPRK 339
Cdd:PRK09060 292 RGVRQGVVDVLGSDHAPHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGK 366
|
410 420
....*....|....*....|
gi 2462618093 340 GRIAVGSDADIVIWDPKGTR 359
Cdd:PRK09060 367 GRIAVGYDADFTIVDLKRRE 386
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
4-436 |
6.79e-19 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 88.96 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 4 PSRLLIRGGRVVNDDFS-EVADVLVEDGVVRALGhdllPPGGAPAGLRVLDAAGKLVLPGGIDTHTHMQFP--------F 74
Cdd:PRK07575 2 MMSLLIRNARILLPSGElLLGDVLVEDGKIVAIA----PEISATAVDTVIDAEGLTLLPGVIDPQVHFREPglehkedlF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 75 MGSR------------------------SIDD--------------FHQGTkVKEEMKILVQDKGVNSFKMFM--AYKDL 114
Cdd:PRK07575 78 TASRacakggvtsflempntkpltttqaALDDklaraaekcvvnygFFIGA-TPDNLPELLTANPTCGIKIFMgsSHGPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 115 YMVTDLELYEAFSRCKEIgaIAqVHAENGDLIAEgAKKMLAlGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIV 194
Cdd:PRK07575 157 LVDEEAALERIFAEGTRL--IA-VHAEDQARIRA-RRAEFA-GISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 195 HVMSKSAAKVIADARRDGKVVYGEPIAASLGTD-----GThywnkewhhAAHhvMGPPLRpDPSTPDFLMNLLANDDLTT 269
Cdd:PRK07575 232 HLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTDayeriGT---------LAQ--MNPPLR-SPEDNEALWQALRDGVIDF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 270 TGTDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRIAVGSDAD 349
Cdd:PRK07575 300 IATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 350 IVIWDpkgtrgcrscvafsdngsvyktnMNlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKV 429
Cdd:PRK07575 375 LVLVD-----------------------LN-------------TYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQI 418
|
....*..
gi 2462618093 430 VYEAGVF 436
Cdd:PRK07575 419 VFDRGQV 425
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-434 |
9.82e-15 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 76.35 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 12 GRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGAPAGlRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQGTK--- 88
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKSQKKP-HVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKaaa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 89 -----------------------VKEEM-----KILVQ----------------------DKGVNSFKMFM---AYKDLY 115
Cdd:PLN02795 128 aggittlvdmplnsfpsttsvetLELKIeaakgKLYVDvgfwgglvpenahnasvleellDAGALGLKSFMcpsGINDFP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 116 MVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAkkMLALGITGPEGHELCRPEAVEAEATLRAITIAS-------AVN 188
Cdd:PLN02795 208 MTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKdtrpggvAEG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 189 CPLYIVHVM-SKSAAKVIADARRDGKVVYGEPIAASLG------TDGthywnkewhhAAHHVMGPPLRpDPSTPDFLMNL 261
Cdd:PLN02795 286 AHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAfsaeeiPDG----------DTRYKCAPPIR-DAANRELLWKA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 262 LANDDLTTTGTDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGkMDENRFVAVTSTNAAKIFNLyPRKGR 341
Cdd:PLN02795 355 LLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-DSKGA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 342 IAVGSDADIVIWDPKGTrgcrscvaFSDNGSVyktnmnlplqclanaRVHMEERTISAKTHHQavnfniFEGMVchgvpL 421
Cdd:PLN02795 433 IAPGKDADIVVWDPEAE--------FVLDESY---------------PIYHKHKSLSPYLGTK------LSGKV-----I 478
|
490
....*....|...
