|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
4-427 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 662.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 4 RVLVIGSGGREHALAWKLAQSRHVKQVLVAPGNAGTACLEKisNTAISVGDHTALAQFCKDEKIEFVVVGPEAPLAAGIV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 84 EDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPaLVVKASGLAAGKGVIVAKS 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 164 KEEACKAVQEIMQEKTFGAAG------------EtvvveellegeeVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTG 231
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGarvvieeflegeE------------ASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 232 GMGACCPAPQVSKDLFLKIKNNILQRTVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYE 311
Cdd:COG0151 227 GMGAYSPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 312 MIQSTLDGLLwSSLPIWLENHTAVTVVMASKGYPGAYTKGVEITGFPDPQALGLQVFHAGTALKDGKVVTSGGRVLTVTA 391
Cdd:COG0151 307 LLLAAAEGRL-DEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTA 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 731275978 392 VRETLKLALEEANKGVAAVKFEGAVYRKDIGFHAIA 427
Cdd:COG0151 386 LGDTLEEARERAYEAVEKIRFEGMFYRRDIGWRALK 421
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
4-426 |
0e+00 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 620.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 4 RVLVIGSGGREHALAWKLAQSRHVKQVLVAPGNAGTACLEKISNTAISVGDHTALAQFCKDEKIEFVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 84 EDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 164 KEEACKAVQEIMQEKtFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGACCPAPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 244 KDLFLKIKNNILQRTVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEMIQSTLDGLLwS 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKL-D 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 324 SLPIWLENHTAVTVVMASKGYPGAYTKGVEITGFPDPQALGLQVFHAGTALKDGKVVTSGGRVLTVTAVRETLKLALEEA 403
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 731275978 404 NKGVAAVKFEGAVYRKDIGFHAI 426
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
431-778 |
0e+00 |
|
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439920 [Multi-domain] Cd Length: 343 Bit Score: 584.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 431 QPRGLTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCDVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHS 510
Cdd:COG0150 1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 511 TIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAV 590
Cdd:COG0150 81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 591 GAMERDQKLPHlEQIVEGDVIVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPSgcGDQTLGDLLLTPTRIYSRSLLPVI 670
Cdd:COG0150 161 GVVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLGEALLEPTRIYVKPVLALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 671 RSGHVKAFAHITGGGLLENIPRVLPKKFGVDLDACTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQIL 750
Cdd:COG0150 238 KAVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAAL 317
|
330 340
....*....|....*....|....*...
gi 731275978 751 RDIQQSQEEAWVIGSVVACPEgsPRVKV 778
Cdd:COG0150 318 ALLKAAGETAYVIGEVVAGEG--EGVVL 343
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
6.06e-176 |
|
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: 513.95 E-value: 6.06e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 469 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTT 548
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 549 EAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLPHlEQIVEGDVIVGIASSGLHSNGFSLVR 628
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 629 KIVAQSSLEYSSLAPSgcGDQTLGDLLLTPTRIYSRSLLPVIRSGHVKAFAHITGGGLLENIPRVLPKKFGVDLDACTWR 708
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 731275978 709 IPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILRDIQQSQEEAWVIGSVV 767
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
435-768 |
3.33e-152 |
|
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273316 [Multi-domain] Cd Length: 332 Bit Score: 454.10 E-value: 3.33e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 435 LTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCDVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQLCNKHSTIGQ 514
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 515 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAME 594
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 595 RDQKLPHlEQIVEGDVIVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPSGCGdQTLGDLLLTPTRIYSRSLLPVIRSGH 674
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFG-KTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 675 VKAFAHITGGGLLENIPRVLPKKFGVDLDACTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILRDIQ 754
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....
gi 731275978 755 QSQEEAWVIGSVVA 768
Cdd:TIGR00878 318 AYGEKAWVIGEVKK 331
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
2.28e-148 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 448.03 E-value: 2.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 6 LVIGSGGREHALAWKLAQSRHVKQVLVAPGNAGTACLEKISNTA-ISVGDHTALAQFCKDEKIEFVVVGPEAPLAAGIVE 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 85 DLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPaLVVKASGLAAGKGVIVAKSK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 165 EEACKAVQEIMQEKTFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGACCPAPQVSK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 245 DLFLKIKNNILQRTVDGMQQEGTPYTGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEMIQSTLDGLLW 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 323 SSLPIWLENhTAVTVVMASKGYPGAYTKGVEITGFPDPQAL--GLQVFHAGTALK-DGKVVTSGGRVLTVTAVRETLKLA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 731275978 400 LEEANKGVAAVKFEGAVYRKDIGFHAIAFLQQPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
434-767 |
2.08e-128 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 394.17 E-value: 2.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 434 GLTYKDSGVDIAAGNMLVKKIQPLAkatsrPGcdvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQLCNKHSTIG 513
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 594 ERDqKLPHLEQIVEGDVIVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPSgcGDQTLGDLLLTPTRIYSRSLLPVIRSG 673
Cdd:PLN02557 204 KKD-AVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPG--ASVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 674 HVKAFAHITGGGLLENIPRVLPKKFGVDLDACTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILRDi 753
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEE- 359
|
330
....*....|....
