|
Name |
Accession |
Description |
Interval |
E-value |
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
16-553 |
1.75e-163 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 476.51 E-value: 1.75e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 16 RTFEKGDLYIQDSMIYHIGEADIIVDQEIDAKGKWIIPGLIDIHMHIESSMTNPNEFSKTVLPMGTTTIVADAHEIGNVF 95
Cdd:COG1001 20 GEILEGDIAIAGGRIAGVGDYIGEATEVIDAAGRYLVPGFIDGHVHIESSMVTPAEFARAVLPHGTTTVIADPHEIANVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 96 GTQGlIDFMdID----TQLDIFYAIPSSVPSTnPFLETTGGIVDEAAVEVLCKHPKVIALGEIMNFKDVISDEDTMTRRI 171
Cdd:COG1001 100 GLEG-VRYM-LEaaegLPLDIFVMLPSCVPAT-PGLETAGAVLGAEDLAELLDHPRVIGLGEVMNFPGVLNGDPRMLAKI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 172 IETFKTCKpgsPIEGHIPRISGLELSRFIQRGIGSDHTLQTKASILERTRMGVLVQMQE----KSLNqETISTLCKHNLH 247
Cdd:COG1001 177 AAALAAGK---VIDGHAPGLSGKDLNAYAAAGIRSDHECTTAEEALEKLRRGMYVMIREgsaaKDLP-ALLPAVTELNSR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 248 gSFCLVTDDVMPDDLIAKGHLNHLIQICNENGMRPEDAIYAATYVPAQRMQLYDRGVLSPGKQADFIILDDLNAFSIHSV 327
Cdd:COG1001 253 -RCALCTDDRHPDDLLEEGHIDHVVRRAIELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDDLEDFKVEKV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 328 YKKG----SNIKDLPEDYFNFNDQYIYNTIKRKPIKRDDLILPISNlegdEVKLRIMHRETTNTFTEELIIPVKTREGAL 403
Cdd:COG1001 332 YADGklvaEDGKLLVDLPKYPYPPWARNTVKLRPLTAEDFAIPAPG----GVKVRVIGVIPGQIITEHLEAELPVEDGEV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 404 QW-QDAGLTMIAVIERYGHQNPIAIGFVdNGF-TEKGAVATSWTHDHHNILVMGTDLDEIVNAVNLLIKVQGGiISSIKN 481
Cdd:COG1001 408 VPdPERDILKIAVVERHGGTGNIGLGFV-KGFgLKRGAIASTVAHDSHNLIVVGTNDEDMALAANRLIEIGGG-IVVVKD 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500175486 482 KH--HKVPLAYGGIVSTNSMESLASDVAQIRQDLKGLGYKAQNELMSFSVLGLLVSPSLKISDKGYVDVRTQEI 553
Cdd:COG1001 486 GKvlAELPLPIAGLMSDEPAEEVAEKLEALRAAARELGCTLEEPFMTLSFLALPVIPELKLTDRGLVDVTTFEF 559
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
45-547 |
2.18e-142 |
|
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: 417.78 E-value: 2.18e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 45 DAKGKWIIPGLIDIHMHIESSMTNPNEFSKTVLPMGTTTIVADAHEIGNVFGTQGlIDFMDID---TQLDIFYAIPSSVP 121
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHIESSMLTPSEFAKAVLPHGTTTVIADPHEIANVAGVDG-IEFMLEDakkTPLDIFWMLPSCVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 122 STNPflETTGGIVDEAAVEVLCKHPKVIALGEIMNFKDVISDEDTMtRRIIETFKtcKPGSPIEGHIPRISGLELSRFIQ 201
Cdd:cd01295 80 ATPF--ETSGAELTAEDIKELLEHPEVVGLGEVMDFPGVIEGDDEM-LAKIQAAK--KAGKPVDGHAPGLSGEELNAYMA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 202 RGIGSDHTLQTKASILERTRMGVLVQMQEKSL--NQETISTLCKHNLHGSFCLVTDDVMPDDLIAKGHLNHLIQICNENG 279
Cdd:cd01295 155 AGISTDHEAMTGEEALEKLRLGMYVMLREGSIakNLEALLPAITEKNFRRFMFCTDDVHPDDLLSEGHLDYIVRRAIEAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 280 MRPEDAIYAATYVPAQRMQLYDRGVLSPGKQADFIILDDLNAFSIHSVYKKGsnikdlpedyfnfndqyiyntikrkpik 359
Cdd:cd01295 235 IPPEDAIQMATINPAECYGLHDLGAIAPGRIADIVILDDLENFNITTVLAKG---------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 360 rddlilpisnlegdevklrimhrettntfteeliipvktregalqwqdagltmIAVIERYGHQNPIAIGFVDnGFTEK-G 438
Cdd:cd01295 287 -----------------------------------------------------IAVVERHGKTGNIGVGFVK-GFGLKeG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 439 AVATSWTHDHHNILVMGTDLDEIVNAVNLLIKVQGGIISSIKNK-HHKVPLAYGGIVSTNSMESLASDVAQIRQDLKGLG 517