gi 2462618093 422 VTISRGKVVYEAG 434
Cdd:PLN02795 479 ATFVRGNLVFLEG 491
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
8-434 |
6.09e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 67.10 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 8 LIRGGRVVNDDFSEvADVLVEDGVVRALGHDLLPpggapaGLRVLDAAGKLVLPGGIDTHTHMQ-FPFMGSRSIDD---- 82
Cdd:PRK04250 1 VLEGKFLLKGRIVE-GGIGIENGRISKISLRDLK------GKEVIKVKGGIILPGLIDVHVHLRdFEESYKETIESgtka 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 83 -FHQGTKVKEEM---KILVQDKGVNSFKMFMAYKDLYMVTDL---------ELYEAFSRCKEIG---AIAQVHAENGDLI 146
Cdd:PRK04250 74 aLHGGITLVFDMpntKPPIMDEKTYEKRMRIAEKKSYADYALnfliagnceKAEEIKADFYKIFmgaSTGGIFSENFEVD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 147 AEGAKKMLALGITGPE--GHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADARRDGKVVYGEPiaasl 224
Cdd:PRK04250 154 YACAPGIVSVHAEDPEliREFPERPPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILKSNLPWVSFEVTP----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 225 gtdgthywnkewhhaaHHVM--------------GPPLRPDPSTPDFLMNL-----LANDDLTTTGTDnctfntcqKALG 285
Cdd:PRK04250 229 ----------------HHLFltrkdyernpllkvYPPLRSEEDRKALWENFskipiIASDHAPHTLED--------KEAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 286 KddftkipNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNlYPRKGrIAVGSDADIVIWDPKgtrgcrscv 365
Cdd:PRK04250 285 A-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMK--------- 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462618093 366 afsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVYEAG 434
Cdd:PRK04250 346 ---------------------------KEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-354 |
6.53e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 66.91 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 2 AAPSRLLIRGGRVV---NDDFSEVADVLVEDGVVRALGHDLLPPggAPAGLRVLDAAGKLVLPGGIDTHTHMqfpFMGSR 78
Cdd:COG1228 5 AQAGTLLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPAADLA--VPAGAEVIDATGKTVLPGLIDAHTHL---GLGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 79 SIDDFHQGTKVKEEMkilvqdkgvnsfkmfmaykDLYMVTDLELYEAFS------RCKEIGAIAqvhaeNGDLIAEGAKK 152
Cdd:COG1228 80 RAVEFEAGGGITPTV-------------------DLVNPADKRLRRALAagvttvRDLPGGPLG-----LRDAIIAGESK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 153 ML--------ALGITGPEGHELCRPEavEAEATLRAITIASAVNCPLYI---VHVMSKSAAKVIAD-ARRDGKVVYG--- 217
Cdd:COG1228 136 LLpgprvlaaGPALSLTGGAHARGPE--EARAALRELLAEGADYIKVFAeggAPDFSLEELRAILEaAHALGLPVAAhah 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 218 --EPI--AASLGTDGthywnkewhhaAHHvmGPPLRPDpstpdfLMNLLANDDLTTTGTDNCTFNTCQKALGKDDFTKIP 293
Cdd:COG1228 214 qaDDIrlAVEAGVDS-----------IEH--GTYLDDE------VADLLAEAGTVVLVPTLSLFLALLEGAAAPVAAKAR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 294 NGVNGVEDRMSVIWEKGV------HSG--------------KMDENRF------VAVTStNAAKIFNLYPRKGRIAVGSD 347
Cdd:COG1228 275 KVREAALANARRLHDAGVpvalgtDAGvgvppgrslhrelaLAVEAGLtpeealRAATI-NAAKALGLDDDVGSLEPGKL 353
|
....*..