gi 731275978 754 qqSQEEAWVIGSVV 767
Cdd:PLN02557 360 --GAYPAYRIGEVI 371
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
2.73e-105 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 326.16 E-value: 2.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 105 SSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKTFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 185 ETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGACCPAPQVSKDLFLKIKNNILQRTVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 731275978 265 EGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
809-991 |
3.46e-102 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 317.41 E-value: 3.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 809 RVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKLYKNREEFDNAIHQVLEEFFTD 888
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 889 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDT 968
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 731275978 969 VATLSERVKVAEHKIFPKALQLV 991
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
807-1004 |
8.98e-101 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 314.28 E-value: 8.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 807 KARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKLYKNREEFDNAIHQVLEEFF 886
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 887 TDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRG 966
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 731275978 967 DTVATLSERVKVAEHKIFPKALQLVASGTIRLgENGKV 1004
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTL-DGRRV 197
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
808-997 |
7.01e-77 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 249.98 E-value: 7.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 808 ARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKLYKNREEFDNAIHQVLEEFFT 887
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGD 967
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180 190
....*....|....*....|....*....|
gi 731275978 968 TVATLSERVKVAEHKIFPKALQLVASGTIR 997
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
808-988 |
3.65e-73 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 239.50 E-value: 3.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 808 ARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKLYKNREEFDNAIHQVLEEFFT 887
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGD 967
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|.
gi 731275978 968 TVATLSERVKVAEHKIFPKAL 988
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
809-1002 |
1.03e-36 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 137.52 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 809 RVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKlyKNREE--FDNAIHQVLEEFF 886
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKT--KGEPDglSPDELVDALRGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 887 TDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKG-----SNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:PLN02331 79 VDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 731275978 962 PVKRGDTVATLSERVKVAEHKIFPKALQLVASGTIRLGENG 1002
Cdd:PLN02331 159 PVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
607-776 |
7.48e-34 |
|
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: 127.46 E-value: 7.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 607 EGDVIVGIASSGLHSNGFSLVRKIvaqssleyssLAPSGCGDQTLGDLLLTPTRIYSRSLLPVIrSGHVKAFAHITGGGL 686
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKG----------LEDSGLAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 687 LENIPRVLPK-KFGVDLDActwRIPRVFSWLQqegqlSEEEMARTFNCGVGAALVVSKDQtEQILRDIQQSQEEAWVIGS 765
Cdd:pfam02769 71 AGALAEMAPAsGVGAEIDL---DKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEEA-EAVLAILEKEGLEAAVIGE 141
|
170
....*....|.
gi 731275978 766 VVACPEGSPRV 776
Cdd:pfam02769 142 VTAGGRLTVIV 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
4-427 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 662.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 4 RVLVIGSGGREHALAWKLAQSRHVKQVLVAPGNAGTACLEKisNTAISVGDHTALAQFCKDEKIEFVVVGPEAPLAAGIV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 84 EDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPaLVVKASGLAAGKGVIVAKS 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 164 KEEACKAVQEIMQEKTFGAAG------------EtvvveellegeeVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTG 231
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGarvvieeflegeE------------ASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 232 GMGACCPAPQVSKDLFLKIKNNILQRTVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYE 311
Cdd:COG0151 227 GMGAYSPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 312 MIQSTLDGLLwSSLPIWLENHTAVTVVMASKGYPGAYTKGVEITGFPDPQALGLQVFHAGTALKDGKVVTSGGRVLTVTA 391
Cdd:COG0151 307 LLLAAAEGRL-DEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTA 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 731275978 392 VRETLKLALEEANKGVAAVKFEGAVYRKDIGFHAIA 427
Cdd:COG0151 386 LGDTLEEARERAYEAVEKIRFEGMFYRRDIGWRALK 421
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
4-426 |
0e+00 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 620.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 4 RVLVIGSGGREHALAWKLAQSRHVKQVLVAPGNAGTACLEKISNTAISVGDHTALAQFCKDEKIEFVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 84 EDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 164 KEEACKAVQEIMQEKtFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGACCPAPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 244 KDLFLKIKNNILQRTVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEMIQSTLDGLLwS 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKL-D 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 324 SLPIWLENHTAVTVVMASKGYPGAYTKGVEITGFPDPQALGLQVFHAGTALKDGKVVTSGGRVLTVTAVRETLKLALEEA 403
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 731275978 404 NKGVAAVKFEGAVYRKDIGFHAI 426
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
431-778 |
0e+00 |
|
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439920 [Multi-domain] Cd Length: 343 Bit Score: 584.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 431 QPRGLTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCDVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHS 510
Cdd:COG0150 1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 511 TIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAV 590
Cdd:COG0150 81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 591 GAMERDQKLPHlEQIVEGDVIVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPSgcGDQTLGDLLLTPTRIYSRSLLPVI 670
Cdd:COG0150 161 GVVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLGEALLEPTRIYVKPVLALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 671 RSGHVKAFAHITGGGLLENIPRVLPKKFGVDLDACTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQIL 750
Cdd:COG0150 238 KAVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAAL 317
|
330 340
....*....|....*....|....*...
