|
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: 665.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTASAGKisNAAVSINDHTALARFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 84 GDLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPaLVVKASGLAAGKGVIVAKS 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 164 KAEACEAVQEIMQEKSFGAAG------------EtvvveellegeeVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTG 231
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGarvvieeflegeE------------ASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 232 GMGAYCPAPQVPKDLLVKIKNTILQRTVDGMQQEGVPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYE 311
Cdd:COG0151 227 GMGAYSPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 312 VIQSTFDGLLSESPPVWLENHsAVTVVMASGGYPGAYTKGVEITGFPEAQALGLQVFHAGTALKDAKVVTSGGRVLTVTA 391
Cdd:COG0151 307 LLLAAAEGRLDEVELEWDDRA-AVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTA 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 1046852587 392 VRENLMSALDEARKGLAALKFEGAVYRKDIGFRAVA 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 1046852587 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTASAGKISNAAVSINDHTALARFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 84 GDLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 164 KAEACEAVQEIMQEKsFGAAGETVVVEELLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTGGMGAYCPAPQVP 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 244 KDLLVKIKNTILQRTVDGMQQEGVPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTFDGLLSE 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 324 SPPVWlENHSAVTVVMASGGYPGAYTKGVEITGFPEAQALGLQVFHAGTALKDAKVVTSGGRVLTVTAVRENLMSALDEA 403
Cdd:TIGR00877 320 VELRF-DNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 1046852587 404 RKGLAALKFEGAVYRKDIGFRAV 426
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
434-778 |
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: 586.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 434 GLTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCSVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDSIG 513
Cdd:COG0150 4 SLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:COG0150 84 IDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 594 ERHQKLPQlERIAEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSG 673
Cdd:COG0150 164 EKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLGEALLEPTRIYVKPVLALLKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 674 RVKAFAHITGGGLLENIPRVLPRKLGVDLDAYTWRVPKVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILHDI 753
Cdd:COG0150 241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
|
330 340
....*....|....*....|....*
gi 1046852587 754 RQHQEDAWVIGSVVECPEdsPRVRV 778
Cdd:COG0150 321 KAAGETAYVIGEVVAGEG--EGVVL 343
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
6.58e-177 |
|
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: 516.26 E-value: 6.58e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 469 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDSIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTT 548
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 549 EAVVAGIAAACRQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERHQKLPQlERIAEGDAVIGVASSGLHSNGFSLVR 628
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 629 KIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSGRVKAFAHITGGGLLENIPRVLPRKLGVDLDAYTWR 708
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852587 709 VPKVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILHDIRQHQEDAWVIGSVV 767
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
7.15e-154 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 462.67 E-value: 7.15e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 6 LVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTASAGKISN-AAVSINDHTALARFCKDEKIELVVVGPEAPLAAGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 85 DLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPaLVVKASGLAAGKGVIVAKSK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 165 AEACEAVQEIMQEKSFGAAGETVVVEELLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTGGMGAYCPAPQVPK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 245 DLLVKIKNTILQRTVDGMQQEGVPYTGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTFDGLLS 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 323 ESPPVWLENhSAVTVVMASGGYPGAYTKGVEITGFPEAQAL--GLQVFHAGTALK-DAKVVTSGGRVLTVTAVRENLMSA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 1046852587 400 LDEARKGLAALKFEGAVYRKDIGFRAVAFLQRPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
435-768 |
1.73e-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: 454.87 E-value: 1.73e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 435 LTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCSVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQLCNKHDSIGQ 514
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 515 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAME 594
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 595 RHQKLPQlERIAEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGGCGdQTLGDLLLTPTRIYSHSLLPIIRSGR 674
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFG-KTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 675 VKAFAHITGGGLLENIPRVLPRKLGVDLDAYTWRVPKVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILHDIR 754
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....
gi 1046852587 755 QHQEDAWVIGSVVE 768
Cdd:TIGR00878 318 AYGEKAWVIGEVKK 331
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
434-768 |
7.49e-129 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 395.33 E-value: 7.49e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 434 GLTYKDSGVDIAAGNMLVKKIQPLAkatsrPGcsvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQLCNKHDSIG 513
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 594 ERhQKLPQLERIAEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSG 673
Cdd:PLN02557 204 KK-DAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPG--ASVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 674 RVKAFAHITGGGLLENIPRVLPRKLGVDLDAYTWRVPKVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILHDi 753
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEE- 359
|
330
....*....|....*
gi 1046852587 754 rqHQEDAWVIGSVVE 768
Cdd:PLN02557 360 --GAYPAYRIGEVIN 372
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
6.38e-107 |
|
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: 330.40 E-value: 6.38e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 105 SSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPALVVKASGLAAGKGVIVAKSKAEACEAVQEIMQEKSFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 185 ETVVVEELLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTGGMGAYCPAPQVPKDLLVKIKNTILQRTVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 1046852587 265 EGVPYTGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
809-991 |
3.39e-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: 3.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKSRVEFDNAVDHVLEEFSVD 888
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 889 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDT 968
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 1046852587 969 VATLSERVKAAEHKIFPAALQLV 991
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
807-1009 |
5.01e-99 |
|
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: 309.66 E-value: 5.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 807 KARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKSRVEFDNAVDHVLEEFS 886
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 887 VDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRD 966
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1046852587 967 DTVATLSERVKAAEHKIFPAALQLVASGAVQLgEDGKIHWARE 1009
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTL-DGRRVRLDGE 202
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
808-994 |
2.05e-75 |
|
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: 245.74 E-value: 2.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 808 ARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKSRVEFDNAVDHVLEEFSV 887
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDD 967
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180
....*....|....*....|....*..
