|
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: 706.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTTCTGKisNAAVSVNDHSALAQFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 84 GDLTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPaLVVKASGLAAGKGVIVAKS 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 164 TAEACKAVQEMMQEKSFGAAGETVVVEEFLEGEEVSCLCFTDGKTVAEMPPAQDHKRLLDGDEGPNTGGMGAYCPAPQVS 243
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 244 KDLLVKIKNTILQRAVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLSA 323
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 324 SLPVWLENHsAVTVVMASEGYPGAYPKGVEITGFPEAQALGLQVFHAGTALKDGRVVTSGGRVLTVTAVQENLMSALTEA 403
Cdd:COG0151 319 VELEWDDRA-AVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERA 397
|
410 420
....*....|....*....|....
gi 1195504543 404 RKGLAALKFEGAVYRKDIGFRAVA 427
Cdd:COG0151 398 YEAVEKIRFEGMFYRRDIGWRALK 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: 651.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTTCTGKISNAAVSVNDHSALAQFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 84 GDLTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 164 TAEACKAVQEMMQEKsFGAAGETVVVEEFLEGEEVSCLCFTDGKTVAEMPPAQDHKRLLDGDEGPNTGGMGAYCPAPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 244 KDLLVKIKNTILQRAVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLsA 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKL-D 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 324 SLPVWLENHSAVTVVMASEGYPGAYPKGVEITGFPEAQALGLQVFHAGTALKDGRVVTSGGRVLTVTAVQENLMSALTEA 403
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 1195504543 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: 582.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 434 GLTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCSVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCRKHDSIG 513
Cdd:COG0150 4 SLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:COG0150 84 IDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 594 ERHQKLPQlERITEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSG 673
Cdd:COG0150 164 EKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLGEALLEPTRIYVKPVLALLKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 674 HVKAFAHITGGGLLENIPRVLPQKFGVDLDACTWRVPKIFSWLQQEGQLSEEEMARTFNCGIGAALVVSQDQAEQILHDI 753
Cdd:COG0150 241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
|
330 340
....*....|....*....|....*
gi 1195504543 754 RQQQEEAWVIGSVVACPEdsPRVRV 778
Cdd:COG0150 321 KAAGETAYVIGEVVAGEG--EGVVL 343
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
2.56e-176 |
|
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100032 [Multi-domain] Cd Length: 297 Bit Score: 514.72 E-value: 2.56e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 469 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCRKHDSIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTT 548
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 549 EAVVAGIAAACQRAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERHQKLPQlERITEGDAVIGVASSGLHSNGFSLVR 628
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 629 KIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSGHVKAFAHITGGGLLENIPRVLPQKFGVDLDACTWR 708
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1195504543 709 VPKIFSWLQQEGQLSEEEMARTFNCGIGAALVVSQDQAEQILHDIRQQQEEAWVIGSVV 767
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
7.46e-169 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 501.19 E-value: 7.46e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 6 LVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTTCTGKISN-AAVSVNDHSALAQFCKDEKIELVVVGPEAPLAAGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 85 DLTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPaLVVKASGLAAGKGVIVAKST 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 165 AEACKAVQEMMQEKSFGAAGETVVVEEFLEGEEVSCLCFTDGKTVAEMPPAQDHKRLLDGDEGPNTGGMGAYCPAPQVSK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 245 DLLVKIKNTILQRAVDGMQQEGTPYTGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLS 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 323 ASLPVWLENhSAVTVVMASEGYPGAYPKGVEITGFPEAQAL--GLQVFHAGTALK-DGRVVTSGGRVLTVTAVQENLMSA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 1195504543 400 LTEARKGLAALKFEGAVYRKDIGFRAVAFLQRPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
435-768 |
2.66e-149 |
|
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: 446.78 E-value: 2.66e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 435 LTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCSVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQLCRKHDSIGQ 514
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 515 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDMYPPGEYDLAGFAVGAME 594
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 595 RHQKLPQlERITEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGGCGdQTLGDLLLTPTRIYSHSLLPIIRSGH 674
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFG-KTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 675 VKAFAHITGGGLLENIPRVLPQKFGVDLDACTWRVPKIFSWLQQEGQLSEEEMARTFNCGIGAALVVSQDQAEQILHDIR 754
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....