gi 2462618093 348 ADIVIWD 354
Cdd:COG1228 354 ADLVLLD 360
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
44-376 |
2.58e-11 |
|
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: 64.83 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 44 GAPAGLRVLDAAGKLVLpgGIdthtHMQFPFMGSRSIDDFHQG----TKVKEEMKILVQDKGVNSFKMFMAYKDlYMVTD 119
Cdd:pfam01979 54 TSTGIEALLEAAEELPL--GL----RFLGPGCSLDTDGELEGRkalrEKLKAGAEFIKGMADGVVFVGLAPHGA-PTFSD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 120 LELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKmlALGITGPEGHELcrpEAVEAEATLRAITIASAVNcplyiVHVMSK 199
Cdd:pfam01979 127 DELKAALEEAKKYGLPVAIHALETKGEVEDAIA--AFGGGIEHGTHL---EVAESGGLLDIIKLILAHG-----VHLSPT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 200 SAAKVIADARRDGkvVYGEPIAASLGTDGThywnkewhhaahhvmgPPLRPdpstpdflmnLLANDDLTTTGTDNCtfnt 279
Cdd:pfam01979 197 EANLLAEHLKGAG--VAHCPFSNSKLRSGR----------------IALRK----------ALEDGVKVGLGTDGA---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 280 cqkaLGKDDFTKIPNGVNGVEDRmsviwekGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIVIWDPKGTr 359
Cdd:pfam01979 245 ----GSGNSLNMLEELRLALELQ-------FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL- 312
|
330
....*....|....*..
gi 2462618093 360 gcRSCVAFSDNGSVYKT 376
Cdd:pfam01979 313 --AAFFGLKPDGNVKKV 327
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
7-354 |
3.96e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 64.49 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVN--DDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMqFPFM--------- 75
Cdd:PRK09237 1 LLLRGGRVIDpaNGIDGVIDIAIEDGKIAAVAGDIDGSQAK----KVIDLSGLYVSPGWIDLHVHV-YPGStpygdepde 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 76 ----------------GSRSIDDFHQGTKVKEEMKILvqdkgvnsfkmfmAYKDLY---MVTDLELYEafSRCKEIGAIA 136
Cdd:PRK09237 76 vgvrsgvttvvdagsaGADNFDDFRKLTIEASKTRVL-------------AFLNISrigLLAQDELAD--LEDIDADAVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 137 QVHAENGDLIAeGAKKMLALGITGPEGhelcrpeaveAEATLRAITIASAVNCPLYiVHVMSKSAA-KVIADARRDGKVV 215
Cdd:PRK09237 141 EAVKRNPDFIV-GIKARMSSSVVGDNG----------IEPLELAKAIAAEANLPLM-VHIGNPPPSlEEILELLRPGDIL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 216 ygepiaaslgtdgTHYWNkewHHAahhvmGPPLRPDPSTPDFLMNLLAND---DLtTTGTDNCTFNTCQKAL-------- 284
Cdd:PRK09237 209 -------------THCFN---GKP-----NRILDEDGELRPSVLEALERGvrlDV-GHGTASFSFKVAEAAIaagilpdt 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462618093 285 -GKDDFTKipNGVNG-VEDrMSVIWEKGVHSGkMDENRFVAVTSTNAAKIFNLyPRKGRIAVGSDADIVIWD 354
Cdd:PRK09237 267 iSTDIYCR--NRINGpVYS-LATVMSKFLALG-MPLEEVIAAVTKNAADALRL-PELGRLQVGSDADLTLFT 333
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
7-69 |
2.97e-10 |
|
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: 61.93 E-value: 2.97e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462618093 7 LLIRGGRVV----NDDFSevADVLVEDGVVRALGHDLLPPGGapaglRVLDAAGKLVLPGGIDTHTH 69
Cdd:cd01297 2 LVIRNGTVVdgtgAPPFT--ADVGIRDGRIAAIGPILSTSAR-----EVIDAAGLVVAPGFIDVHTH 61
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
2-71 |
3.70e-10 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 62.02 E-value: 3.70e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462618093 2 AAPSRLLIRGGRVVNDD--FSEVADVLVEDGVVRALGHDLLppggapAGLRVLDAAGKLVLPGGIDTHTHMQ 71
Cdd:PRK09061 16 MAPYDLVIRNGRVVDPEtgLDAVRDVGIKGGKIAAVGTAAI------EGDRTIDATGLVVAPGFIDLHAHGQ 81
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
6-76 |
4.20e-10 |
|
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: 61.77 E-value: 4.20e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462618093 6 RLLIRGGRVV--NDDFSEVAD--VLVEDGVVRALGHDLLPPGGAPaGLRVLDAAGKLVLPGGIDTHTHM-QFPFMG 76
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELPARYP-AAEVIDAGGKLVLPGLVNTHTHLpQTLLRG 75
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
7-70 |
1.20e-09 |
|