gi 1046852587 968 TVATLSERVKAAEHKIFPAALQLVASG 994
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQG 187
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
808-988 |
9.82e-75 |
|
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: 243.74 E-value: 9.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 808 ARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKSRVEFDNAVDHVLEEFSV 887
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDD 967
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|.
gi 1046852587 968 TVATLSERVKAAEHKIFPAAL 988
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
809-1002 |
3.09e-38 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 141.75 E-value: 3.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVI-NHKLYKSRVEFDNAVDhVLEEFSV 887
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYpKTKGEPDGLSPDELVD-ALRGAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKG-----SNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVP 962
Cdd:PLN02331 80 DFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1046852587 963 VQRDDTVATLSERVKAAEHKIFPAALQLVASGAVQLGEDG 1002
Cdd:PLN02331 160 VLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
607-776 |
1.21e-33 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 126.69 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 607 EGDAVIGVASSGLHSNGFSLVRKIVERSslqysspapgGCGDQTLGDLLLTPTRIYSHSLLPIIrSGRVKAFAHITGGGL 686
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDS----------GLAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 687 LENIPRVLP-RKLGVDLDAytwRVPKVFSWLQqegqlSEEEMARTFNCGVGAALVVSKDQtEQILHDIRQHQEDAWVIGS 765
Cdd:pfam02769 71 AGALAEMAPaSGVGAEIDL---DKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEEA-EAVLAILEKEGLEAAVIGE 141
|
170
....*....|.
gi 1046852587 766 VVECPEDSPRV 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: 665.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTASAGKisNAAVSINDHTALARFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 84 GDLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPaLVVKASGLAAGKGVIVAKS 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 164 KAEACEAVQEIMQEKSFGAAG------------EtvvveellegeeVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTG 231
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGarvvieeflegeE------------ASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 232 GMGAYCPAPQVPKDLLVKIKNTILQRTVDGMQQEGVPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYE 311
Cdd:COG0151 227 GMGAYSPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 312 VIQSTFDGLLSESPPVWLENHsAVTVVMASGGYPGAYTKGVEITGFPEAQALGLQVFHAGTALKDAKVVTSGGRVLTVTA 391
Cdd:COG0151 307 LLLAAAEGRLDEVELEWDDRA-AVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTA 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 1046852587 392 VRENLMSALDEARKGLAALKFEGAVYRKDIGFRAVA 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 1046852587 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTASAGKISNAAVSINDHTALARFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 84 GDLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 164 KAEACEAVQEIMQEKsFGAAGETVVVEELLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTGGMGAYCPAPQVP 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 244 KDLLVKIKNTILQRTVDGMQQEGVPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTFDGLLSE 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 324 SPPVWlENHSAVTVVMASGGYPGAYTKGVEITGFPEAQALGLQVFHAGTALKDAKVVTSGGRVLTVTAVRENLMSALDEA 403
Cdd:TIGR00877 320 VELRF-DNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 1046852587 404 RKGLAALKFEGAVYRKDIGFRAV 426
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
434-778 |
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: 586.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 434 GLTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCSVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDSIG 513
Cdd:COG0150 4 SLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:COG0150 84 IDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 594 ERHQKLPQlERIAEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSG 673
Cdd:COG0150 164 EKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLGEALLEPTRIYVKPVLALLKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 674 RVKAFAHITGGGLLENIPRVLPRKLGVDLDAYTWRVPKVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILHDI 753
Cdd:COG0150 241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
|
330 340
....*....|....*....|....*
gi 1046852587 754 RQHQEDAWVIGSVVECPEdsPRVRV 778
Cdd:COG0150 321 KAAGETAYVIGEVVAGEG--EGVVL 343
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
6.58e-177 |
|
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: 516.26 E-value: 6.58e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 469 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDSIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTT 548
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 549 EAVVAGIAAACRQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERHQKLPQlERIAEGDAVIGVASSGLHSNGFSLVR 628
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 629 KIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSGRVKAFAHITGGGLLENIPRVLPRKLGVDLDAYTWR 708
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852587 709 VPKVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILHDIRQHQEDAWVIGSVV 767
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
7.15e-154 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 462.67 E-value: 7.15e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 6 LVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTASAGKISN-AAVSINDHTALARFCKDEKIELVVVGPEAPLAAGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 85 DLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPaLVVKASGLAAGKGVIVAKSK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 165 AEACEAVQEIMQEKSFGAAGETVVVEELLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTGGMGAYCPAPQVPK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 245 DLLVKIKNTILQRTVDGMQQEGVPYTGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTFDGLLS 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 323 ESPPVWLENhSAVTVVMASGGYPGAYTKGVEITGFPEAQAL--GLQVFHAGTALK-DAKVVTSGGRVLTVTAVRENLMSA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 1046852587 400 LDEARKGLAALKFEGAVYRKDIGFRAVAFLQRPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
435-768 |
1.73e-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: 454.87 E-value: 1.73e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 435 LTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCSVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQLCNKHDSIGQ 514
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 515 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAME 594
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 595 RHQKLPQlERIAEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGGCGdQTLGDLLLTPTRIYSHSLLPIIRSGR 674
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFG-KTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 675 VKAFAHITGGGLLENIPRVLPRKLGVDLDAYTWRVPKVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILHDIR 754
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....
