|
Name |
Accession |
Description |
Interval |
E-value |
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
17-556 |
0e+00 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 635.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 17 TAQADVRMLTAATIHTGDPDAPAATALAwdTDTGRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGT 95
Cdd:COG1574 4 AAAAADLLLTNGRIYTMDPAQPVAEAVA--VRDGRIVAVGSDAEVRALAGPATEViDLGGKTVLPGFIDAHVHLLGGGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 96 LMQADLTGATSSRDIVARLQRFAADNPEG-WLLGSGWDQNRWPDKQFPTVADLDAAFPDRPVWLGRIDGHAGWGNSAALR 174
Cdd:COG1574 82 LLGVDLSGARSLDELLARLRAAAAELPPGeWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 175 AVarqpgqRALKGSWQPAGGRIVRDAKGQPSGVFVDEAMSLVQAAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSR 254
Cdd:COG1574 162 LA------GITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 255 ADLALMRRFADAGKLPLRIDAYADGNGDALADICAQGAYQHAGG-RLEMRGVKLFMDGALGSRGAALLADYSDDPHNRGL 333
Cdd:COG1574 236 DDLAAYRELAAAGELPLRVVLYLGADDEDLEELLALGLRTGYGDdRLRVGGVKLFADGSLGSRTAALLEPYADDPGNRGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 334 LVTSPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQP 413
Cdd:COG1574 316 LLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 414 THATSDMGWAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEQVDPRLGLYAAVTRQDRAGQppgGWQPDQRLTAAEA 493
Cdd:COG1574 396 THATSDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGR---GLGPEERLTVEEA 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784223663 494 LRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVPPAGLADLQVRSTWVDGAPVYEAA 556
Cdd:COG1574 473 LRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
50-524 |
2.33e-162 |
|
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: 471.02 E-value: 2.33e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 50 GRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGTLMQADLTGATSSRDIVARLQRFAADNPEG-WLL 127
Cdd:cd01300 7 GRIVAVGSDAEAKALKGPATEViDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAPPGeWIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 128 GSGWDQNRWPDKQFPTVADLDAAFPDRPVWLGRIDGHAGWGNSAALRAVArqpgqrALKGSWQPAGGRIVRDAKGQPSGV 207
Cdd:cd01300 87 GFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAG------ITRDTPDPPGGEIVRDADGEPTGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 208 FVDEAMSLVQAAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSRAD-LALMRRFADAGKLPLRIDA--YADGNGDAL 284
Cdd:cd01300 161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADdIEAYRRLAAAGELTLRVRValYVSPLAEDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 285 ADICAQGAYQHAGGRLEMRGVKLFMDGALGSRGAALLADYSDDPHNRGLLVTSPDDFETAVRKADTCHVQVATHAIGDRG 364
Cdd:cd01300 241 LEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 365 NRIALDTYQKVLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQPTHATSDMGWAQDR-VGPERILGAYAWRRMLA 443
Cdd:cd01300 321 VDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrLGEERAKRSYPFRSLLD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 444 SGARLALGSDFPVEQVDPRLGLYAAVTRQDRAGQPPGGwqPDQRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFV 523
Cdd:cd01300 401 AGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGN--PEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478
|
.
