|
Name |
Accession |
Description |
Interval |
E-value |
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
31-619 |
0e+00 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 662.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 31 GKRPANMLLRVGRLLDVHTRTWLEDqEIAIRGRRIAWTGPAgtfPGTAAAQAERPGLSAVPGFGEVHKHIESSHITPEYE 110
Cdd:COG1001 1 GREPADLVIKNGRLVNVFTGEILEG-DIAIAGGRIAGVGDY---IGEATEVIDAAGRYLVPGFIDGHVHIESSMVTPAEF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 111 AALVLPRGNTWTCEASHEFSNVDGAHNLEFWLTARRHGsPMKIFPLPGSAVPPT-AYEWGGGYYGYDEQADFLKQSlMVA 189
Cdd:COG1001 77 ARAVLPHGTTTVIADPHEIANVLGLEGVRYMLEAAEGL-PLDIFVMLPSCVPATpGLETAGAVLGAEDLAELLDHP-RVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 190 GLDEVMDWPAVWNPEnpshKRLWGMIQATFEKRGVVEGHGAGLRDLNsINAFAAAGLASDHEGWTAEEVWDKLRHGIFIE 269
Cdd:COG1001 155 GLGEVMNFPGVLNGD----PRMLAKIAAALAAGKVIDGHAPGLSGKD-LNAYAAAGIRSDHECTTAEEALEKLRRGMYVM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 270 IRPHSMPEIIAGLIErGLT--DWSQVAFATDDRSASDTLKRGATDHNVRLAIQSGLTPEIAIQCVTINPARHMRLTPwVG 347
Cdd:COG1001 230 IREGSAAKDLPALLP-AVTelNSRRCALCTDDRHPDDLLEEGHIDHVVRRAIELGLDPVTAIQMATLNAAEHFGLKD-LG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 348 SIAPGRFADIVLLDDVEKLSITEVWADGEPISKGMEYLGPLPAIDWPEWASQTVNIkRRIEPEDFAIAAeKGRETMQAAL 427
Cdd:COG1001 308 AIAPGRRADIVLLDDLEDFKVEKVYADGKLVAEDGKLLVDLPKYPYPPWARNTVKL-RPLTAEDFAIPA-PGGVKVRVIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 428 LRPFHWHDEFITMELSTENDEVQRDPDRNVTKFAIVDRFSGEAKISRMFWLGCGpkTPDTAVGCTVAHDKHNLWIVGSSD 507
Cdd:COG1001 386 VIPGQIITEHLEAELPVEDGEVVPDPERDILKIAVVERHGGTGNIGLGFVKGFG--LKRGAIASTVAHDSHNLIVVGTND 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 508 EAMAMVANRVAEIGGGWVLVSGGKVLAEVRYEIGGLMTQRPAEELDAEMQQLYGAAETIEW-LYEPTFsprwypgfpeRL 586
Cdd:COG1001 464 EDMALAANRLIEIGGGIVVVKDGKVLAELPLPIAGLMSDEPAEEVAEKLEALRAAARELGCtLEEPFM----------TL 533
|
570 580 590
....*....|....*....|....*....|...