gi 1046852587 755 QHQEDAWVIGSVVE 768
Cdd:TIGR00878 318 AYGEKAWVIGEVKK 331
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
434-768 |
7.49e-129 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 395.33 E-value: 7.49e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 434 GLTYKDSGVDIAAGNMLVKKIQPLAkatsrPGcsvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQLCNKHDSIG 513
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 594 ERhQKLPQLERIAEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSG 673
Cdd:PLN02557 204 KK-DAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPG--ASVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 674 RVKAFAHITGGGLLENIPRVLPRKLGVDLDAYTWRVPKVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTEQILHDi 753
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEE- 359
|
330
....*....|....*
gi 1046852587 754 rqHQEDAWVIGSVVE 768
Cdd:PLN02557 360 --GAYPAYRIGEVIN 372
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
6.38e-107 |
|
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: 330.40 E-value: 6.38e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 105 SSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPALVVKASGLAAGKGVIVAKSKAEACEAVQEIMQEKSFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 185 ETVVVEELLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDRGPNTGGMGAYCPAPQVPKDLLVKIKNTILQRTVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 1046852587 265 EGVPYTGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
809-991 |
3.39e-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: 3.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKSRVEFDNAVDHVLEEFSVD 888
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 889 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDT 968
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 1046852587 969 VATLSERVKAAEHKIFPAALQLV 991
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
807-1009 |
5.01e-99 |
|
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: 309.66 E-value: 5.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 807 KARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKSRVEFDNAVDHVLEEFS 886
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 887 VDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRD 966
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1046852587 967 DTVATLSERVKAAEHKIFPAALQLVASGAVQLgEDGKIHWARE 1009
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTL-DGRRVRLDGE 202
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
808-994 |
2.05e-75 |
|
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: 245.74 E-value: 2.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 808 ARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKSRVEFDNAVDHVLEEFSV 887
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDD 967
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180
....*....|....*....|....*..
gi 1046852587 968 TVATLSERVKAAEHKIFPAALQLVASG 994
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQG 187
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
808-988 |
9.82e-75 |
|
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: 243.74 E-value: 9.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 808 ARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKSRVEFDNAVDHVLEEFSV 887
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDD 967
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|.
gi 1046852587 968 TVATLSERVKAAEHKIFPAAL 988
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
4-104 |
9.16e-49 |
|
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: 167.92 E-value: 9.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTASAGKisNAAVSINDHTALARFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:pfam02844 2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 1046852587 84 GDLTS--AGVRCFGPTAQAALLE 104
Cdd:pfam02844 80 DALREraAGIPVFGPSKAAAQLE 102
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
812-990 |
1.25e-43 |
|
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: 155.91 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 812 VLISGTGSNLQALIDSTRDpKSSSHIVLVISNKAAVAGLDRAERAGIptrviNHKLYKSRVEFDNAVDHVLEEFSVDIVC 891
Cdd:cd08369 1 IVILGSGNIGQRVLKALLS-KEGHEIVGVVTHPDSPRGTAQLSLELV-----GGKVYLDSNINTPELLELLKEFAPDLIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 892 LAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVAT 971
Cdd:cd08369 75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154
|
170
....*....|....*....