gi 2784223663 524 V 524
Cdd:cd01300 479 V 479
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
72-553 |
4.95e-82 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 264.01 E-value: 4.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 72 DVGQATVIPGLIDAHAHLMFLGGTLMQADLTGATSSRDIVARLQRFAADnpeGWLLGSGWDQNRWPDKQFP-TVADLDAA 150
Cdd:pfam07969 4 DAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAVVKGQAGRTPKG---RWLVGEGWDEAQFAETRFPyALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 151 FPDRPVWLGRIDGHAGWGNSAALRAVARQPGQRAlkgswqPAGGRIVRDAKG-QPSGVFVDEAmslvQAAIPAPSEAARE 229
Cdd:pfam07969 81 APDGPVLLRALHTHAAVANSAALDLAGITKATED------PPGGEIARDANGeGLTGLLREGA----YALPPLLAREAEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 230 QMLARALDKAVSQGLTGVHDMGV---SRADLALMRRFADAGKLPlridayadgngdALADICAQGAYQHAGGRLEMRGVK 306
Cdd:pfam07969 151 AAVAAALAALPGFGITSVDGGGGnvhSLDDYEPLRELTAAEKLK------------ELLDAPERLGLPHSIYELRIGAMK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 307 LFMDGALGSRGAALLADYSDDPhNRGLLVTSPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVlGERRATDHRW 386
Cdd:pfam07969 219 LFADGVLGSRTAALTEPYFDAP-GTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAV-AEKLGNQGRV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 387 RIEHAQVVAL---EDIPRFAQLGVIASMQPTHATSDMGWAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEQVDPRL 463
Cdd:pfam07969 297 RIEHAQGVVPytySQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 464 GLYAAVTRQDRAGQppGGWQPDQRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVPPAGLADLQVR 543
Cdd:pfam07969 377 RIGAAVMRQTAGGG--EVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVR 454
|
490
....*....|
gi 2784223663 544 STWVDGAPVY 553
Cdd:pfam07969 455 LTVVDGRVVY 464
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
191-555 |
2.48e-18 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 86.94 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 191 PAGGRIVrDAKGQ---PSgvFVDEAMSLVQAAIPAPSEAARE---------QMLARALDKAVSQGLTGVHDMgvSRADLA 258
Cdd:COG1228 50 PAGAEVI-DATGKtvlPG--LIDAHTHLGLGGGRAVEFEAGGgitptvdlvNPADKRLRRALAAGVTTVRDL--PGGPLG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 259 LmRRFADAGKLPLRIDAYADGNGDALAdiCAQGAyqHAGGRLEMRGV--KLFMDGAlgsrgaallaDYSDDPHNRGLLVT 336
Cdd:COG1228 125 L-RDAIIAGESKLLPGPRVLAAGPALS--LTGGA--HARGPEEARAAlrELLAEGA----------DYIKVFAEGGAPDF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 337 SPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVlgerratdhrwrIEHAQVVALEDIPRFAQLGVIAsMQPTHA 416
Cdd:COG1228 190 SLEELRAILEAAHALGLPVAAHAHQADDIRLAVEAGVDS------------IEHGTYLDDEVADLLAEAGTVV-LVPTLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 417 TSDMG------WAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEqVDPRLGLYAAVTRQDRAGqppggwqpdqrLTA 490
Cdd:COG1228 257 LFLALlegaaaPVAAKARKVREAALANARRLHDAGVPVALGTDAGVG-VPPGRSLHRELALAVEAG-----------LTP 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784223663 491 AEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVppagLADLQ-VRSTWVDGAPVYEA 555
