|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
13-736 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 1205.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 13 EKKPYLALGLTEDEYHRFAELIGHQPNDTEIGLASGMWSEHCAYKYSKPILRQFWTKNDRVLMGPGEGAGVIDIGEGKAV 92
Cdd:PRK01213 4 TEELYAEMGLTDDEYERIREILGREPNFTELGMFSVMWSEHCSYKSSKPLLRKFPTKGPRVLQGPGENAGVVDIGDGQAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 93 VFKAESHNHPSAVEPYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGDLNLPHTQHLVDRIVAGIGGYGNAIGIPTVGGE 172
Cdd:PRK01213 84 VFKIESHNHPSAVEPYQGAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTVGGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 173 TNFDHTYARNPLVNAMCVGIMDKDQIQKGKAAGVGNALIYVGAKTGRDGINGASFASGDFSDEEAADRSAVQVGDPFMEK 252
Cdd:PRK01213 164 VYFDESYNGNPLVNAMCVGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGASFASAELSEESEEKRPAVQVGDPFMEK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 253 LLMDACLEITQdhQQALVGIQDMGAAGLVSSSVEMAGKANSGMEMDLDLIPQREANMTPFEIMLSESQERMLLCVRAGFE 332
Cdd:PRK01213 244 LLIEACLELIK--TGLVVGIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGKE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 333 QEVLDVFAAYDLDAAVVGHVIEGHQYRLYHHGKLVCDVPVSSLTDDAPIYEQVGKMPARLAEPAPDFDpivtDPVATWKA 412
Cdd:PRK01213 322 EEVLAIFEKWDLDAAVIGEVTDDGRLRVYHHGEVVADVPAEALADEAPVYDRPYKEPAYLDELQADPE----DLKEALLK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 413 MMGTPTIADKSSLYRRYDAQVQTNTVVLPGSDAAVIRIRGTHRALAMTTDSKGRYLYLDPKVGAAMSVAEAARNLAASGA 492
Cdd:PRK01213 398 LLSSPNIASKEWVYEQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 493 EPLGITDCLNFGDPTKPEAFYELAEAAKGIIAATKAFNAPVISGNVSLYNETNGKAIYPTPMIGMVGLIEDLSTITTANF 572
Cdd:PRK01213 478 TPLAITDCLNFGNPEKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKRTTSGF 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 573 KHADDLLYLVGETHGDFNGSELQKLQTGEVAGRLFDFDLDAEKANQQFVLTAIRQHFVTAAHDLSDGGLLVALAEMGFTN 652
Cdd:PRK01213 558 KKEGDLIYLLGETKDELGGSEYLKVIHGHVGGRPPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMAIAG 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 653 QLGAQVKVDL---PTSWGFSETQGRFLVTVAPEDQAAFEAL----NGPAELIGRVQAapqfDVTTVSHQFSIPLEELQTA 725
Cdd:PRK01213 638 GLGAEVDLSDglrPDALLFSESQGRYVVSVPPENEEAFEALaeaaGVPATRIGVVGG----DALKVKGNDTESLEELREA 713
|
730
....*....|.
gi 504382659 726 FEEALPCYLNQ 736
Cdd:PRK01213 714 WEGALPRLLGG 724
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
1-734 |
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: 1054.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 1 MTHV--EMSPEAIAEKKPYLALGLTEDEYHRFAELIGHQPNDTEIGLASGMWSEHCAYKYSKPILRQFWTKNDRVLMGPG 78
Cdd:COG0046 1 MSTVdlEGGREALEEANRELGLALSDDEYDYIVEILGRNPTDVELGMFSQMWSEHCSYKSSNALLKSLPTEGPRVLSGPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 79 EGAGVIDIGEGKAVVFKAESHNHPSAVEPYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGDLNLP--HTQHLVDRIVAG 156
Cdd:COG0046 81 DNAGVVDIGDGLAVVFKVESHNHPSAIEPYQGAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDQPpaSPRYILIGVVAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 157 IGGYGNAIGIPTVGGETNFDHTYARNPLVNAMCVGIMDKDQIQKGKAAGVGNALIYVGAKTGRDGINGASFASGDFSDEE 236
Cdd:COG0046 161 IADYGNCFGVPTVGGEVRFDESYEGNPLVNAGGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGATFASEELGEDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 237 AADRSAVQVGDPFMEKLLMDACLEITQDHqqALVGIQDMGAAGLVSSSVEMAGKANSGMEMDLDLIPQREANMTPFEIML 316
Cdd:COG0046 241 ELDRPAVQVGDPFMEKRLIEAILELGDTG--LIVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 317 SESQERMLLCVRAGFEQEVLDVFAAYDLDAAVVGHVIEGHQYRLYHHGKLVCDVPVSSLTDDAPIYEqvgkMPARLAEPA 396
Cdd:COG0046 319 SESQERMLLVVKPEKLEEFEAIFERWRLPAAVIGEVTDDGRLVVTDHGETVADLPLDFLAGGAPKYH----RPAKRPAYL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 397 PDFD-PIVTDPVATWKAMMGTPTIADKSSLYRRYDAQVQTNTVVLPG-SDAAVIRIRGTHRALAMTTDSKGRYLYLDPKV 474
Cdd:COG0046 395 EPLDlPEPIDLEEALLRLLSSPNVASKEWLYRQYDREVGGNTVRDPGvADAAVVRVDGTYKGLAMSTGENPRYALLDPYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 475 GAAMSVAEAARNLAASGAEPLGITDCLNFGDPTKPEAFYELAEAAKGIIAATKAFNAPVISGNVSLYNETNG--KAIYPT 552
Cdd:COG0046 475 GARMAVAEAARNLAAVGAEPLAITDCLNWGNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETKDgkVAIPPT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 553 PMIGMVGLIEDLSTITTANFKHADDLLYLVGETHGDFNGSELQKLQtGEVAGRLFDFDLDAEKANQQFVLTAIRQHFVTA 632
Cdd:COG0046 555 PVIGAVGLVDDVRKTVTPDLKKEGDLLYLIGETKNELGGSEYAQVL-GQLGGEPPDVDLEAEKALFEAVQELIREGLILA 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 633 AHDLSDGGLLVALAEMGFTNQLGAQVKVDL-----PTSWGFSETQGRFLVTVAPEDQAAFEAL---NG-PAELIGRVQAA 703
Cdd:COG0046 634 AHDVSDGGLAVALAEMAFAGGLGADIDLDAlgdlrPDAALFSESQGRAVVQVAPEDAEAVEALlaeAGlPAHVIGTVTGD 713
|
730 740 750
....*....|....*....|....*....|..