gi 1046852587 972 LSERVKAAEHKIFPAALQL 990
Cdd:cd08369 155 LYQRLIELGPKLLKEALQK 173
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
809-1002 |
3.09e-38 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 141.75 E-value: 3.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVI-NHKLYKSRVEFDNAVDhVLEEFSV 887
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYpKTKGEPDGLSPDELVD-ALRGAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKG-----SNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVP 962
Cdd:PLN02331 80 DFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1046852587 963 VQRDDTVATLSERVKAAEHKIFPAALQLVASGAVQLGEDG 1002
Cdd:PLN02331 160 VLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-424 |
7.62e-38 |
|
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: 136.42 E-value: 7.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 334 AVTVVMASGGYPGAYTKGVEITGFPEAqalGLQVFHAGTALKDAKVVTSGGRVLTVTAVRENLMSALDEARKGLAALKFE 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA---GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|.
gi 1046852587 414 GAVYRKDIGFR 424
Cdd:pfam02843 78 GMFYRKDIGTR 88
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
801-984 |
1.42e-34 |
|
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: 133.64 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 801 FPSQQKKaRVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLdrAERAGIPTRVINHKLyKSRVEFDNAVDH 880
Cdd:COG0788 81 HDSDRRK-RVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 881 VLEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEA 960
Cdd:COG0788 157 LLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDV 236
|
170 180 190
....*....|....*....|....*....|....*..
gi 1046852587 961 VPVQRDDTVA------------TLSERVKA-AEHKIF 984
Cdd:COG0788 237 ERVDHRDTPEdlvrkgrdvekrVLARAVRWhLEDRVL 273
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
607-776 |
1.21e-33 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 126.69 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 607 EGDAVIGVASSGLHSNGFSLVRKIVERSslqysspapgGCGDQTLGDLLLTPTRIYSHSLLPIIrSGRVKAFAHITGGGL 686
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDS----------GLAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 687 LENIPRVLP-RKLGVDLDAytwRVPKVFSWLQqegqlSEEEMARTFNCGVGAALVVSKDQtEQILHDIRQHQEDAWVIGS 765
Cdd:pfam02769 71 AGALAEMAPaSGVGAEIDL---DKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEEA-EAVLAILEKEGLEAAVIGE 141
|
170
....*....|.
gi 1046852587 766 VVECPEDSPRV 776
Cdd:pfam02769 142 VTAGGRLTVIV 152
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
489-765 |
3.22e-32 |
|
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 100027 [Multi-domain] Cd Length: 222 Bit Score: 125.20 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 489 LASGTDGVGTKLKIaqlcnKHDSIGQDLVAMCVNDILAQGAEPLFFLDYFSCGK-LDLSTTEAVVAGIAAACRQAGCALL 567
Cdd:cd00396 2 LAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 568 GGETAEMPDMYPPgEYDLAGFAVGamerhqklpqleriaegdavigvassglhsngfslvrkIVERSSLQYSSPApggcg 647
Cdd:cd00396 77 GGHTSVSPGTMGH-KLSLAVFAIG--------------------------------------VVEKDRVIDSSGA----- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 648 dqTLGD-LLLTPTRiyshSLLPIIRSGRVKAFAHITGGGLLENIPRVLPRK-LGVDLDAYTWRVPKVFSWLQQEgqlsEE 725
Cdd:cd00396 113 --RPGDvLILTGVD----AVLELVAAGDVHAMHDITDGGLLGTLPELAQASgVGAEIDLEAIPLDEVVRWLCVE----HI 182
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1046852587 726 EMARTFNCGVGAALVVSKDQTEQILHDIRQHQEDAWVIGS 765
Cdd:cd00396 183 EEALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
809-996 |
6.84e-32 |
|
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: 123.44 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLdrAERAGIPTRVIN-HKLYKSRVEfdNAVDHVLEEFSV 887
Cdd:cd08648 2 RVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPL--AERFGIPFHHIPvTKDTKAEAE--AEQLELLEEYGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDD 967
Cdd:cd08648 78 DLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRD 157
|
170 180
....*....|....*....|....*....
gi 1046852587 968 TVATLSERVKAAEHKIFPAALQLVASGAV 996
Cdd:cd08648 158 SVEDLVRKGRDIEKQVLARAVKWHLEDRV 186
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
837-972 |
6.53e-29 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 117.52 E-value: 6.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 837 IVLVISNKAAVAGLdrAERAGIPTRVINH-KLykSRVEFDNAVDHVLEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIH 915
Cdd:PRK06027 119 IAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIH 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046852587 916 PSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVATL 972
Cdd:PRK06027 195 HSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHRDTAEDL 251
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
489-593 |
6.43e-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: 97.13 E-value: 6.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 489 LASGTDGVGTKLKIaqlcNKHDSIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDL--STTEAVVAGIAAACRQAGCAL 566
Cdd:pfam00586 5 VAVTTDGHGTPSLV----DPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEveWVLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*..
