|
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: 669.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 4 RVLVIGSGGREHTLAWKLAQSPRVKQVLVAPGNAGTACLEKisNTAISVGDHTALAQFCKDEKVAFVVVGPEAPLAAGIV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 84 GDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPaLVVKASGLAAGKGVIVAKS 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 164 KEEACKAVQEIMQEKTFGAAG------------EtvvveellegeeVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTG 231
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGarvvieeflegeE------------ASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 232 GMGAYCPAPQISKDLLLKIKNTILQRTVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYE 311
Cdd:COG0151 227 GMGAYSPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 312 VIQSTLDGLLCSSLPSWlENHTAVTVVMASKGYPGAYTKGMEITGIPEAQALGLEVFHAGTALKDGKVVTSGGRVLTVTA 391
Cdd:COG0151 307 LLLAAAEGRLDEVELEW-DDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTA 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 1196716964 392 IRENLKSALEEAKKGLATIKFEGAVYRKDIGFHAIA 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: 627.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 4 RVLVIGSGGREHTLAWKLAQSPRVKQVLVAPGNAGTACLEKISNTAISVGDHTALAQFCKDEKVAFVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 84 GDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 164 KEEACKAVQEIMQEKtFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGAYCPAPQIS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 244 KDLLLKIKNTILQRTVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLCs 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 324 SLPSWLENHTAVTVVMASKGYPGAYTKGMEITGIPEAQALGLEVFHAGTALKDGKVVTSGGRVLTVTAIRENLKSALEEA 403
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 1196716964 404 KKGLATIKFEGAVYRKDIGFHAI 426
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
431-727 |
1.01e-156 |
|
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: 464.51 E-value: 1.01e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 431 QPRGLTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCDVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHS 510
Cdd:COG0150 1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 511 TIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAV 590
Cdd:COG0150 81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 591 GGMERYQKLPHlEQIVEGDVVVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPGgcGDQTL------------------- 651
Cdd:COG0150 161 GVVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLgealleptriyvkpvlall 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 652 --------------------------------DARTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTDHIL 699
Cdd:COG0150 238 kavdvhgmahitggglpenlprvlpeglgaviDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAAL 317
|
330 340
....*....|....*....|....*...
gi 1196716964 700 REIQQRQEEAWVIGSVVACPEgsPRVKV 727
Cdd:COG0150 318 ALLKAAGETAYVIGEVVAGEG--EGVVL 343
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
4.41e-154 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 461.52 E-value: 4.41e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 6 LVIGSGGREHTLAWKLAQSPRVKQVLVAPGNAGTACLEKISNTA-ISVGDHTALAQFCKDEKVAFVVVGPEAPLAAGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 85 DLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPaLVVKASGLAAGKGVIVAKSK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 165 EEACKAVQEIMQEKTFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGAYCPAPQISK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 245 DLLLKIKNTILQRTVDGMQQEGTPYTGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLC 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 323 SSLPSWLENhTAVTVVMASKGYPGAYTKGMEITGIPEAQAL--GLEVFHAGTALK-DGKVVTSGGRVLTVTAIRENLKSA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 1196716964 400 LEEAKKGLATIKFEGAVYRKDIGFHAIAFLQQPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-716 |
1.85e-130 |
|
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: 394.92 E-value: 1.85e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 469 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTT 548
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 549 EAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGGMERYQKLPHlEQIVEGDVVVGIASSGLHSNGFSLVR 628
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 629 KIVAQSSLEYSSLAPGgcGDQTL---------------------------------------------------DARTWR 657
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLgeelltptriyvkpilpllekvlvkgmahitggglpenlprvlpeglgaviDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196716964 658 IPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTDHILREIQQRQEEAWVIGSVV 716
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
435-717 |
8.92e-115 |
|
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: 355.49 E-value: 8.92e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 435 LTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCDVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQLCNKHSTIGQ 514
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 515 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGGME 594
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 595 RYQKLPHlEQIVEGDVVVGIASSGLHSNGFSLVRKIV---AQSSLEYSS-----------LAP----------------- 643
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLediAGLDYEDTPeefgktlgeelLEPtriyvkpileliksviv 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 644 --------GGCGDQTL-----------DARTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTDHILREIQQ 704
Cdd:TIGR00878 239 hglahitgGGLLENIPrrlpdglkaviDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNA 318
|
330
....*....|...
