|
Name |
Accession |
Description |
Interval |
E-value |
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
53-588 |
3.35e-143 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 424.98 E-value: 3.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 53 SQSADQIFTNADIY----GHRESDSIVTHNGKIIFIGNQSQAQTFQGQSTDVIDLNNAFVLPGFIDNHNHVFEAASELGG 128
Cdd:COG1574 5 AAAADLLLTNGRIYtmdpAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 129 nCELDSEATLEEQIPYLEACKinADTDGRGWLMGYGFSlEATLDsDSDYTPLEIIDSIFPERPVVLMEQTSHSMWVNSKA 208
Cdd:COG1574 85 -VDLSGARSLDELLARLRAAA--AELPPGEWILGRGWD-ESLWP-EGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 209 LKIARISQQSPDLQGGAYLKDPDsGKLNGILLDNAGDQVMEMAWnSQSElfEQSYQGLMFGLEEAAAHGITTIGDGRMYw 288
Cdd:COG1574 160 LELAGITADTPDPEGGEIERDAD-GEPTGVLREAAMDLVRAAIP-PPTP--EELRAALRAALRELASLGITSVHDAGLG- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 289 kRGWYDVWLEAEQNQDLTARVSLRPWvypsmAMPSQLEVFEK--MYSDDKSHLLLVDQVKMYSDGIFINGTAKTLAPYLD 366
Cdd:COG1574 235 -PDDLAAYRELAAAGELPLRVVLYLG-----ADDEDLEELLAlgLRTGYGDDRLRVGGVKLFADGSLGSRTAALLEPYAD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 367 TylpQSPNGLNYIPPDQMKEWLTALEKIGFSAHIHAIGDGAVRESLDAIESIRKQGSTK--PYTLTHVELINDEDVPRFR 444
Cdd:COG1574 309 D---PGNRGLLLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRdrRHRIEHAQLVDPDDLARFA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 445 QLDVTADFQVGSDYVARHqhqWAEAFLGARRAKAMMNLDAIIKTDANITLSSDWNVHDINPLVGIA---NSLIMGKTGLT 521
Cdd:COG1574 386 ELGVIASMQPTHATSDGD---WAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYaavTRRTPSGRGLG 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376712965 522 -----DIYTAIDAYTINAASSLGIDDITGSIEVGKSADFTILDRDITTISARQIAKTQVLMTVLRGDMVYEK 588
Cdd:COG1574 463 peerlTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEA 534
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
74-557 |
7.85e-114 |
|
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: 347.76 E-value: 7.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 74 IVTHNGKIIFIGNQSQAQTFQGQSTDVIDLNNAFVLPGFIDNHNHVFEAASELGGnCELDSEATLEEQIPYLEACKinAD 153
Cdd:cd01300 2 VAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLW-LDLSGVTSKEEALARIREDA--AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 154 TDGRGWLMGYGFSleATLDSDSDYTPLEIIDSIFPERPVVLMEQTSHSMWVNSKALKIARISQQSPDLQGGAYLKDPDsG 233
Cdd:cd01300 79 APPGEWILGFGWD--ESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRDTPDPPGGEIVRDAD-G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 234 KLNGILLDNAGDQVMEMAWNSQSELFEQSYQGLMfglEEAAAHGITTIGDGRMYWKrGWYDVWLEAEQNQDLTARVSLRP 313
Cdd:cd01300 156 EPTGVLVEAAAALVLEAVPPPTPEERRAALRAAA---RELASLGVTTVHDAGGGAA-DDIEAYRRLAAAGELTLRVRVAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 314 WVYPSMAMPSQLEVFEKMYSDDKshLLLVDQVKMYSDGIFINGTAKTLAPYLDTYlpqSPNGLNYIPPDQMKEWLTALEK 393
Cdd:cd01300 232 YVSPLAEDLLEELGARKNGAGDD--RLRLGGVKLFADGSLGSRTAALSEPYLDSP---GTGGLLLISPEELEELVRAADE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 394 IGFSAHIHAIGDGAVRESLDAIESIRKQGSTK--PYTLTHVELINDEDVPRFRQLDVTADFQvgsdyvARHQHQWA---- 467