gi 1046852587 567 LGGETAEMPDMYPPgeyDLAGFAVGAM 593
Cdd:pfam00586 81 VGGDTSFDPEGGKP---TISVTAVGIV 104
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
800-989 |
3.77e-23 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 100.21 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 800 NFPSQQKKARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKaavaglDRA---------ERAGIPTrvinHKLYKS 870
Cdd:PLN02828 63 RVPGLDPKYKIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNH------ERGpnthvmrflERHGIPY----HYLPTT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 871 RVefDNAVDHVLEEFS-VDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAED 949
Cdd:PLN02828 133 KE--NKREDEILELVKgTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1046852587 950 VDAGQIILQEAVPVQRDDTVATLSERVKAAEHKIFPAALQ 989
Cdd:PLN02828 211 LDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAIK 250
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
803-984 |
9.22e-22 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 96.59 E-value: 9.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 803 SQQKKARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLdrAERAGIPTRVInhKLYK-SRVEFDNAVDHV 881
Cdd:PRK13011 85 DPAARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPL--AAWHGIPFHHF--PITPdTKPQQEAQVLDV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 882 LEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:PRK13011 161 VEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVE 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 1046852587 962 PVQR----DDTVA--------TLSERVKA-AEHKIF 984
Cdd:PRK13011 241 RVDHayspEDLVAkgrdveclTLARAVKAhIERRVF 276
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
802-984 |
2.41e-19 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 89.47 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 802 PSQQKKaRVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLdrAERAGIPTRVInhKLYK-SRVEFDNAVDH 880
Cdd:PRK13010 89 PDGQRP-KVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPL--AVQHDIPFHHL--PVTPdTKAQQEAQILD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 881 VLEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEA 960
Cdd:PRK13010 164 LIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDV 243
|
170 180 190
....*....|....*....|....*....|....*..
gi 1046852587 961 VPVQ------------RDDTVATLSERVKA-AEHKIF 984
Cdd:PRK13010 244 ERVDhsyspedlvakgRDVECLTLARAVKAfIEHRVF 280
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
821-1008 |
2.37e-18 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 87.08 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 821 LQALIDSTRDpkssshIVLVISNKAAVAGLDR----------AERAGIPtrVINHKLYKSRVEFDnavdhVLEEFSVDIV 890
Cdd:COG0223 16 LEALLAAGHE------VVAVVTQPDRPAGRGRkltpspvkelALEHGIP--VLQPESLKDPEFLE-----ELRALNPDLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 891 CLAGFMRILSGPFvrkWD---GKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDD 967
Cdd:COG0223 83 VVVAYGQILPKEV---LDiprLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046852587 968 TVATLSERVKAAEHKIFPAALQLVASGAVQL---------------GEDGKIHWAR 1008
Cdd:COG0223 160 TAGSLHDKLAELGAELLLETLDALEAGTLTPtpqdesgatyapkisKEDGRIDWSR 215
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
882-1008 |
2.68e-16 |
|
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: 80.91 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 882 LEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:TIGR00460 74 VRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETF 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046852587 962 PVQRDDTVATLSERVKAAEHKIFPAALQLVASGAVQL---------------GEDGKIHWAR 1008
Cdd:TIGR00460 154 PIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPepqdaeeatyapkisKEQERIDWNQ 215
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
806-975 |
1.33e-14 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 76.27 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 806 KKARVAVLisGT----GSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDR----------AERAGIPTRVINHKLYKSR 871
Cdd:PLN02285 5 RKKRLVFL--GTpevaATVLDALLDASQAPDSAFEVAAVVTQPPARRGRGRklmpspvaqlALDRGFPPDLIFTPEKAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 872 VEFDNAvdhvLEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVD 951
Cdd:PLN02285 83 EDFLSA----LRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALD 158
|
170 180
....*....|....*....|....
gi 1046852587 952 AGQIILQEAVPVQRDDTVATLSER 975
Cdd:PLN02285 159 AGPVIAQERVEVDEDIKAPELLPL 182
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
821-975 |
9.81e-13 |
|
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: 68.24 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 821 LQALIdstrdpKSSSHIVLVISNKAAVAGL----------DRAERAGIPTRVINhklyksRVEFDNAVDHvLEEFSVDIV 890
Cdd:cd08646 16 LEALL------KSGHEVVAVVTQPDKPRGRgkkltpspvkELALELGLPVLQPE------KLKDEEFLEE-LKALKPDLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 891 CLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVA 970
Cdd:cd08646 83 VVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAG 162
|
....*
gi 1046852587 971 TLSER 975
Cdd:cd08646 163 ELLDK 167
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
881-988 |
2.51e-12 |
|
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: 65.70 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 881 VLEEFSVDIVCLAGfMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAH-EQVLEAGVTITGCTVHFVAEDVDAGQIILQE 959
Cdd:cd08653 42 ALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGfWALANGDPDNVGVTVHLVDAGIDTGDVLAQA 120
|
90 100
....*....|....*....|....*....
