|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
1-635 |
0e+00 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 913.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:PRK01213 101 GAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTVGGEVYFDESYNGNPLVNAMC 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEED-RELRPTVQVGNPFLEKILIESCLEAVQTGLVD 159
Cdd:PRK01213 181 VGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGAS-FASAELSEEsEEKRPAVQVGDPFMEKLLIEACLELIKTGLVV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 160 GLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIG 239
Cdd:PRK01213 260 GIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGKEEEVLAIFEKWDLDAAVIG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 240 QVVDGDAIELIEEGVTKGHIPINLLTD-PPLYRPDGVKPDYLKDLQSyeldrvplPTASPSAVFLDLIASPNISSRVSVY 318
Cdd:PRK01213 340 EVTDDGRLRVYHHGEVVADVPAEALADeAPVYDRPYKEPAYLDELQA--------DPEDLKEALLKLLSSPNIASKEWVY 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 319 RQYDHQVQTNTVIPPGNEAALLRIKGTSKGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNP 398
Cdd:PRK01213 412 EQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGATPLAITDCLNFGNP 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 399 ENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGASm 478
Cdd:PRK01213 492 EKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKRTTSGFKKEGDLIYLLGET- 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 479 vagyTSSLSGSEYLEVIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFGGTVV 557
Cdd:PRK01213 571 ----KDELGGSEYLKVIHGHVGGRpPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMAIAGGLGAEVDLS 646
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392553 558 IEGRWDAALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNVQEGRFSFSGLIDLPMSQLSEIWTQSLERVAGG 635
Cdd:PRK01213 647 DGLRPDALLFSESQGRYVVSVPPENEEAFEALAEAAGVPATRIGVVGGDALKVKGNDTESLEELREAWEGALPRLLGG 724
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
1-632 |
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: 782.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHE--RNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNA 78
Cdd:COG0046 112 GAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDQPpaSPRYILIGVVAGIADYGNCFGVPTVGGEVRFDESYEGNPLVNA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 79 MCIGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEEDREL-RPTVQVGNPFLEKILIESCLEAVQTGL 157
Cdd:COG0046 192 GGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGAT-FASEELGEDSELdRPAVQVGDPFMEKRLIEAILELGDTGL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 158 VDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTV 237
Cdd:COG0046 271 IVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPEKLEEFEAIFERWRLPAAV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 238 IGQVVDGDAIELIEEGVTKGHIPINLLTD-PPLYRPDGVKPDYLKDLQsyeldrVPLPtASPSAVFLDLIASPNISSRVS 316
Cdd:COG0046 351 IGEVTDDGRLVVTDHGETVADLPLDFLAGgAPKYHRPAKRPAYLEPLD------LPEP-IDLEEALLRLLSSPNVASKEW 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 317 VYRQYDHQVQTNTVI-PPGNEAALLRIKGTSKGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNF 395
Cdd:COG0046 424 LYRQYDREVGGNTVRdPGVADAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARMAVAEAARNLAAVGAEPLAITDCLNW 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 396 GNPENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNET--GNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVL 473
Cdd:COG0046 504 GNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETkdGKVAIPPTPVIGAVGLVDDVRKTVTPDLKKEGDLLYL 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 474 LGASmvagyTSSLSGSEYLEVIhNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGF 552
Cdd:COG0046 584 IGET-----KNELGGSEYAQVL-GQLGGEpPDVDLEAEKALFEAVQELIREGLILAAHDVSDGGLAVALAEMAFAGGLGA 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 553 GGTV--VIEGRWDAALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNV-QEGRFSFSG----LIDLPMSQLSEIW 625
Cdd:COG0046 658 DIDLdaLGDLRPDAALFSESQGRAVVQVAPEDAEAVEALLAEAGLPAHVIGTVtGDDRLVIRRggetLLSLSLAELRDAW 737
|
....*..