Cdd:cd01295 313 AIASSVAHDSHNIIVIGTNDEDMALAVNRLKEIGGGIVVVKNGKvLAELPLPIAGLMSDEPAEEVAEELKKLREALRELG 392
|
490 500 510
....*....|....*....|....*....|
gi 2500175486 518 YKAQNELMSFSVLGLLVSPSLKISDKGYVD 547
Cdd:cd01295 393 YALDDPFMTLSFLSLPVIPELKITDKGLFD 422
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
20-548 |
1.98e-104 |
|
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: 324.80 E-value: 1.98e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 20 KGDLYIQDSMIYHIGEADIIvdQEIDAKGKWIIPGLIDIHMHIESSMTNPNEFSKTVLPMGTTTIVADAHEIGNVFGTQG 99
Cdd:TIGR01178 19 PGDIAIANGHIAGVGKYNGV--KVIDALGEYAVPGFIDAHIHIESSMLTPSEFAKLVLPHGVTTVVSDPHEIANVNGEDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 100 lIDFMDID---TQLDIFYAIPSSVPSTNpfLETTGGIVDEAAVEVLCKHPKVIALGEIMNFKDVISDEDTMTRRiIETFK 176
Cdd:TIGR01178 97 -INFMLNNakkTPLNFYFMLPSCVPALQ--FETSGAVLTAEDIDELMELDEVLGLAEVMDYPGVINADIEMLNK-INSAR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 177 tcKPGSPIEGHIPRISGLELSRFIQRGIGSDHTLQTKASILERTRMGVLVQMQEKSL--NQETISTLCKHNLHGSFCLVT 254
Cdd:TIGR01178 173 --KRNKVIDGHCPGLSGKLLNKYISAGISNDHESTSIEEAREKLRLGMKLMIREGSAakNLEALHPLINEKNCRSLMLCT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 255 DDVMPDDLIAKGHLNHLIQICNENGMRPEDAIYAATYVPAQRMQLYDRGVLSPGKQADFIILDDLNAFSIHSVYKKGSNI 334
Cdd:TIGR01178 251 DDRHVNDILNEGHINHIVRRAIEHGVDPFDALQMASINPAEHFGIDVGGLIAPGDPADFVILKDLRNFKVNKTYVKGKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 335 --KDLPEDYFNF--NDQYIY-NTIKRKPIKRDDLILPISnlEGDEVK-LRIMHRETTntfTEELIIPVKTREGALQWQDa 408
Cdd:TIGR01178 331 dlNEVFNDEISRipLINEIPiNVKARSPKSISDFGIQFK--TGNRIRvIKVISNQLI---THKTSNSVAEEFGSDIEED- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 409 gLTMIAVIERYGHQNPIAIGFVDNGFTEKGAVATSWTHDHHNILVMGTDLDEIVNAVNLLIKVQGGIIsSIKN--KHHKV 486
Cdd:TIGR01178 405 -ILKIAVIERHKDNGKIGKGLIKGFGLKEGAIASTVAHDSHNIIAVGSNDEDLALAVNKLIQIGGGLC-AAKNgeVTIIL 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500175486 487 PLAYGGIVSTNSMESLASDVAQIRQDLKGLGYKAQNELMSFSVLGLLVSPSLKISDKGYVDV 548
Cdd:TIGR01178 483 PLPIAGLMSDDSAERVAEQIIALNDKCRNVGGSRDNPFLTLSFLSLPVIPHLKITDKGLFDV 544
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
42-548 |
5.80e-82 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 267.47 E-value: 5.80e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 42 QEIDAKGKWIIPGLIDIHMHIESSMTNPNEFSKTVLPMGTTTIVADAHEIGNVFGTQGLIDFMDIDTQL--DIFYAIPSS 119
Cdd:PRK10027 73 QRIDARGATAVPGFIDAHLHIESSMMTPVTFETATLPRGLTTVICDPHEIVNVMGEAGFAWFARCAEQArqNQYLQVSSC 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 120 VPSTnPFLETTGGIVDEAAVEVLCKHPKVIALGEIMNFKDVISDEDTMTRRiIETFKTCKpgspIEGHIPRISGLELSRF 199
Cdd:PRK10027 153 VPAL-EGCDVNGASFTLEQMLAWRDHPQVTGLAEMMDYPGVISGQNALLDK-LDAFRHLT----LDGHCPGLGGKELNAY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 200 IQRGIGSDHTLQTKASILERTRMGVLVQMQEKSL--NQETISTLCkHNLHGSFCLV-TDDVMPDDLIAKGHLNHLI-QIC 275
Cdd:PRK10027 227 IAAGIENCHESYQLEEGRRKLQLGMSLMIREGSAarNLNALAPLI-NEFNSPQCMLcTDDRNPWEIAHEGHIDALIrRLI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 276 NENGMRPEDAIYAATYVPAQRMQLYDRGVLSPGKQADFIILDDLNAFSIHSVYKKGSNIKDLP-----EDYFNFNDQYIY 350
Cdd:PRK10027 306 EQHNVPLHVAYRVASWSTARHFGLNHLGLLAPGKQADIVLLSDARKVTVQQVLVKGEPIDAQTlqaeeSARLAQSAPPYG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 351 NTIKRKPIKRDDLILPISNLEGDEVkLRIMHrettntftEELIIPVKT-REGALQWQDAGLTMIAVIERYGHQNPIAIGF 429