gi 1274314359 587 QFATLTCAPwrwvlvaPCEAAPQGFVNVATGQV 619
Cdd:COG1001 534 SFLALPVIP-------ELKLTDRGLVDVTTFEF 559
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
90-575 |
7.06e-89 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 282.19 E-value: 7.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 90 VPGFGEVHKHIESSHITPEYEAALVLPRGNTWTCEASHEFSNVDGAHNLEFWLTARRHgSPMKIFPLPGSAVPPTAYEWG 169
Cdd:cd01295 8 VPGFIDAHLHIESSMLTPSEFAKAVLPHGTTTVIADPHEIANVAGVDGIEFMLEDAKK-TPLDIFWMLPSCVPATPFETS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 170 GGYYGYDEQADFLKQSlMVAGLDEVMDWPAVWNPEnpshKRLWGMIQATFEKRGVVEGHGAGLRDlNSINAFAAAGLASD 249
Cdd:cd01295 87 GAELTAEDIKELLEHP-EVVGLGEVMDFPGVIEGD----DEMLAKIQAAKKAGKPVDGHAPGLSG-EELNAYMAAGISTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 250 HEGWTAEEVWDKLRHGIFIEIRPHSMPEIIAGLIERGL-TDWSQVAFATDDRSASDTLKRGATDHNVRLAIQSGLTPEIA 328
Cdd:cd01295 161 HEAMTGEEALEKLRLGMYVMLREGSIAKNLEALLPAITeKNFRRFMFCTDDVHPDDLLSEGHLDYIVRRAIEAGIPPEDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 329 IQCVTINPARHMRLTPwVGSIAPGRFADIVLLDDVEKLSITEVWADGepiskgmeylgplpaidwpewasqtvnikrrie 408
Cdd:cd01295 241 IQMATINPAECYGLHD-LGAIAPGRIADIVILDDLENFNITTVLAKG--------------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 409 pedfaiaaekgretmqaallrpfhwhdefitmelstendevqrdpdrnvtkFAIVDRFSGEAKISRMFWLGCGPKtpDTA 488
Cdd:cd01295 287 ---------------------------------------------------IAVVERHGKTGNIGVGFVKGFGLK--EGA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 489 VGCTVAHDKHNLWIVGSSDEAMAMVANRVAEIGGGWVLVSGGKVLAEVRYEIGGLMTQRPAEELDAEMQQLYGAAETI-E 567
Cdd:cd01295 314 IASSVAHDSHNIIVIGTNDEDMALAVNRLKEIGGGIVVVKNGKVLAELPLPIAGLMSDEPAEEVAEELKKLREALRELgY 393
|
490
....*....|
gi 1274314359 568 WLYEP--TFS 575
Cdd:cd01295 394 ALDDPfmTLS 403
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
42-566 |
1.79e-84 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 274.73 E-value: 1.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 42 GRLLDVHTRTWLEdQEIAIRGRRIAWTGpagTFPGTAAAQAErpGLSAVPGFGEVHKHIESSHITPEYEAALVLPRGNTW 121
Cdd:TIGR01178 7 AKIIDVYNGEIIP-GDIAIANGHIAGVG---KYNGVKVIDAL--GEYAVPGFIDAHIHIESSMLTPSEFAKLVLPHGVTT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 122 TCEASHEFSNVDGAHNLEFWLTARRHgSPMKIFPLPGSAVPPTAYEwGGGYYGYDEQADFLKQSLMVAGLDEVMDWPAVW 201
Cdd:TIGR01178 81 VVSDPHEIANVNGEDGINFMLNNAKK-TPLNFYFMLPSCVPALQFE-TSGAVLTAEDIDELMELDEVLGLAEVMDYPGVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 202 NPENPSHKRLwgmiqATFEKRG-VVEGHGAGLRDlNSINAFAAAGLASDHEGWTAEEVWDKLRHGIFIEIRPHSMP---E 277
Cdd:TIGR01178 159 NADIEMLNKI-----NSARKRNkVIDGHCPGLSG-KLLNKYISAGISNDHESTSIEEAREKLRLGMKLMIREGSAAknlE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 278 IIAGLIERglTDWSQVAFATDDRSASDTLKRGATDHNVRLAIQSGLTPEIAIQCVTINPARHMRLtPWVGSIAPGRFADI 357