gi 1301392553 626 TQSLERV 632
Cdd:COG0046 738 EETLPRL 744
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
1-632 |
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: 757.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:TIGR01736 89 GAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNGNPLVNVMC 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEED--RELRPTVQVGNPFLEKILIESCLEAVQTGLV 158
Cdd:TIGR01736 169 VGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGAT-FASEELSEEaeEEDRPAVQVGDPFTEKLLIEATLEAVDTGLV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 159 DGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVI 238
Cdd:TIGR01736 248 KGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYELPASVI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 239 GQVVDGDAIELIEEGVTKGHIPINLLTDPPLYRPDGVKPDYlkdlqsYELDRVPLPTASPSAVFLDLIASPNISSRVSVY 318
Cdd:TIGR01736 328 GEVTDEGRIRLYYKGEVVADLPIELLADAPEYERPSEPPKY------PEEEKEPEPPADLEDAFLKVLSSPNIASKEWVY 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 319 RQYDHQVQTNTVIPPGNEAALLRIKGTSK-GLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGN 397
Cdd:TIGR01736 402 RQYDHEVQTRTVVKPGEDAAVLRIKETGKlGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVDCLNFGN 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 398 PENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGAS 477
Cdd:TIGR01736 482 PERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLLTSNFKKEGDAIYLIGET 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 478 mvagyTSSLSGSEYLEVIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFggTV 556
Cdd:TIGR01736 562 -----KDELGGSEYLRVIHGIVSGQvPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGA--EV 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 557 VIEG----RWDAALFGEDQSRIVVSINHKDldlCSSVCEEYSVEWCVLGNVQEGRFSFSGL---IDLPMSQLSEIWTQSL 629
Cdd:TIGR01736 635 DIDEiasaRPDELLFSESNGRAIVAVPEEK---AEEAVKSKGVPAKVIGKTGGDRLTIKTGddtISVSVKELRDAWEEAL 711
|
...
gi 1301392553 630 ERV 632
Cdd:TIGR01736 712 PEY 714
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
1-263 |
9.57e-123 |
|
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: 366.03 E-value: 9.57e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHE--------RNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTG 72
Cdd:cd02203 46 GAATGVGGIIRDILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 73 NPLVNAMCIGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASGlASRTFEEDREL--RPTVQVGNPFLEKILIESCL 150
Cdd:cd02203 126 NPLVNVGCVGIVPKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATF-SSKELSENSSEldRPAVQVGDPFMEKKLQEAIL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 151 EAVQTGLVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDK 230
Cdd:cd02203 205 EARETGLIVGIQDLGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKK 284
|
250 260 270
....*....|....*....|....*....|...
gi 1301392553 231 WDVENTVIGQVVDGDAIELIEegvtKGHIPINL 263
Cdd:cd02203 285 EDLEAAVIGEVTDDGRLRLYY----KGEVVADL 313
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
1-451 |
2.49e-103 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 326.04 E-value: 2.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILAMGARPIALLNSLRFgpldhernRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:PRK14090 81 GAATGVGGIIRDVLAMGARPTAIFDSLHM--------SRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNVLA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEEDRELRPTVQVGNPFLEKILIESCLEAVQTGLVDG 160
Cdd:PRK14090 153 AGVVRNDMLVDSKASRPGQVIVIFGGATGRDGIHGAS-FASEDLTGEKATKLSIQVGDPFAEKMLIEAFLEMVEEGLVEG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 161 LQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIGQ 240
Cdd:PRK14090 232 AQDLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGDIVAE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 241 VVDGDAIELIEEGVTKGHIPINLLTDPPlyrpdgvkpdyLKDLQSYELDRVPlptaspsaVFLDLIASPNISSRvsVYRQ 320
Cdd:PRK14090 312 VIDDPIYRVMYRDDLVMEVPVQLLANAP-----------EEEIVEYTPGEIP--------EFKRVEFEEVNARE--VFEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 321 YDHQVQTNTVIPPGNEAALLRIKGTSkGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNPEN 400
Cdd:PRK14090 371 YDHMVGTDTVLPPGFGAAVMRIKRDG-GYSLVTHSRADLALQDTYWGTFIAVLESVRKTLSVGAEPLAITNCVNYGDPDV 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1301392553 401 PEVyyQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVG 451
Cdd:PRK14090 450 DPV--GLSAMMTALKDACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLG 498
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
336-603 |
7.75e-92 |
|
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: 284.81 E-value: 7.75e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 336 EAALLRIKGTS-KGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNPENPE-VYYQLEHCVRG 413
Cdd:cd02204 1 DAAVLRIPGETdKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKPEgEMGQLVEAVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 414 IVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGASmvagyTSSLSGSEYLE 493
Cdd:cd02204 81 LGDACRALGTPVIGGKDSLYNETEGVAIPPTLVIGAVGVVDDVRKIVTLDFKKEGDLLYLIGET-----KDELGGSEYAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 494 VIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFGGTVVIEGRWDAALFGEDQS 572
Cdd:cd02204 156 AYHGLGGGApPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDDAEDELLFSESLG 235
|
250 260 270
....*....|....*....|....*....|.