Cdd:PRK10027 386 NTIARQPVSASDFALQFTPGKRYRV-IDVIH--------NELITHSRSsVYSENGFDRDDVCFIAVLERYGQRLAPACGL 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 430 VDNGFTEKGAVATSWTHDHHNILVMGTDLDEIVNAVNLLIKVQGG--IISSIKNKHHkVPLAYGGIVSTNSMESLASDVA 507
Cdd:PRK10027 457 LGGFGLNEGALAATVSHDSHNIVVIGRSAEEMALAVNQVIQDGGGlcVVRNGQVQSH-LPLPIAGLMSTDTAQSLAEQID 535
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2500175486 508 QIRQDLKGLGYKAQNELMSFSVLGLLVSPSLKISDKGYVDV 548
Cdd:PRK10027 536 ALKAAARECGPLPDEPFIQMAFLSLPVIPALKLTSQGLFDG 576
|
|
| Adenine_deam_C |
pfam13382 |
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine ... |
387-552 |
2.12e-49 |
|
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: 168.39 E-value: 2.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 387 TFTEELIIPVKTREGALQWQ-DAGLTMIAVIERYGHQNPIAIGFVDNGFTEKGAVATSWTHDHHNILVMGTDLDEIVNAV 465
Cdd:pfam13382 1 LITKELEVELPVKDGVVVPDpERDILKIAVVERHGGTGNIGVGFVKGFGLKRGAIASSVAHDSHNIIVVGTNDEDMALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 466 NLLIKVQGGIISSIKNK-HHKVPLAYGGIVSTNSMESLASDVAQIRQDLKGLGYKAQNELMSFSVLGLLVSPSLKISDKG 544
Cdd:pfam13382 81 NRLIEMGGGIVVVKDGKvLAELPLPIAGLMSDLPAEEVAEKLEELNAALRELGCELDDPFMTLSFLALPVIPELKITDKG 160
|
....*...
gi 2500175486 545 YVDVRTQE 552
Cdd:pfam13382 161 LVDVKKFK 168
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-331 |
1.53e-19 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 90.79 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 13 TSQRTFEKGDLYIQDSMIYHIGEADIIV----DQEIDAKGKWIIPGLIDIHMHIESSMTNPNEFS--------------- 73
Cdd:COG1228 21 TGGGVIENGTVLVEDGKIAAVGPAADLAvpagAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEagggitptvdlvnpa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 74 ----KTVLPMGTTTiVADAHeiGNVFGTQGLIdfmdIDTQLDIFYAipSSVPSTNPFLETTGGIVD------EAAVEVLC 143
Cdd:COG1228 101 dkrlRRALAAGVTT-VRDLP--GGPLGLRDAI----IAGESKLLPG--PRVLAAGPALSLTGGAHArgpeeaRAALRELL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 144 KHP----KVIALGEIMNFkdvisDEDTMtRRIIETfkTCKPGSPIEGHIPRISGLELSrfIQRGIGS-DHTLQTKASILE 218
Cdd:COG1228 172 AEGadyiKVFAEGGAPDF-----SLEEL-RAILEA--AHALGLPVAAHAHQADDIRLA--VEAGVDSiEHGTYLDDEVAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 219 R-----------------------TRMGVLVQMQEKSLNQETISTLCKHNLHgsFCLVTDDvmPDDLIAKGHLNHLIQIC 275
Cdd:COG1228 242 LlaeagtvvlvptlslflallegaAAPVAAKARKVREAALANARRLHDAGVP--VALGTDA--GVGVPPGRSLHRELALA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500175486 276 NENGMRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILD-----DLNAF-SIHSVYKKG 331
Cdd:COG1228 318 VEAGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDgdpleDIAYLeDVRAVMKDG 380
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
50-331 |
2.59e-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: 65.22 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 50 WIIPGLIDIHMHIESSM----TNPNEFSKTVLPMGT-------TTIVADAHeIGNVFGTQGLIDFMDiDTQLDIFYAIPS 118
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLlrgiPVPPEFAYEALRLGIttmlksgTTTVLDMG-ATTSTGIEALLEAAE-ELPLGLRFLGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 119 SVPST----NPFLETTGGIVDEAavEVLCKHPKVIALGEIMNFKDVISDEDTMtRRIIETFKtcKPGSPIEGHIprISGL 194
Cdd:pfam01979 79 CSLDTdgelEGRKALREKLKAGA--EFIKGMADGVVFVGLAPHGAPTFSDDEL-KAALEEAK--KYGLPVAIHA--LETK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 195 ELSRFIQRGIGSDHTLQT------KASILERTRM----GVLVQMQE-----KSLNQETISTLCKHNL------------- 246
