|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
10-1223 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 1729.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 10 RSLFVVEHKTPFTDEEIKRLNWLfgLKEG-TLPQPSVEGIFVGPRSEMISPWSTNAVEIAENMGLKGISRIEE------- 81
Cdd:PRK05297 35 EYVHFADLSAPLSAEEQAKLERL--LTYGpAEHEPAGRLFLVTPRPGTISPWSSKATDIAHNCGLAGIRRIERgiayyve 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 82 --LKEKE----ATTEHDPMLEMVYTHPD-ANIFTHEYEVEPIHYIEDI-------DAYNKSEGLALSPEEVSFLQKLSER 147
Cdd:PRK05297 113 aaLSAEQraalAALLHDRMTESVFADLDdAEALFSHHEPKPLTSVDVLgggraalEAANVELGLALAEDEIDYLVEAFTK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 148 LGRKLTDSELFGFSQVNSEHCRHKIFNGTFIIDGKEQEASLFSMIKSTSEENPNGLVSAYKDNVAFVEGGRAEQFAPISA 227
Cdd:PRK05297 193 LGRNPTDVELMMFAQANSEHCRHKIFNADWTIDGEEQPKSLFKMIKNTHETNPDGVLSAYKDNAAVMEGSKVGRFFPDPD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 228 DKadFYTTQPIDTVLSLKAETHNFPTTVEPFNGAATGTGGEIRDRMAGGKASIPVAGTAVYMTSYPRLKG-----ESKTL 302
Cdd:PRK05297 273 TG--RYGYHQEPAHILMKVETHNHPTAISPFPGAATGSGGEIRDEGATGRGSKPKAGLTGFSVSNLRIPGfeqpwEEDYG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 303 MEARkwlYQHPQAILTKASNGASDFGNKFGQPIITGSLLTFEHQENE-RATRYGFDKVIMLAGGIGYARAQDAIKEEPQP 381
Cdd:PRK05297 351 KPER---IASALDIMIEGPLGGAAFNNEFGRPNLLGYFRTFEQKVNShNEEVRGYHKPIMLAGGIGNIRADHVQKGEIPV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 382 DQLVVMMGGDNYRIGMGGGAVSSVNTGQYSSGIELNAVQRANPEMQKRVCNVVRALAE-GEDNPIISIHDHGAGGHLNCL 460
Cdd:PRK05297 428 GAKLIVLGGPAMRIGLGGGAASSMASGQSSEDLDFASVQRGNPEMERRCQEVIDRCWQlGDDNPILSIHDVGAGGLSNAF 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 461 TELIEAT--GGVIDIDALPVGDKSLSAKEIIGNESQERMGMLIREKDFDRIAAIAERERAPIYKVGHTTNSKELVFK-RD 537
Cdd:PRK05297 508 PELVNDGgrGGRFDLRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELFEAICERERCPFAVVGEATEERHLTLEdSH 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 538 NGEEAIHLAVEDMLAKPPRTIMNDKSVVHHYEDAPYEATQPLQYLEGVLSLEAVACKDWLTNKVDRSVTGRIARQQCCGE 617
Cdd:PRK05297 588 FDNKPVDLPLDVLLGKPPKMHRDVKTVKAKGPALDYSGIDLAEAVERVLRLPTVASKSFLITIGDRSVTGLVARDQMVGP 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 618 LQLPLSDLGAIALDYRGRKGYATSIGHAPQAGLIDSATGSVLAIAEALTNIVFAPLEKgLESVSLSANWMWPCRNEGEDA 697
Cdd:PRK05297 668 WQVPVADCAVTAASYDGYAGEAMAMGERTPVALLDAAASARMAVGEALTNIAAAPIGD-LKRIKLSANWMAAAGHPGEDA 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 698 RLYRAVEACA-QFAIDLGINIPTGKDSLSMTQKYPD---DKPVVSPGTVIISAAAPVSNVRGIITPVIKSAQESHLLYID 773
Cdd:PRK05297 747 RLYDAVKAVGmELCPALGITIPVGKDSLSMKTKWQEggeDKEVTSPLSLIISAFAPVEDVRKTLTPQLRTDKDTALLLID 826
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 774 FSFAPLNLGGSALFQSLGKVGVQAPTIGNADYFADAFEAVQTLISKGLVLAGHDISAGGLITTLLEMCFANvSGGLTIDL 853
Cdd:PRK05297 827 LGRGKNRLGGSALAQVYNQLGDKAPDVDDAEDLKGFFNAIQALVAEGLLLAYHDRSDGGLLTTLAEMAFAG-HCGLDIDL 905
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 854 TAIPEkDLTKLLYAENPGVVLQVK--DFSTVAAILEEAGVG--YALIGTPSATRSIEITKEGEK-LSIDIDKARRTWYEP 928
Cdd:PRK05297 906 DALGD-DALAALFNEELGAVIQVRaaDRDAVEAILAEHGLSdcVHVIGKPNAGDRIVITRNGKTvFSESRTELRRWWSET 984
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 929 SYLLDRFQSTEKLAKERFDNFAHQPiqlrfAPSFDGKLsTLNLNPDR-----KERSGIVAAVVRDKGTNGEREMAYALYL 1003
Cdd:PRK05297 985 SYQMQRLRDNPECADQEFDAILDQA-----DPGLNVKL-TFDPNEDIaapfiATGARPKVAILREQGVNSHVEMAAAFDR 1058
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1004 AGFDVKDVHLTDLTSGRETLEDAQMLVFCGGFSNSDVLGSAKGWAAGILFNERAKAAIDAFYARPDTLSLGICNGCQLMA 1083
Cdd:PRK05297 1059 AGFDAIDVHMSDLLAGRVTLEDFKGLVACGGFSYGDVLGAGEGWAKSILFNPRLRDQFEAFFARPDTFALGVCNGCQMMS 1138
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1084 ELGLIYEDKKPRHRMEHNRSHKYESCFVGLTIPENNTVMLSSLAGSQLGVWCAHGEGRFS-----MDESLDQYNVVARY- 1157
Cdd:PRK05297 1139 NLKEIIPGAEHWPRFVRNRSEQFEARFSLVEVQESPSIFLQGMAGSRLPIAVAHGEGRAEfpdahLAALEAKGLVALRYv 1218
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154824145 1158 -----TYDDYPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFPWQCGFYPEMQHEVTPWIEAFRNAYDWL 1223
Cdd:PRK05297 1219 dnhgqVTETYPANPNGSPNGITGLTTADGRVTIMMPHPERVFRTVQNSWHPEEWGEDSPWMRMFRNARKWV 1289
|
|
| FGAM_synt |
TIGR01735 |
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ... |
6-1223 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This form is found mostly in eukaryotes and Proteobacteria. In Bacillus subtilis PurL (FGAM synthase II) and PurQ (FGAM synthase I), homologous to different parts of this model, perform the equivalent function; the unrelated small protein PurS is also required and may be a third subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 188163 [Multi-domain] Cd Length: 1310 Bit Score: 1104.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 6 LSSERSLFV-VEHKTPFTDEEIKRLNWLFGLKEGTLPQPSVEGIF-VGPRSEMISPWSTNAVEIAENMGLKGISRIE--- 80
Cdd:TIGR01735 30 VYAEFCYFVgWESALTADEEEKLQLLLLAGSVLEPPQSPLGRGLLeVGPRLGTISPWSSKATSIARNCGLAKVDRIErgr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 81 --------ELKEKE----ATTEHDPMLEMVYTHPD--ANIFTHEyEVEPIHYIEDIDA-------YNKSEGLALSPEEVS 139
Cdd:TIGR01735 110 ryylsgahPLSEEQeaqaAALLHDRMTESVLPHEIeaFELFSVP-EPLNLTTIDVLGGgrlalekANQELGLALDEDEID 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 140 FLQKLSERLGRKLTDSELFGFSQVNSEHCRHKIFNGTFIIDGKEQEASLFSMIKSTSEENPNGLVSAYKDNVAFVEGGRA 219
Cdd:TIGR01735 189 YLTKRFQELQRNPSDVELMMFAQANSEHCRHKIFNADWIIDGKKQDKSLFQMIKSTHEANPENTVSAYKDNSSVIEGHKV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 220 EQFAPISADKADFYTTQPIDTVLSLKAETHNFPTTVEPFNGAATGTGGEIRDRMAGGKASIPVAGTAVYMTSYPRLKGES 299
Cdd:TIGR01735 269 GRLRPDPPTRPEYRQHQEDLVHILMKVETHNHPTAIAPFPGASTGAGGEIRDEGATGRGAKPKAGLTGFCVSNLNIPGLE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 300 KtlmearKW--LYQHPQ------AILTKASNGASDFGNKFGQPIITGSLLTFEHQENERAT-RYGFDKVIMLAGGIGYAR 370
Cdd:TIGR01735 349 Q------PWedPFQKPEriasplDIMIEAPLGAAAFNNEFGRPNLLGYFRTFELKASLPGGqVRGYHKPIMLAGGIGSID 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 371 AQDAIKEEPQPDQLVVMMGGDNYRIGMGGGAVSSVNTGQYSSGIELNAVQRANPEMQKRVCNVVRALAE-GEDNPIISIH 449
Cdd:TIGR01735 423 AEHIQKGEIEPGALLIVLGGPAMLIGLGGGAASSMVSGTNTADLDFASVQRGNPEMERRCQEVIDRCWQlGEKNPIISIH 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 450 DHGAGGHLNCLTELIE--ATGGVIDIDALPVGDKSLSAKEIIGNESQERMGMLIREKDFDRIAAIAERERAPIYKVGHTT 527
Cdd:TIGR01735 503 DVGAGGLSNALPELIHdgGRGAVIDLRAVPLDDPGLSPLEIWCNESQERYVLLVRAENLEIFTAICERERCPFAVVGTAT 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 528 NSKELVF-----KRDNGEE---------AIHLAVEDMLAKPPRTIMNDKSVVhhYEDAPYEATQPL---QYLEGVLSLEA 590