gi 504382659 704 PQFDVTTVSH-QFSIPLEELQTAFEEALPCYL 734
Cdd:COG0046 714 DRLVIRRGGEtLLSLSLAELRDAWEETLPRLR 745
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
22-734 |
0e+00 |
|
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: 951.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 22 LTEDEYHRFAELIGHQPNDTEIGLASGMWSEHCAYKYSKPILRQFWTKNDRVLMGPGEGAGVIDIGEGKAVVFKAESHNH 101
Cdd:TIGR01736 1 LSDEEMELIREILGREPNDTELAMFSAMWSEHCSYKSSKKLLKQFPTKGPNVIQGPGEDAGVVDIGDGYAVVFKMESHNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 102 PSAVEPYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGDLNLPHTQHLVDRIVAGIGGYGNAIGIPTVGGETNFDHTYAR 181
Cdd:TIGR01736 81 PSAIEPYNGAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 182 NPLVNAMCVGIMDKDQIQKGKAAGVGNALIYVGAKTGRDGINGASFASGDFSDE-EAADRSAVQVGDPFMEKLLMDACLE 260
Cdd:TIGR01736 161 NPLVNVMCVGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGATFASEELSEEaEEEDRPAVQVGDPFTEKLLIEATLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 261 ITQdhQQALVGIQDMGAAGLVSSSVEMAGKANSGMEMDLDLIPQREANMTPFEIMLSESQERMLLCVRAGFEQEVLDVFA 340
Cdd:TIGR01736 241 AVD--TGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 341 AYDLDAAVVGHVIEGHQYRLYHHGKLVCDVPVSSLTdDAPIYEQVGKMPARLAEPAPDFDPIvtDPVATWKAMMGTPTIA 420
Cdd:TIGR01736 319 KYELPASVIGEVTDEGRIRLYYKGEVVADLPIELLA-DAPEYERPSEPPKYPEEEKEPEPPA--DLEDAFLKVLSSPNIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 421 DKSSLYRRYDAQVQTNTVVLPGSDAAVIRIRGTH-RALAMTTDSKGRYLYLDPKVGAAMSVAEAARNLAASGAEPLGITD 499
Cdd:TIGR01736 396 SKEWVYRQYDHEVQTRTVVKPGEDAAVLRIKETGkLGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 500 CLNFGDPTKPEAFYELAEAAKGIIAATKAFNAPVISGNVSLYNETNGKAIYPTPMIGMVGLIEDLSTITTANFKHADDLL 579
Cdd:TIGR01736 476 CLNFGNPERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLLTSNFKKEGDAI 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 580 YLVGETHGDFNGSELQKLQTGEVAGRLFDFDLDAEKANQQFVLTAIRQHFVTAAHDLSDGGLLVALAEMGFTNQLGAqvK 659
Cdd:TIGR01736 556 YLIGETKDELGGSEYLRVIHGIVSGQVPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGA--E 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 660 VDLPTSWG-------FSETQGRFLVTVAPEDQAAFEALNG-PAELIGRVqAAPQFDVTTVSHQFSIPLEELQTAFEEALP 731
Cdd:TIGR01736 634 VDIDEIASarpdellFSESNGRAIVAVPEEKAEEAVKSKGvPAKVIGKT-GGDRLTIKTGDDTISVSVKELRDAWEEALP 712
|
...
gi 504382659 732 CYL 734
Cdd:TIGR01736 713 EYM 715
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
42-370 |
2.04e-167 |
|
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: 483.90 E-value: 2.04e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 42 EIGLASGMWSEHCAYKYSKPILRQFWtkndrvlmgpgegagvidigegkAVVFKAESHNHPSAVEPYEGAATGVGGIIRD 121
Cdd:cd02203 1 ELGMFAQMWSEHCRHKSFKSLLKMIW-----------------------AVVFKVETHNHPSAIEPFGGAATGVGGIIRD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 122 IFSIGAKPVAMLDSLAFGDLNLP--------HTQHLVDRIVAGIGGYGNAIGIPTVGGETNFDHTYARNPLVNAMCVGIM 193
Cdd:cd02203 58 ILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYGNPLVNVGCVGIV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 194 DKDQIQKGKAAGVGNALIYVGAKTGRDGINGASFASGDFSDEEAA-DRSAVQVGDPFMEKLLMDACLEITQDhqQALVGI 272
Cdd:cd02203 138 PKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATFSSKELSENSSElDRPAVQVGDPFMEKKLQEAILEARET--GLIVGI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 273 QDMGAAGLVSSSVEMAGKANSGMEMDLDLIPQREANMTPFEIMLSESQERMLLCVRAGFEQEVLDVFAAYDLDAAVVGHV 352
Cdd:cd02203 216 QDLGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEV 295
|
330
....*....|....*...