Cdd:pfam01979 152 GEVEDAIAAFGGGIEHGThlevaeSGGLLDIIKLilahGVHLSPTEanllaEHLKGAGVAHCPFSNSklrsgrialrkal 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 247 -HGSFC-LVTDDV-MPD--DLIAKGHLNHLIQICNENGMRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILD--- 317
Cdd:pfam01979 232 eDGVKVgLGTDGAgSGNslNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLDDKvGSIEVGKDADLVVVDldp 311
|
330 340
....*....|....*....|
gi 2500175486 318 ------DLNAFSIHSVYKKG 331
Cdd:pfam01979 312 laaffgLKPDGNVKKVIVKG 331
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
23-331 |
3.26e-10 |
|
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: 61.89 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 23 LYIQDSMIYHIGEADIIV------DQEIDAKGKWIIPGLIDIHMH-----------------------------IESSM- 66
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPapgpaaAEEIDAGGRAVTPGLVDCHTHlvfagdrvdefaarlagasyeeilaagggILSTVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 67 ----TNPNEFSKTVLP-------MGTTTIvadahEIGNVFGtqglidfMDIDTQLDIFYAI-------PSSVPSTnpFL- 127
Cdd:cd01296 81 atraASEDELFASALRrlarmlrHGTTTV-----EVKSGYG-------LDLETELKMLRVIrrlkeegPVDLVST--FLg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 128 ------ETTGgivDEAAVEVLCKH--PKVIALGEImNFKDVISDED----TMTRRIIETFKtcKPGSPIEGH---IPRIS 192
Cdd:cd01296 147 ahavppEYKG---REEYIDLVIEEvlPAVAEENLA-DFCDVFCEKGafslEQSRRILEAAK--EAGLPVKIHadeLSNIG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 193 GLELSRFIQrGIGSDHtlqtkasiLERTRMGVLVQMQEKslnqETISTLCKHNlhgSFCLVTDDVMPDDLIAKG------ 266
Cdd:cd01296 221 GAELAAELG-ALSADH--------LEHTSDEGIAALAEA----GTVAVLLPGT---AFSLRETYPPARKLIDAGvpvalg 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 267 --------HLNHLIQI----CNENGMRPEDAIYAATYVPAQRMQL-YDRGVLSPGKQADFIILD-----------DLNAf 322
Cdd:cd01296 285 tdfnpgssPTSSMPLVmhlaCRLMRMTPEEALTAATINAAAALGLgETVGSLEVGKQADLVILDapsyehlayrfGVNL- 363
|
....*....
gi 2500175486 323 sIHSVYKKG 331
Cdd:cd01296 364 -VEYVIKNG 371
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
15-331 |
1.14e-09 |
|
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: 60.29 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 15 QRTFEKGDLYIQDSMIYHIGEAD--IIVDQEIDAKGKWIIPGLIDIHMH-------IESSMTNPNEFSKTVLPMGTTTIV 85
Cdd:cd00854 11 PGGLEDGAVLVEDGKIVAIGPEDelEEADEIIDLKGQYLVPGFIDIHIHggggadfMDGTAEALKTIAEALAKHGTTSFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 86 A----DAHEignvfgtqglidfmDIDTQLDifyAIPSSVPSTN-----------PFL--ETTGgivdeaavevlCKHPKV 148
Cdd:cd00854 91 PttvtAPPE--------------EIAKALA---AIAEAIAEGQgaeilgihlegPFIspEKKG-----------AHPPEY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 149 IALGEIMNFKDVISDEDTMTRRIietfkTCKPgsPIEGHIPRIsglelSRFIQRGI----GsdHTL----QTKASILERT 220
Cdd:cd00854 143 LRAPDPEELKKWLEAAGGLIKLV-----TLAP--ELDGALELI-----RYLVERGIivsiG--HSDatyeQAVAAFEAGA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 221 RM-------------------GVLVQMQEKS---------LNQETISTLCKHNLHGSFCLVTDDV----MPD-------- 260
Cdd:cd00854 209 THvthlfnamsplhhrepgvvGAALSDDDVYaeliadgihVHPAAVRLAYRAKGADKIVLVTDAMaaagLPDgeyelggq 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 261 -----DLIAK-------GHLNHLIQ----ICNENGMRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILDDlnAFS 323
Cdd:cd00854 289 tvtvkDGVARladgtlaGSTLTMDQavrnMVKWGGCPLEEAVRMASLNPAKLLGLDDRkGSLKPGKDADLVVLDD--DLN 366
|
....*...