Cdd:COG1228 325 EEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLED----IAYLEdVRAVMKDGRVVDRS 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
434-554 |
2.14e-10 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 62.92 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 434 GAYAWRRMLASGARLALGSDFPVEQVDP------RLGLYAAvtrQDRAGQPPggwqpdqRLTAAEALRGFTADAAWAGHD 507
Cdd:COG0402 290 GIAPVPRLLAAGVRVGLGTDGAASNNSLdmfeemRLAALLQ---RLRGGDPT-------ALSAREALEMATLGGARALGL 359
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2784223663 508 EAQVGRLQPGLRADFVVLDRDplSVPPAGLADL-----------QVRSTWVDGAPVYE 554
Cdd:COG0402 360 DDEIGSLEPGKRADLVVLDLD--APHLAPLHDPlsalvyaadgrDVRTVWVAGRVVVR 415
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
233-530 |
1.49e-09 |
|
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: 59.61 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 233 ARALDKAVSQGLTGVHDMGvsRADLALMRRFADAGKLPL-RI----------DAYADGNGDALADICAQGAYQhAGGRLE 301
Cdd:cd01299 45 TRQARAALRAGFTTVRDAG--GADYGLLRDAIDAGLIPGpRVfasgralsqtGGHGDPRGLSGLFPAGGLAAV-VDGVEE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 302 MRG------------VKLFMDGALGSRGaalladysDDPHNRGLlvtSPDDFETAVRKADTCHVQVATHAIGDRGNRIAL 369
Cdd:cd01299 122 VRAavreqlrrgadqIKIMATGGVLSPG--------DPPPDTQF---SEEELRAIVDEAHKAGLYVAAHAYGAEAIRRAI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 370 ----DTyqkvlgerratdhrwrIEHAQVVALEDIPRFAQLGVIASMQPT---------HATSDMGWAQDRVGPERILGAY 436
Cdd:cd01299 191 ragvDT----------------IEHGFLIDDETIELMKEKGIFLVPTLAtyealaaegAAPGLPADSAEKVALVLEAGRD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 437 AWRRMLASGARLALGSD--FPVeqvdprlglyaavtrqdragqPPGGWQPDQ-------RLTAAEALRGFTADAAWAGHD 507
Cdd:cd01299 255 ALRRAHKAGVKIAFGTDagFPV---------------------PPHGWNARElellvkaGGTPAEALRAATANAAELLGL 313
|
330 340
....*....|....*....|...
gi 2784223663 508 EAQVGRLQPGLRADFVVLDRDPL 530
Cdd:cd01299 314 SDELGVIEAGKLADLLVVDGDPL 336
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
220-552 |
1.97e-08 |
|
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: 56.36 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 220 IPAPSEAAREqMLARALDKAVSQGLTGVHDMGVSRAD-LALMRRFADAGKLPLRIDA-----YADGNGDALADICAQGAY 293
Cdd:pfam01979 21 IPVPPEFAYE-ALRLGITTMLKSGTTTVLDMGATTSTgIEALLEAAEELPLGLRFLGpgcslDTDGELEGRKALREKLKA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 294 qhaggrlEMRGVKLFMDGALGSRGAalladysddPHnrGLLVTSPDDFETAVRKADTCHVQVATHAIGDRGnrialDTYQ 373
Cdd:pfam01979 100 -------GAEFIKGMADGVVFVGLA---------PH--GAPTFSDDELKAALEEAKKYGLPVAIHALETKG-----EVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 374 KVLGERRATDHRWRIEHAQVVALEDIPRFA-QLGV---IASMQPTHATSDMGWAQDRVGPERIL--GAYAWRRMLASGAR 447
Cdd:pfam01979 157 AIAAFGGGIEHGTHLEVAESGGLLDIIKLIlAHGVhlsPTEANLLAEHLKGAGVAHCPFSNSKLrsGRIALRKALEDGVK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 448 LALGSDFPVEQVDPRL---GLYAAVTRQDragqppggwqPDQRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVV 524
Cdd:pfam01979 237 VGLGTDGAGSGNSLNMleeLRLALELQFD----------PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVV 306
|
330 340
....*....|....*....|....*...