Cdd:TIGR01735 583 GDGRLTLvddtpVRRNGQGdapshfpnnPVDLPLEVLLGKMPKMTRFVQRKA--PMLQPLDIPPGLdlhEALERVLRLPA 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 591 VACKDWLTNKVDRSVTGRIARQQCCGELQLPLSDLGAIALDYRGRKGYATSIGHAPQAGLIDSATGSVLAIAEALTNIVF 670
Cdd:TIGR01735 661 VASKRFLITIGDRSVGGLVARDQMVGPWQTPLADVAVTAASFDTYTGEAMAIGERPPKALLDPKASARLAVGEAITNLAA 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 671 APLEKgLESVSLSANWMWPCRNEGEDARLYRAVEACAQFAIDLGINIPTGKDSLSMTQKYPDD---KPVVSPGTVIISAA 747
Cdd:TIGR01735 741 ALVGD-LSDVKLSANWMAAAGHPGEDAALYDAVKAVSELCPALGIAIPVGKDSLSMKTRWQDNgetKSVTAPGSLVISAF 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 748 APVSNVRGIITPVIKSAQ-ESHLLYIDFSFAPLNLGGSALFQSLGKVGVQAPTIGNADYFADAFEAVQTLISKGLVLAGH 826
Cdd:TIGR01735 820 APVPDVRKTVTPDLKHDKgDSHLLLVDLGPGKNRLGGSALAQVFGQLGGDCPDLDDPERLKAFFAVMQGLVAEGLLLAYH 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 827 DISAGGLITTLLEMCFANvSGGLTIDLTAiPEKDLTKLLYAENPGVVLQVK--DFSTVAAILEEAGV-GYAL-IGTPSAT 902
Cdd:TIGR01735 900 DRSDGGLVTTLLEMAFAG-HCGLDVDLDA-LGDSLFAVLFNEELGAVIQVAkpDLAAVLELLRAAGLtALILgIGTPTGH 977
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 903 RSIEITKEGEKL-SIDIDKARRTWYEPSYLLDRFQSTEKLAKERFD--NFAHQP---IQLRFAPSFDGKLSTLNLNPDRK 976
Cdd:TIGR01735 978 PMIRISVNGATLlSEKRSELRDIWEETSFQLQRLRDNPECAEEEFEglRDRDGPglkLPLTFDVNEDIAAPFINKGVKPK 1057
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 977 ersgivAAVVRDKGTNGEREMAYALYLAGFDVKDVHLTDLTSGRETLEDAQMLVFCGGFSNSDVLGSAKGWAAGILFNER 1056
Cdd:TIGR01735 1058 ------VAILREQGVNGDREMAAAFDRAGFEAWDVHMSDLLAGRVHLDEFRGLAACGGFSYGDVLGAGKGWAKSILFNPR 1131
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1057 AKAAIDAFYARPDTLSLGICNGCQLMAELGLIYEDKKPRHRMEHNRSHKYESCFVGLTIPENNTVMLSSLAGSQLGVWCA 1136
Cdd:TIGR01735 1132 LRDQFQAFFKRPDTFSLGVCNGCQMLSNLLEWIPGTENWPHFVRNNSERFEARVASVRVGESPSIMLRGMAGSRLPVAVA 1211
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1137 HGEGR--FSMDESLDQYN----VVARYTYDD------YPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFPWQCGFYPE 1204
Cdd:TIGR01735 1212 HGEGYaaFSSPELQAQADasglAALRYIDDDgnpteaYPLNPNGSPGGIAGITSCDGRVTIMMPHPERVFRAWQNSWRPE 1291
|
1290
....*....|....*....
gi 1154824145 1205 MQHEVTPWIEAFRNAYDWL 1223
Cdd:TIGR01735 1292 DWDEDTPWLRLFRNARNWL 1310
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
13-1222 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 1006.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 13 FVVEHKTPFTDEEIKRLNWL----------------FGLKEGTLPQPSVEgifVGPRSEMISPWSTNAVEIAENMGLKGI 76
Cdd:PLN03206 24 FNVGLESPLSAEKLETLKWLlretfepenlgtesflEAKKSEGLNAVVVE---VGPRLSFTTAWSTNAVSICSACGLTEV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 77 SRIEE-----LKEKEATTE----------HDPMLEMVYTHPDANiFTHEYEVEPIHYI-------EDIDAYNKSEGLALS 134
Cdd:PLN03206 101 TRLERsrrylLFSSSPLDEsqinafaamvHDRMTECVYPQPLTS-FESGVVPEPVYTVpvmeegrAALEEINKEMGLAFD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 135 PEEVSFLQKL-SERLGRKLTDSELFGFSQVNSEHCRHKIFNGTFIIDGKEQEASLFSMIKSTSEENPNGLVSAYKDNVAF 213
Cdd:PLN03206 180 EQDLDYYTRLfRDDIKRDPTNVELFDIAQSNSEHSRHWFFSGKLVIDGQPMPKTLFQMVKDTLKANPNNSVIGFKDNSSA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 214 VEGGRAEQFAPISADKADFYTTQPIDTVLSLKAETHNFPTTVEPFNGAATGTGGEIRDRMAGGKASIPVAGTAVYMTSYP 293
Cdd:PLN03206 260 IRGFVVQPLRPVSPGSPSPLAPVDRDLDILLTAETHNFPCAVAPYPGAETGAGGRIRDTHATGRGSFVVAGTAGYCVGNL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 294 RLKGeSKTLMEARKWLY----QHPQAILTKASNGASDFGNKFGQPIITGSLLTFeHQENERATRYGFDKVIMLAGGIGYA 369
Cdd:PLN03206 340 RIEG-SYAPWEDSSFVYpsnlASPLQILIDASNGASDYGNKFGEPLIQGYTRTF-GMRLPNGERREWLKPIMFSGGIGQI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 370 RAQDAIKEEPQPDQLVVMMGGDNYRIGMGGGAVSSVNTGQYSSGIELNAVQRANPEMQKRVCNVVRALAE-GEDNPIISI 448
Cdd:PLN03206 418 DHTHLTKGEPDIGMLVVKIGGPAYRIGMGGGAASSMVSGQNDAELDFNAVQRGDAEMSQKLYRVVRACVEmGEDNPIVSI 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 449 HDHGAGGHLNCLTELIEATGGVIDIDALPVGDKSLSAKEIIGNESQERMGMLIREKDFDRIAAIAERERAPIYKVGHTTN 528
Cdd:PLN03206 498 HDQGAGGNCNVVKEIIYPKGAEIDIRAVVVGDHTLSVLEIWGAEYQEQDALLIKPESRDLLQSICDRERCSMAVIGTIDG 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 529 SKELVFKRDNGEE------------AIHLAVEDMLAKPPRTIMNDKSVVHHYE--DAPYEATQpLQYLEGVLSLEAVACK 594
Cdd:PLN03206 578 SGRVVLVDSAAPEkceanglpppppAVDLDLEKVLGDMPQKTFEFKRVANKLEplDIPPGITV-MDALKRVLRLPSVCSK 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 595 DWLTNKVDRSVTGRIARQQCCGELQLPLSDLGAIALDYRGRKGYATSIGHAPQAGLIDSATGSVLAIAEALTNIVFAPLe 674
Cdd:PLN03206 657 RFLTTKVDRCVTGLVAQQQTVGPLQIPLADVAVIAQTHTGLTGGACAIGEQPIKGLVDPKAMARLAVGEALTNLVWAKV- 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 675 KGLESVSLSANWMWPCRNEGEDARLYRAVEACAQFAIDLGINIPTGKDSLSMTQKyPDDKPVVSPGTVIISAAAPVSNVR 754
Cdd:PLN03206 736 TALSDVKASGNWMYAAKLDGEGADMYDAAVALRDAMIELGVAIDGGKDSLSMAAQ-AGGEVVKAPGNLVISAYVTCPDIT 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 755 GIITPVIKSAQESHLLYIDFSFAPLNLGGSALFQSLGKVGVQAPTIGNADYFADAFEAVQTLISKGLVLAGHDISAGGLI 834
Cdd:PLN03206 815 KTVTPDLKLGDDGVLLHVDLGKGKRRLGGSALAQAYDQIGDDCPDLDDVAYLKKAFEATQDLIAKRLISAGHDISDGGLV 894
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 835 TTLLEMCFANvSGGLTIDLTAiPEKDLTKLLYAENPGVVLQV--KDFSTVAAILEEAGVGYALIGTPSATRSIEITKEGE 912
Cdd:PLN03206 895 VTLLEMAFAG-NCGINVDLPS-SGHSAFETLFAEELGLVLEVsrKNLDAVMEKLAAAGVTAEVIGQVTASPLIEVKVDGA 972
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 913 -KLSIDIDKARRTWYEPSYLLDRFQSTE---KLAKERFdNFAHQPI-QLRFAPSF-DGKLstlnLNPDRKERsgivAAVV 986
Cdd:PLN03206 973 tCLSEKTASLRDMWEETSFQLEKLQRLEscvAQEKEGL-KSRKAPTwKLSFTPAFtDKKI----MNATSKPK----VAII 1043
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 987 RDKGTNGEREMAYALYLAGFDVKDVHLTDLTSGRETLEDAQMLVFCGGFSNSDVLGSAKGWAAGILFNERAKAAIDAFYA 1066
Cdd:PLN03206 1044 REEGSNGDREMAAAFYAAGFEPWDVTMSDLLNGRISLDDFRGIVFVGGFSYADVLDSAKGWAGSIRFNEPLLQQFQEFYN 1123
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1067 RPDTLSLGICNGCQLMAELGLI------------YEDKKPrhRMEHNRSHKYESCFVGLTIPENNTVMLSSLAGSQLGVW 1134
Cdd:PLN03206 1124 RPDTFSLGVCNGCQLMALLGWVpgpqvggglgagGDPSQP--RFVHNESGRFECRFTSVTIEDSPAIMLKGMEGSTLGVW 1201
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1135 CAHGEGRFS------MDESLDQYNVVARYTYDD------YPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFPWQCGFY 1202
Cdd:PLN03206 1202 AAHGEGRAYfpdesvLDEVLKSNLAPVRYCDDDgepteqYPFNPNGSPLGIAALCSPDGRHLAMMPHPERCFLMWQFPWY 1281
|
1290 1300
....*....|....*....|....