gi 2500175486 324 IHSVYKKG 331
Cdd:cd00854 367 VKATWING 374
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
279-331 |
9.60e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 57.42 E-value: 9.60e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2500175486 279 GMRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILDDlnAFSIHSVYKKG 331
Cdd:COG1820 321 GLPLEEAVRMASLNPARALGLDDRkGSIAPGKDADLVVLDD--DLNVRATWVGG 372
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
41-317 |
2.40e-08 |
|
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: 56.15 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 41 DQEIDAKGKWIIPGLIDIHMHIesSMTNPNEFSKTVLPMGTTTIVADAH----------EIGNVfGTQGLIDFMD-IDTQ 109
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHL--GSDPGDLPLDLALPVEYRTIRATRQaraalragftTVRDA-GGADYGLLRDaIDAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 110 L----DIFYAIP----------SSVPSTNPFLETTGGIVD------EAAVEVLCKHP---KVIALGEIMNFKDVISD--- 163
Cdd:cd01299 78 LipgpRVFASGRalsqtgghgdPRGLSGLFPAGGLAAVVDgveevrAAVREQLRRGAdqiKIMATGGVLSPGDPPPDtqf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 164 -EDTMtRRIIETfkTCKPGSPIEGH------IPR-----ISGLELSRFI---------QRGIGSDHTLQTKASIL----E 218
Cdd:cd01299 158 sEEEL-RAIVDE--AHKAGLYVAAHaygaeaIRRairagVDTIEHGFLIddetielmkEKGIFLVPTLATYEALAaegaA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 219 RTRMGVLVQMQEKSLnQETISTLCKHNLHG-SFCLVTDDVMPddLIAKGHLNHLIQICNENGMRPEDAIYAATYVPAQRM 297
Cdd:cd01299 235 PGLPADSAEKVALVL-EAGRDALRRAHKAGvKIAFGTDAGFP--VPPHGWNARELELLVKAGGTPAEALRAATANAAELL 311
|
330 340
....*....|....*....|.
gi 2500175486 298 QL-YDRGVLSPGKQADFIILD 317
Cdd:cd01299 312 GLsDELGVIEAGKLADLLVVD 332
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
13-85 |
2.47e-08 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 56.33 E-value: 2.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500175486 13 TSQRTFeKGDLYIQDSMIYHIGEADiiVDQEIDAKGKWIIPGLIDIHMHIESSM----TNPNEFSKTV--LPMGTTTIV 85
Cdd:PRK08323 12 TADDTY-KADVLIEDGKIAAIGANL--GDEVIDATGKYVMPGGIDPHTHMEMPFggtvSSDDFETGTRaaACGGTTTII 87
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-63 |
2.83e-08 |
|
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: 56.25 E-value: 2.83e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2500175486 18 FEKGDLYIQDSMIYHIGEADIIV--DQEIDAKGKWIIPGLIDIHMHIE 63
Cdd:COG0044 13 LERADVLIEDGRIAAIGPDLAAPeaAEVIDATGLLVLPGLIDLHVHLR 60
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
13-61 |
3.89e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 55.49 E-value: 3.89e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2500175486 13 TSQRTFEKGDLYIQDSMIYHIGEADIIVDQEIDAKGKWIIPGLIDIHMH 61
Cdd:COG1820 9 TGDGVLEDGALLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
20-85 |
6.33e-08 |
|
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: 55.30 E-value: 6.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500175486 20 KGDLYIQDSMIYHIGEaDIIVD---QEIDAKGKWIIPGLIDIHMHIES---SMTNPNEF---SKTVLPMGTTTIV 85
Cdd:cd01314 16 KADILIEDGKIVAIGP-NLEAPggvEVIDATGKYVLPGGIDPHTHLELpfmGTVTADDFesgTRAAAAGGTTTII 89
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
12-105 |
2.38e-07 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 52.86 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 12 NTSQRTFEKGDLYIQDSMIYHIGEaDIIV---DQEIDAKGKWIIPGLIDIHMHIESSMT----NPNEFSktvLPMGTTTI 84
Cdd:COG3964 11 DPANGIDGVMDIAIKDGKIAAVAK-DIDAaeaKKVIDASGLYVTPGLIDLHTHVFPGGTdygvDPDGVG---VRSGVTTV 86
|
90 100
....*....|....*....|.