gi 1046852587 960 AVPVQRDDTVATLSERVKAAEHKIFPAAL 988
Cdd:cd08653 121 RPPLAAGDTLLSLYLRLYRAGVELMVEAI 149
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
912-1008 |
6.16e-11 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 66.54 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 912 LNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVATLSERVKAAEHKIFPAALQLV 991
Cdd:PRK08125 101 FNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAI 180
|
90 100 110
....*....|....*....|....*....|..
gi 1046852587 992 ASGAVQL---------------GEDGKIHWAR 1008
Cdd:PRK08125 181 KHGNIPEipqdesqatyfgrrtPADGLIDWHK 212
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
833-989 |
2.55e-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: 60.53 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 833 SSSHIVLVISN--KAAVAGLDRAERAGIPTRVINHKLyksrvefdnavDHVLEEFSVDIVCLAGFMRILSGPFVRKWDGK 910
Cdd:cd08820 25 GSFEIIAVLTNtsPADVWEGSEPLYDIGSTERNLHKL-----------LEILENKGVDILISVQYHWILPGSILEKAKEI 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852587 911 MLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVATLSERVKAAEHKIFPAALQ 989
Cdd:cd08820 94 AFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYILAHYAAIALFGEHIT 172
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
821-979 |
5.43e-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: 187720 [Multi-domain] Cd Length: 180 Bit Score: 59.59 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 821 LQALIDSTRdpksssHIVLVISNKAAVAG--------LDRAERAGIP---TRVINhklyksrvefDNAVDHVLEEFSVDI 889
Cdd:cd08651 15 LEAILEAGG------EVVGVITLDDSSSNndsdyldlDSFARKNGIPyykFTDIN----------DEEIIEWIKEANPDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 890 VCLAGFMRILSGPFvrkwdgkmLNI--------HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:cd08651 79 IFVFGWSQLLKPEI--------LAIprlgvigfHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPF 150
|
170
....*....|....*...
gi 1046852587 962 PVQRDDTVATLSERVKAA 979
Cdd:cd08651 151 PIDKDDTANSLYDKIMEA 168
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
912-1008 |
7.23e-10 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 61.63 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 912 LNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVATLSERVK-AAEHKIFPAALQL 990
Cdd:PRK06988 103 YNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVTvAAEQTLWRVLPAL 182
|
90 100 110
....*....|....*....|....*....|..
gi 1046852587 991 VASGAVQLG--------------EDGKIHWAR 1008
Cdd:PRK06988 183 LAGEAPHLPndlaqgsyfggrkpEDGRIDWSK 214
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
915-1005 |
1.32e-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: 58.63 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 915 HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVATLSERVkaaehkIFPAALQLVASG 994
Cdd:cd08822 95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRA------LAPMGVKLLTQV 168
|
90
....*....|.
gi 1046852587 995 AVQLGEDGKIH 1005
Cdd:cd08822 169 IDALLRGGNLP 179
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
912-996 |
8.47e-09 |
|
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: 56.59 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 912 LNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVATLSERVKAAEHKIFPAALQLV 991
Cdd:cd08644 101 FNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLARTLPAL 180
|
....*
gi 1046852587 992 ASGAV 996
Cdd:cd08644 181 KAGKA 185
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
882-992 |
2.84e-08 |
|
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: 54.37 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 882 LEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:cd08823 67 LRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFT 146
|
90 100 110
....*....|....*....|....*....|.
gi 1046852587 962 PVQRDDTVATLSERVKAAEHKIFPAALQLVA 992
Cdd:cd08823 147 PIHPDDTYGLLCSRLAMLAVGLLEELYQNLA 177
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
57-294 |
1.11e-07 |
|
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: 54.11 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 57 ALARFCKDEKIELVVVGPEA--PLAAGIVGDLtsaGVRcfGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDAC 134
Cdd:COG0439 8 AAAELARETGIDAVLSESEFavETAAELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 135 SFIMSADFPaLVVKASGLAAGKGVIVAKSKAEACEAVQEIMQEKSFGAAGETVVVEELLEGEEVSCLCF-TDGKTVapmp 213
Cdd:COG0439 83 AFAEEIGYP-VVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLvRDGEVV---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 214 PAQDHKRLLDGDRGPNTGGMgayCPAPqVPKDLLVKIKNTIlQRTVDGMqqeGVPYtGILYAGIMLTKDG-PKVLEFNCR 292
Cdd:COG0439 158 VCSITRKHQKPPYFVELGHE---APSP-LPEELRAEIGELV-ARALRAL---GYRR-GAFHTEFLLTPDGePYLIEINAR 228
|
..