gi 1301392553 573 RIVVSINHKDLDLCSsvCEEYSVEWCVLGNV 603
Cdd:cd02204 236 RVLVEVKPENEEVFE--AEEAGVPATVIGTV 264
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
1-241 |
2.55e-44 |
|
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: 159.38 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILAMG--ARPIALLNSLRFGPLDHERNRYLFEGVvSGISGYGNCIGIPNIGGEVGFATSY-------- 70
Cdd:cd02193 21 GAATGVGGAIRDIAATGidAKPIALSANWMASAGHPGEDAILYDAV-KGVAELCNQLGLPIPVGKDRMSMKTrwqegneq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 71 ---TGNPLVNAMCIGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEEDRELRPTVQVGNPFLEKILIE 147
Cdd:cd02193 100 remTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKGHNGLGGTA-LASVALSYRQLGDKSAQVRDPAQEKGFYE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 148 SCLEAVQTGLVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQV 227
Cdd:cd02193 179 AMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDEPDMEPLEIALFESQERGVIQVRAEDRDAVEEA 258
|
250
....*....|....
gi 1301392553 228 FDKWDVENTVIGQV 241
Cdd:cd02193 259 QYGLADCVHVLGQA 272
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
98-250 |
2.26e-32 |
|
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: 122.07 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 98 GNVLLLVGSgtgrDGIHGASGLASRTFEEDrELRPTVQVGNPFLEKILIES-CLEAVQTGLVDGLQDLGAAGLTSASVEC 176
Cdd:pfam02769 3 GDVLILLGS----SGLHGAGLSLSRKGLED-SGLAAVQLGDPLLEPTLIYVkLLLAALGGLVKAMHDITGGGLAGALAEM 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1301392553 177 ASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIGQVVDGDAIELI 250
Cdd:pfam02769 78 APASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVI 151
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
348-452 |
6.56e-24 |
|
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: 96.36 E-value: 6.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 348 GLSAATDGNSRACYLDPFVG-GVISVAEACRNVSCTGAEPIALTNCLNFgnPENPEVYYQLEHCVRGIVSASESFDAPVI 426
Cdd:pfam00586 4 AVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLAL--PGGPEVEWVLEEIVEGIAEACREAGVPLV 81
|
90 100
....*....|....*....|....*.
gi 1301392553 427 SGNVSLYNETGNksiyPTPVIGAVGL 452
Cdd:pfam00586 82 GGDTSFDPEGGK----PTISVTAVGI 103
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
2-84 |
4.39e-22 |
|
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: 91.35 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 2 AATGVGGIVRDILAMGARPIALLNSLRFGPLDHErnRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYtGNPLVNAMCI 81
Cdd:pfam00586 25 GAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEV--EWVLEEIVEGIAEACREAGVPLVGGDTSFDPEG-GKPTISVTAV 101
|
...
gi 1301392553 82 GLV 84
Cdd:pfam00586 102 GIV 104
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
1-240 |
1.32e-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: 87.84 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERnryLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTG-NPLVNAM 79
Cdd:cd00396 20 GGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVD---ILEDVVDGVAEACNQLGVPIVGGHTSVSPGTMGhKLSLAVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 80 CIGLVEIknlVRATSGDK---GNVLLLVGsgtgrdgihgasglasrtfeedrelrptvqvgnpflekilIESCLEAVQTG 156
Cdd:cd00396 97 AIGVVEK---DRVIDSSGarpGDVLILTG----------------------------------------VDAVLELVAAG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 157 LVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGME-----PYEIMLSETQERMLLSVKRDNLNRVSQVFDKW 231
Cdd:cd00396 134 DVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWlcvehIEEALLFNSSGGLLIAVPAEEADAVLLLLNGN 213
|
....*....