Cdd:TIGR01178 233 ALHPLINE--KNCRSLMLCTDDRHVNDILNEGHINHIVRRAIEHGVDPFDALQMASINPAEHFGI-DVGGLIAPGDPADF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 358 VLLDDVEKLSITEVWADGEPISKGMEYLGPLPAIDWPEWASQTVNIKRRIEPEDFAIAAEKGRetmQAALLRPFhwHDEF 437
Cdd:TIGR01178 310 VILKDLRNFKVNKTYVKGKLLDLNEVFNDEISRIPLINEIPINVKARSPKSISDFGIQFKTGN---RIRVIKVI--SNQL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 438 ITMELSTENDEVQR-DPDRNVTKFAIVDRFSGEAKISRMFWLGCGPKtpDTAVGCTVAHDKHNLWIVGSSDEAMAMVANR 516
Cdd:TIGR01178 385 ITHKTSNSVAEEFGsDIEEDILKIAVIERHKDNGKIGKGLIKGFGLK--EGAIASTVAHDSHNIIAVGSNDEDLALAVNK 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1274314359 517 VAEIGGGWVLVSGGKVLAEVRYEIGGLMTQRPAEELDAEMQQLYGAAETI 566
Cdd:TIGR01178 463 LIQIGGGLCAAKNGEVTIILPLPIAGLMSDDSAERVAEQIIALNDKCRNV 512
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
23-566 |
8.46e-53 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 190.81 E-value: 8.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 23 QDLVLVALGKRPANMLLRVGRLLDVHTRTWLEDqEIAIRGRRIAWTGPAgtFPGTAAAQA-ERPGLSAVPGFGEVHKHIE 101
Cdd:PRK10027 18 QELLAVSRGDAVADYIIDNVSILDLINGGEISG-PIVIKGRYIAGVGAE--YADAPALQRiDARGATAVPGFIDAHLHIE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 102 SSHITP-EYEAAlVLPRGNTWTCEASHEFSNVDGAHNLEfWLTARRHGSPMKIFPLPGSAVPPTA-YEWGGGYYGYDEQA 179
Cdd:PRK10027 95 SSMMTPvTFETA-TLPRGLTTVICDPHEIVNVMGEAGFA-WFARCAEQARQNQYLQVSSCVPALEgCDVNGASFTLEQML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 180 DFlKQSLMVAGLDEVMDWPAVWNPENPSHKRLWGMIQATfekrgvVEGHGAGLRDLnSINAFAAAGLASDHEGWTAEEVW 259
Cdd:PRK10027 173 AW-RDHPQVTGLAEMMDYPGVISGQNALLDKLDAFRHLT------LDGHCPGLGGK-ELNAYIAAGIENCHESYQLEEGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 260 DKLRHGIFIEIRPHSMP---EIIAGLIerglTDWS--QVAFATDDRSASDTLKRGATDHNVRLAIQS-GLTPEIAIQCVT 333
Cdd:PRK10027 245 RKLQLGMSLMIREGSAArnlNALAPLI----NEFNspQCMLCTDDRNPWEIAHEGHIDALIRRLIEQhNVPLHVAYRVAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 334 INPARHMRLTPwVGSIAPGRFADIVLLDDVEKLSITEVWADGEPISKgMEYLGPLPAIDWPEWASQTVNIKRR-IEPEDF 412
Cdd:PRK10027 321 WSTARHFGLNH-LGLLAPGKQADIVLLSDARKVTVQQVLVKGEPIDA-QTLQAEESARLAQSAPPYGNTIARQpVSASDF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 413 AIAAEKGRETMQAALLrpfhwHDEFITMELSTENDEVQRDPDrNVTKFAIVDRFsGEAKISRMFWLGcGPKTPDTAVGCT 492
Cdd:PRK10027 399 ALQFTPGKRYRVIDVI-----HNELITHSRSSVYSENGFDRD-DVCFIAVLERY-GQRLAPACGLLG-GFGLNEGALAAT 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274314359 493 VAHDKHNLWIVGSSDEAMAMVANRVAEIGGGWVLVSGGKVLAEVRYEIGGLMTQRPAEELDAEMQQLYGAAETI 566
Cdd:PRK10027 471 VSHDSHNIVVIGRSAEEMALAVNQVIQDGGGLCVVRNGQVQSHLPLPIAGLMSTDTAQSLAEQIDALKAAAREC 544
|
|
| Adenine_deam_C |
pfam13382 |
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine ... |
438-595 |
3.27e-33 |
|
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine deaminase enzyme.