gi 1196716964 705 RQEEAWVIGSVVA 717
Cdd:TIGR00878 319 YGEKAWVIGEVKK 331
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
5.72e-108 |
|
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: 331.94 E-value: 5.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 105 SSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKTFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 185 ETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGAYCPAPQISKDLLLKIKNTILQRTVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 1196716964 265 EGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
758-940 |
7.86e-103 |
|
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: 318.18 E-value: 7.86e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 758 RVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINHKLYKNREEFDGAIDQVLEEFATD 837
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 838 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDT 917
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 1196716964 918 VATLSEKVKVAEHKIFPKALQLV 940
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
756-953 |
3.15e-101 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 314.66 E-value: 3.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 756 KARVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINHKLYKNREEFDGAIDQVLEEFA 835
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 836 TDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRG 915
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1196716964 916 DTVATLSEKVKVAEHKIFPKALQLVASGTIWLgENNKV 953
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTL-DGRRV 197
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
434-716 |
4.13e-96 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 307.89 E-value: 4.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 434 GLTYKDSGVDIAAGNMLVKKIQPLAkatsrPGcdvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQLCNKHSTIG 513
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGGM 593
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 594 ERyQKLPHLEQIVEGDVVVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPGG---CGD-----------QTLD------- 652
Cdd:PLN02557 204 KK-DAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGAsvtIGEalmaptviyvkQVLDiiskggv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 653 ----------------------------ARTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTDHILREiqq 704
Cdd:PLN02557 283 kgiahitgggftdniprvfpkglgakirTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEE--- 359
|
330
....*....|..
gi 1196716964 705 RQEEAWVIGSVV 716
Cdd:PLN02557 360 GAYPAYRIGEVI 371
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
757-945 |
6.38e-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: 243.82 E-value: 6.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 757 ARVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINHKLYKNREEFDGAIDQVLEEFAT 836
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 837 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGD 916
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180
....*....|....*....|....*....
gi 1196716964 917 TVATLSEKVKVAEHKIFPKALQLVASGTI 945
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRL 189
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
757-937 |
2.26e-72 |
|
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: 236.80 E-value: 2.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 757 ARVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINHKLYKNREEFDGAIDQVLEEFAT 836
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 837 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGD 916
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|.
gi 1196716964 917 TVATLSEKVKVAEHKIFPKAL 937
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
758-945 |
1.31e-36 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 137.13 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 758 RVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINhklyKNREEFDG----AIDQVLEE 833
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYP----KTKGEPDGlspdELVDALRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 834 FATDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKG-----SNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQE 908
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQR 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1196716964 909 AVPVKRGDTVATLSEKVKVAEHKIFPKALQLVASGTI 945
Cdd:PLN02331 157 VVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERI 193
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
489-591 |
1.18e-23 |
|
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 96.36 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 489 LASGTDGVGTKLKIaqlcNKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDL--RTTEAVVAGVAEACKQAGCAL 566
Cdd:pfam00586 5 VAVTTDGHGTPSLV----DPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEveWVLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*
gi 1196716964 567 LGGETAEMPDMYPPgeyDLAGFAVG 591
Cdd:pfam00586 81 VGGDTSFDPEGGKP---TISVTAVG 102
|
|
| |
|
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: 669.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 4 RVLVIGSGGREHTLAWKLAQSPRVKQVLVAPGNAGTACLEKisNTAISVGDHTALAQFCKDEKVAFVVVGPEAPLAAGIV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 84 GDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPaLVVKASGLAAGKGVIVAKS 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 164 KEEACKAVQEIMQEKTFGAAG------------EtvvveellegeeVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTG 231
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGarvvieeflegeE------------ASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 232 GMGAYCPAPQISKDLLLKIKNTILQRTVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYE 311
Cdd:COG0151 227 GMGAYSPAPVVTEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 312 VIQSTLDGLLCSSLPSWlENHTAVTVVMASKGYPGAYTKGMEITGIPEAQALGLEVFHAGTALKDGKVVTSGGRVLTVTA 391
Cdd:COG0151 307 LLLAAAEGRLDEVELEW-DDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTA 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 1196716964 392 IRENLKSALEEAKKGLATIKFEGAVYRKDIGFHAIA 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: 627.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 4 RVLVIGSGGREHTLAWKLAQSPRVKQVLVAPGNAGTACLEKISNTAISVGDHTALAQFCKDEKVAFVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 84 GDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 164 KEEACKAVQEIMQEKtFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGAYCPAPQIS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 244 KDLLLKIKNTILQRTVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLCs 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 324 SLPSWLENHTAVTVVMASKGYPGAYTKGMEITGIPEAQALGLEVFHAGTALKDGKVVTSGGRVLTVTAIRENLKSALEEA 403
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 1196716964 404 KKGLATIKFEGAVYRKDIGFHAI 426
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
431-727 |
1.01e-156 |
|
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: 464.51 E-value: 1.01e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 431 QPRGLTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCDVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHS 510
Cdd:COG0150 1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 511 TIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAV 590
Cdd:COG0150 81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 591 GGMERYQKLPHlEQIVEGDVVVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPGgcGDQTL------------------- 651
Cdd:COG0150 161 GVVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLgealleptriyvkpvlall 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 652 --------------------------------DARTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTDHIL 699
Cdd:COG0150 238 kavdvhgmahitggglpenlprvlpeglgaviDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAAL 317
|
330 340
....*....|....*....|....*...