gi 1154824145 1203 PEMQH----EVTPWIEAFRNAYDW 1222
Cdd:PLN03206 1282 PKEWGvdpaGPSPWLKMFQNAREW 1305
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
111-937 |
0e+00 |
|
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439816 [Multi-domain] Cd Length: 747 Bit Score: 796.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 111 YEVEPIHYIEDIDAYNKSEGLALSPEEVsflQKLSERLGRKLTDSELFGFSQVNSEHCRHKIFNGTFiidgkeqeaslfs 190
Cdd:COG0046 2 STVDLEGGREALEEANRELGLALSDDEY---DYIVEILGRNPTDVELGMFSQMWSEHCSYKSSNALL------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 191 miKSTSEENPnGLVSAYKDNVAFVEGGraeqfapisadkadfyttqpIDTVLSLKAETHNFPTTVEPFNGAATGTGGEIR 270
Cdd:COG0046 66 --KSLPTEGP-RVLSGPGDNAGVVDIG--------------------DGLAVVFKVESHNHPSAIEPYQGAATGVGGIIR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 271 DRMagGKASIPVAGTAVYMTSYPRLKGesktlmearkwlyQHPQAILTKASNGASDFGNKFGQPIITGSLLTFEHQEner 350
Cdd:COG0046 123 DIF--GMGARPIAGLDSLRFGNLDQPP-------------ASPRYILIGVVAGIADYGNCFGVPTVGGEVRFDESYE--- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 351 atrygfDKVIMLAGGIGYARAQDAIK-EEPQPDQLVVMMGGDNYRIGMGGGAVSSVNTGQYSSgIELNAVQRANPEMQKR 429
Cdd:COG0046 185 ------GNPLVNAGGVGIIRADHIFKaKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDSE-LDRPAVQVGDPFMEKR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 430 VCNVVRALaeGEDNPIISIHDHGAGGHLNCLTELIEAT--GGVIDIDALPVGDKSLSAKEIIGNESQERMGMLIREKDFD 507
Cdd:COG0046 258 LIEAILEL--GDTGLIVGIQDMGAGGLSSASSEMAAKGglGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPEKLE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 508 RIAAIAERERAPIYKVGHTTNSKELVFkRDNGEEAIHLAVEDMLAKPPRTIMNDKSVVHHYEDAPYEATQPLQYLEGVLS 587
Cdd:COG0046 336 EFEAIFERWRLPAAVIGEVTDDGRLVV-TDHGETVADLPLDFLAGGAPKYHRPAKRPAYLEPLDLPEPIDLEEALLRLLS 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 588 LEAVACKDWLTNKVDRSVTGRIARQQccgelqlPLSDLGAIALDyRGRKGYATSIGHAPQAGLIDSATGSVLAIAEALTN 667
Cdd:COG0046 415 SPNVASKEWLYRQYDREVGGNTVRDP-------GVADAAVVRVD-GTYKGLAMSTGENPRYALLDPYAGARMAVAEAARN 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 668 IVFAPLEKglESVSLSANWMWPCrNEGEDARLYRAVEACAQFAIDLGINIPTGKDSLSMTQKypdDKPVVSPGTVIISAA 747
Cdd:COG0046 487 LAAVGAEP--LAITDCLNWGNPE-KPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETK---DGKVAIPPTPVIGAV 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 748 APVSNVRGIITPVIKSAqESHLLYIdfSFAPLNLGGSALFQSLGKVGVQAPTIgNADYFADAFEAVQTLISKGLVLAGHD 827
Cdd:COG0046 561 GLVDDVRKTVTPDLKKE-GDLLYLI--GETKNELGGSEYAQVLGQLGGEPPDV-DLEAEKALFEAVQELIREGLILAAHD 636
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 828 ISAGGLITTLLEMCFANvSGGLTIDLTAIPEKDLTKLLYAENPG-VVLQVK--DFSTVAAILEEAGVGYALIGTPSATRS 904
Cdd:COG0046 637 VSDGGLAVALAEMAFAG-GLGADIDLDALGDLRPDAALFSESQGrAVVQVApeDAEAVEALLAEAGLPAHVIGTVTGDDR 715
|
810 820 830
....*....|....*....|....*....|....
gi 1154824145 905 IEITKEGEKL-SIDIDKARRTWYEPsylLDRFQS 937
Cdd:COG0046 716 LVIRRGGETLlSLSLAELRDAWEET---LPRLRD 746
|
|
| GATase_5 |
pfam13507 |
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
983-1223 |
5.52e-113 |
|
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not found in pfam00310, pfam07685 and pfam13230.
Pssm-ID: 463904 [Multi-domain] Cd Length: 260 Bit Score: 353.34 E-value: 5.52e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 983 AAVVRDKGTNGEREMAYALYLAGFDVKDVHLTDLTSGRETLEDAQMLVFCGGFSNSDVLGSAKGWAAGILFNERAKAAID 1062
Cdd:pfam13507 4 VAILREPGTNGEYEMAAAFERAGFDAVDVHMSDLLSGRVSLDDFQGLAAPGGFSYGDVLGSGKGWAASILFNPKLRDAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1063 AFYARPDTLSLGICNGCQLMAELGLI------YEDKKPrhRMEHNRSHKYESCFVGLTIPEN-NTVMLSSLAGSqlGVWC 1135
Cdd:pfam13507 84 AFFNRPDTFSLGICNGCQLLSKLGLIpggegdLAERWP--TLTRNDSGRFESRWVNVKISEKsPSVFLRGMDGS--GLPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1136 AHGEGRFS------MDESLDQYNVVARYTYD------DYPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFPWQCGFYP 1203
Cdd:pfam13507 160 AHGEGRFVfrseevLARLEANGQVALRYVDNagnpteEYPFNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWQWPHWP 239
|
250 260
....*....|....*....|.