gi 1301392553 232 DVENTVIGQ 240
Cdd:cd00396 214 GIDAAVIGR 222
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
328-623 |
9.53e-17 |
|
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: 84.28 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 328 NTVIPPGNEAALLRIKGtskGLSAATDGNSR--ACYLDPF------VGGVIsvaeacRNVSCTGAEPIALTNCLNFGNPE 399
Cdd:TIGR01736 51 NVIQGPGEDAGVVDIGD---GYAVVFKMESHnhPSAIEPYngaatgVGGIL------RDILSMGARPIALLDSLRFGPLD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 400 NPEVYYQLEHCVRGIVSASESFDAPVISGNVS---LYNEtgnksiYPTPVIGAVGLTenvsRHCDIAF---KEVGDIVVL 473
Cdd:TIGR01736 122 DPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEfdeSYNG------NPLVNVMCVGLV----RKDDIVTgkaKGPGNKLVL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 474 LGASM----VAGYT-SSLSGSEYLEV-------IHNLVAGQPSIDidkelsvqaACRRLISEGLAKSAHDCSDGGLAVAI 541
Cdd:TIGR01736 192 VGGKTgrdgIGGATfASEELSEEAEEedrpavqVGDPFTEKLLIE---------ATLEAVDTGLVKGIKDLGAAGLTSAS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 542 VESSIQGnlGFGGTVVIE---------GRWDAALfGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNV-QEGRF--S 609
Cdd:TIGR01736 263 SEMAAKG--GLGAEIYLDkvplrepgmTPYEIML-SESQERMLLVVAPEDVEEVLEIFEKYELPASVIGEVtDEGRIrlY 339
|
330
....*....|....*.
gi 1301392553 610 FSG--LIDLPMSQLSE 623
Cdd:TIGR01736 340 YKGevVADLPIELLAD 355
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
1-241 |
1.04e-16 |
|
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: 80.27 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILAMGARPIALLNSLRFG-PLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGF--ATSYTGNP--L 75
Cdd:cd02204 33 GAALAVAEAVRNLVAVGADPLAITDCLNFGnPEKPEGEMGQLVEAVLGLGDACRALGTPVIGGKDSLynETEGVAIPptL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 76 VNAMcIGLVE-IKNLVRATSGDKGNVLLLVGSGTGRDGihgASGLASRTFEEDRELRPTVqvgNPFLEKILIESCLEAVQ 154
Cdd:cd02204 113 VIGA-VGVVDdVRKIVTLDFKKEGDLLYLIGETKDELG---GSEYALAYHGLGGGAPPLV---DLEREKALFDAVQELIK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 155 TGLVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDdgmepyEIMLSETQERMLLSVKRDNLNRVSQVFdkWDVE 234
Cdd:cd02204 186 EGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDDAED------ELLFSESLGRVLVEVKPENEEVFEAEE--AGVP 257
|
....*..
gi 1301392553 235 NTVIGQV 241
Cdd:cd02204 258 ATVIGTV 264
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
360-608 |
3.32e-15 |
|
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: 76.74 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 360 CYLDPF------VGGVIsvaeacRNVSCTGAEPIALTNCLNFGNPENPEVY--------YQLEHCVRGIVSASESFDAPV 425
Cdd:cd02203 39 SAIEPFggaatgVGGII------RDILSMGARPIALLDGLRFGDLDIPGYEpkgklsprRILDGVVAGISDYGNCIGIPT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 426 ISGNVSLYnetGNKSIYPTPVIGAVGL--TENVSRHCDIafkEVGDIVVLLG-------------ASMVAGYTSSLSGSe 490
Cdd:cd02203 113 VGGEVRFD---PSYYGNPLVNVGCVGIvpKDHIVKSKAP---GPGDLVVLVGgrtgrdgiggatfSSKELSENSSELDR- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 491 ylevihnlvagqPSIDI-DKELS--VQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGfggtVVIEgrWDAALF 567
Cdd:cd02203 186 ------------PAVQVgDPFMEkkLQEAILEARETGLIVGIQDLGAGGLSSAVSEMAAKGGLG----AEID--LDKVPL 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1301392553 568 GED------------QSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNV-QEGRF 608
Cdd:cd02203 248 REPgmspweiwisesQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVtDDGRL 301