gi 1196716964 700 REIQQRQEEAWVIGSVVACPEgsPRVKV 727
Cdd:COG0150 318 ALLKAAGETAYVIGEVVAGEG--EGVVL 343
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
4.41e-154 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 461.52 E-value: 4.41e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 6 LVIGSGGREHTLAWKLAQSPRVKQVLVAPGNAGTACLEKISNTA-ISVGDHTALAQFCKDEKVAFVVVGPEAPLAAGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 85 DLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPaLVVKASGLAAGKGVIVAKSK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 165 EEACKAVQEIMQEKTFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGAYCPAPQISK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 245 DLLLKIKNTILQRTVDGMQQEGTPYTGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLC 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 323 SSLPSWLENhTAVTVVMASKGYPGAYTKGMEITGIPEAQAL--GLEVFHAGTALK-DGKVVTSGGRVLTVTAIRENLKSA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 1196716964 400 LEEAKKGLATIKFEGAVYRKDIGFHAIAFLQQPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-716 |
1.85e-130 |
|
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: 394.92 E-value: 1.85e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 469 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTT 548
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 549 EAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGGMERYQKLPHlEQIVEGDVVVGIASSGLHSNGFSLVR 628
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 629 KIVAQSSLEYSSLAPGgcGDQTL---------------------------------------------------DARTWR 657
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLgeelltptriyvkpilpllekvlvkgmahitggglpenlprvlpeglgaviDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196716964 658 IPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTDHILREIQQRQEEAWVIGSVV 716
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
435-717 |
8.92e-115 |
|
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: 355.49 E-value: 8.92e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 435 LTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCDVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQLCNKHSTIGQ 514
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 515 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGGME 594
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 595 RYQKLPHlEQIVEGDVVVGIASSGLHSNGFSLVRKIV---AQSSLEYSS-----------LAP----------------- 643
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLediAGLDYEDTPeefgktlgeelLEPtriyvkpileliksviv 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 644 --------GGCGDQTL-----------DARTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTDHILREIQQ 704
Cdd:TIGR00878 239 hglahitgGGLLENIPrrlpdglkaviDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNA 318
|
330
....*....|...
gi 1196716964 705 RQEEAWVIGSVVA 717
Cdd:TIGR00878 319 YGEKAWVIGEVKK 331
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
5.72e-108 |
|
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: 331.94 E-value: 5.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 105 SSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKTFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 185 ETVVVEELLEGEEVSCLCFTDGRTVVPMPPAQDHKRLLEGDLGPNTGGMGAYCPAPQISKDLLLKIKNTILQRTVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 1196716964 265 EGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
758-940 |
7.86e-103 |
|
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: 318.18 E-value: 7.86e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 758 RVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINHKLYKNREEFDGAIDQVLEEFATD 837
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 838 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDT 917
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 1196716964 918 VATLSEKVKVAEHKIFPKALQLV 940
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
756-953 |
3.15e-101 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 314.66 E-value: 3.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 756 KARVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINHKLYKNREEFDGAIDQVLEEFA 835
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 836 TDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRG 915
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1196716964 916 DTVATLSEKVKVAEHKIFPKALQLVASGTIWLgENNKV 953
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTL-DGRRV 197
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
434-716 |
4.13e-96 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 307.89 E-value: 4.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 434 GLTYKDSGVDIAAGNMLVKKIQPLAkatsrPGcdvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQLCNKHSTIG 513
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMYPPGEYDLAGFAVGGM 593
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 594 ERyQKLPHLEQIVEGDVVVGIASSGLHSNGFSLVRKIVAQSSLEYSSLAPGG---CGD-----------QTLD------- 652
Cdd:PLN02557 204 KK-DAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGAsvtIGEalmaptviyvkQVLDiiskggv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 653 ----------------------------ARTWRIPRVFSWLQQEGQLSEEEMARTFNCGVGAALVVSKDQTDHILREiqq 704
Cdd:PLN02557 283 kgiahitgggftdniprvfpkglgakirTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEE--- 359
|
330
....*....|..