gi 731275978 751 RDIQQSQEEAWVIGSVVACPEgsPRVKV 778
Cdd:COG0150 318 ALLKAAGETAYVIGEVVAGEG--EGVVL 343
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
6.06e-176 |
|
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: 513.95 E-value: 6.06e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 469 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTT 548
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 549 EAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLPHlEQIVEGDVIVGIASSGLHSNGFSLVR 628
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 629 KIVAQSSLEYSSLAPSgcGDQTLGDLLLTPTRIYSRSLLPVIRSGHVKAFAHITGGGLLENIPRVLPKKFGVDLDACTWR 708
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 731275978 709 IPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILRDIQQSQEEAWVIGSVV 767
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
435-768 |
3.33e-152 |
|
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273316 [Multi-domain] Cd Length: 332 Bit Score: 454.10 E-value: 3.33e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 435 LTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCDVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQLCNKHSTIGQ 514
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 515 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAME 594
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 595 RDQKLPHlEQIVEGDVIVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPSGCGdQTLGDLLLTPTRIYSRSLLPVIRSGH 674
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFG-KTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 675 VKAFAHITGGGLLENIPRVLPKKFGVDLDACTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILRDIQ 754
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....
gi 731275978 755 QSQEEAWVIGSVVA 768
Cdd:TIGR00878 318 AYGEKAWVIGEVKK 331
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
2.28e-148 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 448.03 E-value: 2.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 6 LVIGSGGREHALAWKLAQSRHVKQVLVAPGNAGTACLEKISNTA-ISVGDHTALAQFCKDEKIEFVVVGPEAPLAAGIVE 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 85 DLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPaLVVKASGLAAGKGVIVAKSK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 165 EEACKAVQEIMQEKTFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGACCPAPQVSK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 245 DLFLKIKNNILQRTVDGMQQEGTPYTGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEMIQSTLDGLLW 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 323 SSLPIWLENhTAVTVVMASKGYPGAYTKGVEITGFPDPQAL--GLQVFHAGTALK-DGKVVTSGGRVLTVTAVRETLKLA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 731275978 400 LEEANKGVAAVKFEGAVYRKDIGFHAIAFLQQPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
434-767 |
2.08e-128 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 394.17 E-value: 2.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 434 GLTYKDSGVDIAAGNMLVKKIQPLAkatsrPGcdvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQLCNKHSTIG 513
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 594 ERDqKLPHLEQIVEGDVIVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPSgcGDQTLGDLLLTPTRIYSRSLLPVIRSG 673
Cdd:PLN02557 204 KKD-AVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPG--ASVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 674 HVKAFAHITGGGLLENIPRVLPKKFGVDLDACTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILRDi 753
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEE- 359
|
330
....*....|....
gi 731275978 754 qqSQEEAWVIGSVV 767
Cdd:PLN02557 360 --GAYPAYRIGEVI 371
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
2.73e-105 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 326.16 E-value: 2.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 105 SSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKTFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 185 ETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGACCPAPQVSKDLFLKIKNNILQRTVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 731275978 265 EGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
809-991 |
3.46e-102 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 317.41 E-value: 3.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 809 RVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKLYKNREEFDNAIHQVLEEFFTD 888
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 889 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDT 968
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 731275978 969 VATLSERVKVAEHKIFPKALQLV 991
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
807-1004 |
8.98e-101 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 314.28 E-value: 8.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 807 KARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKLYKNREEFDNAIHQVLEEFF 886
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 887 TDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRG 966
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 731275978 967 DTVATLSERVKVAEHKIFPKALQLVASGTIRLgENGKV 1004
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTL-DGRRV 197
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
808-997 |
7.01e-77 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 249.98 E-value: 7.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 808 ARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKLYKNREEFDNAIHQVLEEFFT 887
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGD 967
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180 190
....*....|....*....|....*....|
gi 731275978 968 TVATLSERVKVAEHKIFPKALQLVASGTIR 997
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
808-988 |
3.65e-73 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 239.50 E-value: 3.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 808 ARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKLYKNREEFDNAIHQVLEEFFT 887
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGD 967
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|.
gi 731275978 968 TVATLSERVKVAEHKIFPKAL 988
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
4-104 |
1.62e-50 |
|
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam00289). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460723 [Multi-domain] Cd Length: 102 Bit Score: 172.93 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 4 RVLVIGSGGREHALAWKLAQSRHVKQVLVAPGNAGTACLEKisNTAISVGDHTALAQFCKDEKIEFVVVGPEAPLAAGIV 83
Cdd:pfam02844 2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 731275978 84 EDL--ASAGVRCFGPTAEAAQLE 104
Cdd:pfam02844 80 DALreRAAGIPVFGPSKAAAQLE 102
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
812-990 |
3.26e-42 |
|
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.
Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 152.06 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 812 VLISGTGSNLQALIDSTRDpNSSAHIVVVISNKAAVAGLSKAEKAGIptrviNHKLYKNREEFDNAIHQVLEEFFTDIVC 891
Cdd:cd08369 1 IVILGSGNIGQRVLKALLS-KEGHEIVGVVTHPDSPRGTAQLSLELV-----GGKVYLDSNINTPELLELLKEFAPDLIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 892 LAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVAT 971
Cdd:cd08369 75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154
|
170
....*....|....*....
gi 731275978 972 LSERVKVAEHKIFPKALQL 990
Cdd:cd08369 155 LYQRLIELGPKLLKEALQK 173
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-423 |
2.83e-39 |
|
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02787).