Pssm-ID: 463864 [Multi-domain] Cd Length: 168 Bit Score: 124.86 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 438 ITMELSTENDEVQRDPDRNVTKFAIVDRFSGEAKISRMFWLGCGPKTPdtAVGCTVAHDKHNLWIVGSSDEAMAMVANRV 517
Cdd:pfam13382 6 LEVELPVKDGVVVPDPERDILKIAVVERHGGTGNIGVGFVKGFGLKRG--AIASSVAHDSHNIIVVGTNDEDMALAVNRL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274314359 518 AEIGGGWVLVSGGKVLAEVRYEIGGLMTQRPAEELDAEMQQLYGAAETIEW-LYEPTFSprwypgfperLQFATLTCAP 595
Cdd:pfam13382 84 IEMGGGIVVVKDGKVLAELPLPIAGLMSDLPAEEVAEKLEELNAALRELGCeLDDPFMT----------LSFLALPVIP 152
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
32-381 |
5.93e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 83.09 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 32 KRPANMLLRVGRLLDVHTRTWLEDQEIAIRGRRIAWTGPAGTFPGTAAAQ---AErpGLSAVPGFGEVHKHI-------- 100
Cdd:COG1228 5 AQAGTLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEvidAT--GKTVLPGLIDAHTHLglgggrav 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 101 ---ESSHITPEYEAALV--------LPRGNTwTCEASH--EFSNVDG-AHNLEFWLTARR---HGSPMKIFPLPGSAVPP 163
Cdd:COG1228 83 efeAGGGITPTVDLVNPadkrlrraLAAGVT-TVRDLPggPLGLRDAiIAGESKLLPGPRvlaAGPALSLTGGAHARGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 164 TAyeWGGGYYGYDEQADFLKqsLMVAGLDEVMDWPAVwnpenpshkrlwgmiqatfekRGVVEG-HGAGLR------DLN 236
Cdd:COG1228 162 EA--RAALRELLAEGADYIK--VFAEGGAPDFSLEEL---------------------RAILEAaHALGLPvaahahQAD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 237 SINAFAAAGLAS-DHEGWTAEEVWDKL-RHGIFIEIRPHSMPEIIAGLIERGLTDWSQVAFATDDRSASDTLKRG----- 309
Cdd:COG1228 217 DIRLAVEAGVDSiEHGTYLDDEVADLLaEAGTVVLVPTLSLFLALLEGAAAPVAAKARKVREAALANARRLHDAGvpval 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 310 ATDHNV------------RLAIQSGLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVLLD-----DVEKL-SITEV 371
Cdd:COG1228 297 GTDAGVgvppgrslhrelALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDgdpleDIAYLeDVRAV 376
|
410
....*....|
gi 1274314359 372 WADGEPISKG 381
Cdd:COG1228 377 MKDGRVVDRS 386
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
309-376 |
6.43e-11 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 64.35 E-value: 6.43e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274314359 309 GAT---DHNVRLAIQ-SGLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVLLDDveKLSITEVWADGE 376
Cdd:COG1820 304 GSTltmDDAVRNLVEwTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDD--DLNVRATWVGGE 373
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
90-378 |
1.83e-10 |
|
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: 62.90 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 90 VPGFGEVHKHIESSHI----TPEYEAALVLPRGNTWTCEASHEFSNVDGAHNLEFWLTARR--HGSPMKIFPLPGSAVPP 163
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALLEaaEELPLGLRFLGPGCSLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 164 TAYEWGGGYYGY---DEQADFLKQSLMVAGLDEVMDWPAVWNPENpshkrlwgMIQATFE---KRGV-VEGHGAGLRDL- 235
Cdd:pfam01979 83 TDGELEGRKALReklKAGAEFIKGMADGVVFVGLAPHGAPTFSDD--------ELKAALEeakKYGLpVAIHALETKGEv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 236 -NSINAFAAAGLASDH-----EGWTAEEVWDKLRHGIFIE-------------------------IRPHSMPeiIAGLIE 284
Cdd:pfam01979 155 eDAIAAFGGGIEHGTHlevaeSGGLLDIIKLILAHGVHLSpteanllaehlkgagvahcpfsnskLRSGRIA--LRKALE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 285 RGLTdwsqVAFATDDRSASDTLK-RGATDHNVRLAIQS--GLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVLLD 361
Cdd:pfam01979 233 DGVK----VGLGTDGAGSGNSLNmLEELRLALELQFDPegGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVD 308
|
330
....*....|....*..