gi 504382659 353 IEGHQYRLYHHGKLVCDV 370
Cdd:cd02203 296 TDDGRLRLYYKGEVVADL 313
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
32-559 |
1.16e-132 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 405.39 E-value: 1.16e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 32 ELIGHQPNDTEIGLASGMWSEHCAYKYSKPILRQFwtkndrVLMGPGEGAGVIDIGEGKAVVFKAESHNHPSAVEPYEGA 111
Cdd:PRK14090 9 EKLGREPTFVELQAFSVMWSEHCGYSHTKKYIRRL------PKTGFEGNAGVVNLDDYYSIAFKIESHNHPSAIEPYNGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 112 ATGVGGIIRDIFSIGAKPVAMLDSLafgdlnlpHTQHLVDRIVAGIGGYGNAIGIPTVGGETNFDHTYARNPLVNAMCVG 191
Cdd:PRK14090 83 ATGVGGIIRDVLAMGARPTAIFDSL--------HMSRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNVLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 192 IMDKDQIQKGKAAGVGNALIYVGAKTGRDGINGASFASGDFSDEEAADRSaVQVGDPFMEKLLMDACLEITqdhQQALV- 270
Cdd:PRK14090 155 VVRNDMLVDSKASRPGQVIVIFGGATGRDGIHGASFASEDLTGEKATKLS-IQVGDPFAEKMLIEAFLEMV---EEGLVe 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 271 GIQDMGAAGLVSSSVEMAGKANSGMEMDLDLIPQREANMTPFEIMLSESQERMLLCVRAGFEQEVLDVFAAYDLDAAVVG 350
Cdd:PRK14090 231 GAQDLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGDIVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 351 HVIEGHQYRLYHHGKLVCDVPVsSLTDDAPIYEQVGKMPARLaepaPDFDPIVTDPVatwkammgtptiaDKSSLYRRYD 430
Cdd:PRK14090 311 EVIDDPIYRVMYRDDLVMEVPV-QLLANAPEEEIVEYTPGEI----PEFKRVEFEEV-------------NAREVFEQYD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 431 AQVQTNTVVLPGSDAAVIRIRGTHrALAMTTDSKGRYLYLDPKVGAAMSVAEAARNLAASGAEPLGITDCLNFGDP-TKP 509
Cdd:PRK14090 373 HMVGTDTVLPPGFGAAVMRIKRDG-GYSLVTHSRADLALQDTYWGTFIAVLESVRKTLSVGAEPLAITNCVNYGDPdVDP 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 504382659 510 EAfyeLAEAAKGIIAATKAFNAPVISGNVSLYNETNGKAIYPTPMIGMVG 559
Cdd:PRK14090 452 VG---LSAMMTALKDACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLG 498
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
444-700 |
2.33e-113 |
|
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: 343.36 E-value: 2.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 444 DAAVIRIRG-THRALAMTTDSKGRYLYLDPKVGAAMSVAEAARNLAASGAEPLGITDCLNFGDPTKPEA-FYELAEAAKG 521
Cdd:cd02204 1 DAAVLRIPGeTDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKPEGeMGQLVEAVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 522 IIAATKAFNAPVISGNVSLYNETNGKAIYPTPMIGMVGLIEDLSTITTANFKHADDLLYLVGETHGDFNGSELQKLQTGE 601
Cdd:cd02204 81 LGDACRALGTPVIGGKDSLYNETEGVAIPPTLVIGAVGVVDDVRKIVTLDFKKEGDLLYLIGETKDELGGSEYALAYHGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 602 VAGRLFDFDLDAEKANQQFVLTAIRQHFVTAAHDLSDGGLLVALAEMGFTNQLGAQV---KVDLPTSWGFSETQGRFLVT 678
Cdd:cd02204 161 GGGAPPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVdlsKDDAEDELLFSESLGRVLVE 240
|
250 260
....*....|....*....|....
gi 504382659 679 VAPEDQAAFEA--LNGPAELIGRV 700
Cdd:cd02204 241 VKPENEEVFEAeeAGVPATVIGTV 264
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
92-353 |
7.84e-54 |
|
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: 186.73 E-value: 7.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 92 VVFKAESHNHPSAVEPYEGAATGVGGIIRDIFS--IGAKPVAMLDSLAFGDLNlPHTQHLVDRIVAGIGGYGNAIGIPTV 169
Cdd:cd02193 3 EAMKIEEHNHPAAIDPAAGAATGVGGAIRDIAAtgIDAKPIALSANWMASAGH-PGEDAILYDAVKGVAELCNQLGLPIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 170 GG-----------ETNFDHTYARNPLVNAMCVGIMDKDQIQKGKAAGVGNALIYVGAKTGRDGINGASFASGDFSDEEAA 238
Cdd:cd02193 82 VGkdrmsmktrwqEGNEQREMTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKGHNGLGGTALASVALSYRQLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 239 DRSaVQVGDPFMEKLLMDACLEITQdhQQALVGIQDMGAAGLVSSSVEMAGKANSGMEMDLDLIPQREANMTPFEIMLSE 318
Cdd:cd02193 162 DKS-AQVRDPAQEKGFYEAMQALVA--AGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDEPDMEPLEIALFE 238
|
250 260 270
....*....|....*....|....*....|....*
gi 504382659 319 SQERMLLCVRAgfeqEVLDVFAAYDLDAAVVGHVI 353
Cdd:cd02193 239 SQERGVIQVRA----EDRDAVEEAQYGLADCVHVL 269
|
|
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
95-728 |
4.02e-39 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 156.11 E-value: 4.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 95 KAESHNHPSAVEPYEGAATGVGGIIRDIFS--IGAKPVAMLDSLAFGDLNLPHTQH-------LVDRIV--------AGI 157
Cdd:PRK05297 288 KVETHNHPTAISPFPGAATGSGGEIRDEGAtgRGSKPKAGLTGFSVSNLRIPGFEQpweedygKPERIAsaldimieGPL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 158 GG--YGNAIGIPTVGG-----ETNFDHTYAR-----NPLVNAMCVGIMDKDQIQKGKAAgVGNALIYVGAKTGRDGINGA 225
Cdd:PRK05297 368 GGaaFNNEFGRPNLLGyfrtfEQKVNSHNEEvrgyhKPIMLAGGIGNIRADHVQKGEIP-VGAKLIVLGGPAMRIGLGGG 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 226 ---SFASGDFSdeEAADRSAVQVGDPFMEKL---LMDACLEITQDHqqALVGIQDMGAAGLVSSSVEMAGKANSGMEMDL 299
Cdd:PRK05297 447 aasSMASGQSS--EDLDFASVQRGNPEMERRcqeVIDRCWQLGDDN--PILSIHDVGAGGLSNAFPELVNDGGRGGRFDL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 300 DLIPQREANMTPFEIMLSESQERMLLCVRagfeQEVLDVFAA--------YdldaAVVGHVIEGHQYRLY--HHGKLVCD 369
Cdd:PRK05297 523 RKIPNDEPGMSPLEIWCNESQERYVLAIA----PEDLELFEAicerercpF----AVVGEATEERHLTLEdsHFDNKPVD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 370 VPVSSLtddapiyeqVGKMP------ARLAEPAPDFDPIVTDPVATWKAMMGTPTIADKSSLYRRYDAQVqTNTVV---- 439