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
466-607 |
2.81e-12 |
|
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: 64.67 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 466 EVGDIVVLLGasmvagyTSSLSGSEYLEVIHNL----VAGQPSIDIDKELSVQAACRRLI-SEGLAKSAHDCSDGGLAVA 540
Cdd:pfam02769 1 KPGDVLILLG-------SSGLHGAGLSLSRKGLedsgLAAVQLGDPLLEPTLIYVKLLLAaLGGLVKAMHDITGGGLAGA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1301392553 541 IVESSIQGNLGF-----GGTVVIEGRWD-AALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNVQEGR 607
Cdd:pfam02769 74 LAEMAPASGVGAeidldKVPIFEELMLPlEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGG 146
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
352-551 |
5.23e-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: 65.88 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 352 ATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNPENPEVyyqLEHCVRGIVSASESFDAPVISGNVS 431
Cdd:cd00396 5 STDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDI---LEDVVDGVAEACNQLGVPIVGGHTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 432 LYNETGnkSIYPTPVIGAVGLTENVsRHCDIAFKEVGDIVVLLGasmvagytsslsgseYLEVIHnlvagqpsididkel 511
Cdd:cd00396 82 VSPGTM--GHKLSLAVFAIGVVEKD-RVIDSSGARPGDVLILTG---------------VDAVLE--------------- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1301392553 512 svqaacrrLISEGLAKSAHDCSDGGLAVAIVESSIQGNLG 551
Cdd:cd00396 129 --------LVAAGDVHAMHDITDGGLLGTLPELAQASGVG 160
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
362-603 |
1.89e-11 |
|
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: 65.01 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 362 LDPFVGGVISVAEACRNVSCTG--AEPIALTNCLNFGNPeNPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNK 439
Cdd:cd02193 16 IDPAAGAATGVGGAIRDIAATGidAKPIALSANWMASAG-HPGEDAILYDAVKGVAELCNQLGLPIPVGKDRMSMKTRWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 440 SIY--------PTPVIGAVGLTENVsRHCDIAFKEVGDIVVLLGASmvAGYTSSLSGSEYLEVIHNLVAGQPSIDID--- 508
Cdd:cd02193 95 EGNeqremthpPSLVISAFGRVRDD-RHTLPQLSTEGNALLLIGGG--KGHNGLGGTALASVALSYRQLGDKSAQVRdpa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 509 KELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLgfGGTVVIE---------GRWDAALFgEDQSRIVVSIN 579
Cdd:cd02193 172 QEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHC--GVQVDLAalgddepdmEPLEIALF-ESQERGVIQVR 248
|
250 260
....*....|....*....|....
gi 1301392553 580 HKDLDLCSSVCEEYSVEWCVLGNV 603
Cdd:cd02193 249 AEDRDAVEEAQYGLADCVHVLGQA 272
|
|
| PRK05297 |
PRK05297 |
phosphoribosylformylglycinamidine synthase; Provisional |
1-224 |
4.16e-11 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 66.36 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 1 GAATGVGGIVRDILA--MGARPIALL------NsLR-----------FG-------PLDhernrYLFEGVVSGiSGYGNC 54
Cdd:PRK05297 303 GAATGSGGEIRDEGAtgRGSKPKAGLtgfsvsN-LRipgfeqpweedYGkperiasALD-----IMIEGPLGG-AAFNNE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 55 IGIPNIGG--------EVGFATSYTG--NPLVNAMCIG-----LVEIKNLvraTSGDKGNVL----LLVGSGTGrdgihG 115
Cdd:PRK05297 376 FGRPNLLGyfrtfeqkVNSHNEEVRGyhKPIMLAGGIGniradHVQKGEI---PVGAKLIVLggpaMRIGLGGG-----A 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 116 ASGLASRTFEEDRELrPTVQVGNPFLEKI---LIESCleaVQTGlvDG-----LQDLGAAGLTSASVECASNGGTGIKLF 187
Cdd:PRK05297 448 ASSMASGQSSEDLDF-ASVQRGNPEMERRcqeVIDRC---WQLG--DDnpilsIHDVGAGGLSNAFPELVNDGGRGGRFD 521
|
250 260 270
....*....|....*....|....*....|....*..