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: 60.29 E-value: 1.20e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462618093 7 LLIRGGRVVNDDFSEV---ADVLVEDGVVRALGHDLlpPGGAPAGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPAL--PLPAYPADEVIDAKGKVVMPGLVNTHTHL 65
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
24-356 |
4.64e-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: 58.11 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 24 DVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMqFPFM----------------------GSRSID 81
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAAT----QIVDAGGCYVSPGWIDLHVHV-YQGGtrygdrpdmigvksgvttvvdaGSAGAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 82 DFHqgtkvkEEMKILVQDKGVNSFkmfmAYKDLYMVTDLELYEAFS-RCKEIGAIAQVHAENGDLIAeGAKKMLALGITG 160
Cdd:cd01307 76 NID------GFRYTVIERSATRVY----AFLNISRVGLVAQDELPDpDNIDEDAVVAAAREYPDVIV-GLKARASKSVVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 161 PEGHELCRpeaveaeatlRAITIASAVNCPLYiVHVMSKSA--AKVIADARRdGKVVygepiaaslgtdgTHYWNK---- 234
Cdd:cd01307 145 EWGIKPLE----------LAKKIAKEADLPLM-VHIGSPPPilDEVVPLLRR-GDVL-------------THCFNGkpng 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 235 ------EWHHAAHHVMGPPLRPDpstpdflmnlLANddltttGTDNCTFNTCQKA---------LGKDDFTKipNGVNGV 299
Cdd:cd01307 200 ivdeegEVLPLVRRARERGVIFD----------VGH------GTASFSFRVARAAiaagllpdtISSDIHGR--NRTNGP 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462618093 300 EDRMSVIWEKGVHSGKMDENRFVAVTsTNAAKIFNLyPRKGRIAVGSDADIVIWDPK 356
Cdd:cd01307 262 VYALATTLSKLLALGMPLEEVIEAVT-ANPARMLGL-AEIGTLAVGYDADLTVFDLK 316
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
2-70 |
9.06e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 57.89 E-value: 9.06e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462618093 2 AAPSRLLIRGGRV--VNDDFSEVADVLVEDGVVRALGHDLLPPGGAPAGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:COG1574 5 AAAADLLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
5-69 |
1.68e-08 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 56.74 E-value: 1.68e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462618093 5 SRLLIRGGRV---VNDDFSEVADVLVEDGVVRALghdllPPGGAPAglRVLDAAGKLVLPGGIDTHTH 69
Cdd:COG1229 1 MELIIKNGRVydpANGIDGEVMDIAIKDGKIVEE-----PSDPKDA--KVIDASGKVVMAGGVDIHTH 61
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
4-69 |
2.02e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 56.55 E-value: 2.02e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 4 PSRLLIRGGRVVNDD----FSEVADVLVEDGVVRALGhdllpPGGAPAGLRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK08204 1 MKRTLIRGGTVLTMDpaigDLPRGDILIEGDRIAAVA-----PSIEAPDAEVVDARGMIVMPGLVDTHRH 65
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
7-358 |
8.39e-08 |
|
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: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGhdllPPGGAPAGLRVLDAAGKLVLPGGIDTHTHmqfpfmGSRSIdDFHQG 86
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIG----PEDELEEADEIIDLKGQYLVPGFIDIHIH------GGGGA-DFMDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 87 TkvKEEMKILVQ---DKGVNSFkmfmaYKDLYMVTDLELYEAFSRCKE-----IGA-IAQVHAEnGDLIAEGAKkmlalg 157
Cdd:cd00854 70 T--AEALKTIAEalaKHGTTSF-----LPTTVTAPPEEIAKALAAIAEaiaegQGAeILGIHLE-GPFISPEKK------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 158 itGPEGHELCRPEAVE--------AEATLRAITIAsavncplyIVHVMSKSAAKVIADArrdGKVV--------YGEPIA 221
Cdd:cd00854 136 --GAHPPEYLRAPDPEelkkwleaAGGLIKLVTLA--------PELDGALELIRYLVER---GIIVsighsdatYEQAVA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 222 A-SLGTDG-THYWN--KEWHH-------AA--------------HHVmgpplrpDPSTPDFLMNLlanddlttTGTDNCT 276
Cdd:cd00854 203 AfEAGATHvTHLFNamSPLHHrepgvvgAAlsdddvyaeliadgIHV-------HPAAVRLAYRA--------KGADKIV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 277 FNT-CQKALGKDDFT-KIPNGVNGVEDRMSVIwEKGVHSG---KMDE--NRFV---------AV--TSTNAAKIFNLYPR 338
Cdd:cd00854 268 LVTdAMAAAGLPDGEyELGGQTVTVKDGVARL-ADGTLAGstlTMDQavRNMVkwggcpleeAVrmASLNPAKLLGLDDR 346
|
410 420