Cdd:PRK05297 595 LPLDVL---------LGKPPkmhrdvKTVKAKGPALDYSGIDLAEAVERVLRLPTVASKSFLITIGDRSV-TGLVArdqm 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 440 -----LPGSDAAVirirgthralaMTTDSKGRY-------------LyLDPKVGAAMSVAEAARNLAASGAEPLG-ITDC 500
Cdd:PRK05297 665 vgpwqVPVADCAV-----------TAASYDGYAgeamamgertpvaL-LDAAASARMAVGEALTNIAAAPIGDLKrIKLS 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 501 LNF----GDPTKPEAFYELAEA-------AKGIiaatkafNAPVisGNVSL-----YNETNG-KAIYpTPM---IGMVGL 560
Cdd:PRK05297 733 ANWmaaaGHPGEDARLYDAVKAvgmelcpALGI-------TIPV--GKDSLsmktkWQEGGEdKEVT-SPLsliISAFAP 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 561 IEDLS-TITTANFKHADDLLYLVGETHGDFN--GSEL-QKL-QTGEVAGrlfDFDlDAEKANQQF--VLTAIRQHFVTAA 633
Cdd:PRK05297 803 VEDVRkTLTPQLRTDKDTALLLIDLGRGKNRlgGSALaQVYnQLGDKAP---DVD-DAEDLKGFFnaIQALVAEGLLLAY 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 634 HDLSDGGLLVALAEMGFTNQLGAQVKVDlptSWG-------FSETQGrFLVTVAPEDQAAFEA------LNGPAELIGRV 700
Cdd:PRK05297 879 HDRSDGGLLTTLAEMAFAGHCGLDIDLD---ALGddalaalFNEELG-AVIQVRAADRDAVEAilaehgLSDCVHVIGKP 954
|
730 740 750
....*....|....*....|....*....|..
gi 504382659 701 QAAPQFdvtTVSHQ----FSIPLEELQTAFEE 728
Cdd:PRK05297 955 NAGDRI---VITRNgktvFSESRTELRRWWSE 983
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
205-362 |
4.00e-33 |
|
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: 124.77 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 205 GVGNALIYVGAktgrDGINGASFASGDFSDEEAaDRSAVQVGDPFMEKLLMDACLEITQDHQQAlVGIQDMGAAGLVSSS 284
Cdd:pfam02769 1 KPGDVLILLGS----SGLHGAGLSLSRKGLEDS-GLAAVQLGDPLLEPTLIYVKLLLAALGGLV-KAMHDITGGGLAGAL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504382659 285 VEMAGKANSGMEMDLDLIPQREANMTPFEIMLSESQERMLLCVRAGFEQEVLDVFAAYDLDAAVVGHVIEGHQYRLYH 362
Cdd:pfam02769 75 AEMAPASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
91-350 |
5.47e-32 |
|
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: 124.05 E-value: 5.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 91 AVVFKAESHNHPSAVEPYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGDlnlPHTQHLVDRIVAGIGGYGNAIGIPTVG 170
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSN---GLEVDILEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 171 GETNFD-HTYARNPLVNAMCVGIMDKDQIQKGKAAGVGNALIYvgakTGRDGINGASFASGdfsdeeaadrsavqvgdpf 249
Cdd:cd00396 78 GHTSVSpGTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLIL----TGVDAVLELVAAGD------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 250 mekllmdacleitqdhqqaLVGIQDMGAAGLVSSSVEMAGKANSGMEMDLDLIPQREANM-----TPFEIMLSESQERML 324
Cdd:cd00396 135 -------------------VHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRwlcveHIEEALLFNSSGGLL 195
|
250 260
....*....|....*....|....*.
gi 504382659 325 LCVRAGFEQEVLDVFAAYDLDAAVVG 350
Cdd:cd00396 196 IAVPAEEADAVLLLLNGNGIDAAVIG 221
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
92-709 |
3.38e-30 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 128.35 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 92 VVFKAESHNHPSAVEPYEGAATGVGGIIRDIFS--IGAKPVAMLDSLAFGDLNLPHT-------------------QHLV 150
Cdd:PLN03206 288 ILLTAETHNFPCAVAPYPGAETGAGGRIRDTHAtgRGSFVVAGTAGYCVGNLRIEGSyapwedssfvypsnlasplQILI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 151 DrIVAGIGGYGNAIGIPTVGGETnfdHTYAR-----------NPLVNAMCVGIMDKDQIQKGkAAGVGNALIYVGAKTGR 219
Cdd:PLN03206 368 D-ASNGASDYGNKFGEPLIQGYT---RTFGMrlpngerrewlKPIMFSGGIGQIDHTHLTKG-EPDIGMLVVKIGGPAYR 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 220 DGING---ASFASGdfSDEEAADRSAVQVGDPFME-KL--LMDACLEITQDHqqALVGIQDMGAAG---LVSSSVEMAGK 290
Cdd:PLN03206 443 IGMGGgaaSSMVSG--QNDAELDFNAVQRGDAEMSqKLyrVVRACVEMGEDN--PIVSIHDQGAGGncnVVKEIIYPKGA 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 291 ansgmEMDLDLIPQREANMTPFEIMLSESQERMLLCVRAGFEQEVLDVFAAYDLDAAVVGhVIEGhqyrlyhHGKLV--- 367
Cdd:PLN03206 519 -----EIDIRAVVVGDHTLSVLEIWGAEYQEQDALLIKPESRDLLQSICDRERCSMAVIG-TIDG-------SGRVVlvd 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 368 ---------CDVPVSSLTDDAPIYEQVGKMPAR---LAEPAPDFDPIVTDPVAT----WKAMMGTPTIADKSSLYRRYD- 430
Cdd:PLN03206 586 saapekceaNGLPPPPPAVDLDLEKVLGDMPQKtfeFKRVANKLEPLDIPPGITvmdaLKRVLRLPSVCSKRFLTTKVDr 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 431 ------AQVQT-NTVVLPGSDAAVirIRGTHRALAMTTDS------KGrylYLDPKVGAAMSVAEAARNLAAsgAEPLGI 497
Cdd:PLN03206 666 cvtglvAQQQTvGPLQIPLADVAV--IAQTHTGLTGGACAigeqpiKG---LVDPKAMARLAVGEALTNLVW--AKVTAL 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 498 TDCLNFGD-------PTKPEAFYELAEAAKgiiAATKAFNAPVISGNVSLY------NETNgKAIYPTPMIGMVGlIEDL 564
Cdd:PLN03206 739 SDVKASGNwmyaaklDGEGADMYDAAVALR---DAMIELGVAIDGGKDSLSmaaqagGEVV-KAPGNLVISAYVT-CPDI 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 565 STITTANFKHADD--LLYL-VGETHGDFNGSELQKL--QTGEVAGRLFDFDL--DAEKANQQFvltaIRQHFVTAAHDLS 637
Cdd:PLN03206 814 TKTVTPDLKLGDDgvLLHVdLGKGKRRLGGSALAQAydQIGDDCPDLDDVAYlkKAFEATQDL----IAKRLISAGHDIS 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 638 DGGLLVALAEMGFTNQLGaqVKVDLPTSWG------FSETQGrFLVTVAPEDQ----AAFEALNGPAELIGRVQAAPQFD 707
Cdd:PLN03206 890 DGGLVVTLLEMAFAGNCG--INVDLPSSGHsafetlFAEELG-LVLEVSRKNLdavmEKLAAAGVTAEVIGQVTASPLIE 966
|
..