gi 2500175486 85 VaDAheignvfGTQGLIDFMD 105
Cdd:COG3964 87 V-DA-------GSAGAANFDG 99
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
16-67 |
2.91e-07 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 52.97 E-value: 2.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2500175486 16 RTFEKGDLYIQDSMIYHIGEAD----IIVDQEIDAKGKWIIPGLIDIHMHieSSMT 67
Cdd:cd01298 15 RVLEDGDVLVEDGRIVAVGPALplpaYPADEVIDAKGKVVMPGLVNTHTH--LAMT 68
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
12-67 |
4.95e-07 |
|
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: 52.14 E-value: 4.95e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500175486 12 NTSQRTFEKGDLYIQDSMIYHIGEADII-----VDQEIDAKGKWIIPGLIDIHMHIESSMT 67
Cdd:COG0402 13 DPAGGVLEDGAVLVEDGRIAAVGPGAELparypAAEVIDAGGKLVLPGLVNTHTHLPQTLL 73
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
20-93 |
1.78e-06 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 50.56 E-value: 1.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500175486 20 KGDLYIQDSMIYHIGE-ADIIVDQEIDAKGKWIIPGLIDIHMHIESSMTNPNEFSKTVLpMGTTTIVadaheIGN 93
Cdd:COG3653 21 RADVAIKGGRIVAVGDlAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSLR-QGVTTVV-----MGN 89
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
16-61 |
1.97e-06 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 50.25 E-value: 1.97e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2500175486 16 RTFEkGDLYIQDSMIYHIGE--ADIIVDQEIDAKGKWIIPGLIDIHMH 61
Cdd:PRK09236 16 KIFE-GDVLIENGRIAKIASsiSAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
19-61 |
2.59e-06 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 49.81 E-value: 2.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2500175486 19 EKGDLYIQDSMIYHIGEADIIVDQE-IDAKGKWIIPGLIDIHMH 61
Cdd:PRK09357 18 EVADVLIDDGKIAAIGENIEAEGAEvIDATGLVVAPGLVDLHVH 61
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
20-331 |
3.31e-06 |
|
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: 49.60 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 20 KGDLYIQDSMIYHIGEADII-VDQEIDAKGKWIIPGLIDIHMHIESSMTNPNEFSKTVLpMGTTTIV------------- 85
Cdd:cd01297 19 TADVGIRDGRIAAIGPILSTsAREVIDAAGLVVAPGFIDVHTHYDGQVFWDPDLRPSSR-QGVTTVVlgncgvspapanp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 86 -ADAHEIGNVFGTQGLI-----------DFMDI----DTQLDIFYAIPSS-----------VPSTNPFLETTGGIVDEA- 137
Cdd:cd01297 98 dDLARLIMLMEGLVALGeglpwgwatfaEYLDAlearPPAVNVAALVGHAalrravmgldaREATEEELAKMRELLREAl 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 138 ---AVEV---LCKHPK-------VIALGEIMNFKDVI--SDEDTMTRRIIETFKTCkpgspieghiprisgLELSRFIQR 202
Cdd:cd01297 178 eagALGIstgLAYAPRlyagtaeLVALARVAARYGGVyqTHVRYEGDSILEALDEL---------------LRLGRETGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 203 GIGSDHTlqTKASILERTRMGVLVQMQEKSLNQetistlckhnlhGSFclVTDDVMP------DDLIA----KGHLN--- 269
Cdd:cd01297 243 PVHISHL--KSAGAPNWGKIDRLLALIEAARAE------------GLQ--VTADVYPygagseDDVRRimahPVVMGgsd 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 270 -------HLIQIC-----------NENGMRPEDAIYAATYVPAQRMQLYDRGVLSPGKQADFIILD-----------DLN 320
Cdd:cd01297 307 ggalgkpHPRSYGdftrvlghyvrERKLLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVFDpdtladratftRPN 386
|
410
....*....|...
gi 2500175486 321 AFS--IHSVYKKG 331
Cdd:cd01297 387 QPAegIEAVLVNG 399
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
1-66 |
7.79e-06 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 48.52 E-value: 7.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500175486 1 MITKYTDAFL--YNTSQRTFEKGDLYIQDSMIYHIGEADII----VDQEIDAKGKWIIPGLIDIHMHIESSM 66
Cdd:PRK15493 1 MKTTYVNATIvtMNEQNEVIENGYIIVENDQIIDVNSGEFAsdfeVDEVIDMKGKWVLPGLVNTHTHVVMSL 72
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
13-103 |
1.11e-05 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 48.16 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 13 TSQRTFeKGDLYIQDSMIYHIGEADIIVDQEIDAKGKWIIPGLIDIHMHIESsmtnpnefsktvlPMGTTTIVADAHEIG 92
Cdd:PRK13404 15 TATDTF-QADIGIRGGRIAALGEGLGPGAREIDATGRLVLPGGVDSHCHIDQ-------------PSGDGIMMADDFYTG 80
|
90
....*....|....*
gi 2500175486 93 NVF----GTQGLIDF 103
Cdd:PRK13404 81 TVSaafgGTTTVIPF 95
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
14-61 |
1.24e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 47.69 E-value: 1.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2500175486 14 SQRTFEKGDLYIQDSMIYHIGEADII--VDQEIDAKGKWIIPGLIDIHMH 61
Cdd:PRK07228 15 AKREIVDGDVLIEDDRIAAVGDRLDLedYDDHIDATGKVVIPGLIQGHIH 64
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
21-67 |
1.26e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 47.48 E-value: 1.26e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2500175486 21 GDLYIQDSMIYHIGEADIIVDQEIDAKGKWIIPGLIDIHM-HIESSMT 67
Cdd:PRK15446 20 GSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTdNLEKHLA 67
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
18-66 |
1.30e-05 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 47.62 E-value: 1.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2500175486 18 FEKGDLYIQDSMIYHIGEADIIVD-----QEIDAKGKWIIPGLIDIHMHIESSM 66
Cdd:PRK07203 19 IEDGAIAIEGNVIVEIGTTDELKAkypdaEFIDAKGKLIMPGLINSHNHIYSGL 72
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