gi 1196716964 705 RQEEAWVIGSVV 716
Cdd:PLN02557 360 GAYPAYRIGEVI 371
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
757-945 |
6.38e-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: 243.82 E-value: 6.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 757 ARVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINHKLYKNREEFDGAIDQVLEEFAT 836
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 837 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGD 916
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180
....*....|....*....|....*....
gi 1196716964 917 TVATLSEKVKVAEHKIFPKALQLVASGTI 945
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRL 189
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
757-937 |
2.26e-72 |
|
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: 236.80 E-value: 2.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 757 ARVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINHKLYKNREEFDGAIDQVLEEFAT 836
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 837 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGD 916
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|.
gi 1196716964 917 TVATLSEKVKVAEHKIFPKAL 937
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
4-104 |
1.22e-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: 170.23 E-value: 1.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 4 RVLVIGSGGREHTLAWKLAQSPRVKQVLVAPGNAGTACLEKisNTAISVGDHTALAQFCKDEKVAFVVVGPEAPLAAGIV 83
Cdd:pfam02844 2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 1196716964 84 GDL--ASAGVRCFGPTAEAAQLE 104
Cdd:pfam02844 80 DALreRAAGIPVFGPSKAAAQLE 102
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
761-939 |
9.75e-42 |
|
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.
Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 150.52 E-value: 9.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 761 VLISGTGSNLQALIDSTQDPNSAaHIVVVISNKPAVAGLNKAEKAGIptrviNHKLYKNREEFDGAIDQVLEEFATDIVC 840
Cdd:cd08369 1 IVILGSGNIGQRVLKALLSKEGH-EIVGVVTHPDSPRGTAQLSLELV-----GGKVYLDSNINTPELLELLKEFAPDLIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 841 LAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVAT 920
Cdd:cd08369 75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154
|
170
....*....|....*....
gi 1196716964 921 LSEKVKVAEHKIFPKALQL 939
Cdd:cd08369 155 LYQRLIELGPKLLKEALQK 173
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-423 |
1.82e-40 |
|
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: 143.74 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 334 AVTVVMASKGYPGAYTKGMEITGIPEAqalGLEVFHAGTALKDGKVVTSGGRVLTVTAIRENLKSALEEAKKGLATIKFE 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA---GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|
gi 1196716964 414 GAVYRKDIGF 423
Cdd:pfam02843 78 GMFYRKDIGT 87
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
749-933 |
2.56e-39 |
|
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440551 [Multi-domain] Cd Length: 282 Bit Score: 147.50 E-value: 2.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 749 HFPAQQKkaRVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLnkAEKAGIPTRVINHKLyKNREEFDGAID 828
Cdd:COG0788 81 HDSDRRK--RVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 829 QVLEEFATDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQE 908
Cdd:COG0788 156 ELLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQD 235
|
170 180 190
....*....|....*....|....*....|....*...
gi 1196716964 909 AVPVKRGDTVA------------TLSEKVK-VAEHKIF 933
Cdd:COG0788 236 VERVDHRDTPEdlvrkgrdvekrVLARAVRwHLEDRVL 273
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
758-945 |
1.31e-36 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 137.13 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 758 RVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNKAEKAGIPTRVINhklyKNREEFDG----AIDQVLEE 833
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYP----KTKGEPDGlspdELVDALRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 834 FATDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKG-----SNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQE 908
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQR 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1196716964 909 AVPVKRGDTVATLSEKVKVAEHKIFPKALQLVASGTI 945
Cdd:PLN02331 157 VVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERI 193
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
758-953 |
1.09e-35 |
|
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: 134.23 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 758 RVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLnkAEKAGIPTRVIN-HKlyKNREEFDGAIDQVLEEFAT 836
Cdd:cd08648 2 RVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPL--AERFGIPFHHIPvTK--DTKAEAEAEQLELLEEYGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 837 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGD 916
Cdd:cd08648 78 DLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRD 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1196716964 917 TVATLSEKVKVAEHKIFPKALQLVASGTIWLGENNKV 953
Cdd:cd08648 158 SVEDLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTV 194
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
749-921 |
3.37e-31 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 124.06 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 749 HFPAQQKkaRVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLnkAEKAGIPTRVINH-KLykNREEFDGAI 827
Cdd:PRK06027 84 LDSAERK--RVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEARL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 828 DQVLEEFATDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQ 907
Cdd:PRK06027 158 LELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQ 237
|
170
....*....|....