....*....|....*....|
gi 2462618093 339 KGRIAVGSDADIVIWDPKGT 358
Cdd:cd00854 347 KGSLKPGKDADLVVLDDDLN 366
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
8-70 |
1.13e-07 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 53.79 E-value: 1.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462618093 8 LIRGGRVVNDDFSEVaDVLVEDGVVRALGHDLLPPGGAPaglrVLDAAGKLVLPGGIDTHTHM 70
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAE----EVDAKGRLVLPAFVDPHIHL 58
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
5-69 |
1.27e-07 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 53.72 E-value: 1.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462618093 5 SRLLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSAD----TVIDAAGRYLLPGMIDDQVH 62
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
8-69 |
1.45e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.56 E-value: 1.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462618093 8 LIRGGRVVNDD-FSEVADVLVEDGVVRALGhdllppGGAPAGLRVLDAAGKLVLPGGIDTHTH 69
Cdd:COG1820 1 AITNARIFTGDgVLEDGALLIEDGRIAAIG------PGAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-104 |
1.78e-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: 53.03 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 25 VLVEDGVVRALG--HDLLPPGGAPAglRVLDAAGKLVLPGGIDTHTHmqFPFMGSRSiDDFHQGTKVKEEMKILVQDKGV 102
Cdd:cd01296 1 IAIRDGRIAAVGpaASLPAPGPAAA--EEIDAGGRAVTPGLVDCHTH--LVFAGDRV-DEFAARLAGASYEEILAAGGGI 75
|
..
gi 2462618093 103 NS 104
Cdd:cd01296 76 LS 77
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
25-73 |
2.14e-07 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 53.27 E-value: 2.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2462618093 25 VLVEDGVVRALGH--DLLPpgGAPAGLRVLDAAGKLVLPGGIDTHTHmqFP 73
Cdd:PRK09228 34 LLVEDGRIVAAGPyaELRA--QLPADAEVTDYRGKLILPGFIDTHIH--YP 80
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
5-70 |
2.60e-07 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 52.93 E-value: 2.60e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462618093 5 SRLLIRGGRVV---NDDFSEVAD--VLVEDGVVRALGhdllpPGGAP--AGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:PRK08203 1 TTLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVG-----PGGALpqPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
7-78 |
3.47e-07 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 52.34 E-value: 3.47e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462618093 7 LLIRGGRVVND--DFSEVADVLVEDGVVRALGHDLLPpGGAPAGLRVLDAAGKLVLPGGIDTHTHMQFPFMGSR 78
Cdd:PRK09059 5 ILLANARIIDPsrGLDEIGTVLIEDGVIVAAGKGAGN-QGAPEGAEIVDCAGKAVAPGLVDARVFVGEPGAEHR 77
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
7-78 |
4.69e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 51.86 E-value: 4.69e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462618093 7 LLIRGGRvvnDDFSEVADVLVEDGVVRALGhdllPPGGAPAGLRVLDAAGKLVLPGGIDTHTHMQFPFMGSR 78
Cdd:PRK05985 4 LLFRNVR---PAGGAAVDILIRDGRIAAIG----PALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDP 68
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
4-68 |
2.77e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 49.41 E-value: 2.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462618093 4 PSRLLIRGGRVVNDDfsEV--ADVLVEDGVVRALGhdllpPGGAPAGlRVLDAAGKLVLPGGIDTHT 68
Cdd:PRK15446 1 MMEMILSNARLVLPD--EVvdGSLLIEDGRIAAID-----PGASALP-GAIDAEGDYLLPGLVDLHT 59
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
295-356 |
2.79e-06 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 49.70 E-value: 2.79e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462618093 295 GVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLypRKGRIAVGSDADIVIWDPK 356
Cdd:PRK08417 294 GIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPN 353
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
322-355 |
4.52e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.94 E-value: 4.52e-06
10 20 30
....*....|....*....|....*....|....