gi 1301392553 188 MDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRV 224
Cdd:PRK05297 522 LRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELF 558
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
12-241 |
2.41e-09 |
|
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: 58.76 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 12 DILAMGARPIALLNSLRFgPLDHERNRylFEGVVSGISGYGNCIGIPNIGGEVGFATSyTGNPLVNAMCIGLVEIKNLVR 91
Cdd:cd06061 70 DIATSGARPRWLLVTLLL-PPGTDEEE--LKAIMREINEAAKELGVSIVGGHTEVTPG-VTRPIISVTAIGKGEKDKLVT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 92 ATSGDKGNVLLLVGSGtgrdGIhGASGLASRTFEE-------DRELRPTVQvgnpFLEKI-LIESCLEAVQTGlVDGLQD 163
Cdd:cd06061 146 PSGAKPGDDIVMTKGA----GI-EGTAILANDFEEelkkrlsEEELREAAK----LFYKIsVVKEALIAAEAG-VTAMHD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 164 LGAAGLTSASVECASNGGTGIKLFMDKIPLRDD--------GMEPYEIMLSETqerMLLSVKRDNLNRVSQVFDKWDVEN 235
Cdd:cd06061 216 ATEGGILGALWEVAEASGVGLRIEKDKIPIRQEtkeicealGIDPLRLISSGT---LLITVPPEKGDELVDALEEAGIPA 292
|
....*.
gi 1301392553 236 TVIGQV 241
Cdd:cd06061 293 SVIGKI 298
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
12-250 |
2.05e-07 |
|
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440376 [Multi-domain] Cd Length: 321 Bit Score: 53.23 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 12 DILAMGARPIALLNSLRFGP-LDHERnrylFEGVVSGISGYGNCIGIPNIGGEvgfaTSyTGNPLV-NAMCIGLVEIKNL 89
Cdd:COG0611 73 DLAAMGARPLAALLSLALPPdTDVEW----LEEFARGLAEAADRYGVDLVGGD----TT-RSPELTiSVTAIGEVPGGRP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 90 VR---ATSGDkgnvLLLVgSGTgrdgiHGASGLA-------SRTFEEDRE------LRPTVQVGnpflekiLIescLEAV 153
Cdd:COG0611 144 LLrsgARPGD----LVYV-TGT-----LGDAAAGlalllrgLRVPLEAREyllerhLRPEPRLA-------LG---RALA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 154 QTGLV-------DGL-QDLGAagLTSASvecasngGTGIKLFMDKIPLRDD------GMEPYEIMLS-----EtqerMLL 214
Cdd:COG0611 204 EAGLAtamidisDGLaADLGH--IAEAS-------GVGAEIDLDALPLSPAlreaalGLDPLELALTggedyE----LLF 270
|
250 260 270
....*....|....*....|....*....|....*.
gi 1301392553 215 SVKRDNLNRVSQVFDKWDVenTVIGQVVDGDAIELI 250
Cdd:COG0611 271 TVPPEALEALEAAALGVPL--TVIGRVTEGEGVTLD 304
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
95-255 |
2.42e-06 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 50.92 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 95 GDKGnVLLLVGSGTGRDGIhGASGLAsRTFEedrelrptvQVGN--PFLEKIL-IESCLEAVQTGLVDGL----QDLGAA 167
Cdd:PLN03206 824 GDDG-VLLHVDLGKGKRRL-GGSALA-QAYD---------QIGDdcPDLDDVAyLKKAFEATQDLIAKRLisagHDISDG 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 168 GLTSASVECASNGGTGIKLfmdKIPLRDDGmePYEIMLSEtQERMLLSVKRDNLNRVSQVFDKWDVENTVIGQVVDGDAI 247
Cdd:PLN03206 892 GLVVTLLEMAFAGNCGINV---DLPSSGHS--AFETLFAE-ELGLVLEVSRKNLDAVMEKLAAAGVTAEVIGQVTASPLI 965
|
....*...