gi 2784223663 525 LDRDPLSVPPAGLADLQVRSTWVDGAPV 552
Cdd:pfam01979 307 VDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
376-557 |
3.48e-06 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 49.46 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 376 LGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQPThatsdmgwaqdrvgPERIL--GAYAWRRMLASGARLALGSD 453
Cdd:PRK09229 257 LLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPT--------------TEANLgdGIFPAVDYLAAGGRFGIGSD 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 454 FPVEqVDPRLGL----YAA--VTRQDRAGQPPGGWQPDQRLTAAeALRGFTADAAWAghdeaqVGRLQPGLRADFVVLDR 527
Cdd:PRK09229 323 SHVS-IDLVEELrlleYGQrlRDRRRNVLAAAAQPSVGRRLFDA-ALAGGAQALGRA------IGGLAVGARADLVVLDL 394
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2784223663 528 DPLS---VPPAGLAD--------LQVRSTWVDGAPVYEAAR 557
Cdd:PRK09229 395 DHPAlagREGDALLDrwvfaggdAAVRDVWVAGRWVVRDGR 435
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
218-502 |
1.03e-05 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 47.33 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 218 AAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSRADlalmrrfadaGKLPLRIDAYADGNGDA--LADICAQGAYQH 295
Cdd:cd01292 23 KEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP----------TTTKAAIEAVAEAARASagIRVVLGLGIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 296 AGGRLEMRGV----KLFMDGALGSRGAALLADYSDDPHNrgllvtsPDDFETAVRKADTCHVQVATHAIGDRGNRIALDT 371
Cdd:cd01292 93 PAAVDEDAEAllleLLRRGLELGAVGLKLAGPYTATGLS-------DESLRRVLEEARKLGLPVVIHAGELPDPTRALED 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 372 YQKVLGErratDHRWRIEHAQVVALEDIPRFAQLGVIASMQPTHATSDMGWAQDRvgperilgaYAWRRMLASGARLALG 451
Cdd:cd01292 166 LVALLRL----GGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDGEGA---------EALRRLLELGIRVTLG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2784223663 452 SDFPVEQVDPRLGLYAAVTRQDRAGQppggwqpdqrLTAAEALRGFTADAA 502
Cdd:cd01292 233 TDGPPHPLGTDLLALLRLLLKVLRLG----------LSLEEALRLATINPA 273
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
441-553 |
1.33e-05 |
|
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: 47.31 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 441 MLASGARLALGSDFPVEQVDpRLGLYAAVTRqdRAGqppggwqpdqrLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRA 520
Cdd:cd01309 267 LKKGGVAFAISSDHPVLNIR-NLNLEAAKAV--KYG-----------LSYEEALKAITINPAKILGIEDRVGSLEPGKDA 332
|
90 100 110
....*....|....*....|....*....|...
gi 2784223663 521 DFVVLDRDPLSVppaglaDLQVRSTWVDGAPVY 553
Cdd:cd01309 333 DLVVWNGDPLEP------TSKPEQVYIDGRLVY 359
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
486-554 |
7.97e-05 |
|
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: 45.37 E-value: 7.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784223663 486 QRLTAAEALRGFTAD-AAWAGHDEAqvGRLQPGLRADFVVLDRDPLSVPPAGLADLQ----VRSTWVDGAPVYE 554
Cdd:cd01297 333 KLLSLEEAVRKMTGLpARVFGLADR--GRIAPGYRADIVVFDPDTLADRATFTRPNQpaegIEAVLVNGVPVVR 404
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
337-554 |
1.97e-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: 44.12 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 337 SPDDFETAVRKADTCHVQVATH-AIGDRGNRIALDTYQK----VLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASM 411
Cdd:cd01298 192 SDELLREVAELAREYGVPLHIHlAETEDEVEESLEKYGKrpveYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAH 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 412 QPThatSDMGWAqdrVGPERIlgayawRRMLASGARLALGSDFP--------VEQVdpRLglyAAVTRQDRAGQPPGgwq 483
Cdd:cd01298 272 NPA---SNMKLA---SGIAPV------PEMLEAGVNVGLGTDGAasnnnldmFEEM--RL---AALLQKLAHGDPTA--- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 484 pdqrLTAAEALRGFTADAAWA-GHDEaqVGRLQPGLRADFVVLD-RDPLSVPPAGLADL--------QVRSTWVDGAPVY 553
Cdd:cd01298 332 ----LPAEEALEMATIGGAKAlGLDE--IGSLEVGKKADLILIDlDGPHLLPVHDPISHlvysanggDVDTVIVNGRVVM 405
|
.
gi 2784223663 554 E 554
Cdd:cd01298 406 E 406
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
376-549 |
2.06e-04 |
|
Metallo-dependent hydrolases, subgroup D 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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 43.98 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 376 LGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQPThatsdmgwaqdrvgPERIL--GAYAWRRMLASGARLALGSD 453
Cdd:cd01313 248 LLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPT--------------TEANLgdGIFPAAALLAAGGRIGIGSD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 454 FPVeQVDPRLGLYAAVTRQDRAGQPPGGWQPDQRLTAAEALRGFTADAAWAGhdEAQVGRLQPGLRADFVVLDRDPLSVP 533
Cdd:cd01313 314 SNA-RIDLLEELRQLEYSQRLRDRARNVLATAGGSSARALLDAALAGGAQAL--GLATGALEAGARADLLSLDLDHPSLA 390
|
170 180
....*....|....*....|....*..