Pssm-ID: 460722 [Multi-domain] Cd Length: 88 Bit Score: 140.28 E-value: 2.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 334 AVTVVMASKGYPGAYTKGVEITGFPDPqalGLQVFHAGTALKDGKVVTSGGRVLTVTAVRETLKLALEEANKGVAAVKFE 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA---GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|
gi 731275978 414 GAVYRKDIGF 423
Cdd:pfam02843 78 GMFYRKDIGT 87
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
800-984 |
3.42e-39 |
|
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440551 [Multi-domain] Cd Length: 282 Bit Score: 147.12 E-value: 3.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 800 HFPAQhkKARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLskAEKAGIPTRVINHKLyKNREEFDNAIH 879
Cdd:COG0788 81 HDSDR--RKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 880 QVLEEFFTDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQE 959
Cdd:COG0788 156 ELLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQD 235
|
170 180 190
....*....|....*....|....*....|....*...
gi 731275978 960 AVPVKRGDTVA------------TLSERVK-VAEHKIF 984
Cdd:COG0788 236 VERVDHRDTPEdlvrkgrdvekrVLARAVRwHLEDRVL 273
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
809-1002 |
1.03e-36 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 137.52 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 809 RVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKAEKAGIPTRVINHKlyKNREE--FDNAIHQVLEEFF 886
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKT--KGEPDglSPDELVDALRGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 887 TDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKG-----SNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:PLN02331 79 VDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 731275978 962 PVKRGDTVATLSERVKVAEHKIFPKALQLVASGTIRLGENG 1002
Cdd:PLN02331 159 PVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
809-1004 |
2.74e-34 |
|
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine.
Pssm-ID: 187717 [Multi-domain] Cd Length: 196 Bit Score: 129.99 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 809 RVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLskAEKAGIPTRVIN-HKlyKNREEFDNAIHQVLEEFFT 887
Cdd:cd08648 2 RVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPL--AERFGIPFHHIPvTK--DTKAEAEAEQLELLEEYGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGD 967
Cdd:cd08648 78 DLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRD 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 731275978 968 TVATLSERVKVAEHKIFPKALQLVASGTIRLGENGKV 1004
Cdd:cd08648 158 SVEDLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTV 194
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
607-776 |
7.48e-34 |
|
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: 127.46 E-value: 7.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 607 EGDVIVGIASSGLHSNGFSLVRKIvaqssleyssLAPSGCGDQTLGDLLLTPTRIYSRSLLPVIrSGHVKAFAHITGGGL 686
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKG----------LEDSGLAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 687 LENIPRVLPK-KFGVDLDActwRIPRVFSWLQqegqlSEEEMARTFNCGVGAALVVSKDQtEQILRDIQQSQEEAWVIGS 765
Cdd:pfam02769 71 AGALAEMAPAsGVGAEIDL---DKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEEA-EAVLAILEKEGLEAAVIGE 141
|
170
....*....|.
gi 731275978 766 VVACPEGSPRV 776
Cdd:pfam02769 142 VTAGGRLTVIV 152
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
800-972 |
1.39e-31 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 125.22 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 800 HFPAQHKkaRVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLskAEKAGIPTRVINH-KLykNREEFDNAI 878
Cdd:PRK06027 84 LDSAERK--RVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEARL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 879 HQVLEEFFTDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQ 958
Cdd:PRK06027 158 LELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQ 237
|
170
....*....|....
gi 731275978 959 EAVPVKRGDTVATL 972
Cdd:PRK06027 238 DVIRVDHRDTAEDL 251
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
489-765 |
3.84e-29 |
|
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: 116.34 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 489 LASGTDGVGTKLKIaqlcnKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGK-LDLRTTEAVVAGVAEACKQAGCALL 567
Cdd:cd00396 2 LAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 568 GGETAEMPDMYPPgEYDLAGFAVGAMERDqKLPHLEQIVEGDVIvgiassglhsngfsLVRKIvaqssleysslapsgcg 647
Cdd:cd00396 77 GGHTSVSPGTMGH-KLSLAVFAIGVVEKD-RVIDSSGARPGDVL--------------ILTGV----------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 648 dqtlgdllltptriysRSLLPVIRSGHVKAFAHITGGGLLENIPRVLPK---KFGVDLDACTWRIPrvFSWLQQEgqlsE 724
Cdd:cd00396 124 ----------------DAVLELVAAGDVHAMHDITDGGLLGTLPELAQAsgvGAEIDLEAIPLDEV--VRWLCVE----H 181
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 731275978 725 EEMARTFNCGVGAALVVSKDQTEQILRDIQQSQEEAWVIGS 765
Cdd:cd00396 182 IEEALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
803-984 |
5.99e-24 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 103.14 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 803 AQHKKARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLskAEKAGIPTRVInhKLYK-NREEFDNAIHQV 881
Cdd:PRK13011 85 DPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPL--AAWHGIPFHHF--PITPdTKPQQEAQVLDV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 882 LEEFFTDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:PRK13011 161 VEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVE 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 731275978 962 PVKRG----DTVA--------TLSERVK-VAEHKIF 984
Cdd:PRK13011 241 RVDHAyspeDLVAkgrdveclTLARAVKaHIERRVF 276
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
489-593 |
8.44e-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: 96.75 E-value: 8.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 489 LASGTDGVGTKLKIaqlcNKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDL--RTTEAVVAGVAEACKQAGCAL 566
Cdd:pfam00586 5 VAVTTDGHGTPSLV----DPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEveWVLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*..