Cdd:cd01300 307 AGLQVAIHAIGDRAVDTVLDALEAALKDNPRAdhRHRIEHAQLVSPDDIPRFAKLGVIASVQ------PNHLYSDGdaae 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 468 EAFLGARRAKAMMNLDAIIKTDANITLSSDWNVHDINPLVGIAnSLIMGKTGLT----------DIYTAIDAYTINAASS 537
Cdd:cd01300 381 DRRLGEERAKRSYPFRSLLDAGVPVALGSDAPVAPPDPLLGIW-AAVTRKTPGGgvlgnpeerlSLEEALRAYTIGAAYA 459
|
490 500
....*....|....*....|
gi 1376712965 538 LGIDDITGSIEVGKSADFTI 557
Cdd:cd01300 460 IGEEDEKGSLEPGKLADFVV 479
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
99-586 |
5.55e-82 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 264.78 E-value: 5.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 99 DVIDLNNAFVLPGFIDNHNHVFEAASELggnceldSEATLEEQIPYLEACKINADTDGRGWLMGYGFSlEATLDSDSDYT 178
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNL-------RELRLPDVLPNAVVKGQAGRTPKGRWLVGEGWD-EAQFAETRFPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 179 PLEIIDSIFPERPVVLMEQTSHSMWVNSKALKIARISQQSPDLQGGAYLKDPDSGKLNGILLDNAGDQVMEMAwnsqsel 258
Cdd:pfam07969 73 ALADLDEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEGLTGLLREGAYALPPLLA------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 259 FEQSYQGLMFGLEEAAAHGITTI-GDGRMYWKRGWYDVWLEAEQNQDLTarvslrpwvypsmampSQLEVFEKMYSDDKS 337
Cdd:pfam07969 146 REAEAAAVAAALAALPGFGITSVdGGGGNVHSLDDYEPLRELTAAEKLK----------------ELLDAPERLGLPHSI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 338 HLLLVDQVKMYSDGIFINGTAKTLAPYLDTYLPqspnGLNYIPPDQMKEWLTALEKIGFSAHIHAIGDGAVRESLDAIES 417
Cdd:pfam07969 210 YELRIGAMKLFADGVLGSRTAALTEPYFDAPGT----GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 418 IRKQ-GSTKPYTLTH---VELINDEDVPRFRQLDVTADFQVGSDYVARHQHQWaeaFLGARRAKAMMNLDAIIKTDANIT 493
Cdd:pfam07969 286 VAEKlGNQGRVRIEHaqgVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQD---RLGAERARGLTPVKELLNAGVKVA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 494 LSSDWNVHDINPLVGIAnSLIMGKTGLT----------DIYTAIDAYTINAASSLGIDDITGSIEVGKSADFTILDRDIT 563
Cdd:pfam07969 363 LGSDAPVGPFDPWPRIG-AAVMRQTAGGgevlgpdeelSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPL 441
|
490 500
....*....|....*....|...
gi 1376712965 564 TISARQIAKTQVLMTVLRGDMVY 586
Cdd:pfam07969 442 TVDPPAIADIRVRLTVVDGRVVY 464
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
49-588 |
9.04e-18 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 85.40 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 49 TAVKSQSADQIFTNADIY-----GHRESDSIVTHNGKIIFIGNQSQAQTFQGqsTDVIDLNNAFVLPGFIDNHNHVFEAA 123
Cdd:COG1228 1 KKAPAQAGTLLITNATLVdgtggGVIENGTVLVEDGKIAAVGPAADLAVPAG--AEVIDATGKTVLPGLIDAHTHLGLGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 124 SELGgnceldsEATLEEQIPYLEACKINADTDGRGWLMgYGFsleatldsdsdyTpleiidsifperpvvlmeqTSHSMW 203
Cdd:COG1228 79 GRAV-------EFEAGGGITPTVDLVNPADKRLRRALA-AGV------------T-------------------TVRDLP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 204 VNSKALKIARISQQSPDLQGGAYLKdpdsgklngilldnagdqvmemawnsqselfeqsyqglmfgleeaAAHGITTIGD 283