gi 504382659 708 VT 709
Cdd:PLN03206 967 VK 968
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
91-193 |
6.09e-28 |
|
AIR synthase related protein, N-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 N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 108.30 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 91 AVVFKAESHNHPSAVEPYEG-AATGVGGIIRDIFSIGAKPVAMLDSLAFGDlnLPHTQHLVDRIVAGIGGYGNAIGIPTV 169
Cdd:pfam00586 4 AVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLALPG--GPEVEWVLEEIVEGIAEACREAGVPLV 81
|
90 100
....*....|....*....|....
gi 504382659 170 GGETNFDHTYArNPLVNAMCVGIM 193
Cdd:pfam00586 82 GGDTSFDPEGG-KPTISVTAVGIV 104
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
456-561 |
1.34e-25 |
|
AIR synthase related protein, N-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 N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 101.37 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 456 ALAMTTDSKGRYLYLDPKVG-AAMSVAEAARNLAASGAEPLGITDCLNFGDPTKPEafYELAEAAKGIIAATKAFNAPVI 534
Cdd:pfam00586 4 AVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVE--WVLEEIVEGIAEACREAGVPLV 81
|
90 100
....*....|....*....|....*..
gi 504382659 535 SGNVSLYNETngkaIYPTPMIGMVGLI 561
Cdd:pfam00586 82 GGDTSFDPEG----GKPTISVTAVGIV 104
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
456-694 |
9.79e-19 |
|
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: 85.53 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 456 ALAMTTDSKGRYLYLDPKVGAAMSVAEAARNLAASGAEPLGITDCLNFGDPTKPEafyELAEAAKGIIAATKAFNAPVIS 535
Cdd:cd00396 1 SLAMSTDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVD---ILEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 536 GNVSLYNETNGkaIYPTPMIGMVGLIEDlstittanfkhaddllylvgethgdfngSELQKLQTGEVAGRLFDFDLDAEK 615
Cdd:cd00396 78 GHTSVSPGTMG--HKLSLAVFAIGVVEK----------------------------DRVIDSSGARPGDVLILTGVDAVL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 616 ANQQFVLtairqhfVTAAHDLSDGGLLVALAEMGFTNQLGAQVK-----VDLPTSWG---------FSETQGRFLVTVAP 681
Cdd:cd00396 128 ELVAAGD-------VHAMHDITDGGLLGTLPELAQASGVGAEIDleaipLDEVVRWLcvehieealLFNSSGGLLIAVPA 200
|
250
....*....|...
gi 504382659 682 EDQAAFEALNGPA 694
Cdd:cd00396 201 EEADAVLLLLNGN 213
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
577-709 |
8.90e-17 |
|
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: 77.77 E-value: 8.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 577 DLLYLVGeTHGDFNGSELQKLQTGEVAGRLFDF--DLDAEKANQQFVLTAIRQHF-VTAAHDLSDGGLLVALAEMGFTNQ 653
Cdd:pfam02769 4 DVLILLG-SSGLHGAGLSLSRKGLEDSGLAAVQlgDPLLEPTLIYVKLLLAALGGlVKAMHDITGGGLAGALAEMAPASG 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504382659 654 LGAQVKVDLPT--SWG-------FSETQGRFLVTVAPEDQ----AAFEALNGPAELIGRVQAAPQFDVT 709
Cdd:pfam02769 83 VGAEIDLDKVPifEELmlplemlLSENQGRGLVVVAPEEAeavlAILEKEGLEAAVIGEVTAGGRLTVI 151
|
|
| FGAR-AT_linker |
pfam18072 |
Formylglycinamide ribonucleotide amidotransferase linker domain; This is the linker domain ... |
11-57 |
2.87e-14 |
|
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: 67.49 E-value: 2.87e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 504382659 11 IAEKKPYLALGLTEDEYHRFAEL---IGHQPNDTEIGLASGMWSEHCAYK 57
Cdd:pfam18072 1 LEEANRYLGLALSDDEIDYLVEYfagLGRNPTDVELGMFAQMWSEHCRHK 50
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
458-690 |
1.95e-13 |
|
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: 71.17 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 458 AMTTDSKGRYLYLDPKVGAAMSVAEAARNLAASG--AEPLGITDCLNFGDpTKPEAFYELAEAAKGIIAATKAFNAPVIS 535
Cdd:cd02193 4 AMKIEEHNHPAAIDPAAGAATGVGGAIRDIAATGidAKPIALSANWMASA-GHPGEDAILYDAVKGVAELCNQLGLPIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 536 GNVSLY--------NETNGKAIYPTPMIGMVGLIEDlSTITTANFKHADDLLYLVGETHGDfNGSELQKLQTGEVAGRLF 607
Cdd:cd02193 83 GKDRMSmktrwqegNEQREMTHPPSLVISAFGRVRD-DRHTLPQLSTEGNALLLIGGGKGH-NGLGGTALASVALSYRQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 608 DF------DLDAEKANQQFVLTAIRQHFVTAAHDLSDGGLLVALAEMGFTNQLGAQVKVD---------LPTSWGFSETQ 672
Cdd:cd02193 161 GDksaqvrDPAQEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAalgddepdmEPLEIALFESQ 240
|
250
....*....|....*...