gi 731275978 567 LGGETAEMPDMYPPgeyDLAGFAVGAM 593
Cdd:pfam00586 81 VGGDTSFDPEGGKP---TISVTAVGIV 104
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
802-989 |
1.96e-23 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 100.98 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 802 PAQHKKARVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISN--KAAVAGLSK-AEKAGIPTRVINHKLYKNREEfdnai 878
Cdd:PLN02828 65 PGLDPKYKIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNheRGPNTHVMRfLERHGIPYHYLPTTKENKRED----- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 879 hQVLEEFF-TDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIIL 957
Cdd:PLN02828 140 -EILELVKgTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIE 218
|
170 180 190
....*....|....*....|....*....|..
gi 731275978 958 QEAVPVKRGDTVATLSERVKVAEHKIFPKALQ 989
Cdd:PLN02828 219 QMVERVSHRDNLRSFVQKSENLEKQCLAKAIK 250
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
802-984 |
1.02e-20 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 93.71 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 802 PAQHKKaRVAVLISGTGSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSKaeKAGIPTRVInhKLYK-NREEFDNAIHQ 880
Cdd:PRK13010 89 PDGQRP-KVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPLAV--QHDIPFHHL--PVTPdTKAQQEAQILD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 881 VLEEFFTDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEA 960
Cdd:PRK13010 164 LIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDV 243
|
170 180 190
....*....|....*....|....*....|....*..
gi 731275978 961 VPVKRG----DTVA--------TLSERVKV-AEHKIF 984
Cdd:PRK13010 244 ERVDHSyspeDLVAkgrdveclTLARAVKAfIEHRVF 280
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
821-996 |
2.43e-17 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 84.00 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 821 LQALIDSTRDpnssahIVVVISNKAAVAGLSK----------AEKAGIPtrVIN-HKLykNREEFdnaiHQVLEEFFTDI 889
Cdd:COG0223 16 LEALLAAGHE------VVAVVTQPDRPAGRGRkltpspvkelALEHGIP--VLQpESL--KDPEF----LEELRALNPDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 890 VCLAGFMRILSGPFvrkWD---GKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRG 966
Cdd:COG0223 82 IVVVAYGQILPKEV---LDiprLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPD 158
|
170 180 190
....*....|....*....|....*....|
gi 731275978 967 DTVATLSERVKVAEHKIFPKALQLVASGTI 996
Cdd:COG0223 159 DTAGSLHDKLAELGAELLLETLDALEAGTL 188
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
851-997 |
1.16e-15 |
|
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 78.98 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 851 SKAEKAGIPtrVINHKLYKNREEFdnaihQVLEEFFTDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQ 930
Cdd:TIGR00460 50 VLAEEKGIP--VFQPEKQRQLEEL-----PLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQR 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731275978 931 VLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKVAEHKIFPKALQLVASGTIR 997
Cdd:TIGR00460 123 AILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNK 189
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
806-975 |
9.01e-15 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 76.66 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 806 KKARVAVLisGT----GSNLQALIDSTRDPNSSAHIVVVISNKAAVAGLSK----------AEKAGIPTRVINHKLYKNR 871
Cdd:PLN02285 5 RKKRLVFL--GTpevaATVLDALLDASQAPDSAFEVAAVVTQPPARRGRGRklmpspvaqlALDRGFPPDLIFTPEKAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 872 EEFDNAihqvLEEFFTDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVD 951
Cdd:PLN02285 83 EDFLSA----LRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALD 158
|
170 180
....*....|....*....|....
gi 731275978 952 AGQIILQEAVPVKRGDTVATLSER 975
Cdd:PLN02285 159 AGPVIAQERVEVDEDIKAPELLPL 182
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
879-988 |
2.41e-11 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 62.61 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 879 HQVLEEFFTDIVCLAGfMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAH-EQVLEAGVKITGCTVHFVAEDVDAGQIIL 957
Cdd:cd08653 40 VAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGfWALANGDPDNVGVTVHLVDAGIDTGDVLA 118
|
90 100 110
....*....|....*....|....*....|.
gi 731275978 958 QEAVPVKRGDTVATLSERVKVAEHKIFPKAL 988
Cdd:cd08653 119 QARPPLAAGDTLLSLYLRLYRAGVELMVEAI 149
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
821-975 |
2.45e-11 |
|
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 64.00 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 821 LQALIDStrdpnsSAHIVVVISNKAAVAGLSK----------AEKAGIPTRVINhKLykNREEFDNAIHQVLEEFFtdIV 890
Cdd:cd08646 16 LEALLKS------GHEVVAVVTQPDKPRGRGKkltpspvkelALELGLPVLQPE-KL--KDEEFLEELKALKPDLI--VV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 891 CLAGFM---RILSGPfvrkwDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGD 967
Cdd:cd08646 85 VAYGQIlpkEILDLP-----PYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDD 159
|
....*...
gi 731275978 968 TVATLSER 975
Cdd:cd08646 160 TAGELLDK 167
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
912-997 |
8.73e-10 |
|
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.
Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 59.67 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 912 LNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKVAEHKIFPKALQLV 991
Cdd:cd08644 101 FNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLARTLPAL 180
|
....*.
gi 731275978 992 ASGTIR 997
Cdd:cd08644 181 KAGKAR 186
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
832-989 |
9.89e-10 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 58.61 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 832 NSSAHIVVVISN--KAAVAGLSKAEKAGIPTRVINHKLyknreefdnaiHQVLEEFFTDIVCLAGFMRILSGPFVRKWDG 909
Cdd:cd08820 24 RGSFEIIAVLTNtsPADVWEGSEPLYDIGSTERNLHKL-----------LEILENKGVDILISVQYHWILPGSILEKAKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 910 KMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKVAEHKIFPKALQ 989
Cdd:cd08820 93 IAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYILAHYAAIALFGEHIT 172
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
57-294 |
2.51e-09 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 59.12 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 57 ALAQFCKDEKIEFVVVGPEA--PLAAGIVEDLasaGVRcfGPTAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEAC 134
Cdd:COG0439 8 AAAELARETGIDAVLSESEFavETAAELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 135 SFIVSADFPaLVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKTFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPP 214
Cdd:COG0439 83 AFAEEIGYP-VVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 215 AQDHKrllegdLGPNTGGMGACCPAPqVSKDLFLKIKnNILQRTVD--GMQqegtpyTGILYAGIMLTKDG-PKVLEFNC 291
Cdd:COG0439 162 TRKHQ------KPPYFVELGHEAPSP-LPEELRAEIG-ELVARALRalGYR------RGAFHTEFLLTPDGePYLIEINA 227
|
...
gi 731275978 292 RFG 294
Cdd:COG0439 228 RLG 230
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
912-998 |
3.01e-09 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 60.77 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 912 LNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKVAEHKIFPKALQLV 991
Cdd:PRK08125 101 FNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAI 180
|
....*..
gi 731275978 992 ASGTIRL 998
Cdd:PRK08125 181 KHGNIPE 187
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
915-992 |
3.91e-09 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 57.47 E-value: 3.91e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 731275978 915 HPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVkvaehkIFPKALQLVA 992
Cdd:cd08822 95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRA------LAPMGVKLLT 166
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
821-988 |
4.16e-09 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 56.89 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 821 LQALIDStrdpnsSAHIVVVISNKAAVAG--------LSKAEKAGIP---TRVINhklyknreefDNAIHQVLEEFFTDI 889
Cdd:cd08651 15 LEAILEA------GGEVVGVITLDDSSSNndsdyldlDSFARKNGIPyykFTDIN----------DEEIIEWIKEANPDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 890 VCLAGFMRILSGPFvrkwdgkmLNI--------HPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:cd08651 79 IFVFGWSQLLKPEI--------LAIprlgvigfHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPF 150
|
170 180
....*....|....*....|....*..
gi 731275978 962 PVKRGDTVATLSERVKVAEHKIFPKAL 988
Cdd:cd08651 151 PIDKDDTANSLYDKIMEAAKQQIDKFL 177
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
880-992 |
1.95e-07 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 52.06 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 880 QVLEEFFTDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQE 959
Cdd:cd08823 65 EWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQ 144
|
90 100 110
....*....|....*....|....*....|...
gi 731275978 960 AVPVKRGDTVATLSERVKVAEHKIFPKALQLVA 992
Cdd:cd08823 145 FTPIHPDDTYGLLCSRLAMLAVGLLEELYQNLA 177
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
915-995 |
5.18e-07 |
|
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.
Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 51.30 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 915 HPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKVAEH-KIFPKALQLVAS 993
Cdd:cd08647 106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPEGiKAMVEAVRLIAE 185
|
..
gi 731275978 994 GT 995
Cdd:cd08647 186 GK 187
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
912-996 |
1.39e-06 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 51.23 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 912 LNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKVAEHKIFPKALQLV 991
Cdd:PRK06988 103 YNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVTVAAEQTLWRVLPAL 182
|
....*
gi 731275978 992 ASGTI 996
Cdd:PRK06988 183 LAGEA 187
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
836-972 |
2.08e-06 |
|
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.