Cdd:COG1228 120 GGPLGLRDAIIAGESKLLPGPRVLA---------------------------------------------AGPALSLTGG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 284 GRMYWkrgwydvwleaeqnqdltarvslrpwvyPSMAMpsqlEVFEKMYSDDkshlllVDQVKMYSDGIFINGTAKTLAP 363
Cdd:COG1228 155 AHARG----------------------------PEEAR----AALRELLAEG------ADYIKVFAEGGAPDFSLEELRA 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 364 YLDTylpqspnglnyippdqmkewltAlEKIGFSAHIHAIGDGAVRESLDA-IESIrkqgstkpytlTHVELINDEDVPR 442
Cdd:COG1228 197 ILEA----------------------A-HALGLPVAAHAHQADDIRLAVEAgVDSI-----------EHGTYLDDEVADL 242
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 443 FRQ-----LDVTADFqvgSDYVARHQHQWAEAFLGARRAKAMMNLDAIIKTDANITLSSDWNVHDInplVGIANSLIMGK 517
Cdd:COG1228 243 LAEagtvvLVPTLSL---FLALLEGAAAPVAAKARKVREAALANARRLHDAGVPVALGTDAGVGVP---PGRSLHRELAL 316
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376712965 518 T---GLTdIYTAIDAYTINAASSLGIDDITGSIEVGKSADFTILDRDITT-ISARQiaktQVLMTVLRGDMVYEK 588
Cdd:COG1228 317 AveaGLT-PEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEdIAYLE----DVRAVMKDGRVVDRS 386
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
260-585 |
2.23e-16 |
|
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: 80.62 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 260 EQSYQGLMFGLEEAAAHGITTIGDgrMYWKRGWYDVWL--EAEQnqdltARVSLRPWV-YPSMAMPSQLEVFEKmysddk 336
Cdd:pfam01979 26 EFAYEALRLGITTMLKSGTTTVLD--MGATTSTGIEALleAAEE-----LPLGLRFLGpGCSLDTDGELEGRKA------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 337 shllLVDQVKMYSDGIFINGTAKTLApYLDTYLPQSpnglnyIPPDQMKEWLTALEKIGFSAHIHAIG-DGAVRESLDAI 415
Cdd:pfam01979 93 ----LREKLKAGAEFIKGMADGVVFV-GLAPHGAPT------FSDDELKAALEEAKKYGLPVAIHALEtKGEVEDAIAAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 416 ESIRKQGstkpytlTHVELINDEDVPRFRQLdVTAD--FQVGSDYVARHQHQWAE-----AFLGARRAKAMMNLDAIIKT 488
Cdd:pfam01979 162 GGGIEHG-------THLEVAESGGLLDIIKL-ILAHgvHLSPTEANLLAEHLKGAgvahcPFSNSKLRSGRIALRKALED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 489 DANITLSSDWNVHDINP--LVGIANSLIM--GKTGLTDIYTAIDAYTINAASSLGIDDITGSIEVGKSADFTILDRDITT 564
Cdd:pfam01979 234 GVKVGLGTDGAGSGNSLnmLEELRLALELqfDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLA 313
|
330 340
....*....|....*....|.
gi 1376712965 565 ISARQIAKTQVLMTVLRGDMV 585
Cdd:pfam01979 314 AFFGLKPDGNVKKVIVKGKIV 334
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
74-559 |
3.32e-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: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 74 IVTHNGKIIFIGNQSQAQTFQGQSTDVIDLNNAFVLPGFIDNHNH-VFeaaselGGNceldseatleeqipyleackina 152
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHlVF------AGD----------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 153 dtdgrgwlmgygfsleatldsdsdytpleiidsifpeRpvvlmeqtshsmwVNSKALKIARISQQSPDLQGGaylkdpds 232
Cdd:cd01296 52 -------------------------------------R-------------VDEFAARLAGASYEEILAAGG-------- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 233 gklnGILldnagDQVMEMAWNSQSELFEQSyqglMFGLEEAAAHGITTIgdgrmYWKRGwYDVWLEAEQNQDLTAR---- 308