gi 2784223663 534 ---PAGLAD--------LQVRSTWVDG 549
Cdd:cd01313 391 galPDTLLDawvfaagdREVRDVVVGG 417
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
486-556 |
2.18e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 43.64 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 486 QRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDrdplsvPPAG------------LADL-----------QV 542
Cdd:PRK09228 346 YRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLD------PAATpllalrtaraesLEELlfalmtlgddrAV 419
|
90
....*....|....
gi 2784223663 543 RSTWVDGAPVYEAA 556
Cdd:PRK09228 420 AETYVAGRPVYRRL 433
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
50-113 |
2.19e-04 |
|
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: 43.79 E-value: 2.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784223663 50 GRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGTL--MQADLTGATSSrDIVAR 113
Cdd:cd01296 6 GRIAAVGPAASLPAPGPAAAEEiDAGGRAVTPGLVDCHTHLVFAGDRVdeFAARLAGASYE-EILAA 71
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
488-549 |
2.39e-04 |
|
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: 43.72 E-value: 2.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784223663 488 LTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRdplsvppaglaDLQVRSTWVDG 549
Cdd:cd00854 324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDD-----------DLNVKATWING 374
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
488-549 |
1.08e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 41.62 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784223663 488 LTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRdplsvppaglaDLQVRSTWVDG 549
Cdd:COG1820 322 LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDD-----------DLNVRATWVGG 372
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
439-526 |
1.13e-03 |
|
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: 41.47 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 439 RRMLASGARLALGSDF-PVEQVDPRLGLYA--AVTrqdragqppggwqpDQRLTAAEALRGFTADAAWAGHDEAQVGRLQ 515
Cdd:cd01296 272 RKLIDAGVPVALGTDFnPGSSPTSSMPLVMhlACR--------------LMRMTPEEALTAATINAAAALGLGETVGSLE 337
|
90
....*....|.
gi 2784223663 516 PGLRADFVVLD 526
Cdd:cd01296 338 VGKQADLVILD 348
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
512-556 |
2.74e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.16 E-value: 2.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2784223663 512 GRLQPGLRADFVVLDRDPlSVPpagladlQVRSTWVDGAPVYEAA 556
Cdd:PRK15446 347 GEIAPGKRADLVRVRRAG-GLP-------VVRAVWRGGRRVFLAG 383
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
440-552 |
3.47e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 39.99 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 440 RMLASGARLALGSDfpVEQVDP-------RLGLYAAVTRQDRAGQPPGGWQPDQ-RLTAAEALRGFTADAAWAGHDEAQV 511
Cdd:PRK08204 288 RLLAHGVRPSLGVD--VVTSTGgdmftqmRFALQAERARDNAVHLREGGMPPPRlTLTARQVLEWATIEGARALGLEDRI 365
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2784223663 512 GRLQPGLRADFVVLDRDPLSVPP-----------AGLADlqVRSTWVDGAPV 552
Cdd:PRK08204 366 GSLTPGKQADLVLIDATDLNLAPvhdpvgavvqsAHPGN--VDSVMVAGRAV 415
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
20-88 |
3.91e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 39.79 E-value: 3.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784223663 20 ADVRMLTAATIH-TGDPDAPAAT-ALAWDTD------TGRVLAVGDRQAMLTLYP-LAALTDVGQATVIPGLIDAHAH 88
Cdd:PRK09228 1 MTTKAYRGRLLHfTADPAEVDDEdALRYIEDglllveDGRIVAAGPYAELRAQLPaDAEVTDYRGKLILPGFIDTHIH 78
|
|
|