gi 1301392553 248 ELIEEGVT 255
Cdd:PLN03206 966 EVKVDGAT 973
|
|
| PHA03366 |
PHA03366 |
FGAM-synthase; Provisional |
362-634 |
4.68e-06 |
|
FGAM-synthase; Provisional
Pssm-ID: 223058 [Multi-domain] Cd Length: 1304 Bit Score: 50.02 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 362 LDPFVGGVISVAEACRNvsctgaepIALTNCLNFGN---------PENPEVYYQLEHCVRG-------------IVSASE 419
Cdd:PHA03366 704 LDPILGAKYAIVEALTN--------LMLAPVANLEDititlsvtwPPTDQAASELYRALAAckefcrelgvnftFTSASS 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 420 SFDAPVISGNVSLYNE---TGN---KSIYP--TPVigavgltenvsrhcdiaFKEVGDIVVLLgaSMVAGYTssLSGSEY 491
Cdd:PHA03366 776 SPRQDQPPQPGPLFNTivfTASapvPSSTPrlTPD-----------------LKKPGSALVHL--SISPEYT--LAGSVF 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 492 lEVIHNLVAGQPsIDID----KEL--SVQAacrrLISEGLAKSAHDCSDGGLAVAIVESSIQGnlGFGGTVVIEGRWDAA 565
Cdd:PHA03366 835 -EQIFGLKSGTL-PDISpsylKNLfrAVQH----LISEGLVVSGHDVSDGGLIACLAEMALAG--GRGVTITVPAGEDPL 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1301392553 566 --LFGEDQSrIVVSINHKDLDLCSSVCEEYSVEWCVLGNV----QEGRFSFSglidlpmSQLSEIWTQSLERVAG 634
Cdd:PHA03366 907 qfLFSETPG-VVIEVPPSHLSAVLTRLRSRNIICYPIGTVgpsgPSNTFSVS-------HNGTVLFRESLSSLRS 973
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
520-631 |
6.56e-06 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 49.38 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 520 LISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFGGTVVIEGRWD-AALFGEDQSrIVVSINHKDLDLCSSVCEEYSVEWC 598
Cdd:PLN03206 876 LIAKRLISAGHDISDGGLVVTLLEMAFAGNCGINVDLPSSGHSAfETLFAEELG-LVLEVSRKNLDAVMEKLAAAGVTAE 954
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1301392553 599 VLGNVQEGR---FSFSGL--IDLPMSQLSEIWTQS---LER 631
Cdd:PLN03206 955 VIGQVTASPlieVKVDGAtcLSEKTASLRDMWEETsfqLEK 995
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
329-552 |
1.33e-05 |
|
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: 47.59 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 329 TVIPPGNE--AALLRIKGtsKGLSAATDgnsrACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNF--GNPENpevy 404
Cdd:cd06061 25 VLVGPGGGedAAVVDFGG--KVLVVSTD----PITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLppGTDEE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 405 yQLEHCVRGIVSASESFDAPVISGNVslynETGNKSIYPTPVIGAVGLTENVSRHCDIAFKeVGDIVVLLGASMVAGyTS 484
Cdd:cd06061 95 -ELKAIMREINEAAKELGVSIVGGHT----EVTPGVTRPIISVTAIGKGEKDKLVTPSGAK-PGDDIVMTKGAGIEG-TA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 485 SLSGSEYLEVIHNLVAG--QPSIDIDKELSVQAAcRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGF 552
Cdd:cd06061 168 ILANDFEEELKKRLSEEelREAAKLFYKISVVKE-ALIAAEAGVTAMHDATEGGILGALWEVAEASGVGL 236
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
12-242 |
1.20e-04 |
|
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: 44.47 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 12 DILAMGARPIALLNSLRFGPLDHERNrylFEGVVSGISGYGNCIGIPNIGGEvgfaTSyTGNPLV-NAMCIGLVEIKNLV 90
Cdd:cd02194 70 DLAAMGARPLGFLLSLGLPPDTDEEW---LEEFYRGLAEAADRYGVPLVGGD----TT-SGSELViSVTALGEVEKGKPL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 91 R---ATSGDkgnvlLLVGSGTgrdgiHGASGLASRTFEEDRELRPTvqvGNPFLEKILI--ESCLEAVQ---TGLV---- 158
Cdd:cd02194 142 RrsgAKPGD-----LLYVTGT-----LGDAAAGLALLLGGLKLPEE---LYEELIERHLrpEPRLELGRalaEGLAtami 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 159 ---DGL-QDLGaagltsasvECASNGGTGIKLFMDKIPL------RDDGMEPYEIMLS--ETQErMLLSVKRDNLNRVSQ 226
Cdd:cd02194 209 disDGLlADLG---------HIAEASGVGAVIDLDKLPLspalraAELGEDALELALSggEDYE-LLFTVPPENAEAAAA 278
|
250
....*....|....*.