gi 1196716964 908 EAVPVKRGDTVATL 921
Cdd:PRK06027 238 DVIRVDHRDTAEDL 251
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
751-952 |
6.35e-25 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 105.21 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 751 PAQQKKARVAVLISGTGSNLQALIDSTQDPNSAAHIVVVISNK---PAVAGLNKAEKAGIPTRVINHKLYKNREefdgai 827
Cdd:PLN02828 65 PGLDPKYKIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNHergPNTHVMRFLERHGIPYHYLPTTKENKRE------ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 828 DQVLEEFA-TDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIIL 906
Cdd:PLN02828 139 DEILELVKgTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIE 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1196716964 907 QEAVPVKRGDTVATLSEKVKVAEHKIFPKALQLVASGTIWLGENNK 952
Cdd:PLN02828 219 QMVERVSHRDNLRSFVQKSENLEKQCLAKAIKSYCELRVLPYGTNK 264
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
489-714 |
1.60e-24 |
|
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: 102.86 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 489 LASGTDGVGTKLKIaqlcnKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGK-LDLRTTEAVVAGVAEACKQAGCALL 567
Cdd:cd00396 2 LAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 568 GGETAEMPDMYPPgEYDLAGFAVGGMERyQKLPHLEQIVEGDVVvgIASSGLHSNGFSLVRKIVAQSSL-------EYSS 640
Cdd:cd00396 77 GGHTSVSPGTMGH-KLSLAVFAIGVVEK-DRVIDSSGARPGDVL--ILTGVDAVLELVAAGDVHAMHDItdggllgTLPE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196716964 641 LAP-GGCGDQtLDARTWRIPRVFSWLQQEgqlsEEEMARTFNCGVGAALVVSKDQTDHILREIQQRQEEAWVIGS 714
Cdd:cd00396 153 LAQaSGVGAE-IDLEAIPLDEVVRWLCVE----HIEEALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
786-933 |
3.95e-24 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 103.52 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 786 IVVVISNKPAVAGLnkAEKAGIPTRVInhKLYK-NREEFDGAIDQVLEEFATDIVCLAGFMRILSGPFVRKWDGKMLNIH 864
Cdd:PRK13011 119 IVGVVSNHPDLEPL--AAWHGIPFHHF--PITPdTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 865 PSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRG----DTVA--------TLSEKVK-VAEHK 931
Cdd:PRK13011 195 HSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAyspeDLVAkgrdveclTLARAVKaHIERR 274
|
..
gi 1196716964 932 IF 933
Cdd:PRK13011 275 VF 276
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
489-591 |
1.18e-23 |
|
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 96.36 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 489 LASGTDGVGTKLKIaqlcNKHSTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDL--RTTEAVVAGVAEACKQAGCAL 566
Cdd:pfam00586 5 VAVTTDGHGTPSLV----DPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEveWVLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*
gi 1196716964 567 LGGETAEMPDMYPPgeyDLAGFAVG 591
Cdd:pfam00586 81 VGGDTSFDPEGGKP---TISVTAVG 102
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
786-933 |
3.47e-21 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 94.86 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 786 IVVVISNKPAVAGLnkAEKAGIPTRVInhKLYK-NREEFDGAIDQVLEEFATDIVCLAGFMRILSGPFVRKWDGKMLNIH 864
Cdd:PRK13010 123 IVGIISNHPDLQPL--AVQHDIPFHHL--PVTPdTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIH 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 865 PSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRG----DTVA--------TLSEKVKV-AEHK 931
Cdd:PRK13010 199 HSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSyspeDLVAkgrdveclTLARAVKAfIEHR 278
|
..
gi 1196716964 932 IF 933
Cdd:PRK13010 279 VF 280
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
770-945 |
3.84e-19 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 89.39 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 770 LQALIDStqdpnsAAHIVVVISNKPAVAGLNK----------AEKAGIPtrVIN-HKLykNREEFdgaIDQvLEEFATDI 838
Cdd:COG0223 16 LEALLAA------GHEVVAVVTQPDRPAGRGRkltpspvkelALEHGIP--VLQpESL--KDPEF---LEE-LRALNPDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 839 VCLAGFMRILSGPFvrkWD---GKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRG 915
Cdd:COG0223 82 IVVVAYGQILPKEV---LDiprLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPD 158
|
170 180 190
....*....|....*....|....*....|
gi 1196716964 916 DTVATLSEKVKVAEHKIFPKALQLVASGTI 945
Cdd:COG0223 159 DTAGSLHDKLAELGAELLLETLDALEAGTL 188
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
802-945 |
4.32e-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: 80.14 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 802 AEKAGIPtrVINHKLYKNREEFdgaidQVLEEFATDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVL 881
Cdd:TIGR00460 52 AEEKGIP--VFQPEKQRQLEEL-----PLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAI 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196716964 882 EAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSEKVKVAEHKIFPKALQLVASGTI 945
Cdd:TIGR00460 125 LNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKN 188
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
755-924 |
2.59e-15 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 78.20 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 755 KKARVAVLisGT----GSNLQALIDSTQDPNSAAHIVVVISNKPAVAGLNK----------AEKAGIPTRVINHKLYKNR 820
Cdd:PLN02285 5 RKKRLVFL--GTpevaATVLDALLDASQAPDSAFEVAAVVTQPPARRGRGRklmpspvaqlALDRGFPPDLIFTPEKAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 821 EEFDGAidqvLEEFATDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVD 900
Cdd:PLN02285 83 EDFLSA----LRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALD 158
|
170 180
....*....|....*....|....