gi 1154824145 1204 -EMQHEVTPWIEAFRNAYDWL 1223
Cdd:pfam13507 240 pGEWEEVSPWLRLFRNARKWV 260
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
156-545 |
7.93e-102 |
|
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100034 [Multi-domain] Cd Length: 313 Bit Score: 325.20 E-value: 7.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 156 ELFGFSQVNSEHCRHKIFNgtfiidgkeqeaSLFSMIkstseenpnglvsaykDNVAFveggraeqfapisadkadfytt 235
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFK------------SLLKMI----------------WAVVF---------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 236 qpidtvlslKAETHNFPTTVEPFNGAATGTGGEIRDRMAGGkaSIPVAGTAVYMTSYPRLKGESKTLMearkwlyQHPQA 315
Cdd:cd02203 31 ---------KVETHNHPSAIEPFGGAATGVGGIIRDILSMG--ARPIALLDGLRFGDLDIPGYEPKGK-------LSPRR 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 316 ILTKASNGASDFGNKFGQPIITGSLLTFEhqeneraTRYGfdKVIMLAGGIGYARAQDAIK-EEPQPDQLVVMMGGDNYR 394
Cdd:cd02203 93 ILDGVVAGISDYGNCIGIPTVGGEVRFDP-------SYYG--NPLVNVGCVGIVPKDHIVKsKAPGPGDLVVLVGGRTGR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 395 IGMGGGAVSSVNTGQYSSGIELNAVQRANPEMQKRVCNVVRALAEgeDNPIISIHDHGAGGHLNCLTELIEA--TGGVID 472
Cdd:cd02203 164 DGIGGATFSSKELSENSSELDRPAVQVGDPFMEKKLQEAILEARE--TGLIVGIQDLGAGGLSSAVSEMAAKggLGAEID 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154824145 473 IDALPVGDKSLSAKEIIGNESQERMGMLIREKDFDRIAAIAERERAPIYKVGHTTNSKELVFkRDNGEEAIHL 545
Cdd:cd02203 242 LDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVTDDGRLRL-YYKGEVVADL 313
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
983-1220 |
4.45e-92 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 295.68 E-value: 4.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 983 AAVVRDKGTNGEREMAYALYLAGFDVKDVHLTDLTSGRETLEDAQMLVFCGGFSNSDVLGSAKGWAAGILFNErakaAID 1062
Cdd:cd01740 1 VAVLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLLAGRKDLDDYDGVVLPGGFSYGDYLRAGAIAAASPLLME----EVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1063 AFyARPDTLSLGICNGCQLMAELGLIYEDKKPRHRMEHNRSHKYesCFVGLTIPENNTVMLSSL-AGSQLGVWCAHGEGR 1141
Cdd:cd01740 77 EF-AERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWQN--RFVTLRVENNDSPFTKGYmEGEVLRIPVAHGEGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1142 FSMD-ESLDQYNV---VARYTYDD------YPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFPWQCgfypEMQHEVTP 1211
Cdd:cd01740 154 FYADdETLAELEEngqIAQYVDDDgnvterYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPWQW----ERLLGGSD 229
|
....*....
gi 1154824145 1212 WIEAFRNAY 1220
Cdd:cd01740 230 GLKLFRNAV 238
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
379-1222 |
1.14e-84 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 302.33 E-value: 1.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 379 PQPDQLVVMMGgdNYRIGMGGGAVSSVNTgqySSGIELNAVQRAnpemqkrvCNVVRALAEGednPIIS--IHDHGAGGH 456
Cdd:PHA03366 372 YRPGQYIVALG--SFEPSSGPDTPPYLYR---DSGLEANKILQA--------LKLFYSLLPG---PCISgsSRPLGPASV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 457 LNCLTELIEATGGVIDIDALPvgDKSLSAKEIIGNESQERMGMLIREKDF------------------------DRIAAI 512
Cdd:PHA03366 436 LEHLLALCPPGGLLLFLSALP--EDVVSGLKPFSASNRETNEEIVKQYFLnvycsvvflvikntheggegvtplDALKRA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 513 AERERAPIYKVGHTTNSKELVFKRDNGE---EAIHLAveDMLAKPPRTIMNDKSVVHHYEDAPYEATQP---------LQ 580
Cdd:PHA03366 514 CRLAGCPVHILGRTVPLPGIHFVNDLGNpvyGELRDD--QFKPTFPLQPSRPLSPVSATSEDTRPSPQDesidwalfnLN 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 581 Y-LEGVLSLEAVACKDWLTNKVDRSVTGRIARQQCCGELQLPLSDLGAIALDYrgrkgYATSIGHAPQAGLID------- 652
Cdd:PHA03366 592 StLLQILSHPTVGSKEYIVRHIDRCGNGRVAQQPGVGPLDLPVSDYSIVVHSS-----VKTRRAIETPSSTEDltyqead 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 653 --------------------------SA-------------TGSVLAIAEALTNIVFAPLEKgLESVSLSANWMWPcrnE 693
Cdd:PHA03366 667 elinspltwfdpddesvlhpavpgtcSAlgeqgykvqldpiLGAKYAIVEALTNLMLAPVAN-LEDITITLSVTWP---P 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 694 GEDAR--LYRAVEACAQFAIDLGINIPTGK--DSLSMTQKYPDDKPVvspGTVIISAAAPVSNVRGIITPVIKSAqESHL 769
Cdd:PHA03366 743 TDQAAseLYRALAACKEFCRELGVNFTFTSasSSPRQDQPPQPGPLF---NTIVFTASAPVPSSTPRLTPDLKKP-GSAL 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 770 LYIDFSfAPLNLGGSaLFQSLGKVGVQAPTIGNADYFADAFEAVQTLISKGLVLAGHDISAGGLITTLLEMCFAnvsGGL 849
Cdd:PHA03366 819 VHLSIS-PEYTLAGS-VFEQIFGLKSGTLPDISPSYLKNLFRAVQHLISEGLVVSGHDVSDGGLIACLAEMALA---GGR 893
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 850 TIDLTAIPEKDLTKLLYAENPGVVLQV--KDFSTVAAILEEAGVGYALIGT-----PSATrsIEITKEGEKL-SIDIDKA 921
Cdd:PHA03366 894 GVTITVPAGEDPLQFLFSETPGVVIEVppSHLSAVLTRLRSRNIICYPIGTvgpsgPSNT--FSVSHNGTVLfRESLSSL 971
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 922 RRTW----------YEPSYLLDRFQSTEKLAKErfDNFAHQPIQLRFAPsfdgklSTLNLNPDRKERsgiVAAVVRdKGT 991
Cdd:PHA03366 972 RSTWrsfsdeqfelLRPDLTEESMYRKDYGNNE--VDLGPLEEGLTTSP------LRLYTCPDKRHR---VAVLLL-PGC 1039
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 992 NGEREMAYALYLAGFDVKDVHLTDLTSGrETLEDAQMLVFCGGFSNSDVLGSAKGWAAGILFNERAKAAIDAFYARPDTL 1071
Cdd:PHA03366 1040 PGPHALLAAFTNAGFDPYPVSIEELKDG-TFLDEFSGLVIGGSSGAEDSYTGARAAVAALLSNPAVRDALLRFLNRPDTF 1118
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1072 SLGICN-GCQLMAELGLIYEDKKPRH-----------RMEHNRSHKYESCFVGLTIPEN-NTVMLSSLAGSQLGVWcAHG 1138
Cdd:PHA03366 1119 SLGCGElGCQILFALKAVGSTAPSPVpgteteeqwpiTLEPNASGLYESRWLNFYIPETtKSVALRPLRGSVLPCW-AQG 1197
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1139 E--G-RF---SMDESLDQYNVVARYTYD----------DYPANPNG-SPegIAAVASRDGRHLAMMPHPERSIFPWQCGF 1201
Cdd:PHA03366 1198 ThlGfRYpndGMEYILRNSGQIAATFHGadvdpgnparHYPRNPTGnSN--VAGLCSADGRHLALLFDPSLSFHPWQWQH 1275
|
970 980
....*....|....*....|...
gi 1154824145 1202 YPEMQHE--VTPWIEAFRNAYDW 1222
Cdd:PHA03366 1276 VPPENGPlkVSPWKLMFQDLHLW 1298
|
|
| PurL2 |
COG0047 |
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
983-1224 |
5.20e-71 |
|
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439817 [Multi-domain] Cd Length: 236 Bit Score: 236.88 E-value: 5.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 983 AAVVRDKGTNGEREMAYALYLAGFDVKDVHLTDLtsgRETLEDAQMLVFCGGFSNSDVLGSAKGWAAgilfnERAKAAID 1062
Cdd:COG0047 3 VAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDL---RTDLDDFDGLVLPGGFSYGDYLRAGAIAAF-----SPIMDAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1063 AFyARPDTLSLGICNGCQLMAELGLIyedkkPRH--RMEHNRSHKYESCFVGLTIPENNTVMLSSL-AGSQLGVWCAHGE 1139
Cdd:COG0047 75 EF-ARRGGLVLGICNGFQILTELGLL-----PGIwpALTRNRSLRFICRWVYLRVENNDSPFTSGMeAGEVIPIPIAHGE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1140 GRFSMDES-LDQYN----VVARYTYDD----YPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFPWQCgfypemQHEVT 1210
Cdd:COG0047 149 GRYVADEEtLAELEangqVAFRYVDADgnvtYPANPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLG------PGEST 222
|
250
....*....|....