gi 1195504543 755 QQQEEAWVIGSVVA 768
Cdd:TIGR00878 318 AYGEKAWVIGEVKK 331
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
434-767 |
1.46e-127 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 391.86 E-value: 1.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 434 GLTYKDSGVDIAAGNMLVKKIQPLAkatsrPGcsvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQLCRKHDSIG 513
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 594 ERhQKLPQLERITEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSG 673
Cdd:PLN02557 204 KK-DAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPG--ASVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 674 HVKAFAHITGGGLLENIPRVLPQKFGVDLDACTWRVPKIFSWLQQEGQLSEEEMARTFNCGIGAALVVSQDQAEQILHDi 753
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEE- 359
|
330
....*....|....
gi 1195504543 754 rqQQEEAWVIGSVV 767
Cdd:PLN02557 360 --GAYPAYRIGEVI 371
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
2.92e-120 |
|
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: 365.45 E-value: 2.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 105 SSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPALVVKASGLAAGKGVIVAKSTAEACKAVQEMMQEKSFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 185 ETVVVEEFLEGEEVSCLCFTDGKTVAEMPPAQDHKRLLDGDEGPNTGGMGAYCPAPQVSKDLLVKIKNTILQRAVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 1195504543 265 EGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
809-991 |
2.05e-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: 318.18 E-value: 2.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFSVD 888
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 889 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDT 968
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 1195504543 969 VATLSERVKVAEHKIFPAALQLV 991
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
807-1009 |
4.54e-100 |
|
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: 312.74 E-value: 4.54e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 807 KARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFS 886
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 887 VDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRG 966
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1195504543 967 DTVATLSERVKVAEHKIFPAALQLVASGAVQLqEDGKLHWTNE 1009
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTL-DGRRVRLDGE 202
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
808-994 |
3.09e-76 |
|
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: 248.05 E-value: 3.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 808 ARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFSV 887
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGD 967
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180
....*....|....*....|....*..
gi 1195504543 968 TVATLSERVKVAEHKIFPAALQLVASG 994
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQG 187
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
808-988 |
9.05e-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: 9.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 808 ARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFSV 887
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGD 967
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|.
gi 1195504543 968 TVATLSERVKVAEHKIFPAAL 988
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
809-1002 |
2.77e-37 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 139.06 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFSVD 888
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 889 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKG-----SNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPV 963
Cdd:PLN02331 81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1195504543 964 HRGDTVATLSERVKVAEHKIFPAALQLVASGAVQLQEDG 1002
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
607-776 |
7.99e-35 |
|
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: 130.16 E-value: 7.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 607 EGDAVIGVASSGLHSNGFSLVRKIVERSslqysspapgGCGDQTLGDLLLTPTRIYSHSLLPIIrSGHVKAFAHITGGGL 686
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDS----------GLAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 687 LENIPRVLPQ-KFGVDLDActwRVPKIFSWLQqegqlSEEEMARTFNCGIGAALVVSQDqAEQILHDIRQQQEEAWVIGS 765
Cdd:pfam02769 71 AGALAEMAPAsGVGAEIDL---DKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEE-AEAVLAILEKEGLEAAVIGE 141
|
170
....*....|.
gi 1195504543 766 VVACPEDSPRV 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: 706.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTTCTGKisNAAVSVNDHSALAQFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 84 GDLTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPaLVVKASGLAAGKGVIVAKS 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 164 TAEACKAVQEMMQEKSFGAAGETVVVEEFLEGEEVSCLCFTDGKTVAEMPPAQDHKRLLDGDEGPNTGGMGAYCPAPQVS 243
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 244 KDLLVKIKNTILQRAVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLSA 323
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 324 SLPVWLENHsAVTVVMASEGYPGAYPKGVEITGFPEAQALGLQVFHAGTALKDGRVVTSGGRVLTVTAVQENLMSALTEA 403
Cdd:COG0151 319 VELEWDDRA-AVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERA 397
|
410 420
....*....|....*....|....