gi 1046852587 293 FG 294
Cdd:COG0439 229 LG 230
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
836-972 |
1.64e-07 |
|
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: 51.88 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 836 HIVLVISNKAAVAglDRAERAGIPtrvinhklyksRVEFDNAVDHVLEEFSVD----IVCLagfmRILSGPFVRKWDGKM 911
Cdd:cd08649 24 RIAAVVSTDPAIR--AWAAAEGIA-----------VLEPGEALEELLSDEPFDwlfsIVNL----RILPSEVLALPRKGA 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046852587 912 LNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVATL 972
Cdd:cd08649 87 INFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
915-1003 |
3.91e-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: 51.68 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 915 HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVQRDDTVATLSERVkaaehkIFPAALQLVASg 994
Cdd:cd08647 106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPEGIKAMVE- 178
|
....*....
gi 1046852587 995 AVQLGEDGK 1003
Cdd:cd08647 179 AVRLIAEGK 187
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
40-174 |
1.54e-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: 51.61 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 40 ASAGKISNAAV--SINDHTALARFCKD------EkIELVvvgPEAPLAAgivgdLTSAG-VRcfgPTAQAalLESSK-KF 109
Cdd:COG0026 26 SPAAQVADEHIvaDYDDEEALREFAERcdvvtfE-FENV---PAEALEA-----LEAEVpVR---PGPEA--LEIAQdRL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046852587 110 A-KEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPAlVVKasglAA-----GKGVIVAKSKAEACEAVQEI 174
Cdd:COG0026 92 LeKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPA-VLK----TRrggydGKGQVVIKSAADLEAAWAAL 157
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
86-290 |
5.15e-06 |
|
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: 49.55 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 86 LTSAGVRCFGPtAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPaLVVKASGLAAGKGVIVAKSKA 165
Cdd:COG0189 77 LEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGP-VVLKPLDGSGGRGVFLVEDED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 166 EA---CEAVQE------IMQEKSFGAAGETvvveellegeeVSCLCFtDGKTVAPM---PPAQDHKRlldgdrgpNT--G 231
Cdd:COG0189 155 ALesiLEALTElgsepvLVQEFIPEEDGRD-----------IRVLVV-GGEPVAAIrriPAEGEFRT--------NLarG 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046852587 232 GMGAYCPAPQVPKDLLVKIkntilqrtvdgmqqegVPYTGILYAGI--MLTKDGPKVLEFN 290
Cdd:COG0189 215 GRAEPVELTDEERELALRA----------------APALGLDFAGVdlIEDDDGPLVLEVN 259
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
512-620 |
5.92e-06 |
|
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: 49.09 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 512 IGQDLVAMCVNDILAQGAEPLFFLdyFSCG---KLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDMYppgeydLAGF 588
Cdd:cd02194 59 IGWKALAVNLSDLAAMGARPLGFL--LSLGlppDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELV------ISVT 130
|
90 100 110
....*....|....*....|....*....|....*....
gi 1046852587 589 AVGAMERHQKLPqleR--IAEGDAV-----IGVASSGLH 620
Cdd:cd02194 131 ALGEVEKGKPLR---RsgAKPGDLLyvtgtLGDAAAGLA 166
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-174 |
6.60e-06 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 6.60e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852587 110 AKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPALVVKASGLAAGK----GVIVAKSKAEACEAVQEI 174
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEM 75
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
65-166 |
2.78e-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: 48.46 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 65 EKIELVVVGPEAPLAAGIVGDLTSAGVRCFGPTAQAA-LLESSKKFAkEFMDRHGVPTAQWRAFTSPEDACSFIMSADFP 143
Cdd:TIGR01369 628 EKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIdRAEDREKFS-ELLDELGIPQPKWKTATSVEEAVEFASEIGYP 706
|
90 100
....*....|....*....|...
gi 1046852587 144 ALvVKASGLAAGKGVIVAKSKAE 166
Cdd:TIGR01369 707 VL-VRPSYVLGGRAMEIVYNEEE 728
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
111-174 |
4.35e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 47.07 E-value: 4.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852587 111 KEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPAlVVKasglAA-----GKGVIVAKSKAEACEAVQEI 174
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPA-VLK----TRrggydGKGQWVIRSAEDLEAAWALL 168
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
521-612 |
7.95e-05 |
|
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: 45.90 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 521 VNDILAQGAEPLffldYFSCG-----KLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDmyppGEYD-----LAGfaV 590
Cdd:cd02197 67 VNDLAMMGAKPL----YLSLGfileeGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPK----GKADgifinTTG--I 136
|
90 100
....*....|....*....|..
gi 1046852587 591 GAMERHQKLPqLERIAEGDAVI 612
Cdd:cd02197 137 GVIPRGVIIS-PSNIRPGDKII 157
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
110-174 |
9.71e-05 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 45.85 E-value: 9.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852587 110 AKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPALVVKASGLAAGKG----VIVAKSKAEACEAVQEI 174
Cdd:PRK00696 8 AKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGkaggVKLAKSPEEAREFAKQI 76
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
89-181 |
1.59e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 45.36 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 89 AGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWR--AFTSPEDACSFIMSADFPaLVVKASGLAAGKGVIVAKSKAE 166
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTeeGIEDIEEAKEIAEEIGYP-VIIKASAGGGGIGMRVVYSEEE 176
|
90
....*....|....*..