Cdd:cd01296 74 ----GIL-----STVRATRAASEDELFASA----LRRLARMLRHGTTTV-----EVKSG-YGLDLETELKMLRVIRrlke 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 309 ---VSLRPWVYPSMAMPSQLEVFEKMYSDDKSHLLlvDQVKmysdgifingtAKTLAPYLDTYLPQspnglNYIPPDQMK 385
Cdd:cd01296 135 egpVDLVSTFLGAHAVPPEYKGREEYIDLVIEEVL--PAVA-----------EENLADFCDVFCEK-----GAFSLEQSR 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 386 EWLTALEKIGFSAHIHAigdgavrESLDAIESIRKQGSTKPYTLTHVELINDEDVPRFRQLDVTADFQVGSDYvarhqhq 465
Cdd:cd01296 197 RILEAAKEAGLPVKIHA-------DELSNIGGAELAAELGALSADHLEHTSDEGIAALAEAGTVAVLLPGTAF------- 262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 466 waeaFLGARRAKAmmnlDAIIKTDANITLSSDwnvhdINPLVGIANSLIM------GKTGLTDIyTAIDAYTINAASSLG 539
Cdd:cd01296 263 ----SLRETYPPA----RKLIDAGVPVALGTD-----FNPGSSPTSSMPLvmhlacRLMRMTPE-EALTAATINAAAALG 328
|
490 500
....*....|....*....|
gi 1376712965 540 IDDITGSIEVGKSADFTILD 559
Cdd:cd01296 329 LGETVGSLEVGKQADLVILD 348
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
260-535 |
6.00e-09 |
|
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: 57.34 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 260 EQSYQGLMFGLEEAAAHGITTIGD----GRMYWKRGWYDVWLE-AEQNQDLTARVSL----RPWVYPSMAMPSQLEVFEK 330
Cdd:cd01292 31 EDLYEDTLRALEALLAGGVTTVVDmgstPPPTTTKAAIEAVAEaARASAGIRVVLGLgipgVPAAVDEDAEALLLELLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 331 MYsddkshlllvdqvkmysdgifingtaKTLAPYLDTYLPQSPNGLnyiPPDQMKEWLTALEKIGFSAHIHA-IGDGAVR 409
Cdd:cd01292 111 GL--------------------------ELGAVGLKLAGPYTATGL---SDESLRRVLEEARKLGLPVVIHAgELPDPTR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 410 ESLDAIESIRKQGSTkpyTLTHVELINDEDVPRFRQLDVTADFqvgSDYVARHQHQWAEAFLGARRAKAMmnldaiiktD 489
Cdd:cd01292 162 ALEDLVALLRLGGRV---VIGHVSHLDPELLELLKEAGVSLEV---CPLSNYLLGRDGEGAEALRRLLEL---------G 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1376712965 490 ANITLSSDWNVH--DINPLVGIANSLIMGKTGLTdIYTAIDAYTINAA 535
Cdd:cd01292 227 IRVTLGTDGPPHplGTDLLALLRLLLKVLRLGLS-LEEALRLATINPA 273
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
342-565 |
5.76e-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: 54.99 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 342 VDQVKMYSDGIFINGTaktlapyldtylpqSPNGLNYIPPDQMKEWLTALEKIGFSAHIHAIGDGAVRESLDA-IESIrk 420
Cdd:cd01299 134 ADQIKIMATGGVLSPG--------------DPPPDTQFSEEELRAIVDEAHKAGLYVAAHAYGAEAIRRAIRAgVDTI-- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 421 qgstkpytlTHVELINDEDVPRFRQLDVT---------------ADFQVGSDYVARHQHQWAEAFLGARRAKammnlDAI 485
Cdd:cd01299 198 ---------EHGFLIDDETIELMKEKGIFlvptlatyealaaegAAPGLPADSAEKVALVLEAGRDALRRAH-----KAG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 486 IK----TDA-NITLSSDWNVHDINplvgianslIMGKTGLTdIYTAIDAYTINAASSLGIDDITGSIEVGKSADFTILD- 559
Cdd:cd01299 264 VKiafgTDAgFPVPPHGWNARELE---------LLVKAGGT-PAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDg 333
|
....*....