gi 504382659 673 GRFLVTVAPEDQAAFEAL 690
Cdd:cd02193 241 ERGVIQVRAEDRDAVEEA 258
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
470-723 |
9.63e-13 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 71.98 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 470 LDPKVGAAMSVAEAARNLA-ASGAEPLGITDCLNFG-DPTKPEAF--YELAEAAK----------------------GII 523
Cdd:PHA03366 704 LDPILGAKYAIVEALTNLMlAPVANLEDITITLSVTwPPTDQAASelYRALAACKefcrelgvnftftsasssprqdQPP 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 524 AATKAFNAPVISGNVslynetngkaiyPTPMIGmvgliedlsTITTANFKHADDLLYLV----GETHGdfnGSELQKLqT 599
Cdd:PHA03366 784 QPGPLFNTIVFTASA------------PVPSST---------PRLTPDLKKPGSALVHLsispEYTLA---GSVFEQI-F 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 600 GEVAGRLFDFDLDAEKANQQFVLTAIRQHFVTAAHDLSDGGLLVALAEMGFTNQLGAQVKV---DLPTSWGFSETQGrFL 676
Cdd:PHA03366 839 GLKSGTLPDISPSYLKNLFRAVQHLISEGLVVSGHDVSDGGLIACLAEMALAGGRGVTITVpagEDPLQFLFSETPG-VV 917
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 504382659 677 VTVAPED-QAAFEALNGP---AELIGRVQAAPQFDVTTVSHQ----FSIPLEELQ 723
Cdd:PHA03366 918 IEVPPSHlSAVLTRLRSRniiCYPIGTVGPSGPSNTFSVSHNgtvlFRESLSSLR 972
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
81-352 |
2.07e-12 |
|
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: 67.95 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 81 AGVIDIGE--GKAVVFKAESHNHPSAVEPYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGD-LNLPHTQHLVDRIVAGI 157
Cdd:cd02204 2 AAVLRIPGetDKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNpEKPEGEMGQLVEAVLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 158 GGYGNAIGIPTVGG------ETNfDHTYARNPLVNAmcVGIM-DKDQIQKGKAAGVGNALIYVGAKTGRDGINGASFASG 230
Cdd:cd02204 82 GDACRALGTPVIGGkdslynETE-GVAIPPTLVIGA--VGVVdDVRKIVTLDFKKEGDLLYLIGETKDELGGSEYALAYH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 231 DFSDEeaadrsAVQVGDPFMEKLLMDACLEITQDHQqaLVGIQDMGAAGLVSSSVEMAGKANSGMEMDLDLIPqreanmT 310
Cdd:cd02204 159 GLGGG------APPLVDLEREKALFDAVQELIKEGL--VLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDD------A 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 504382659 311 PFEIMLSESQERMLLCVRAgfEQEVLDVFAAYDLDAAVVGHV 352
Cdd:cd02204 225 EDELLFSESLGRVLVEVKP--ENEEVFEAEEAGVPATVIGTV 264
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
427-700 |
1.85e-11 |
|
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).
Pssm-ID: 100030 [Multi-domain] Cd Length: 291 Bit Score: 65.65 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 427 RRY--DAQVQTNTVVLPGSDAAVIRIRGthRALAMTTDS--KGR--YLYLDPKVGAAMSVAEAARNLAASGAEPLGITdc 500
Cdd:cd02194 7 DRLfkRLGAGPGVLLGIGDDAAVLKPPG--GRLVVTTDTlvEGVhfPPDTTPEDIGWKALAVNLSDLAAMGARPLGFL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 501 LNFG-DPTKPEAFyeLAEAAKGIIAATKAFNAPVISGNVslyNETNGKAIyptpMIGMVGLIEDLSTITTANFKhADDLL 579
Cdd:cd02194 83 LSLGlPPDTDEEW--LEEFYRGLAEAADRYGVPLVGGDT---TSGSELVI----SVTALGEVEKGKPLRRSGAK-PGDLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 580 YLVGeTHGD-FNGseLQKLQTGevagrLFDFDLDAEKANQQF--------VLTAIRQHFVTAAHDLSDgGLLVALAEMGF 650
Cdd:cd02194 153 YVTG-TLGDaAAG--LALLLGG-----LKLPEELYEELIERHlrpeprleLGRALAEGLATAMIDISD-GLLADLGHIAE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504382659 651 TNQLGAQVKVD-LPTSWGFSETQGR---------------FLVTVAPED-QAAFEALNGPAELIGRV 700
Cdd:cd02194 224 ASGVGAVIDLDkLPLSPALRAAELGedalelalsggedyeLLFTVPPENaEAAAAKLGVPVTVIGRV 290
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
62-352 |
2.61e-11 |
|
AIR synthase (PurM) related protein, subgroup 1 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: 100037 [Multi-domain] Cd Length: 298 Bit Score: 65.31 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 62 ILRQFWTKNDRVLMGPGEG--AGVIDIGEGKAVVfkaeshnhpsAVEPYEGAATGVG--GIIR---DIFSIGAKPVAMLD 134
Cdd:cd06061 14 ILKNLGADRDEVLVGPGGGedAAVVDFGGKVLVV----------STDPITGAGKDAGwlAVHIaanDIATSGARPRWLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 135 slafgDLNLP--HTQHLVDRIVAGIGGYGNAIGIPTVGGETNFdhTYARN-PLVNAMCVGIMDKDQIQKGKAAGVGNALI 211
Cdd:cd06061 84 -----TLLLPpgTDEEELKAIMREINEAAKELGVSIVGGHTEV--TPGVTrPIISVTAIGKGEKDKLVTPSGAKPGDDIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 212 YvgakTGRDGINGASFASGDFsDEEAADRsavqVGDPFMEKLL-MDACLEITQDHQQAL-VGIQDMGAA---GLVSSSVE 286
Cdd:cd06061 157 M----TKGAGIEGTAILANDF-EEELKKR----LSEEELREAAkLFYKISVVKEALIAAeAGVTAMHDAtegGILGALWE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504382659 287 MAGKANSGMEMDLDLIPQREA--------NMTPFEIMLSESqerMLLCVRAGFEQEVLDVFAAYDLDAAVVGHV 352