gi 1196716964 901 AGQIILQEAVPVKRGDTVATLSEK 924
Cdd:PLN02285 159 AGPVIAQERVEVDEDIKAPELLPL 182
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
770-924 |
2.19e-12 |
|
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: 67.08 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 770 LQALIDSTqdpnsaAHIVVVISNKPAVAGLNK----------AEKAGIPTrvinHKLYKNREEfdgAIDQVLEEFATDIV 839
Cdd:cd08646 16 LEALLKSG------HEVVAVVTQPDKPRGRGKkltpspvkelALELGLPV----LQPEKLKDE---EFLEELKALKPDLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 840 CLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVA 919
Cdd:cd08646 83 VVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAG 162
|
....*
gi 1196716964 920 TLSEK 924
Cdd:cd08646 163 ELLDK 167
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
829-921 |
3.83e-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: 64.93 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 829 QVLEEFATDIVCLAGfMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAH-EQVLEAGVTITGCTVHFVAEDVDAGQIILQ 907
Cdd:cd08653 41 AALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGfWALANGDPDNVGVTVHLVDAGIDTGDVLAQ 119
|
90
....*....|....
gi 1196716964 908 EAVPVKRGDTVATL 921
Cdd:cd08653 120 ARPPLAAGDTLLSL 133
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
607-725 |
4.19e-12 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 65.06 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 607 EGDVVVGIASSGLHSNGFSLVRKIVAQSSLEYSSLA---------------------------PGGCG----------DQ 649
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGLAAVQLGdplleptliyvklllaalgglvkamhdITGGGlagalaemapAS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196716964 650 TLDAR-TWRIPRVFSWLQqegqlSEEEMARTFNCGVGAALVVSKDQtDHILREIQQRQEEAWVIGSVVACPEGSPRV 725
Cdd:pfam02769 82 GVGAEiDLDKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEEA-EAVLAILEKEGLEAAVIGEVTAGGRLTVIV 152
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
801-945 |
2.36e-10 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 64.23 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 801 KAEKAGIPTRV---INHKLYKNReefdgaidqvLEEFATDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAH 877
Cdd:PRK08125 48 LAAELGIPVYApedVNHPLWVER----------IRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPL 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196716964 878 EQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSEKVKVAEHKIFPKALQLVASGTI 945
Cdd:PRK08125 118 NWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAIKHGNI 185
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
800-945 |
3.76e-10 |
|
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.
Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 60.44 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 800 NKAEKAGIPT---RVINHKLYKNReefdgaidqvLEEFATDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNA 876
Cdd:cd08644 47 QLAREHGIPVftpDDINHPEWVER----------LRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAP 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196716964 877 HEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSEKVKVAEHKIFPKALQLVASGTI 945
Cdd:cd08644 117 LNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLARTLPALKAGKA 185
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
770-937 |
1.68e-09 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 58.05 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 770 LQALIDSTqdpnsaAHIVVVISNKPAVAG--------LNKAEKAGIPTRVINHKlykNREEfdgaIDQVLEEFATDIVCL 841
Cdd:cd08651 15 LEAILEAG------GEVVGVITLDDSSSNndsdyldlDSFARKNGIPYYKFTDI---NDEE----IIEWIKEANPDIIFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 842 AGFMRILSGPFvrkwdgkmLNI--------HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVK 913
Cdd:cd08651 82 FGWSQLLKPEI--------LAIprlgvigfHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPID 153
|
170 180
....*....|....*....|....