gi 1301392553 227 VFdkwDVENTVIGQVV 242
Cdd:cd02194 279 KL---GVPVTVIGRVT 291
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
10-239 |
2.20e-04 |
|
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: 43.35 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 10 VRDILAMGARPIALLNSLRFGplDHERNRYLFEGVVSGISGYgnciGIPNIGGEVGFATSYTGnplVNAMCIGLVEiKNL 89
Cdd:cd02192 76 VSDIAAMGGRPLAMVDALWSP--SAEAAAQVLEGMRDAAEKF----GVPIVGGHTHPDSPYNA---LSVAILGRAR-KDL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 90 VRATSGDKGNVLLLVGSGTGRdgIHGASGLA--SRTFEEDRELRPTvqvgnpflekilIESCLEAVQTGLVDGLQDLGAA 167
Cdd:cd02192 146 LISFGAKPGDRLILAIDLDGR--VHPSPPPNwdATTMKSPALLRRQ------------IALLPELAERGLVHAAKDISNP 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1301392553 168 GLTSASVECASNGGTGIKLFMDKIPlRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIG 239
Cdd:cd02192 212 GIIGTLGMLLEASGVGAEIDLDAIP-RPEGVDLERWLKCFPGFGFLLTARPENADEVVAVFAAVGITAAVIG 282
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
12-255 |
4.00e-04 |
|
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that converts thiamine monophosphate into thiamine pyrophosphate (TPP, coenzyme B1), an enzyme cofactor. Thiamine monophosphate may be derived from de novo synthesis or from unphosphorylated thiamine, known as vitamin B1. Proteins scoring between the trusted and noise cutoff for this model include short forms from the Thermoplasmas (which lack the N-terminal region) and a highly derived form from Campylobacter jejuni. Eukaryotes lack this enzyme, and add pyrophosphate from ATP to unphosphorylated thiamine in a single step. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273589 [Multi-domain] Cd Length: 317 Bit Score: 43.09 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 12 DILAMGARPIALLNSLRFgPLDHERNRylFEGVVSGISGYGNCIGIPNIGGEvgfaTSYTGNPLVNAMCIGLVEiKNLVR 91
Cdd:TIGR01379 71 DLAAMGATPKWFLLSLGL-PSDLDEAW--LEAFYDGLFEAAKQYGVPLVGGD----TVSSPELVVTVTAIGEAP-KGRAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 92 ATSGDKGNVLLLVgsgTGRDGIHGA------SGLASRTFEED-----RELRPTVQVGnpflEKILIescleavqTGLVDG 160
Cdd:TIGR01379 143 LRSGAKPGDLVFV---TGTLGDSAAglalllKGKKEPDEEDDeallqRHLRPEPRVE----EGLAL--------AGYANA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 161 LQDLgAAGLTSASVECASNGGTGIKLFMDKIPLRD------DGMEPYEIMLS--ETQErMLLSVKRDNLNRVSQVFDKwd 232
Cdd:TIGR01379 208 AIDV-SDGLAADLGHIAEASGVGIVIDLDRLPLSSelaawaEGKNPLEWALSggEDYE-LVFTVPPERREALLDAAKG-- 283
|
250 260
....*....|....*....|...
gi 1301392553 233 vENTVIGQVVDGDAIELIEEGVT 255
Cdd:TIGR01379 284 -PLTRIGRVTEGEGVVLLADGKT 305
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
10-161 |
6.57e-04 |
|
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: 42.08 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 10 VRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGisgygnCI--GIPNIGGE---------------VGFatsytg 72
Cdd:cd02196 54 VNDILCQGAEPLFFLDYIATGKLDPEVAAEIVKGIAEG------CRqaGCALLGGEtaempgvyaegeydlAGF------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 73 nplvnamCIGLVEIKNLVratSGDK---GNVLLLVGSgtgrDGIH--GASgLASRTFEE------DRELRPTVQVGNPFL 141
Cdd:cd02196 122 -------AVGVVEKDKII---DGSKikpGDVLIGLPS----SGLHsnGYS-LVRKILFEegldydDPEPGLGKTLGEELL 186
|
170 180
....*....|....*....|..
gi 1301392553 142 E--KILIESCLEAVQTGLVDGL 161
Cdd:cd02196 187 TptRIYVKPILPLLEKVLVKGM 208
|
|
| |