gi 1154824145 1211 PWIEAFRNAYDWLK 1224
Cdd:COG0047 223 DGLRIFRSAVKYFG 236
|
|
| FGAM-synthase |
TIGR01857 |
phosphoribosylformylglycinamidine synthase, clade II; This model represents a single-molecule ... |
120-1193 |
1.34e-65 |
|
phosphoribosylformylglycinamidine synthase, clade II; This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This model represents a second clade of these enzymes found in Clostridia, Bifidobacteria and Streptococcus species. This enzyme performs the fourth step in IMP biosynthesis (the precursor of all purines) from PRPP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 130916 [Multi-domain] Cd Length: 1239 Bit Score: 243.59 E-value: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 120 EDIDAYNKSEGLALSPEEVSFLQKLSERLGRKLTDSELFGFSQVNSEHCRHKIFnGTFIIDGKEQEASLFSMIKSTSEEN 199
Cdd:TIGR01857 174 EDLAKFKAEQGLAMSLEDLKFIQDYFKSIGRNPTETEIKVLDTYWSDHCRHTTF-ETELKHVTFSDSKFQKQLKKAYEDY 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 200 PNGLVSAYKDN--VAFVE----GGRAEQ-------------------FAPISADKADFyttqpiDTVLSLKAETHNFPTT 254
Cdd:TIGR01857 253 LAMREELGRSEkpVTLMDmatiFAKYLRkngklddlevseeinacsvEIEVDVDGVKE------PWLLMFKNETHNHPTE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 255 VEPFNGAATGTGGEIRDrmaggkasiPVAGTAvYMTSYPRLKGE---SKTLMEARKW-LYQhpQAILTKASNGASDFGNK 330
Cdd:TIGR01857 327 IEPFGGAATCIGGAIRD---------PLSGRS-YVYQAMRVTGAgdpTVPISETLKGkLPQ--RKITTTAAHGYSSYGNQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 331 FGqpIITGSLLTFEHqENERATRygfdkviMLAGG-IGYARAQDAIKEEPQPDQLVVMMGGDNYRIGMGGGAVSSVNTGQ 409
Cdd:TIGR01857 395 IG--LATGQVSEIYH-PGYVAKR-------MEVGAvVAATPKENVVREKPEPGDVIILLGGKTGRDGIGGATGSSKEHTV 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 410 YSSGIELNAVQRAN-PEMQKrvcnVVRALAEGEDNPIIS-IHDHGAGGHLNCLTELieATGGVIDIDALPVGDKSLSAKE 487
Cdd:TIGR01857 465 ESLELCGAEVQKGNaPEERK----IQRLFRNGNVTRLIKkCNDFGAGGVSVAIGEL--ADGLEIDLNKVPKKYEGLNGTE 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 488 IIGNESQERMGMLIREKDFDRIAAIAERERAPIYKVGHTTNSKELVFKRdNGEEAIHLAvEDMLAKPPRTIMNDKSVVHH 567
Cdd:TIGR01857 539 LAISESQERMAVVVSPEDVDAFLAYCNEENLEATVVATVTEKPRLVMNW-NGKTIVDLS-RRFLDTNGVRQVIDAKVVDK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 568 YEDAPYEatqplQYLEGVLSLEavacKDWLTNKVDRSVT---GRIARQQCC-----------GELQLPLSDLGAIALDYR 633
Cdd:TIGR01857 617 DVKLPEE-----RQKTSAETLE----EDWLKVLSDLNVAsqkGLQERFDSSvgagtvlmplgGKYQLTPTEASVAKLPVL 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 634 GRKGYATSI---GHAPQAGLIDSATGSVLAIAEALTNIVFAPLEkgLESVSLS-ANWMWPCRNEGED-----ARLYRAVE 704
Cdd:TIGR01857 688 GGETHTASAiawGFNPYIAEWSPYHGAAYAVIESLAKLVAAGAD--YKKARLSfQEYFEKLDKDAERwgkpfAALLGAIK 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 705 AcaqfAIDLGINIPTGKDSLSMTQKYPDDKPvvspgtVIISAAAPVSNVRGIITPVIKSAQEShLLYIDfsfaplnlgGS 784
Cdd:TIGR01857 766 A----QIDLGLPAIGGKDSMSGTFEELTVPP------TLISFAVTTANSRRVISPEFKAAGEN-IYLIP---------GQ 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 785 ALfqslgkvgvQAPTIgNADYFADAFEAVQTLISKGLVLAGHDISAGGLITTLLEMCFANVSGgltIDLTAIPEKDLTKL 864
Cdd:TIGR01857 826 AL---------EDGTI-DFDLLKENFAQIEELIADHKVVSASAVKYGGVAESLAKMTFGNRIG---AELNNPELEDLFTA 892
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 865 LYAenpGVVLQVKDfstvaailEEAGVGYALIGTpsATRSIEITKEGEKLSID-IDKARRTWYEPSYlldRFQSTEKLAK 943
Cdd:TIGR01857 893 QYG---SFIFESPE--------ELSIANVEKIGQ--TTADFVLKVNGEKLDLEeLESAWEGKLEEVF---PSKFEDKKET 956
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 944 ERFDNFaHQPIQLRFAPSfdgklstlnlnpdRKERSGIVAAVVrdKGTNGEREMAYALYLAGFDVKDVHLTDLTSG---- 1019
Cdd:TIGR01857 957 VEVPAV-ASEKKVIKAKE-------------KVEKPRVVIPVF--PGTNSEYDSAKAFEKEGAEVNLVIFRNLNEEalve 1020
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1020 -----RETLEDAQMLVFCGGFSNSDVL-GSAKgWAAGILFNERAKAAIDAFYARpDTLSLGICNGCQLMAELGLI-YEDK 1092
Cdd:TIGR01857 1021 svetmVDEIDKSQILMLPGGFSAGDEPdGSAK-FIAAILRNPKVRVAIDSFLAR-DGLILGICNGFQALVKSGLLpYGNI 1098
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1093 KPRHR----MEHNRSHKYESCFVGLTIPENNTVMLSSLA-GSQLGVWCAHGEGRF-SMDESLDQY----NVVARYT---- 1158
Cdd:TIGR01857 1099 EAANEtsptLTYNDINRHVSKIVRTRIASTNSPWLSGVSvGDIHAIPVSHGEGRFvASDEVLAELrengQIATQYVdfng 1178
|
1130 1140 1150
....*....|....*....|....*....|....*..