gi 1274314359 362 DVEKLSITEVWADGEPI 378
Cdd:pfam01979 309 LDPLAAFFGLKPDGNVK 325
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
310-378 |
5.20e-10 |
|
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: 61.56 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 310 ATDHNV----------RLAIQSGLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVLLDDvEKLS----ITEVWADG 375
Cdd:cd01309 277 SSDHPVlnirnlnleaAKAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNG-DPLEptskPEQVYIDG 355
|
...
gi 1274314359 376 EPI 378
Cdd:cd01309 356 RLV 358
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
300-375 |
7.59e-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: 54.89 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 300 RSASDTLKrGAT---DHNVRLAIQ-SGLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVLLDDveKLSITEVWADG 375
Cdd:cd00854 298 RLADGTLA-GSTltmDQAVRNMVKwGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDD--DLNVKATWING 374
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
323-378 |
4.94e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 49.41 E-value: 4.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274314359 323 LTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVLLD------DVEKLSITEVWA---DGEPI 378
Cdd:COG1574 467 LTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDrdpltvPPEEIKDIKVLLtvvGGRVV 531
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
282-361 |
2.02e-05 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 47.25 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 282 LIERGLTdwsqVAFATDDRSASdtlkrgATDHNVRLAIQ-----SGLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFAD 356
Cdd:cd01296 274 LIDAGVP----VALGTDFNPGS------SPTSSMPLVMHlacrlMRMTPEEALTAATINAAAALGLGETVGSLEVGKQAD 343
|
....*
gi 1274314359 357 IVLLD 361
Cdd:cd01296 344 LVILD 348
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
123-338 |
4.05e-05 |
|
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: 45.79 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 123 CEASHEFSNVDGAHNLEFWLTARRHGSPMKIFPLPGSAVPPTAYEWGGGYYGYDEQADFLKqsLMVAGLDEVMDWPAVWN 202
Cdd:cd01292 53 VDMGSTPPPTTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLE--LGAVGLKLAGPYTATGL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 203 PEnPSHKRLWGM-----IQATFEKRGVVEGHGAGLRDLNSInaFAAAGLASDHEGWTAEEVWDKLR-HGIFIEIRP---- 272
Cdd:cd01292 131 SD-ESLRRVLEEarklgLPVVIHAGELPDPTRALEDLVALL--RLGGRVVIGHVSHLDPELLELLKeAGVSLEVCPlsny 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274314359 273 --HSMPEIIAGLIeRGLTDWSQVAFATDDRSASDTLKRGATDHNVRLAIQSGLTPEIAIQCVTINPAR 338
Cdd:cd01292 208 llGRDGEGAEALR-RLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLGLSLEEALRLATINPAR 274
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
261-361 |
4.99e-05 |
|
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: 45.97 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 261 KLRHGIFieirphsmPeiIAGLIERGLTdwsqVAFATD------DRSASDTLKRGATDHNVRLAIQSGLTPEIAIQCVTI 334
Cdd:COG0402 286 KLGSGIA--------P--VPRLLAAGVR----VGLGTDgaasnnSLDMFEEMRLAALLQRLRGGDPTALSAREALEMATL 351
|
90 100
....*....|....*....|....*..