gi 1376712965 560 ---RDITTI 565
Cdd:cd01299 334 dplEDIAVL 342
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
487-586 |
6.28e-08 |
|
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: 55.01 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 487 KTDANITLSSDWNVHDINPLVGIANslIMGKTGLTdIYTAIDAYTINAASSLGIDDITGSIEVGKSADFTILDRDITTIS 566
Cdd:cd01309 269 KGGVAFAISSDHPVLNIRNLNLEAA--KAVKYGLS-YEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPT 345
|
90 100
....*....|....*....|
gi 1376712965 567 ARqiaktqVLMTVLRGDMVY 586
Cdd:cd01309 346 SK------PEQVYIDGRLVY 359
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
526-582 |
1.13e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 54.33 E-value: 1.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1376712965 526 AIDAYTINAASSLGIDDITGSIEVGKSADFTILDRDIttisarqiaktQVLMTVLRG 582
Cdd:COG1820 327 AVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDL-----------NVRATWVGG 372
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
70-559 |
1.43e-07 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 53.95 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 70 ESDSIVTHNGKIIFIGNQSQAQTFQGqsTDVIDLNNAFVLPGFIDNHNH-VFeaaselGGNCELDSEATLeEQIPYLEac 148
Cdd:TIGR01224 2 EDAVILIHGGKIVWIGQLAALPGEEA--TEIIDCGGGLVTPGLVDPHTHlVF------AGDRVNEFEMKL-QGASYLE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 149 kinadtdgrgwlmgygfsleatldsdsdytpleiidsifperpvvlmeqtshsmwvnskalkIARisqqspdlQGGaylk 228
Cdd:TIGR01224 71 --------------------------------------------------------------ILA--------QGG---- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 229 dpdsgklnGILldnagDQVMEMAWNSQSELFEQsyqgLMFGLEEAAAHGITTigdgrMYWKRGwYDVWLEAEQNQDLTAR 308
Cdd:TIGR01224 77 --------GIL-----STVRATRAASEEELLKL----ALFRLKSMLRSGTTT-----AEVKSG-YGLDLETELKMLRAAK 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 309 -------VSLRPWVYPSMAMPSqlEVFEKMYsddkshlllvDQVKMYSDGIFINGTAKTLAPYLDTYLPQspnglNYIPP 381
Cdd:TIGR01224 134 alheeqpVDVVTTFLGAHAVPP--EFQGRPD----------DYVDGICEELIPQVAEEGLASFADVFCEA-----GVFSV 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 382 DQMKEWLTALEKIGFSAHIHAigdgavrESLDAIESIRKQGSTKPYTLTHVELINDEDVPRFRQLDVTADFQVGSDYVAR 461
Cdd:TIGR01224 197 EQSRRILQAAQEAGLPVKLHA-------EELSNLGGAELAAKLGAVSADHLEHASDAGIKALAEAGTVAVLLPGTTFYLR 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 462 HQHQWAEAFLGARRAKAmmnldaiIKTDANITLSSdwnVHDInplvgianSLIMGKTGLTDIYT---AIDAYTINAASSL 538
Cdd:TIGR01224 270 ETYPPARQLIDYGVPVA-------LATDLNPGSSP---TLSM--------QLIMSLACRLMKMTpeeALHAATVNAAYAL 331
|
490 500
....*....|....*....|.
gi 1376712965 539 GIDDITGSIEVGKSADFTILD 559
Cdd:TIGR01224 332 GLGEERGTLEAGRDADLVILS 352
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
524-561 |
7.52e-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: 51.75 E-value: 7.52e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1376712965 524 YTAIDAYTINAASSLGIDDITGSIEVGKSADFTILDRD 561
Cdd:COG0402 343 REALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLD 380
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
525-559 |
1.70e-06 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 50.68 E-value: 1.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1376712965 525 TAIDAY------TINAASSLGIDDITGSIEVGKSADFTILD 559
Cdd:PRK09045 338 TALPAHtalrmaTLNGARALGLDDEIGSLEPGKQADLVAVD 378
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
514-588 |
3.50e-06 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 49.81 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 514 IMGKTGLTDIYTAIDAYTINAASSLGIDDitGSIEVGKSADFTILDRDIT-TISARQIA-------------KTQVLMTV 579
Cdd:PRK09357 337 TLVKTGLLDLEQLLEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEwTVDGEDFAskgkntpfigmklKGKVVYTI 414
|
....*....
gi 1376712965 580 LRGDMVYEK 588
Cdd:PRK09357 415 VDGKIVYQD 423
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
526-582 |
3.83e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 49.50 E-value: 3.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1376712965 526 AIDAYTINAASSLGIDDITGSIEVGKSADFTILDRDITtisarqiaktqVLMTVLRG 582
Cdd:cd00854 329 AVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLN-----------VKATWING 374
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
56-119 |
2.35e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 47.40 E-value: 2.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376712965 56 ADQIFTNA---DIY-GHRESDSIVTHNGKIIFIGNqsqaqtFQGQSTDVIDLNNAFVLPGFIDNHNHV 119
Cdd:COG1001 5 ADLVIKNGrlvNVFtGEILEGDIAIAGGRIAGVGD------YIGEATEVIDAAGRYLVPGFIDGHVHI 66
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
370-588 |
2.99e-05 |
|
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: 46.81 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 370 PQSPNglnYIPPDQMKEWLTALEKIGFSAHIHaigdgaVRESLDAIESIRKQ-GST------------KPYTLTHVELIN 436
Cdd:cd01298 185 PHAPY---TCSDELLREVAELAREYGVPLHIH------LAETEDEVEESLEKyGKRpveyleelgllgPDVVLAHCVWLT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 437 DEDVPRFRQLDV------TADFQVGSdyvarhqhqwaeaflGARRAKAMmnLDAIIktdaNITLSSDwnvhdinplvGIA 510
Cdd:cd01298 256 DEEIELLAETGTgvahnpASNMKLAS---------------GIAPVPEM--LEAGV----NVGLGTD----------GAA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 511 --NSLIM---------------GKTGLTDIYTAIDAYTINAASSLGIDDItGSIEVGKSADFTILD-RDITTISARQIAK 572
Cdd:cd01298 305 snNNLDMfeemrlaallqklahGDPTALPAEEALEMATIGGAKALGLDEI-GSLEVGKKADLILIDlDGPHLLPVHDPIS 383
|
250 260
....*....|....*....|....