gi 1196716964 914 RGDTVATLSEKVKVAEHKIFPKAL 937
Cdd:cd08651 154 KDDTANSLYDKIMEAAKQQIDKFL 177
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
781-938 |
1.75e-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: 187722 [Multi-domain] Cd Length: 173 Bit Score: 57.84 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 781 NSAAHIVVVISNKPAVAGLNKAEKAGI--PTRVINHKLyknreefdgaiDQVLEEFATDIVCLAGFMRILSGPFVRKWDG 858
Cdd:cd08820 24 RGSFEIIAVLTNTSPADVWEGSEPLYDigSTERNLHKL-----------LEILENKGVDILISVQYHWILPGSILEKAKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 859 KMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSEKVKVAEHKIFPKALQ 938
Cdd:cd08820 93 IAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYILAHYAAIALFGEHIT 172
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
864-953 |
1.36e-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: 187724 [Multi-domain] Cd Length: 192 Bit Score: 55.54 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 864 HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSEKVkvaehkIFPKALQLVASG 943
Cdd:cd08822 95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRA------LAPMGVKLLTQV 168
|
90
....*....|
gi 1196716964 944 TIWLGENNKV 953
Cdd:cd08822 169 IDALLRGGNL 178
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
861-945 |
2.27e-08 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 57.01 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 861 LNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSEKVKVAEHKIFPKALQLV 940
Cdd:PRK06988 103 YNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVTVAAEQTLWRVLPAL 182
|
....*
gi 1196716964 941 ASGTI 945
Cdd:PRK06988 183 LAGEA 187
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
759-941 |
5.07e-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: 53.60 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 759 VAVLISGtgSNLQALIDSTQDPNSAAHIVVVISNkpAVAGLNKAEKAGIPTRVINHKLYKNREEfdGAIDQVLEEFATDI 838
Cdd:cd08823 1 IVILCNT--SMAAPLLGQLLSEGRLAGIAVPAHN--ASYFPQIFVFTGIRRLVSKQRVDTANLK--EQLAEWLRALAADT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 839 VCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTV 918
Cdd:cd08823 75 VVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTY 154
|
170 180
....*....|....*....|...
gi 1196716964 919 ATLSEKVKVAEHKIFPKALQLVA 941
Cdd:cd08823 155 GLLCSRLAMLAVGLLEELYQNLA 177
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
785-924 |
1.67e-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: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 785 HIVVVISNKPAVAglNKAEKAGIPtrvinhkLYKNREEFDGAIDQVLEEFATDIVCLagfmRILSGPFVRKWDGKMLNIH 864
Cdd:cd08649 24 RIAAVVSTDPAIR--AWAAAEGIA-------VLEPGEALEELLSDEPFDWLFSIVNL----RILPSEVLALPRKGAINFH 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 865 PSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSEK 924
Cdd:cd08649 91 DGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSLNLK 150
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
57-294 |
1.07e-06 |
|
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: 51.03 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 57 ALAQFCKDEKVAFVVVGPEA--PLAAGIVGDLasaGVRcfGPTAEAAQLESSKRFAKEFMDRHRIPTAQWRAFTKAEKAC 134
Cdd:COG0439 8 AAAELARETGIDAVLSESEFavETAAELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 135 SFIMSADFPaLVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKTFGAAGETVVVEELLEGEEVSCLCFTDGRTVVPMPP 214
Cdd:COG0439 83 AFAEEIGYP-VVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 215 AQDHKrllegdLGPNTGGMGAYCPAPqISKDLLLKIKNTIlQRTVD--GMQqegtpyTGILYAGIMLTKDG-PKVLEFNC 291
Cdd:COG0439 162 TRKHQ------KPPYFVELGHEAPSP-LPEELRAEIGELV-ARALRalGYR------RGAFHTEFLLTPDGePYLIEINA 227
|
...
gi 1196716964 292 RFG 294
Cdd:COG0439 228 RLG 230
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
864-944 |
1.39e-05 |
|
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: 47.06 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 864 HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSEKVKVAEH-KIFPKALQLVAS 942
Cdd:cd08647 106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPEGiKAMVEAVRLIAE 185
|
..
gi 1196716964 943 GT 944
Cdd:cd08647 186 GK 187
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
512-571 |
3.01e-05 |
|
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).
Pssm-ID: 100030 [Multi-domain] Cd Length: 291 Bit Score: 46.78 E-value: 3.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196716964 512 IGQDLVAMCVNDILAQGAEPLFFLdyFSCG---KLDLRTTEAVVAGVAEACKQAGCALLGGET 571
Cdd:cd02194 59 IGWKALAVNLSDLAAMGARPLGFL--LSLGlppDTDEEWLEEFYRGLAEAADRYGVPLVGGDT 119
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
520-612 |
2.97e-04 |
|
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100031 [Multi-domain] Cd Length: 287 Bit Score: 43.66 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 520 CVNDILAQGAEPLFFLDYFSC----GKLDLRTTEAVVAGVAEACKQAGCALLGGETAEMPDMyppgeydLAGFAVGGMER 595
Cdd:cd02195 80 ALSDIYAMGAKPLSALAIVTLprklPALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEP-------KYGLSVTGLVH 152
|
90
....*....|....*..