gi 1274314359 335 NPARHMRLTPWVGSIAPGRFADIVLLD 361
Cdd:COG0402 352 GGARALGLDDEIGSLEPGKRADLVVLD 378
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
221-378 |
5.41e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.99 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 221 KRGVVEGHGAGLRDLNSINAFAAAGLASDHEGWTAEEVWDKLRHGIFIEIRPHSMPeiIAGLIERGLTdwsqVAFATDDR 300
Cdd:pfam07969 295 RVRIEHAQGVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTP--VKELLNAGVK----VALGSDAP 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 301 ----------SASDTLKRGATDHnvRLAIQSGLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVLLD------DVE 364
Cdd:pfam07969 369 vgpfdpwpriGAAVMRQTAGGGE--VLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDddpltvDPP 446
|
170
....*....|....*..
gi 1274314359 365 KL---SITEVWADGEPI 378
Cdd:pfam07969 447 AIadiRVRLTVVDGRVV 463
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
316-378 |
5.65e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 45.94 E-value: 5.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274314359 316 RLAIQSGLTPEIAIQCVTINPARHMRLTPwVGSIAPGRFADIVLLDDVEKL-SITEVWADGEPI 378
Cdd:PRK15446 317 RLADDGGLDLPQAVALVTANPARAAGLDD-RGEIAPGKRADLVRVRRAGGLpVVRAVWRGGRRV 379
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
322-365 |
6.56e-05 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 45.54 E-value: 6.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1274314359 322 GLTPEIAIQCVTINPARHMRLtPWVGSIAPGRFADIVLLDDVEK 365
Cdd:COG3964 295 GMPLEEVIAAVTWNPARAIGL-PELGTLSVGADADITIFDLREG 337
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
262-361 |
1.62e-04 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 44.21 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 262 LRHGIFIEIRPHSMPEIIAGLIERGLTDWSQVAFATDDRSASDTLKRGA---------TD---------HNVR-LAIQS- 321
Cdd:cd01299 212 KEKGIFLVPTLATYEALAAEGAAPGLPADSAEKVALVLEAGRDALRRAHkagvkiafgTDagfpvpphgWNAReLELLVk 291
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1274314359 322 -GLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVLLD 361
Cdd:cd01299 292 aGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
316-375 |
4.73e-04 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 42.65 E-value: 4.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274314359 316 RLAIQSGLTPEIAIQCVTINPARHMRLTPwVGSIAPGRFADIVLLDDVEKL-SITEVWADG 375
Cdd:cd01306 266 RLADLGGWSLPEAVALVSANPARAVGLTD-RGSIAPGKRADLILVDDMDGVpVVRTVWRGG 325
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
323-359 |
1.10e-03 |
|
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: 41.91 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1274314359 323 LTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVL 359
Cdd:cd01300 443 LSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
279-361 |
1.77e-03 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 41.03 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274314359 279 IAGLIERGLTdwsqVAFATDDRSASDTL------KRGATDHNVRLAIQSGLTPEIAIQCVTINPARHMRLtPWVGSIAPG 352
Cdd:cd01298 286 VPEMLEAGVN----VGLGTDGAASNNNLdmfeemRLAALLQKLAHGDPTALPAEEALEMATIGGAKALGL-DEIGSLEVG 360
|
....*....
gi 1274314359 353 RFADIVLLD 361
Cdd:cd01298 361 KKADLILID 369
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
322-364 |
2.11e-03 |
|
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: 40.77 E-value: 2.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1274314359 322 GLTPEIAIQCVTINPARHMRLtPWVGSIAPGRFADIVLLDDVE 364
Cdd:cd01307 276 GMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDLKD 317
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
322-359 |
2.87e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 40.51 E-value: 2.87e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1274314359 322 GLTPEIAIQCVTINPARHMRLTPWVGSIAPGRFADIVL 359
Cdd:PRK12394 300 GMALEDVINACTHTPAVLMGMAAEIGTLAPGAFADIAI 337
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
323-361 |
9.50e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 38.64 E-value: 9.50e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1274314359 323 LTPEIAIQCVTINPARHMRLTPwvGSIAPGRFADIVLLD 361
Cdd:PRK09357 344 LDLEQLLEKMTINPARILGLPA--GPLAEGEPADLVIFD 380
|
|
| |