gi 1376712965 573 T--------QVLMTVLRGDMVYEK 588
Cdd:cd01298 384 HlvysanggDVDTVIVNGRVVMED 407
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
55-118 |
3.30e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 46.46 E-value: 3.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376712965 55 SADQIFTNADIYGHRESDsIVTHNGKIIFIGNQSQAQtfqgQSTDVIDLNNAFVLPGFIDNHNH 118
Cdd:PRK05985 1 MTDLLFRNVRPAGGAAVD-ILIRDGRIAAIGPALAAP----PGAEVEDGGGALALPGLVDGHIH 59
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
78-129 |
6.47e-05 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 45.61 E-value: 6.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1376712965 78 NGKIIFIGNQSQAqtfqGQSTDVIDLNNAFVLPGFIDNHNHVFEAASELGGN 129
Cdd:PRK09237 25 DGKIAAVAGDIDG----SQAKKVIDLSGLYVSPGWIDLHVHVYPGSTPYGDE 72
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
59-118 |
9.94e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 44.70 E-value: 9.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376712965 59 IFTNADIY---GHRESDSIVTHNGKIIFIGNQSQAQTfqgqstDVIDLNNAFVLPGFIDNHNH 118
Cdd:COG1820 1 AITNARIFtgdGVLEDGALLIEDGRIAAIGPGAEPDA------EVIDLGGGYLAPGFIDLHVH 57
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
78-127 |
1.24e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 44.39 E-value: 1.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1376712965 78 NGKIIFIGNQSQAqtfqGQSTDVIDLNNAFVLPGFIDNHNHVFEAASELG 127
Cdd:COG3964 26 DGKIAAVAKDIDA----AEAKKVIDASGLYVTPGLIDLHTHVFPGGTDYG 71
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
527-560 |
1.48e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 44.70 E-value: 1.48e-04
10 20 30
....*....|....*....|....*....|....
gi 1376712965 527 IDAYTINAASSLGIDDITGSIEVGKSADFTILDR 560
Cdd:PRK13308 406 IAKYTINPAITFGIDDHIGSLEPGKLADIVLWRP 439
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
59-118 |
2.27e-04 |
|
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: 43.77 E-value: 2.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1376712965 59 IFTNADIY-GHRESDSIVTHNGKIIFIGNQSQAQTFQgqstDVIDLNNAFVLPGFIDNHNH 118
Cdd:cd01293 1 LLRNARLAdGGTALVDIAIEDGRIAAIGPALAVPPDA----EEVDAKGRLVLPAFVDPHIH 57
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
57-129 |
2.37e-04 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 43.60 E-value: 2.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376712965 57 DQIFTNADIY----GHRESDSIVTHNGKIIFIGNQSQAQtfqgqSTDVIDLNNAFVLPGFIDNHNHVFEAASELGGN 129
Cdd:PRK12394 4 DILITNGHIIdparNINEINNLRIINDIIVDADKYPVAS-----ETRIIHADGCIVTPGLIDYHAHVFYDGTEGGVR 75
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
55-119 |
3.47e-04 |
|
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: 43.36 E-value: 3.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376712965 55 SADQIFtNADIYghresdsIVthNGKIIFIGNQSQAQTfqgqSTDVIDLNNAFVLPGFIDNHNHV 119
Cdd:cd01314 10 TADGSF-KADIL-------IE--DGKIVAIGPNLEAPG----GVEVIDATGKYVLPGGIDPHTHL 60
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
523-558 |
5.15e-04 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 42.68 E-value: 5.15e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1376712965 523 IYTAIDAYTINAASSLGIDDITGSIEVGKSADFTIL 558
Cdd:PRK06687 336 IETALKVLTIEGAKALGMENQIGSLEVGKQADFLVI 371
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
525-588 |
5.48e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 42.68 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 525 TAIDAY------TINAASSLGIDDITGSIEVGKSADFTILDRDIT--------------TISARqiaKTQVLMTVLRGDM 584
Cdd:PRK07228 335 TAMPARtvfemaTLGGAKAAGFEDEIGSLEEGKKADLAILDLDGLhatpshgvdvlshlVYAAH---GSDVETTMVDGKI 411
|
....