gi 1154824145 1159 --YDDYPANPNGSPEGIAAVASRDGRHLAMMPHPERS 1193
Cdd:TIGR01857 1179 kpSMDSKYNPNGSSLAIEGITSPDGRIFGKMGHSERY 1215
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
624-898 |
3.65e-64 |
|
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100035 [Multi-domain] Cd Length: 264 Bit Score: 218.56 E-value: 3.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 624 DLGAIALDYRGRKGYATSIGHAPQAGLIDSATGSVLAIAEALTNIVFAPLEKglESVSLSANWMWPCRNEGEDARLYRAV 703
Cdd:cd02204 1 DAAVLRIPGETDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADP--LAITDCLNFGNPEKPEGEMGQLVEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 704 EACAQFAIDLGINIPTGKDSLSMTQKYpddkpVVSPGTVIISAAAPVSNVRGIITPVIKSAqESHLLYIDFSFAPLNLGG 783
Cdd:cd02204 79 LGLGDACRALGTPVIGGKDSLYNETEG-----VAIPPTLVIGAVGVVDDVRKIVTLDFKKE-GDLLYLIGETKDELGGSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 784 SALfQSLGKVGVQAPTIgNADYFADAFEAVQTLISKGLVLAGHDISAGGLITTLLEMCFANvSGGLTIDLTAIPEKDltK 863
Cdd:cd02204 153 YAL-AYHGLGGGAPPLV-DLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAG-GLGAEVDLSKDDAED--E 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1154824145 864 LLYAENPGVVLQVKDFSTVAAI-LEEAGVGYALIGT 898
Cdd:cd02204 228 LLFSESLGRVLVEVKPENEEVFeAEEAGVPATVIGT 263
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
133-928 |
7.85e-62 |
|
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273781 [Multi-domain] Cd Length: 715 Bit Score: 225.64 E-value: 7.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 133 LSPEEvsfLQKLSERLGRKLTDSELFGFSQVNSEHCRHKifngtfiidgkeQEASLFSMIKSTSEEnpngLVSAYKDNVA 212
Cdd:TIGR01736 1 LSDEE---MELIREILGREPNDTELAMFSAMWSEHCSYK------------SSKKLLKQFPTKGPN----VIQGPGEDAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 213 FVEGGRaeqfapisadkadfyttqpiDTVLSLKAETHNFPTTVEPFNGAATGTGGEIRDRMAGGkaSIPVAgtavymtsy 292
Cdd:TIGR01736 62 VVDIGD--------------------GYAVVFKMESHNHPSAIEPYNGAATGVGGILRDILSMG--ARPIA--------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 293 prlkgesktLMEArkwLY------QHPQAILTKASNGASDFGNKFGQPIITGSLlTFEhqenERATRYgfdkVIMLAGGI 366
Cdd:TIGR01736 111 ---------LLDS---LRfgplddPKNRYLFEGVVAGISDYGNRIGVPTVGGEV-EFD----ESYNGN----PLVNVMCV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 367 GYARAQDAIKEE-PQPDQLVVMMGGDNYRIGMGGGAVSSVNTGQYSSGIELNAVQRANPEMQKRVCNVVRALAE-GEdnp 444
Cdd:TIGR01736 170 GLVRKDDIVTGKaKGPGNKLVLVGGKTGRDGIGGATFASEELSEEAEEEDRPAVQVGDPFTEKLLIEATLEAVDtGL--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 445 IISIHDHGAGGHLNCLTELIEA--TGGVIDIDALPVGDKSLSAKEIIGNESQERMGMLIREKDFDRIAAIAERERAPIYK 522
Cdd:TIGR01736 247 VKGIKDLGAAGLTSASSEMAAKggLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYELPASV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 523 VGHTTNSKELVFKRDnGEEAIHLAVEdMLAKPPRTIMndKSVVHHYEDAPYEATQPLQY---LEGVLSLEAVACKDWLTN 599
Cdd:TIGR01736 327 IGEVTDEGRIRLYYK-GEVVADLPIE-LLADAPEYER--PSEPPKYPEEEKEPEPPADLedaFLKVLSSPNIASKEWVYR 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 600 KVDRSVTGRiarqqccgELQLPLSDLGAIALDYRGRKGYATSIGHAPQAGLIDSATGSVLAIAEALTNIVfaplEKGLES 679
Cdd:TIGR01736 403 QYDHEVQTR--------TVVKPGEDAAVLRIKETGKLGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLA----AVGAEP 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 680 VSLSanwmwPCRNEG--EDARLY----RAVEACAQFAIDLGINIPTGKDSLsmtqkYPDDKPVVSPGTVIISAAAPVSNV 753
Cdd:TIGR01736 471 LAAV-----DCLNFGnpERPEVYwqfvEAVKGLGDACRALGTPVVGGNVSL-----YNETNGVPIAPTPTIGMVGLVEDV 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 754 RGIITpvIKSAQESHLLYIDFSFAPlNLGGSALFQSL-GKVGVQAPTIgnaDYFAD--AFEAVQTLISKGLVLAGHDISA 830
Cdd:TIGR01736 541 EKLLT--SNFKKEGDAIYLIGETKD-ELGGSEYLRVIhGIVSGQVPAV---DLEEEkeLADAVREAIRAGLVSAAHDVSR 614
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 831 GGLITTLLEMCFANvSGGLTIDLTAIPEKDLTKLLYAENPG-VVLQVKDfSTVAAILEEAGVGYALIGTPSATRsIEITK 909
Cdd:TIGR01736 615 GGLAVALAEMAAAS-GIGAEVDIDEIASARPDELLFSESNGrAIVAVPE-EKAEEAVKSKGVPAKVIGKTGGDR-LTIKT 691
|
810
....*....|....*....
gi 1154824145 910 EGEKLSIDIDKARRTWYEP 928
Cdd:TIGR01736 692 GDDTISVSVKELRDAWEEA 710
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
131-931 |
1.44e-46 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 179.53 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 131 LALSPEEvsfLQKLSERLGRKLTDSELFGFSQVNSEHCRHK---IFNGTFiidgkeqeaslfsmikstSEENPNGLVSAy 207
Cdd:PRK01213 11 MGLTDDE---YERIREILGREPNFTELGMFSVMWSEHCSYKsskPLLRKF------------------PTKGPRVLQGP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 208 KDNVAFVEGGRaeqfapisadkadfyttqpiDTVLSLKAETHNFPTTVEPFNGAATGTGGEIRDRMA-GGKasiPVAgta 286
Cdd:PRK01213 69 GENAGVVDIGD--------------------GQAVVFKIESHNHPSAVEPYQGAATGVGGILRDIFSmGAR---PIA--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 287 vymtsyprlkgesktLMEArkwLY------QHPQAILTKASNGASDFGNKFGQPIITGSLltfehqeneratryGFDKV- 359
Cdd:PRK01213 123 ---------------LLDS---LRfgeldhPKTRYLLEGVVAGIGGYGNCIGVPTVGGEV--------------YFDESy 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 360 ----IMLAGGIGYARAQDAIKEEPQ-PDQLVVMMGGDNYRIGMGGGAVSSvntGQYSSGIE--LNAVQRANPEMQKRVCN 432
Cdd:PRK01213 171 ngnpLVNAMCVGLVRHDDIVLAKASgVGNPVVYVGAKTGRDGIGGASFAS---AELSEESEekRPAVQVGDPFMEKLLIE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 433 VVR-ALAEGEdnpIISIHDHGAGGhLNC-LTELIeATGGV---IDIDALPVGDKSLSAKEIIGNESQERMGMLIREKDFD 507
Cdd:PRK01213 248 ACLeLIKTGL---VVGIQDMGAAG-LTCsSSEMA-AKGGLgieLDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGKEE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 508 RIAAIAER---ERAPIykvGHTTNSKELVFKrDNGEEAIHLAVEDMLAKPPrtiMNDKSVVhhyEDAPYEATQPLQY--- 581
Cdd:PRK01213 323 EVLAIFEKwdlDAAVI---GEVTDDGRLRVY-HHGEVVADVPAEALADEAP---VYDRPYK---EPAYLDELQADPEdlk 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 582 --LEGVLSLEAVACKDWLTNKVDRSVTGRIArqqccgelQLPLSDLGAIALDyRGRKGYATSIGHAPQAGLIDSATGSVL 659
Cdd:PRK01213 393 eaLLKLLSSPNIASKEWVYEQYDHEVQTNTV--------VKPGGDAAVLRIR-GGGKGLALTTDCNPRYVYLDPYEGAKL 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 660 AIAEALTNIVFA---PLekgleSVSLSANW--------MWpcrnegedaRLYRAVEACAQFAIDLGINIPTGKDSLsmtq 728
Cdd:PRK01213 464 AVAEAARNLAAVgatPL-----AITDCLNFgnpekpevMW---------QFVEAVRGLADACRALGTPVVGGNVSL---- 525
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 729 kYPDDKPVVSPGTVIISAAAPVSNVRGIITPVIKsaQESHLLYIdFSFAPLNLGGSALFQSL-GKVGVQAPTIgnaDYFA 807
Cdd:PRK01213 526 -YNETGGTAIYPTPVIGMVGLIDDVSKRTTSGFK--KEGDLIYL-LGETKDELGGSEYLKVIhGHVGGRPPKV---DLEA 598
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 808 DAF--EAVQTLISKGLVLAGHDISAGGLITTLLEMCFAnvSG-GLTIDLTAipEKDLTKLLYAENPG-VVLQVK--DFST 881
Cdd:PRK01213 599 EKRlqELVREAIREGLVTSAHDVSEGGLAVALAEMAIA--GGlGAEVDLSD--GLRPDALLFSESQGrYVVSVPpeNEEA 674
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1154824145 882 VAAILEEAGVGYALIGTpSATRSIEITKEGEklsIDIDKARRTWYE--PSYL 931
Cdd:PRK01213 675 FEALAEAAGVPATRIGV-VGGDALKVKGNDT---ESLEELREAWEGalPRLL 722
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
244-524 |
7.31e-43 |
|
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100029 [Multi-domain] Cd Length: 272 Bit Score: 157.84 E-value: 7.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 244 LKAETHNFPTTVEPFNGAATGTGGEIRDRMAGGKASIPVAGTAVYMTSYPRLKGEsktlmearkwlyqhpqAILTKASNG 323
Cdd:cd02193 5 MKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGIDAKPIALSANWMASAGHPGED----------------AILYDAVKG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 324 ASDFGNKFGQPIITGSLLTFEHQENERAT--RYGFDKVIMLAGGIGYARAQDAIK-EEPQPDQLVVMMGGDNYRIGMGGG 400
Cdd:cd02193 69 VAELCNQLGLPIPVGKDRMSMKTRWQEGNeqREMTHPPSLVISAFGRVRDDRHTLpQLSTEGNALLLIGGGKGHNGLGGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 401 AVSSVNtgQYSSGIELNAVQRANPEMQKRVCNVVRALAegEDNPIISIHDHGAGGHLNCLTELIEA--TGGVIDIDALPV 478
Cdd:cd02193 149 ALASVA--LSYRQLGDKSAQVRDPAQEKGFYEAMQALV--AAGKLLAWHDRGAGGLLVALAELVFAghCGVQVDLAALGD 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1154824145 479 GDKSLSAKEIIGNESQERMGMLIREKDFDRIAAIAERERAPIYKVG 524
Cdd:cd02193 225 DEPDMEPLEIALFESQERGVIQVRAEDRDAVEEAQYGLADCVHVLG 270
|
|
| PRK01175 |
PRK01175 |
phosphoribosylformylglycinamidine synthase I; Provisional |
981-1225 |
7.52e-37 |
|
phosphoribosylformylglycinamidine synthase I; Provisional
Pssm-ID: 234913 [Multi-domain] Cd Length: 261 Bit Score: 140.28 E-value: 7.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 981 IVAAVVRDKGTNGEREMAYALYLAGFDVKDVHLTDLTSGRETLEDAQMLVFCGGFSNSDVLgsakgwAAGILFNERAKAA 1060
Cdd:PRK01175 4 IRVAVLRMEGTNCEDETVKAFRRLGVEPEYVHINDLAAERKSVSDYDCLVIPGGFSAGDYI------RAGAIFAARLKAV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1061 ----IDAFY--ARPdtlSLGICNGCQLMAELGL------IYEdkKPRHRMEHNRSHKYESCFVGLTIPENNTVMLSSLAG 1128
Cdd:PRK01175 78 lrkdIEEFIdeGYP---IIGICNGFQVLVELGLlpgfdeIAE--KPEMALTVNESNRFECRPTYLKKENRKCIFTKLLKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1129 SQLGVWCAHGEGR--FSMDESLDQY----NVVARYT-----YDDYPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFPW 1197
Cdd:PRK01175 153 DVFQVPVAHAEGRvvFSEEEILERLiendQIVFRYVdengnYAGYPWNPNGSIYNIAGITNEKGNVIGLMPHPERAFYGY 232
|
250 260
....*....|....*....|....*...