gi 1046852587 167 ACEAVQEIMQ--EKSFG 181
Cdd:PRK08654 177 LEDAIESTQSiaQSAFG 193
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
110-175 |
1.72e-04 |
|
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: 45.04 E-value: 1.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 110 AKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPALVVKASGLAAGK----GVIVAKSKAEACEAVQEIM 175
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEIL 77
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
86-177 |
2.11e-04 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 44.33 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 86 LTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPA-LVVKASGLAAGKGVIVAKSK 164
Cdd:COG1181 75 LELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLpLFVKPAREGSSVGVSKVKNA 154
|
90
....*....|...
gi 1046852587 165 AEACEAVQEIMQE 177
Cdd:COG1181 155 EELAAALEEAFKY 167
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
86-290 |
6.58e-04 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 42.72 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 86 LTSAGVRCFGPTaQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSADFPAlVVKASGLAAGKGVIVAKSKA 165
Cdd:TIGR00768 69 LESLGVPVINSS-DAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPV-VLKPVFGSWGRGVSLARDRQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 166 EACEAVQEIMQEKSFGAAGETVVVEELLEGEEVSCLCfTDGKTVAPMppaqdhKRLLDGDRGPNT--GGMGAYCPAPQVP 243
Cdd:TIGR00768 147 AAESLLEHFEQLNGPQNLFLVQEYIKKPGGRDIRVFV-VGDEVVAAI------YRITSGHWRSNLarGGKAEPCSLTEEI 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1046852587 244 KDLLVKIKNTIlqrtvdgmqqeGVPYTGIlyaGIMLTKDGPKVLEFN 290
Cdd:TIGR00768 220 EELAIKAAKAL-----------GLDVAGV---DLLESEDGLLVNEVN 252
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
115-178 |
1.44e-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: 1.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046852587 115 DRHGVPTAQWRAFTSPEDACSFIMSADFPAlVVKASGLA-AGKGVIVAKSKAEACEAVQEIMQEK 178
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPC-VVKARRGGyDGKGQYVVRSEADLPQAWEELGDGP 64
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
523-573 |
1.78e-03 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 41.60 E-value: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1046852587 523 DILAQGAEPLFFLDY--FSCGKLDLSTTEAVVAGIAAACRQAGCALLGGETAE 573
Cdd:COG0709 89 DVYAMGGRPLTALAIvgFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSID 141
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
62-173 |
2.65e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 41.88 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 62 CKDEKIELVVVGPEAPLAAGIVGDLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPEDACSFIMSAD 141
Cdd:PRK12815 626 AEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIG 705
|
90 100 110
....*....|....*....|....*....|..
gi 1046852587 142 FPALvVKASGLAAGKGVIVAKSKAEACEAVQE 173
Cdd:PRK12815 706 YPVL-IRPSYVIGGQGMAVVYDEPALEAYLAE 736
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
57-294 |
3.05e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 41.02 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 57 ALARFCKDEKIELVVVG--PEAPLAAGIVGDLTSAGVRCFGPTAQAALLESSKKFAKEFMDRHGVPTAQWRAFTSPED-- 132
Cdd:PRK12767 60 RLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDfk 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 133 ACSFIMSADFPaLVVKASGLAAGKGVIVAKSKAE---ACEA-----VQEIMQEKSFGAAgetvvveellegeevsCLCFT 204
Cdd:PRK12767 140 AALAKGELQFP-LFVKPRDGSASIGVFKVNDKEElefLLEYvpnliIQEFIEGQEYTVD----------------VLCDL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852587 205 DGKTVAPMPpaqdHKRL--LDG--DRGpntggmgaycpapqvpkdllVKIKNTILQRTVDGMQQEgVPYTGILYAGIMLT 280
Cdd:PRK12767 203 NGEVISIVP----RKRIevRAGetSKG--------------------VTVKDPELFKLAERLAEA-LGARGPLNIQCFVT 257
|
250
....*....|....
gi 1046852587 281 KDGPKVLEFNCRFG 294
Cdd:PRK12767 258 DGEPYLFEINPRFG 271
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
518-577 |
6.28e-03 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 39.81 E-value: 6.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046852587 518 AMCVN--DILAQGAEPLFFLdyFSCG---KLDLSTTEAVVAGIAAACRQAGCALLGGETAEMPDM 577
Cdd:PRK05731 66 ALAVNlsDLAAMGARPAAFL--LALAlpkDLDEAWLEALADGLFELADRYGAELIGGDTTRGPDL 128
|
|
| |