gi 1196716964 596 YQKLPHLEQIVEGDVVV 612
Cdd:cd02195 153 PNKILRNSGAKPGDVLI 169
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
65-166 |
3.00e-04 |
|
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: 44.99 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 65 EKVAFVVVGPEAPLAAGIVGDLASAGVRCFGPTAEAA-QLESSKRFAkEFMDRHRIPTAQWRAFTKAEKACSFIMSADFP 143
Cdd:TIGR01369 628 EKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIdRAEDREKFS-ELLDELGIPQPKWKTATSVEEAVEFASEIGYP 706
|
90 100
....*....|....*....|...
gi 1196716964 144 ALvVKASGLAAGKGVIVAKSKEE 166
Cdd:TIGR01369 707 VL-VRPSYVLGGRAMEIVYNEEE 728
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
86-290 |
3.03e-04 |
|
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: 43.78 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 86 LASAGVRCFGPtAEAAQLESSKRFAKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPaLVVKASGLAAGKGVIVAKSKE 165
Cdd:COG0189 77 LEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGP-VVLKPLDGSGGRGVFLVEDED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 166 EACKAVQE---------IMQEKTFGAAGETVvveellegeevSCLCFtDGRTVVPM---PPAQDHKRllegdlgpNT--G 231
Cdd:COG0189 155 ALESILEAltelgsepvLVQEFIPEEDGRDI-----------RVLVV-GGEPVAAIrriPAEGEFRT--------NLarG 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196716964 232 GMGAYCPAPQISKDLLLKIkntilqrtvdgmqqegTPYTGILYAGI--MLTKDGPKVLEFN 290
Cdd:COG0189 215 GRAEPVELTDEERELALRA----------------APALGLDFAGVdlIEDDDGPLVLEVN 259
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
523-573 |
3.73e-04 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 43.91 E-value: 3.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1196716964 523 DILAQGAEPLFFLDY--FSCGKLDLRTTEAVVAGVAEACKQAGCALLGGETAE 573
Cdd:COG0709 89 DVYAMGGRPLTALAIvgFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSID 141
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-174 |
5.09e-04 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 42.25 E-value: 5.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196716964 110 AKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPALVVKASGLAAGK----GVIVAKSKEEACKAVQEI 174
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEM 75
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
521-575 |
9.87e-04 |
|
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100033 [Multi-domain] Cd Length: 293 Bit Score: 42.05 E-value: 9.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 521 VNDILAQGAEPLffldYFSCG-----KLDLRTTEAVVAGVAEACKQAGCALLGGETAEMP 575
Cdd:cd02197 67 VNDLAMMGAKPL----YLSLGfileeGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVP 122
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
111-174 |
2.39e-03 |
|
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: 41.21 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196716964 111 KEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPAlVVKasglAA-----GKGVIVAKSKEEACKAVQEI 174
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPA-VLK----TRrggydGKGQVVIKSAADLEAAWAAL 157
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
78-166 |
2.54e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 41.88 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 78 LAAGIvgdLASAGVRCFGPTAEAAQL-ESSKRFaKEFMDRHRIPTAQWRAFTKAEKACSFIMSADFPALVVKASGLaAGK 156
Cdd:PRK12815 103 HEDGI---LEQYGVELLGTNIEAIQKgEDRERF-RALMKELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTL-GGT 177
|
90
....*....|
gi 1196716964 157 GVIVAKSKEE 166
Cdd:PRK12815 178 GGGIAENLEE 187
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
89-181 |
3.95e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 40.74 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 89 AGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTAQWR--AFTKAEKACSFIMSADFPaLVVKASGLAAGKGVIVAKSKEE 166
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTeeGIEDIEEAKEIAEEIGYP-VIIKASAGGGGIGMRVVYSEEE 176
|
90
....*....|....*..
gi 1196716964 167 ACKAVQEIMQ--EKTFG 181
Cdd:PRK08654 177 LEDAIESTQSiaQSAFG 193
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
57-177 |
4.07e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 40.64 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196716964 57 ALAQFCKDEKVAFVVVG--PEAPLAAGIVGDLASAGVRCFGPTAEAAQLESSKRFAKEFMDRHRIPTAqwRAFTKAE--- 131
Cdd:PRK12767 60 RLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTP--KSYLPESled 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1196716964 132 -KACSFIMSADFPaLVVKASGLAAGKGVIVAKSKEE---ACKAVQEIM-QE 177
Cdd:PRK12767 138 fKAALAKGELQFP-LFVKPRDGSASIGVFKVNDKEElefLLEYVPNLIiQE 187
|
|
| |