gi 1195504543 404 RKGLAALKFEGAVYRKDIGFRAVA 427
Cdd:COG0151 398 YEAVEKIRFEGMFYRRDIGWRALK 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: 651.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTTCTGKISNAAVSVNDHSALAQFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 84 GDLTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 164 TAEACKAVQEMMQEKsFGAAGETVVVEEFLEGEEVSCLCFTDGKTVAEMPPAQDHKRLLDGDEGPNTGGMGAYCPAPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 244 KDLLVKIKNTILQRAVDGMQQEGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLsA 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKL-D 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 324 SLPVWLENHSAVTVVMASEGYPGAYPKGVEITGFPEAQALGLQVFHAGTALKDGRVVTSGGRVLTVTAVQENLMSALTEA 403
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 1195504543 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: 582.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 434 GLTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCSVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCRKHDSIG 513
Cdd:COG0150 4 SLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:COG0150 84 IDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 594 ERHQKLPQlERITEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSG 673
Cdd:COG0150 164 EKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLGEALLEPTRIYVKPVLALLKAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 674 HVKAFAHITGGGLLENIPRVLPQKFGVDLDACTWRVPKIFSWLQQEGQLSEEEMARTFNCGIGAALVVSQDQAEQILHDI 753
Cdd:COG0150 241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
|
330 340
....*....|....*....|....*
gi 1195504543 754 RQQQEEAWVIGSVVACPEdsPRVRV 778
Cdd:COG0150 321 KAAGETAYVIGEVVAGEG--EGVVL 343
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
2.56e-176 |
|
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100032 [Multi-domain] Cd Length: 297 Bit Score: 514.72 E-value: 2.56e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 469 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCRKHDSIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTT 548
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 549 EAVVAGIAAACQRAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERHQKLPQlERITEGDAVIGVASSGLHSNGFSLVR 628
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 629 KIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSGHVKAFAHITGGGLLENIPRVLPQKFGVDLDACTWR 708
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1195504543 709 VPKIFSWLQQEGQLSEEEMARTFNCGIGAALVVSQDQAEQILHDIRQQQEEAWVIGSVV 767
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
7.46e-169 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 501.19 E-value: 7.46e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 6 LVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTTCTGKISN-AAVSVNDHSALAQFCKDEKIELVVVGPEAPLAAGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 85 DLTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPaLVVKASGLAAGKGVIVAKST 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 165 AEACKAVQEMMQEKSFGAAGETVVVEEFLEGEEVSCLCFTDGKTVAEMPPAQDHKRLLDGDEGPNTGGMGAYCPAPQVSK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 245 DLLVKIKNTILQRAVDGMQQEGTPYTGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLS 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 323 ASLPVWLENhSAVTVVMASEGYPGAYPKGVEITGFPEAQAL--GLQVFHAGTALK-DGRVVTSGGRVLTVTAVQENLMSA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 1195504543 400 LTEARKGLAALKFEGAVYRKDIGFRAVAFLQRPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
435-768 |
2.66e-149 |
|
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: 446.78 E-value: 2.66e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 435 LTYKDSGVDIAAGNMLVKKIQPLAKATSRPGCSVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQLCRKHDSIGQ 514
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 515 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDMYPPGEYDLAGFAVGAME 594
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 595 RHQKLPQlERITEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGGCGdQTLGDLLLTPTRIYSHSLLPIIRSGH 674
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFG-KTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 675 VKAFAHITGGGLLENIPRVLPQKFGVDLDACTWRVPKIFSWLQQEGQLSEEEMARTFNCGIGAALVVSQDQAEQILHDIR 754
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....