gi 1154824145 1198 QCGFYPEMQHEVTPWIeAFRNAYDWLKE 1225
Cdd:PRK01175 233 QHPYWEKEEDYGDGKI-FFDSLINYLRK 259
|
|
| FGAM_synth_I |
TIGR01737 |
phosphoribosylformylglycinamidine synthase I; In some species, ... |
984-1196 |
6.01e-29 |
|
phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273782 [Multi-domain] Cd Length: 227 Bit Score: 116.32 E-value: 6.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 984 AVVRDKGTNGEREMAYALYLAGFDVKDVHLTDltsgrETLEDAQMLVFCGGFSNSDVLGSAKGWAAGILFNERAKAAIDA 1063
Cdd:TIGR01737 4 AVIRFPGTNCDRDTVYALRLLGVDAEIVWYED-----GSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1064 FYArpdtlsLGICNGCQLMAELGLIyedkkpRHRMEHNRSHKYESCFVGLTIPENNTVMLSSLA-GSQLGVWCAHGEGRF 1142
Cdd:TIGR01737 79 VPV------LGICNGFQILVEAGLL------PGALLPNDSLRFICRWVYLRVENADTIFTKNYKkGEVIRIPIAHGEGRY 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154824145 1143 SMD-------ESLDQynVVARYTYDD----YPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFP 1196
Cdd:TIGR01737 147 YADdetlarlESNDQ--VVFRYCDEDgdvaEEANPNGSVGNIAGIVNERGNVLGMMPHPERASEK 209
|
|
| PRK03619 |
PRK03619 |
phosphoribosylformylglycinamidine synthase subunit PurQ; |
983-1196 |
3.72e-28 |
|
phosphoribosylformylglycinamidine synthase subunit PurQ;
Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 113.67 E-value: 3.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 983 AAVVRDKGTNGEREMAYAL-YLAGFDVKDVHLTDltsgrETLEDAQMLVFCGGFSNSDVLgsakgwaagilfneRAkAAI 1061
Cdd:PRK03619 3 VAVIVFPGSNCDRDMARALrDLLGAEPEYVWHKE-----TDLDGVDAVVLPGGFSYGDYL--------------RC-GAI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 1062 DAF---------YARPDTLSLGICNGCQLMAELGLIyedkkPrHRMEHNRSHKYESCFVGLTIpENNTVMLSSL--AGSQ 1130
Cdd:PRK03619 63 AAFspimkavkeFAEKGKPVLGICNGFQILTEAGLL-----P-GALTRNASLKFICRDVHLRV-ENNDTPFTSGyeKGEV 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154824145 1131 LGVWCAHGEGRFSMD-ESLDQ----YNVVARYTyddyPANPNGSPEGIAAVASRDGRHLAMMPHPERSIFP 1196
Cdd:PRK03619 136 IRIPIAHGEGNYYADeETLKRlegnGQVVFRYC----DENPNGSVNDIAGIVNEKGNVLGMMPHPERAVEP 202
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
140-515 |
2.30e-22 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 103.40 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 140 FLQKLSERLGRKLTDSELFGFSQVNSEHCrhkifngtfiidGKEQEASLFSMIKSTSEENPNGLVSAykdnvafveggra 219
Cdd:PRK14090 3 YLNILEEKLGREPTFVELQAFSVMWSEHC------------GYSHTKKYIRRLPKTGFEGNAGVVNL------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 220 eqfapisadkADFYTtqpidtvLSLKAETHNFPTTVEPFNGAATGTGGEIRDRMAGGKASipvagTAVYMTsyprlkges 299
Cdd:PRK14090 58 ----------DDYYS-------IAFKIESHNHPSAIEPYNGAATGVGGIIRDVLAMGARP-----TAIFDS--------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 300 ktlmearkwlyQHPQAILTKASNGASDFGNKFGQPIITGSLL---TFEHQEneratrygfdKVIMLAGGIGyaRAQDAIK 376
Cdd:PRK14090 107 -----------LHMSRIIDGIIEGIADYGNSIGVPTVGGELRissLYAHNP----------LVNVLAAGVV--RNDMLVD 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 377 EEP-QPDQLVVMMGGDNYRIGMGGGAVSSVN-TGQYSSGIelnAVQRANPEMQKrvcNVVRALAEG-EDNPIISIHDHGA 453
Cdd:PRK14090 164 SKAsRPGQVIVIFGGATGRDGIHGASFASEDlTGEKATKL---SIQVGDPFAEK---MLIEAFLEMvEEGLVEGAQDLGA 237
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154824145 454 GGHLNCLTELIeATGG---VIDIDALPVGDKSLSAKEIIGNESQERMGMLIREKDFDRIAAIAER 515
Cdd:PRK14090 238 GGVLSATSELV-AKGGlgaIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKK 301
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
380-534 |
3.33e-22 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 94.34 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 380 QPDQLVVMMGGDnyriGMGGGAVSSVNTGQYSSGieLNAVQRANPEMQKRVCNVVRALAEgEDNPIISIHDHGAGGHLNC 459
Cdd:pfam02769 1 KPGDVLILLGSS----GLHGAGLSLSRKGLEDSG--LAAVQLGDPLLEPTLIYVKLLLAA-LGGLVKAMHDITGGGLAGA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154824145 460 LTELIEA--TGGVIDIDALPVGDKSLSAKEIIGNESQERMGMLIREKDFDRIAAIAERERAPIYKVGHTTNSKELVF 534
Cdd:pfam02769 74 LAEMAPAsgVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTV 150
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
637-897 |
5.94e-22 |
|
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100029 [Multi-domain] Cd Length: 272 Bit Score: 97.37 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 637 GYATSIG-HAPQAgLIDSATGSVLAIAEALTNIvfAPLEKGLESVSLSANWMWPCRNEGEDARLYRAVEACAQFAIDLGI 715
Cdd:cd02193 2 GEAMKIEeHNHPA-AIDPAAGAATGVGGAIRDI--AATGIDAKPIALSANWMASAGHPGEDAILYDAVKGVAELCNQLGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 716 NIPTGKDSLSM---TQKYPDDKPVVSPGTVIISAAAPVSNVRGIITPVIKSAQEshLLYIDFSFAPLNLGGSALFQ---- 788
Cdd:cd02193 79 PIPVGKDRMSMktrWQEGNEQREMTHPPSLVISAFGRVRDDRHTLPQLSTEGNA--LLLIGGGKGHNGLGGTALASvals 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 789 --SLGKVGVQaptIGNADYFADAFEAVQTLISKGLVLAGHDISAGGLITTLLEMCFANVSGGLtIDLTAIPEKD-----L 861
Cdd:cd02193 157 yrQLGDKSAQ---VRDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQ-VDLAALGDDEpdmepL 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 1154824145 862 TKLLYAENPGVVLQVK--DFSTVAAILEEAGVGYALIG 897
Cdd:cd02193 233 EIALFESQERGVIQVRaeDRDAVEEAQYGLADCVHVLG 270
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
122-171 |
1.11e-20 |
|
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT), also known as Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3), PurL and formylglycinamidine ribonucleotide (FGAM) synthase. This enzyme catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. The structure analysis of Salmonella typhimurium FGAR-AT reveals that this linker domain is made up of a long hydrophilic belt with an extended conformation.