gi 2462618093 322 VAVTSTNAAKIFNLYPRKGRIAVGSDADIVIWDP 355
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDD 361
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
23-70 |
4.84e-06 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 48.83 E-value: 4.84e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2462618093 23 ADVLVEDGVVRALghdlLPPGGAPAGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:PRK07583 41 VDIEIADGKIAAI----LPAGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
7-69 |
1.42e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 47.49 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462618093 7 LLIRGGRVVNDDFSEV--ADVLVEDGVVRALGHDLLPPGGApaglrVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK08393 3 ILIKNGYVIYGENLKVirADVLIEGNKIVEVKRNINKPADT-----VIDASGSVVSPGFINAHTH 62
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
16-354 |
1.99e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 46.77 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 16 NDDFSEVAdVLVEDGVVRALGHDLlppGGAPAglRVLDAAgklVLPGGIDTHTHMQFPfmGSRSIDDFHQG--------T 87
Cdd:PRK01211 10 KGKFDYLE-IEVEDGKIKSIKKDA---GNIGK--KELKGA---ILPAATDIHVHFRTP--GETEKEDFSTGtlsaifggT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 88 KVKEEM---KILVQDkgVNSFKMFMAYKDLYMVTDLELYEAFS-------RCKEIGA---IAQVHAENGDLIAEG-AKKM 153
Cdd:PRK01211 79 TFIMDMpnnNIPIKD--YNAFSDKLGRVAPKAYVDFSLYSMETgnnalilDERSIGLkvyMGGTTNTNGTDIEGGeIKKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 154 LALGITGPEGHEL--CRPEAVEAEATLRAITIASAVNCPLYIVHVMSK--SAAKVIAdarrdgKVVYGEPIAASLGTDGT 229
Cdd:PRK01211 157 NEANIPVFFHAELseCLRKHQFESKNLRDHDLARPIECEIKAVKYVKNldLKTKIIA------HVSSIDVIGRFLREVTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462618093 230 HYW--NKEWHHAAHHVMGPPLRpDPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKAlgkdDFTKIPNGVNGVEDRMSVIW 307
Cdd:PRK01211 231 HHLllNDDMPLGSYGKVNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ----EFEYAKSGIIGVETRVPLFL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2462618093 308 EKgVHSGKMDENRFVAVTSTNAAKIFNLypRKGRIAVGSDADIVIWD 354
Cdd:PRK01211 306 AL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFD 349
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
7-70 |
2.21e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 47.02 E-value: 2.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462618093 7 LLIRGGRVVNDDFSEV--ADVLVEDGVVRALGHDLLPpggapaGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:COG1001 7 LVIKNGRLVNVFTGEIleGDIAIAGGRIAGVGDYIGE------ATEVIDAAGRYLVPGFIDGHVHI 66
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
9-69 |
2.27e-05 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 47.02 E-value: 2.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462618093 9 IRGGRVV---NDDFSEVADVLVEDGVVRAlghdllPPGGAPAGlRVLDAAGKLVLPGGIDTHTH 69
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVE------SSSGAKPA-KVIDASGKVVMAGGVDMHSH 57
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
5-69 |
3.30e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 46.15 E-value: 3.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462618093 5 SRLLIRGGRVVNDDFSEV---ADVLVEDGVVRALGhDLLPPGGAPaglRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK07228 1 MTILIKNAGIVTMNAKREivdGDVLIEDDRIAAVG-DRLDLEDYD---DHIDATGKVVIPGLIQGHIH 64
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
24-70 |
7.74e-05 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 44.99 E-value: 7.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2462618093 24 DVLVEDGVVRALGHDLLPPGGAPAGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
7-69 |