Pssm-ID: 187718 [Multi-domain] Cd Length: 166 Bit Score: 48.79 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 836 HIVVVISNKAAVAglSKAEKAGIPtrvinhkLYKNREEFDNAIHQVLEEFFTDIVCLagfmRILSGPFVRKWDGKMLNIH 915
Cdd:cd08649 24 RIAAVVSTDPAIR--AWAAAEGIA-------VLEPGEALEELLSDEPFDWLFSIVNL----RILPSEVLALPRKGAINFH 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 731275978 916 PSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATL 972
Cdd:cd08649 91 DGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
52-174 |
9.15e-06 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 48.92 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 52 VGDHT---ALAQFCKD------EkIEFVvvgPEAPLAAgivedLASAG-VRcfgPTAEA---AQlesSKRFAKEFMDRHR 118
Cdd:COG0026 37 VADYDdeeALREFAERcdvvtfE-FENV---PAEALEA-----LEAEVpVR---PGPEAleiAQ---DRLLEKAFLAELG 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 731275978 119 IPTARWRAFTKAEEACSFIVSADFPAlVVKasglAA-----GKGVIVAKSKEEACKAVQEI 174
Cdd:COG0026 102 IPVAPFAAVDSLEDLEAAIAELGLPA-VLK----TRrggydGKGQVVIKSAADLEAAWAAL 157
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
512-620 |
2.32e-05 |
|
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: 47.55 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 512 IGQDLVAMCVNDILAQGAEPLFFLdyFSCG---KLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYppgeydLAGF 588
Cdd:cd02194 59 IGWKALAVNLSDLAAMGARPLGFL--LSLGlppDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELV------ISVT 130
|
90 100 110
....*....|....*....|....*....|....*..
gi 731275978 589 AVGAMERDQKLpHLEQIVEGDVIV-----GIASSGLH 620
Cdd:cd02194 131 ALGEVEKGKPL-RRSGAKPGDLLYvtgtlGDAAAGLA 166
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
65-166 |
3.32e-05 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 48.07 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 65 EKIEFVVVGPEAPLAAGIVEDLASAGVRCFGPTAEAA-QLESSKRFAkEFMDRHRIPTARWRAFTKAEEACSFIVSADFP 143
Cdd:TIGR01369 628 EKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIdRAEDREKFS-ELLDELGIPQPKWKTATSVEEAVEFASEIGYP 706
|
90 100
....*....|....*....|...
gi 731275978 144 ALvVKASGLAAGKGVIVAKSKEE 166
Cdd:TIGR01369 707 VL-VRPSYVLGGRAMEIVYNEEE 728
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-174 |
3.76e-05 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 45.71 E-value: 3.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 731275978 110 AKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPALVVKASGLAAGK----GVIVAKSKEEACKAVQEI 174
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEM 75
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
79-313 |
3.78e-05 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 46.86 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 79 AAGIVEDLASAGVRCFGPtAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPaLVVKASGLAAGKGV 158
Cdd:COG0189 70 GLALLRQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGP-VVLKPLDGSGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 159 IVAKSKEEACKAVQE---------IMQEKTFGAAGETvvveellegeeVSCLCFtDGRTVVPM---PPAQDHKRllegdl 226
Cdd:COG0189 148 FLVEDEDALESILEAltelgsepvLVQEFIPEEDGRD-----------IRVLVV-GGEPVAAIrriPAEGEFRT------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 227 gpNT--GGMGACCPAPQVSKDLFLKIknnilqrtvdgmqqegTPYTGILYAGI--MLTKDGPKVLEFNCRFGDPEcqvIL 302
Cdd:COG0189 210 --NLarGGRAEPVELTDEERELALRA----------------APALGLDFAGVdlIEDDDGPLVLEVNVTPGFRG---LE 268
|
250
....*....|.
gi 731275978 303 PLLKSDLYEMI 313
Cdd:COG0189 269 RATGVDIAEAI 279
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
520-612 |
8.17e-05 |
|
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: 45.59 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 520 CVNDILAQGAEPLFFLDYFSC----GKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMyppgeydLAGFAVGAMER 595
Cdd:cd02195 80 ALSDIYAMGAKPLSALAIVTLprklPALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEP-------KYGLSVTGLVH 152
|
90
....*....|....*..
gi 731275978 596 DQKLPHLEQIVEGDVIV 612
Cdd:cd02195 153 PNKILRNSGAKPGDVLI 169
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
523-573 |
3.83e-04 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 43.91 E-value: 3.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 731275978 523 DILAQGAEPLFFLDY--FSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAE 573
Cdd:COG0709 89 DVYAMGGRPLTALAIvgFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSID 141
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
62-173 |
4.55e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 44.19 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 62 CKDEKIEFVVVGPEAPLAAGIVEDLASAGVRCFGPTAEAA-QLESSKRFaKEFMDRHRIPTARWRAFTKAEEACSFIVSA 140
Cdd:PRK12815 626 AEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIdRLEDRDRF-YQLLDELGLPHVPGLTATDEEEAFAFAKRI 704
|
90 100 110
....*....|....*....|....*....|...
gi 731275978 141 DFPALvVKASGLAAGKGVIVAKSKEEACKAVQE 173
Cdd:PRK12815 705 GYPVL-IRPSYVIGGQGMAVVYDEPALEAYLAE 736
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
521-612 |
5.64e-04 |
|
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100033 [Multi-domain] Cd Length: 293 Bit Score: 43.21 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 521 VNDILAQGAEPLffldYFSCG-----KLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDmyppGEYD-----LAGfaV 590
Cdd:cd02197 67 VNDLAMMGAKPL----YLSLGfileeGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPK----GKADgifinTTG--I 136
|
90 100
....*....|....*....|..