gi 1376712965 585 VYEK 588
Cdd:PRK07228 412 VMED 415
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
57-121 |
6.67e-04 |
|
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: 42.28 E-value: 6.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376712965 57 DQIFTNADI---YGHRESDsIVTHNGKIIFIGnqsqAQTFQGQSTDVIDLNNAFVLPGFIDNHNHVFE 121
Cdd:cd01315 1 DLVIKNGRVvtpDGVREAD-IAVKGGKIAAIG----PDIANTEAEEVIDAGGLVVMPGLIDTHVHINE 63
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
59-121 |
8.25e-04 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 42.19 E-value: 8.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376712965 59 IFTNADIYGHRESDsIVTHNGKIIFIGnqSQAQTFQGQSTDVIDLNNAFVLPGFIDNHNHVFE 121
Cdd:cd01298 8 IVTTDPRRVLEDGD-VLVEDGRIVAVG--PALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAM 67
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
527-559 |
1.32e-03 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 41.55 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|...
gi 1376712965 527 IDAYTINAASSLGIDDITGSIEVGKSADFTILD 559
Cdd:cd00375 405 IAKYTINPAIAHGISHEVGSVEVGKLADLVLWE 437
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
533-588 |
1.66e-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: 41.12 E-value: 1.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 533 NAASSLGIDDITGSIEVGKSADFTILDRDI-TTISARQIA-------------KTQVLMTVLRGDMVYEK 588
Cdd:cd01315 365 NPAKLFGLSHQKGRIAVGYDADFVVWDPEEeFTVDAEDLYyknkispyvgrtlKGRVHATILRGTVVYQD 434
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
493-559 |
1.67e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 40.99 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376712965 493 TLSSDwnVHDINPLVGIANSL--IMGK-----TGLTDIytaIDAYTINAASSLGIDDItGSIEVGKSADFTILD 559
Cdd:PRK09237 266 TISTD--IYCRNRINGPVYSLatVMSKflalgMPLEEV---IAAVTKNAADALRLPEL-GRLQVGSDADLTLFT 333
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
378-559 |
1.73e-03 |
|
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: 41.06 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 378 YIPPDQMKEWLT-----AL-EKIGFSAHIHaiGDgavRESLDAIESIRKQGSTKpytLTHVELINDEDVPRFRQLDVTAD 451
Cdd:cd01295 89 ELTAEDIKELLEhpevvGLgEVMDFPGVIE--GD---DEMLAKIQAAKKAGKPV---DGHAPGLSGEELNAYMAAGISTD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 452 fqvgsdyvarHQHQWAEAFLGARRA--KAMM-------NLDAIIKTDA-----NITLSSDwNVH--------DINPLVGI 509
Cdd:cd01295 161 ----------HEAMTGEEALEKLRLgmYVMLregsiakNLEALLPAITeknfrRFMFCTD-DVHpddllsegHLDYIVRR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1376712965 510 AnslImgKTGLtDIYTAIDAYTINAASSLGIDDItGSIEVGKSADFTILD 559
Cdd:cd01295 230 A---I--EAGI-PPEDAIQMATINPAECYGLHDL-GAIAPGRIADIVILD 272
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
67-118 |
2.40e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 40.80 E-value: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1376712965 67 GHR--ESDSIVTHNGKIIFIGNQsqaqtFQGQSTDVIDLNNAFVLPGFIDNHNH 118
Cdd:PRK06151 17 DHRllRDGEVVFEGDRILFVGHR-----FDGEVDRVIDAGNALVGPGFIDLDAL 65
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
531-561 |
3.42e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 39.99 E-value: 3.42e-03
10 20 30
....*....|....*....|....*....|.