2.49e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 43.39 E-value: 2.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462618093 7 LLIRGGRVVNDD----FSEVADVLVEDGVVRALGH--DLlppGGAPAGLRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK07203 2 LLIGNGTAITRDpakpVIEDGAIAIEGNVIVEIGTtdEL---KAKYPDAEFIDAKGKLIMPGLINSHNH 67
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
17-77 |
3.18e-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: 43.04 E-value: 3.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462618093 17 DDFSEVADVL--VEDGVVRALGHDLLPPGG-------APAGLRVLDAAGKLVLPGGIDTHTHM-QFPFMGS 77
Cdd:cd01303 12 PELELVEDALrvVEDGLIVVVDGNIIAAGAaetlkraAKPGARVIDSPNQFILPGFIDTHIHApQYANIGS 82
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
6-65 |
9.39e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 41.59 E-value: 9.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462618093 6 RLLIRGGRVVN--DDFSEVADVLVEDGVVRALGHdllppggAPAGL---RVLDAAGKLVLPGGID 65
Cdd:PRK07627 2 KIHIKGGRLIDpaAGTDRQADLYVAAGKIAAIGQ-------APAGFnadKTIDASGLIVCPGLVD 59
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
322-355 |
1.03e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 41.36 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....
gi 2462618093 322 VAVTSTNAAKIFNLYPRKGRIAVGSDADIVIWDP 355
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDD 438
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
7-70 |
1.04e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 41.54 E-value: 1.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462618093 7 LLIRGGRVvnDDFSEVADVLVEDGVVRALGHDLlppgGAPAGlRVLDAAGKLVLPGGIDTHTHM 70
Cdd:PRK07572 4 LIVRNANL--PDGRTGIDIGIAGGRIAAVEPGL----QAEAA-EEIDAAGRLVSPPFVDPHFHM 60
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
50-70 |
1.39e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 40.98 E-value: 1.39e-03
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
323-354 |
2.90e-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: 39.99 E-value: 2.90e-03
10 20 30
....*....|....*....|....*....|..
gi 2462618093 323 AVTStNAAKIFNLYPRKGRIAVGSDADIVIWD 354
Cdd:cd01309 308 AITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
7-69 |
2.93e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.12 E-value: 2.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462618093 7 LLIRGGRVVNDDFSEV--ADVLVEDGVVRALGHDllPPGGAPaglRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDAD---TVIDAKGSVVMPGLVNTHTH 63
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
324-356 |
3.67e-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: 39.68 E-value: 3.67e-03
10 20 30
....*....|....*....|....*....|...
gi 2462618093 324 VTSTNAAKIFNLYPrKGRIAVGSDADIVIWDPK 356
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD 361
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
23-70 |
5.57e-03 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 39.28 E-value: 5.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2462618093 23 ADVLVEDGVVRALGHdlLPPggaPAGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:PRK12393 26 PDIRIRDGRIAAIGA--LTP---LPGERVIDATDCVVYPGWVNTHHHL 68
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
7-70 |
6.09e-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: 38.91 E-value: 6.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462618093 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYE--NVTVVDLHGKILVPGFIDQHVHI 63
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
29-69 |
6.54e-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: 6.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2462618093 29 DGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTH 69
Cdd:cd01309 1 DGKIVAVGAEITTPADA----EVIDAKGKHVTPGLIDAHSH 37
|
|
| |