19-97 |
2.11e-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: 47.41 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 19 EKGDLYIQDSMIYHIGEADIiVDQEIDAKGKWIIPGLIDIHMHIESSMTN------PNEFSKTVLPMGTTTIVADAHEIG 92
Cdd:cd01304 16 EKMDIFIRDGKIVESSSGAK-PAKVIDASGKVVMAGGVDMHSHIAGGKVNvgrilrPEDHRRDPVPKGALRRAGVGFSVP 94
|
....*
gi 2500175486 93 NVFGT 97
Cdd:cd01304 95 STLAT 99
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
18-66 |
2.20e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 46.92 E-value: 2.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2500175486 18 FEKGDLYIQDSMIYHIGEA-DIIVDQEIDAKGKWIIPGLIDIHMHI-ESSM 66
Cdd:PRK08204 21 LPRGDILIEGDRIAAVAPSiEAPDAEVVDARGMIVMPGLVDTHRHTwQSVL 71
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
6-315 |
3.14e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 46.29 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 6 TDAFLYNTSQRTFEKGDLYIQDSMIYHIGEADI-IVDQEIDAKGKWIIPGLIDIHMHIESSMT----NPNEFSktvLPMG 80
Cdd:PRK12394 8 TNGHIIDPARNINEINNLRIINDIIVDADKYPVaSETRIIHADGCIVTPGLIDYHAHVFYDGTeggvRPDMYM---PPNG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 81 TTTIVaDAheignvfGTQGLIDFmdidtqlDIFYA---IPSSVPSTNPFLETTGGIVDEAAVEVLckHPKVIALGEIMNF 157
Cdd:PRK12394 85 VTTVV-DA-------GSAGTANF-------DAFYRtviCASKVRIKAFLTVSPPGQTWSGYQENY--DPDNIDENKIHAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 158 ----KDVI-------SDEDT---MTRRIIETFKTC-KPGSPIEGHI--PRISGLELSRFIQRG-------IGSDHTL--- 210
Cdd:PRK12394 148 frqyRNVLqglklrvQTEDIaeyGLKPLTETLRIAnDLRCPVAVHSthPVLPMKELVSLLRRGdiiahafHGKGSTIlte 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 211 --QTKASILERTRMGVL-----------VQMQEKSLNQ----ETIST-LCKHNlhgsfcLVTDDVMPDDLIAKGHLNHli 272
Cdd:PRK12394 228 egAVLAEVRQARERGVIfdaangrshfdMNVARRAIANgflpDIISSdLSTIT------KLAWPVYSLPWVLSKYLAL-- 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2500175486 273 qicnenGMRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFII 315
Cdd:PRK12394 300 ------GMALEDVINACTHTPAVLMGMAAEiGTLAPGAFADIAI 337
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
42-116 |
3.63e-05 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 46.00 E-value: 3.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500175486 42 QEIDAKGKWIIPGLIDIHMHIESSMT----NPNEFSKTVlpmGTTTIVaDAheignvfGTQGLIDFmdidtqlDIFYAI 116
Cdd:PRK09237 42 KVIDLSGLYVSPGWIDLHVHVYPGSTpygdEPDEVGVRS---GVTTVV-DA-------GSAGADNF-------DDFRKL 102
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
22-62 |
4.84e-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: 46.15 E-value: 4.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2500175486 22 DLYIQDSMIYHIGEADIIVD------QEIDAKGKWIIPGLIDIHMHI 62
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKAlkgpatEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
16-62 |
6.13e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 45.64 E-value: 6.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2500175486 16 RTFEKGDLYIQDSMIYHIGEADIIVDQEIDAKGKWIIPGLIDIHMHI 62
Cdd:PRK06380 17 REILQGNVYIEGNKIVYVGDVNEEADYIIDATGKVVMPGLINTHAHV 63
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
282-331 |
7.20e-05 |
|
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: 45.46 E-value: 7.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2500175486 282 PEDAIYAATYVPAQRMQLYDRGVLSPGKQADFIILDDlnAFSIHSVYKKG 331
Cdd:cd01308 324 LEVALRVITSNVARILKLRKKGEIQPGFDADLVILDK--DLDINSVIAKG 371
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
19-62 |
1.08e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 44.80 E-value: 1.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2500175486 19 EKGDLYIQDSMIyhIGE-ADIIVDQEIDAKGKWIIPGLIDIHMHI 62
Cdd:COG1229 20 EVMDIAIKDGKI--VEEpSDPKDAKVIDASGKVVMAGGVDIHTHI 62
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
250-318 |
1.38e-04 |
|
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: 44.22 E-value: 1.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 250 FCLVTDDvmPDDLIAkgHLNHLIQICNENGMRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILDD 318
Cdd:cd01309 274 FAISSDH--PVLNIR--NLNLEAAKAVKYGLSYEEALKAITINPAKILGIEDRvGSLEPGKDADLVVWNG 339
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
18-61 |
1.78e-04 |
|
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: 43.97 E-value: 1.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2500175486 18 FEKGDLYIQDSMIYHIGEADIIVDQE-IDAKGKWIIPGLIDIHMH 61
Cdd:TIGR00857 3 ETEVDILVEGGRIKKIGKLRIPPDAEvIDAKGLLVLPGFIDLHVH 47
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
19-61 |
1.93e-04 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 43.92 E-value: 1.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2500175486 19 EKGDLYIQDSMIYHIGEA-DIIVDQEIDAKGKWIIPGLIDIHMH 61
Cdd:PRK06189 19 YRADIGIKNGKIAEIAPEiSSPAREIIDADGLYVFPGMIDVHVH 62
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
22-105 |
2.14e-04 |
|
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: 43.47 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 22 DLYIQDSMIYHIGeADIIVD---QEIDAKGKWIIPGLIDIHMHIESSMT----NPNEFSktvLPMGTTTIVaDAheignv 94
Cdd:cd01307 1 DVAIENGKIAAVG-AALAAPaatQIVDAGGCYVSPGWIDLHVHVYQGGTrygdRPDMIG---VKSGVTTVV-DA------ 69
|
90
....*....|.