Cdd:cd06061 228 VAEASGVGLRIEKDKIPIRQEtkeicealGIDPLRLISSGT---LLITVPPEKGDELVDALEEAGIPASVIGKI 298
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
469-709 |
3.02e-11 |
|
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: 65.19 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 469 YLDPKVGAAMSVAEAARNLAASGAEPLGITDCLNFGDPTKPEAFYE--------LAEAAKGIIAATKAFNAPVISGNVSL 540
Cdd:cd02203 40 AIEPFGGAATGVGGIIRDILSMGARPIALLDGLRFGDLDIPGYEPKgklsprriLDGVVAGISDYGNCIGIPTVGGEVRF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 541 YNETNGKAIyptpMIGM-VGLIEDlSTITTANFKHADDLLYLVGET------HG--------DFNGSELQK--LQTGeva 603
Cdd:cd02203 120 DPSYYGNPL----VNVGcVGIVPK-DHIVKSKAPGPGDLVVLVGGRtgrdgiGGatfsskelSENSSELDRpaVQVG--- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 604 grlfdfDLDAEKANQQFVLTAIRQHFVTAAHDLSDGGLLVALAEMGFTNQLGAQVKVDL---------PTS-WGfSETQG 673
Cdd:cd02203 192 ------DPFMEKKLQEAILEARETGLIVGIQDLGAGGLSSAVSEMAAKGGLGAEIDLDKvplrepgmsPWEiWI-SESQE 264
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 504382659 674 RFLVTVAPEDQAAFEAL----NGPAELIGRVQAAPQFDVT 709
Cdd:cd02203 265 RMLLVVPPEDLEEFLAIckkeDLEAAVIGEVTDDGRLRLY 304
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
442-700 |
3.70e-11 |
|
AIR synthase (PurM) related protein, subgroup 1 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: 100037 [Multi-domain] Cd Length: 298 Bit Score: 64.93 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 442 GSDAAVIRIRGthRALAMTTDSkgryLYLDPKVGAAMSVAEAARNLAASGAEPLGITDCLNFGDPTKPEafyELAEAAKG 521
Cdd:cd06061 32 GEDAAVVDFGG--KVLVVSTDP----ITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEE---ELKAIMRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 522 IIAATKAFNAPVISGNVslynetngkAIYP--TPMIG---MVGLIEDLSTITTANFKHADDLL----------YLVGETH 586
Cdd:cd06061 103 INEAAKELGVSIVGGHT---------EVTPgvTRPIIsvtAIGKGEKDKLVTPSGAKPGDDIVmtkgagiegtAILANDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 587 GDfngsELQKLQTGEV---AGRLFDFDLDAEKAnqqfvlTAIRQHFVTAAHDLSDGGLLVALAEMGFTNQLGAQVKVDLP 663
Cdd:cd06061 174 EE----ELKKRLSEEElreAAKLFYKISVVKEA------LIAAEAGVTAMHDATEGGILGALWEVAEASGVGLRIEKDKI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 504382659 664 TSWgfSETQ----------------GRFLVTVAPED----QAAFEALNGPAELIGRV 700
Cdd:cd06061 244 PIR--QETKeicealgidplrlissGTLLITVPPEKgdelVDALEEAGIPASVIGKI 298
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
68-362 |
5.24e-11 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 64.42 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 68 TKNDRVLMGPGEGAGVIDIGEGkAVVFKAESHnHPSAVE--PYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGDLNlpH 145
Cdd:COG2144 33 ASSGGTAAAFGDDAAAIPDGDG-YLLLAAEGI-WPKFVEadPWFAGYCSVLVNVSDIAAMGGRPLAVVDALWSSDEE--A 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 146 TQHLVDRIVAGIGGYGnaigIPTVGGETNFDHTYarnplvNAMCVGIMdkdqiqkGKAAgvgnALIYV-GAKTGRDGI-- 222
Cdd:COG2144 109 AAPVLAGMRAASRKFG----VPIVGGHTHPDTPY------NALAVAIL-------GRAK----KLLTSfTARPGDRLIaa 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 223 ---NGASFASGDFSDeEAADRSAVQVGDPFM------EKLLMDACLEITQdhqqalvgiqdmgaAGLVSSSVEMAGKANS 293
Cdd:COG2144 168 idlDGRYHPPFPYWD-ATTGKPPERLRAQLEllpelaEAGLVTAAKDISN--------------PGIIGTLGMLLECSGV 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504382659 294 GMEMDLDLIPqREANMtPFEIMLsesqeRM------LLCVRAGFEQEVLDVFAAYDLDAAVVGHVIEGHQYRLYH 362
Cdd:COG2144 233 GATIDLDAIP-RPEGV-DLERWL-----KAfpsfgfLLTVPPENVDEVLARFAARGITAAVIGEVTDSRRLTLRD 300
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
77-351 |
5.91e-11 |
|
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: 63.77 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 77 PGEGAGVIdIGEGKAVVFKAESHnHPSAVE--PYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGDlnlphtQHLVDRIV 154
Cdd:cd02192 34 LGDDAAAI-PDGDGYLLLAADGI-WPSLVEadPWWAGYCSVLVNVSDIAAMGGRPLAMVDALWSPS------AEAAAQVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 155 AGIGGYGNAIGIPTVGGETNFDHTYarnplvNAMCV---GIMDKDQIQKGKAAgVGNALIYVGAKTGRDGINGASF--AS 229
Cdd:cd02192 106 EGMRDAAEKFGVPIVGGHTHPDSPY------NALSVailGRARKDLLISFGAK-PGDRLILAIDLDGRVHPSPPPNwdAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 230 GDFSDEEAADRSAVQVGdpFMEKLLMDACLEITQdhqqalvgiqdmgaAGLVSSSVEMAGKANSGMEMDLDLIPqREANM 309