gi 731275978 591 GAMERDQKLpHLEQIVEGDVIV 612
Cdd:cd02197 137 GVIPRGVII-SPSNIRPGDKII 157
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
89-181 |
8.00e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 43.05 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 89 AGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTARWR--AFTKAEEACSFIVSADFPaLVVKASGLAAGKGVIVAKSKEE 166
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTeeGIEDIEEAKEIAEEIGYP-VIIKASAGGGGIGMRVVYSEEE 176
|
90
....*....|....*..
gi 731275978 167 ACKAVQEIMQ--EKTFG 181
Cdd:PRK08654 177 LEDAIESTQSiaQSAFG 193
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
1-174 |
8.09e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 42.83 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 1 MAARVLVIGSG--GREHALAwklAQSRHVKQVLVAPGNAGTACleKISNTAI--SVGDHTALAQFCKD------EkIEFV 70
Cdd:PRK06019 1 GMKTIGIIGGGqlGRMLALA---AAPLGYKVIVLDPDPDSPAA--QVADEVIvaDYDDVAALRELAEQcdvityE-FENV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 71 vvgPEAPLAAgivedLASAgvRCFGPTAEAAQLESSKRFAKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPAlVVKas 150
Cdd:PRK06019 75 ---PAEALDA-----LAAR--VPVPPGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPA-VLK-- 141
|
170 180
....*....|....*....|....*....
gi 731275978 151 glAA-----GKGVIVAKSKEEACKAVQEI 174
Cdd:PRK06019 142 --TRrggydGKGQWVIRSAEDLEAAWALL 168
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
78-166 |
8.89e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 43.42 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 78 LAAGIvedLASAGVRCFGPTAEAAQL-ESSKRFaKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPALVVKASGLaAGK 156
Cdd:PRK12815 103 HEDGI---LEQYGVELLGTNIEAIQKgEDRERF-RALMKELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTL-GGT 177
|
90
....*....|
gi 731275978 157 GVIVAKSKEE 166
Cdd:PRK12815 178 GGGIAENLEE 187
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
115-178 |
1.36e-03 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 40.70 E-value: 1.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 731275978 115 DRHRIPTARWRAFTKAEEACSFIVSADFPAlVVKASGLA-AGKGVIVAKSKEEACKAVQEIMQEK 178
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPC-VVKARRGGyDGKGQYVVRSEADLPQAWEELGDGP 64
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
57-177 |
2.34e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 41.41 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 57 ALAQFCKDEKIEFVVVG--PEAPLAAGIVEDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTArwRAFTKAE--- 131
Cdd:PRK12767 60 RLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTP--KSYLPESled 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 731275978 132 -EACSFIVSADFPaLVVKASGLAAGKGVIVAKSKEE---ACKAVQEIM-QE 177
Cdd:PRK12767 138 fKAALAKGELQFP-LFVKPRDGSASIGVFKVNDKEElefLLEYVPNLIiQE 187
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
110-174 |
2.36e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 41.61 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 731275978 110 AKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPALVVKASGLAAGK----GVIVAKSKEEACKAVQEI 174
Cdd:PRK00696 8 AKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQI 76
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
1-294 |
4.60e-03 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 40.68 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 1 MAARVLVIGsgGREHALAwkLAQS---RHVKQVLVAPGNAGTACLEKISNTAISVGDHT--------ALAQFCKDEKIEF 69
Cdd:COG3919 4 MRFRVVVLG--GDINALA--VARSlgeAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGddpeafvdALLELAERHGPDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 70 VV-VGPEAPLAAGIVEDLASAGVRCFGPTAEA-AQLESSKRFAkEFMDRHRIPTARWRAFTKAEEACSFIVSADFPaLVV 147
Cdd:COG3919 80 LIpTGDEYVELLSRHRDELEEHYRLPYPDADLlDRLLDKERFY-ELAEELGVPVPKTVVLDSADDLDALAEDLGFP-VVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 148 KAS--------GLAAGKGVIVAKSKEEACKAVQE--------IMQEKTFGAAGETVVVeellegeevSCLCFTDGRTVVp 211
Cdd:COG3919 158 KPAdsvgydelSFPGKKKVFYVDDREELLALLRRiaaagyelIVQEYIPGDDGEMRGL---------TAYVDRDGEVVA- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 212 mppAQDHKRLLEGdlgPNTGGMGACC---PAPQV---SKDLFlkiknnilqrtvdgmqqEGTPYTGILYAGIMLT-KDG- 283
Cdd:COG3919 228 ---TFTGRKLRHY---PPAGGNSAAResvDDPELeeaARRLL-----------------EALGYHGFANVEFKRDpRDGe 284
|
330
....*....|.
gi 731275978 284 PKVLEFNCRFG 294
Cdd:COG3919 285 YKLIEINPRFW 295
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
110-175 |
8.45e-03 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 39.65 E-value: 8.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731275978 110 AKEFMDRHRIPTARWRAFTKAEEACSFIVSADFPALVVKASGLAAGK----GVIVAKSKEEACKAVQEIM 175
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEIL 77
|
|
| |