gi 2500175486 95 fGTQGLIDFMD 105
Cdd:cd01307 70 -GSAGADNIDG 79
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
267-325 |
3.78e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 43.07 E-value: 3.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500175486 267 HLNHLIQICNENGMRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILD--DLNAFSIH 325
Cdd:PRK08204 329 HLREGGMPPPRLTLTARQVLEWATIEGARALGLEDRiGSLTPGKQADLVLIDatDLNLAPVH 390
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
42-62 |
7.46e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 42.13 E-value: 7.46e-04
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
283-320 |
1.43e-03 |
|
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: 41.11 E-value: 1.43e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2500175486 283 EDAIYAATYVPAQRMQLYDRGVLSPGKQADFIILDDLN 320
Cdd:cd01306 276 PEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMD 313
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
21-61 |
1.92e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 40.83 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2500175486 21 GDLYIQDSMIYHIGEADIIVDQEIDAKGKWIIPGLIDIHMH 61
Cdd:PRK09061 39 RDVGIKGGKIAAVGTAAIEGDRTIDATGLVVAPGFIDLHAH 79
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
277-318 |
2.49e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 40.55 E-value: 2.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2500175486 277 ENGMRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILDD 318
Cdd:COG1574 464 EERLTVEEALRAYTIGAAYAAFEEDEkGSLEPGKLADFVVLDR 506
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
6-85 |
2.89e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 40.41 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 6 TDAFLYNTsqRTFEKGDLY-----IQDSMIYHIGEA--DIIVDQEIDAKGKWIIPGLIDIHMHI-ESSMTNPNEF---SK 74
Cdd:PRK02382 2 RDALLKDG--RVYYNNSLQprdvrIDGGKITAVGKDldGSSSEEVIDARGMLLLPGGIDVHVHFrEPGYTHKETWytgSR 79
|
90
....*....|.
gi 2500175486 75 TVLPMGTTTIV 85
Cdd:PRK02382 80 SAAAGGVTTVV 90
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
283-325 |
3.17e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 40.21 E-value: 3.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2500175486 283 EDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILDDlNAFSIH 325
Cdd:pfam07969 402 EEALALYTSGPAKALGLEDRkGTLGVGKDADLVVLDD-DPLTVD 444
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
280-317 |
3.39e-03 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 40.20 E-value: 3.39e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2500175486 280 MRPEDAIYAATYVPAQRMQLYDR-GVLSPGKQADFIILD 317
Cdd:COG0402 340 LSAREALEMATLGGARALGLDDEiGSLEPGKRADLVVLD 378
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
9-85 |
3.73e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 39.75 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500175486 9 FLYNtsQRTFEkGDLYIQDSMIYHIGEADIIVDQEIDAKGKWIIPGLIDIHMHI----ESSMTNPNEFSKTVLPMGTTTI 84
Cdd:PRK04250 6 FLLK--GRIVE-GGIGIENGRISKISLRDLKGKEVIKVKGGIILPGLIDVHVHLrdfeESYKETIESGTKAALHGGITLV 82
|
.
gi 2500175486 85 V 85
Cdd:PRK04250 83 F 83
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
19-85 |
3.80e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 39.83 E-value: 3.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2500175486 19 EKGDLYIQDSMIYHIGeADIIVDQE---IDAKGKWIIPGLIDIHMHIE----SSMTNPNEFSKT--VLPMGTTTIV 85
Cdd:PLN02942 21 ELADVYVEDGIIVAVA-PNLKVPDDvrvIDATGKFVMPGGIDPHTHLAmpfmGTETIDDFFSGQaaALAGGTTMHI 95
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
19-62 |
5.49e-03 |
|
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: 39.58 E-value: 5.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2500175486 19 EKGDLYIQDSMIYHIGEADIIVDQE--IDAKGKWIIPGLIDIHMHI 62
Cdd:cd01315 16 READIAVKGGKIAAIGPDIANTEAEevIDAGGLVVMPGLIDTHVHI 61
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
41-62 |
6.65e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 39.40 E-value: 6.65e-03
|
| |