Cdd:cd02192 179 TMKSPALLRRQIALLPE--LAERGLVHAAKDISN--------------PGIIGTLGMLLEASGVGAEIDLDAIP-RPEGV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 504382659 310 TPFEIMLSESQERMLLCVRAGFEQEVLDVFAAYDLDAAVVGH 351
Cdd:cd02192 242 DLERWLKCFPGFGFLLTARPENADEVVAVFAAVGITAAVIGE 283
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
412-708 |
1.44e-06 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 50.99 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 412 AMMGtptiadKSSLYRRYDAQVQTNTVVLPGSDAAVIRIRGTHRaLAMTTDS--KGRYLYLDPkvgaaMSVAEAAR---- 485
Cdd:PRK05731 1 MAMG------EFDLIARLFARRPSSRELGIGDDAALLGPPPGQR-LVVSTDMlvEGVHFRPDW-----SSPEDLGYkala 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 486 -NL---AASGAEPLGITdcLNFGDPTK-PEAfyELAEAAKGIIAATKAFNAPVISGNVslyneTNGKAIYPTpmIGMVGL 560
Cdd:PRK05731 69 vNLsdlAAMGARPAAFL--LALALPKDlDEA--WLEALADGLFELADRYGAELIGGDT-----TRGPDLSIS--VTAIGD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 561 IEDLSTITTANFKhADDLLYLVGeTHGDfNGSELQKLQTGEVAGRLFDFDL-DAEKANQ---QFVLtAIRQhFVTAAHDL 636
Cdd:PRK05731 138 VPGGRALRRSGAK-PGDLVAVTG-TLGD-SAAGLALLLNGLRVPDADAAALiSRHLRPQprvGLGQ-ALAG-LASAAIDI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 637 SDgGLLVALAEMGFTNQLGAQVKVD-LPTSWGFSETQGR---------------FLVTVAPED----QAAFEALNGPAEL 696
Cdd:PRK05731 213 SD-GLAADLGHIAEASGVGADIDLDaLPISPALREAAEGedalrwalsggedyeLLFTFPPENrgalLAAAGHLGVGVTI 291
|
330
....*....|..
gi 504382659 697 IGRVQAAPQFDV 708
Cdd:PRK05731 292 IGRVTEGEGVVV 303
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
121-211 |
3.46e-05 |
|
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100032 [Multi-domain] Cd Length: 297 Bit Score: 46.31 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 121 DIFSIGAKPVAMLDSLAFGDLNLPhtqhLVDRIVAGIGGYGNAIGIPTVGGET----------NFDhtyarnplVNAMCV 190
Cdd:cd02196 56 DILCQGAEPLFFLDYIATGKLDPE----VAAEIVKGIAEGCRQAGCALLGGETaempgvyaegEYD--------LAGFAV 123
|
90 100
....*....|....*....|.
gi 504382659 191 GIMDKDQIQKGKAAGVGNALI 211
Cdd:cd02196 124 GVVEKDKIIDGSKIKPGDVLI 144
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
441-700 |
9.47e-04 |
|
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100031 [Multi-domain] Cd Length: 287 Bit Score: 41.74 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 441 PGSDAAVIRIRGThRALAMTTDskgrYLY---LDPKVGAAMSVAEAARNLAASGAEPLGITDCLNFgdPTKPEAFYE--L 515
Cdd:cd02195 40 TGDDAAVYRLPGG-LALVQTTD----FFPpivDDPYLFGRIAAANALSDIYAMGAKPLSALAIVTL--PRKLPALQEevL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 516 AEAAKGIIAATKAFNAPVISGNvSLYNetngkaiyPTPMIGMV--GLIEDLSTITTANFKHADDLLylvgethgdfngse 593
Cdd:cd02195 113 REILAGGKDKLREAGAVLVGGH-TIEG--------PEPKYGLSvtGLVHPNKILRNSGAKPGDVLI-------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 594 LQK------LQTGEVAGRLFDFDLDA-----EKANQQFVLtAIRQHFVTAAHDLSDGGLLVALAEMGFTNQLGAQVKVD- 661
Cdd:cd02195 170 LTKplgtgiLFAAEMAGLARGEDIDAalesmARLNRAAAE-LLRKYGAHACTDVTGFGLLGHLLEMARASGVSAEIDLDk 248
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 504382659 662 LPtswgFSETQGRFLVTVAPEDQAAFEAL----NGPAELIGRV 700
Cdd:cd02195 249 LP----LLQTSGGLLAAVPPEDAAALLALlkagGPPAAIIGEV 287
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
266-376 |
2.81e-03 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 41.16 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 266 QQALVGIQDMGAAGLVSSSVEMAGKANSGMEMDldlIPQREanmTPFEIMLSESQErMLLCVRAGFEQEVLDVFAAYDLD 345
Cdd:PHA03366 866 EGLVVSGHDVSDGGLIACLAEMALAGGRGVTIT---VPAGE---DPLQFLFSETPG-VVIEVPPSHLSAVLTRLRSRNII 938
|
90 100 110
....*....|....*....|....*....|....
gi 504382659 346 AAVVGHVIE---GHQYRLYHHGKLVCDVPVSSLT 376
Cdd:PHA03366 939 CYPIGTVGPsgpSNTFSVSHNGTVLFRESLSSLR 972
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
31-200 |
4.03e-03 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 40.61 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 31 AELIGHQPNDTEIGLASGMWSEHCAYKYSKPILRQFWTKNDRV-----LMGPGEGAGVIDIGEGKAVVFKAESHNHPSAV 105
Cdd:PRK14090 332 VQLLANAPEEEIVEYTPGEIPEFKRVEFEEVNAREVFEQYDHMvgtdtVLPPGFGAAVMRIKRDGGYSLVTHSRADLALQ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382659 106 EPYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGDlnlPHTQHLvdRIVAGIGGYGNAI---GIPTVGGETNFDHTYARN 182
Cdd:PRK14090 412 DTYWGTFIAVLESVRKTLSVGAEPLAITNCVNYGD---PDVDPV--GLSAMMTALKDACefsGVPVASGNASLYNTYQGK 486
|
170
....*....|....*...
gi 504382659 183 PLVNAMCVGIMDKDQIQK 200
Cdd:PRK14090 487 PIPPTLVVGMLGKVNPQK 504
|
|
| |