gi 1376712965 531 TINAASSLGIDDITGSIEVGKSADFTILDRD 561
Cdd:PRK08204 352 TIEGARALGLEDRIGSLTPGKQADLVLIDAT 382
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
49-118 |
3.48e-03 |
|
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: 39.95 E-value: 3.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376712965 49 TAVKSQSADQIFTNADIYGHRESDSIVTHNGKIIFIGNQSQAQTFQGQSTDVIDLNNAFVLPGFIDNHNH 118
Cdd:cd01303 4 TFIHTKSLPELELVEDALRVVEDGLIVVVDGNIIAAGAAETLKRAAKPGARVIDSPNQFILPGFIDTHIH 73
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
530-559 |
3.51e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 40.08 E-value: 3.51e-03
10 20 30
....*....|....*....|....*....|
gi 1376712965 530 YTINAASSLGIDDITGSIEVGKSADFTILD 559
Cdd:PRK13206 413 YTICPAVAHGIDHEIGSVEVGKLADLVLWE 442
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
525-569 |
3.53e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.08 E-value: 3.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1376712965 525 TAIDAYTINAASSLGIDDItGSIEVGKSADFTILDrDITTISARQ 569
Cdd:COG1001 288 TAIQMATLNAAEHFGLKDL-GAIAPGRRADIVLLD-DLEDFKVEK 330
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
530-554 |
4.51e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 39.78 E-value: 4.51e-03
10 20
....*....|....*....|....*
gi 1376712965 530 YTINAASSLGIDDITGSIEVGKSAD 554
Cdd:PRK13207 408 YTINPAIAHGISHEVGSVEVGKLAD 432
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
56-119 |
4.83e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 39.73 E-value: 4.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376712965 56 ADQIFTNADIYGHRESD----SIVTHNGKIIFIGNQSQaqtfqGQSTDVIDLNNAFVLPGFIDNHNHV 119
Cdd:PRK06038 2 ADIIIKNAYVLTMDAGDlkkgSVVIEDGTITEVSESTP-----GDADTVIDAKGSVVMPGLVNTHTHA 64
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
59-121 |
5.23e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 39.41 E-value: 5.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376712965 59 IFTNADIY---GHRESDSIVTHNGKIIFIGnqsqaQTFQGQSTDVIDLNNAFVLPGFIDNHNHVFE 121
Cdd:PRK09357 4 LIKNGRVIdpkGLDEVADVLIDDGKIAAIG-----ENIEAEGAEVIDATGLVVAPGLVDLHVHLRE 64
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
59-118 |
5.27e-03 |
|
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: 39.48 E-value: 5.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376712965 59 IFTNADIYGHR--ESDSIVTHNGKIIFIGnqsqAQTFQGQSTDVIDLNNAFVLPGFIDNHNH 118
Cdd:cd00854 2 IIKNARILTPGglEDGAVLVEDGKIVAIG----PEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
100-147 |
5.57e-03 |
|
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: 39.20 E-value: 5.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1376712965 100 VIDLNNAFVLPGFIDNHNHVFEAASELGGNCELDSEATLEEQIPYLEA 147
Cdd:cd01299 3 VIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYRTIRATRQARA 50
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
59-119 |
5.92e-03 |
|
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: 39.30 E-value: 5.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376712965 59 IFTNADIY---GHRESDsIVTHNGKIIFIGNQSQAqtfqGQSTDVIDLNNAFVLPGFIDNHNHV 119
Cdd:COG0044 1 LIKNGRVVdpgGLERAD-VLIEDGRIAAIGPDLAA----PEAAEVIDATGLLVLPGLIDLHVHL 59
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
517-561 |
7.19e-03 |
|
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: 39.14 E-value: 7.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1376712965 517 KTGLTDIYTAIDAYTINAASSLGIDDitGSIEVGKSADFTILDRD 561
Cdd:cd01317 301 KGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPD 343
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
531-559 |
7.70e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 39.02 E-value: 7.70e-03
10 20
....*....|....*....|....*....
gi 1376712965 531 TINAASSLGIDDITGSIEVGKSADFTILD 559
Cdd:PRK09228 358 TLGGARALGLDDRIGNLAPGKEADFVVLD 386
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
74-127 |
8.58e-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: 38.46 E-value: 8.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1376712965 74 IVTHNGKIIFIGNQSQAqtfqGQSTDVIDLNNAFVLPGFIDNHNHVFEAASELG 127
Cdd:cd01307 2 VAIENGKIAAVGAALAA----PAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYG 51
|
|
| |