Pssm-ID: 465632 [Multi-domain] Cd Length: 50 Bit Score: 86.37 E-value: 1.11e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1154824145 122 IDAYNKSEGLALSPEEVSFLQKLSERLGRKLTDSELFGFSQVNSEHCRHK 171
Cdd:pfam18072 1 LEEANRYLGLALSDDEIDYLVEYFAGLGRNPTDVELGMFAQMWSEHCRHK 50
|
|
| FGAR-AT_N |
pfam18076 |
Formylglycinamide ribonucleotide amidotransferase N-terminal; This is the N-terminal domain ... |
12-104 |
8.60e-16 |
|
Formylglycinamide ribonucleotide amidotransferase N-terminal; This is the N-terminal domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT), also known as Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3), PurL and formylglycinamidine ribonucleotide (FGAM) synthase. This enzyme catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide and glutamine to formylglycinamidine ribonucleotide, ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway.
Pssm-ID: 465635 [Multi-domain] Cd Length: 115 Bit Score: 74.43 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 12 LFVVEHKTPFTDEEIKRLNWLfgLKEG---TLPQPSVEGIFVGPRSEMISPWSTNAVEIAENMGLKGISRIE-----ELK 83
Cdd:pfam18076 3 VHFVELEAPLSAAERARLEQL--LTYGpplEEPEPEGELLLVTPRLGTISPWSSKATDIAHNCGLDAVRRIErgiayYLT 80
|
90 100 110
....*....|....*....|....*....|
gi 1154824145 84 EKEATTE---------HDPMLEMVYTHPDA 104
Cdd:pfam18076 81 GKPLSAAelaalaallHDRMTESVLTDLED 110
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
641-898 |
3.70e-14 |
|
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 100027 [Multi-domain] Cd Length: 222 Bit Score: 73.20 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 641 SIGHAPqagLIDSATGSVLAIAEALTNIVfaplEKGLESVSLSANWMWPcrNEGEDARLYRAVEACAQFAIDLGINIPTG 720
Cdd:cd00396 8 GINPPL---AINPWAGGRLAVGGAVNDIA----AMGARPIALLASLSLS--NGLEVDILEDVVDGVAEACNQLGVPIVGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 721 KDSLSMTQKYPDdkpvvspgtvIISAAAPVSNVRGIITPVIKSAQEshllyidfsfaplnlgGSALFQSlgkvGVqapti 800
Cdd:cd00396 79 HTSVSPGTMGHK----------LSLAVFAIGVVEKDRVIDSSGARP----------------GDVLILT----GV----- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 801 gnadyfadafEAVQTLISKGLVLAGHDISAGGLITTLLEMCFAnvSG-GLTIDLTAIPEKDLTK----------LLYAEN 869
Cdd:cd00396 124 ----------DAVLELVAAGDVHAMHDITDGGLLGTLPELAQA--SGvGAEIDLEAIPLDEVVRwlcvehieeaLLFNSS 191
|
250 260 270
....*....|....*....|....*....|.
gi 1154824145 870 PGVVLQVK--DFSTVAAILEEAGVGYALIGT 898
Cdd:cd00396 192 GGLLIAVPaeEADAVLLLLNGNGIDAAVIGR 222
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
777-908 |
6.17e-13 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 67.76 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 777 APLNLGGSALFQS---LGKVGVQAPTIGNADYFADAFEAVQTLI-SKGLVLAGHDISAGGLITTLLEMCFANvSGGLTID 852
Cdd:pfam02769 10 GSSGLHGAGLSLSrkgLEDSGLAAVQLGDPLLEPTLIYVKLLLAaLGGLVKAMHDITGGGLAGALAEMAPAS-GVGAEID 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154824145 853 LTAIPEKDLTKL----LYAENPGVVLQV---KDFSTVAAILEEAGVGYALIGTPSATRSIEIT 908
Cdd:pfam02769 89 LDKVPIFEELMLplemLLSENQGRGLVVvapEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVI 151
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
241-524 |
1.62e-12 |
|
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 100027 [Multi-domain] Cd Length: 222 Bit Score: 68.19 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 241 VLSLKAETHNFPTTVEPFNGAATGTGGEIRDRMA-GGKasiPVAGTAVYMTSYPrlkgesktlmearkwlyqHPQAILTK 319
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAmGAR---PIALLASLSLSNG------------------LEVDILED 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 320 ASNGASDFGNKFGQPIITGSLltfehqenERATRYGFDKVIMLAGGIGYARAQDAIKE-EPQPDQLVVMMGGDNyrigmg 398
Cdd:cd00396 60 VVDGVAEACNQLGVPIVGGHT--------SVSPGTMGHKLSLAVFAIGVVEKDRVIDSsGARPGDVLILTGVDA------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 399 ggavssvntgqyssgielnavqranpeMQKRVcnvvralaegEDNPIISIHDHGAGGHLNCLTELIEA--TGGVIDIDAL 476
Cdd:cd00396 126 ---------------------------VLELV----------AAGDVHAMHDITDGGLLGTLPELAQAsgVGAEIDLEAI 168
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1154824145 477 PV--GDKSLSAKEIIG---NESQERMGMLIREKDFDRIAAIAERERAPIYKVG 524
Cdd:cd00396 169 PLdeVVRWLCVEHIEEallFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIG 221
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
803-913 |
9.87e-09 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 58.25 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 803 ADYFADAFEAVQTLISKGLVLAGHDISAGGLITTLLEMCfaNVSG-GLTIDLTAIP---EKDLTKLLYAeNP--GVVLQV 876
Cdd:COG2144 189 PERLRAQLELLPELAEAGLVTAAKDISNPGIIGTLGMLL--ECSGvGATIDLDAIPrpeGVDLERWLKA-FPsfGFLLTV 265
|
90 100 110
....*....|....*....|....*....|....*....
gi 1154824145 877 K--DFSTVAAILEEAGVGYALIGTPSATRSIEITKEGEK 913
Cdd:COG2144 266 PpeNVDEVLARFAARGITAAVIGEVTDSRRLTLRDGGER 304
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
984-1082 |
5.88e-06 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 46.44 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 984 AVVRDKGTNGE--REMAYALYLAGFDVKDVHLTDLTSGRET-LEDAQMLVFCGGFSNSDVLgsakgwaagiLFNERAKAA 1060
Cdd:cd01653 2 AVLLFPGFEELelASPLDALREAGAEVDVVSPDGGPVESDVdLDDYDGLILPGGPGTPDDL----------ARDEALLAL 71
|
90 100
....*....|....*....|..
gi 1154824145 1061 IDAFYARpDTLSLGICNGCQLM 1082
Cdd:cd01653 72 LREAAAA-GKPILGICLGAQLL 92
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
802-857 |
9.24e-06 |
|
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100028 [Multi-domain] Cd Length: 283 Bit Score: 48.75 E-value: 9.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154824145 802 NADYFADAFEAVQTLISKGLVLAGHDISAGGLITTLLeMcFANVSG-GLTIDLTAIP 857
Cdd:cd02192 182 SPALLRRQIALLPELAERGLVHAAKDISNPGIIGTLG-M-LLEASGvGAEIDLDAIP 236
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
982-1082 |
9.88e-06 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 45.27 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154824145 982 VAAVVRDKGTNGEREMAY-ALYLAGFDVKDVHLTDLTSGRET-LEDAQMLVFCGGFSNSDVLgsakgwaagiLFNERAKA 1059
Cdd:cd03128 1 VAVLLFGGSEELELASPLdALREAGAEVDVVSPDGGPVESDVdLDDYDGLILPGGPGTPDDL----------AWDEALLA 70
|
90 100
....*....|....*....|...
gi 1154824145 1060 AIDAFYARpDTLSLGICNGCQLM 1082
Cdd:cd03128 71 LLREAAAA-GKPVLGICLGAQLL 92
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
811-918 |
3.07e-05 |
|
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100034 [Multi-domain] Cd Length: 313 Bit Score: 47.47 E-value: 3.07e-05
10 20 30 40 50 60 70 80
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gi 1154824145 811 EAVQTLISKGLVLAGHDISAGGLITTLLEMCfANVSGGLTIDLTAIP--EKDLT--KLL---YAENPGVVLQVKDFSTVA 883
Cdd:cd02203 201 EAILEARETGLIVGIQDLGAGGLSSAVSEMA-AKGGLGAEIDLDKVPlrEPGMSpwEIWiseSQERMLLVVPPEDLEEFL 279
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90 100 110
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gi 1154824145 884 AILEEAGVGYALIGTPSATRSIEITKEGEKLsIDI 918
Cdd:cd02203 280 AICKKEDLEAAVIGEVTDDGRLRLYYKGEVV-ADL 313
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