gi 1195504543 755 QQQEEAWVIGSVVA 768
Cdd:TIGR00878 318 AYGEKAWVIGEVKK 331
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
434-767 |
1.46e-127 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 391.86 E-value: 1.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 434 GLTYKDSGVDIAAGNMLVKKIQPLAkatsrPGcsvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQLCRKHDSIG 513
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 514 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDMYPPGEYDLAGFAVGAM 593
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 594 ERhQKLPQLERITEGDAVIGVASSGLHSNGFSLVRKIVERSSLQYSSPAPGgcGDQTLGDLLLTPTRIYSHSLLPIIRSG 673
Cdd:PLN02557 204 KK-DAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPG--ASVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 674 HVKAFAHITGGGLLENIPRVLPQKFGVDLDACTWRVPKIFSWLQQEGQLSEEEMARTFNCGIGAALVVSQDQAEQILHDi 753
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEE- 359
|
330
....*....|....
gi 1195504543 754 rqQQEEAWVIGSVV 767
Cdd:PLN02557 360 --GAYPAYRIGEVI 371
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
2.92e-120 |
|
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: 365.45 E-value: 2.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 105 SSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPALVVKASGLAAGKGVIVAKSTAEACKAVQEMMQEKSFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 185 ETVVVEEFLEGEEVSCLCFTDGKTVAEMPPAQDHKRLLDGDEGPNTGGMGAYCPAPQVSKDLLVKIKNTILQRAVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 1195504543 265 EGTPYTGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
809-991 |
2.05e-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: 318.18 E-value: 2.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFSVD 888
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 889 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDT 968
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 1195504543 969 VATLSERVKVAEHKIFPAALQLV 991
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
807-1009 |
4.54e-100 |
|
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: 312.74 E-value: 4.54e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 807 KARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFS 886
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 887 VDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRG 966
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1195504543 967 DTVATLSERVKVAEHKIFPAALQLVASGAVQLqEDGKLHWTNE 1009
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTL-DGRRVRLDGE 202
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
808-994 |
3.09e-76 |
|
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: 248.05 E-value: 3.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 808 ARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFSV 887
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGD 967
Cdd:TIGR00639 81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160
|
170 180
....*....|....*....|....*..
gi 1195504543 968 TVATLSERVKVAEHKIFPAALQLVASG 994
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQG 187
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
808-988 |
9.05e-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: 9.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 808 ARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFSV 887
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGD 967
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|.
gi 1195504543 968 TVATLSERVKVAEHKIFPAAL 988
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
4-104 |
1.45e-48 |
|
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: 167.53 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 4 RVLVIGSGGREHTLAWKLAQSPHVKQVLVAPGNAGTTCTGKisNAAVSVNDHSALAQFCKDEKIELVVVGPEAPLAAGIV 83
Cdd:pfam02844 2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 1195504543 84 GDLTS--AGVRCFGPTAQAAQLE 104
Cdd:pfam02844 80 DALREraAGIPVFGPSKAAAQLE 102
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
812-990 |
1.02e-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: 153.60 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 812 VLISGTGSNLQALIDSTRDpKSSSHIVLVISNKAAVAGLDRAERAGIptrviNHKLYKNRAEFDNAVDRVLEEFSVDIVC 891
Cdd:cd08369 1 IVILGSGNIGQRVLKALLS-KEGHEIVGVVTHPDSPRGTAQLSLELV-----GGKVYLDSNINTPELLELLKEFAPDLIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 892 LAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVAT 971
Cdd:cd08369 75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154
|
170
....*....|....*....
gi 1195504543 972 LSERVKVAEHKIFPAALQL 990
Cdd:cd08369 155 LYQRLIELGPKLLKEALQK 173
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-424 |
5.81e-39 |
|
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02787).
Pssm-ID: 460722 [Multi-domain] Cd Length: 88 Bit Score: 139.50 E-value: 5.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 334 AVTVVMASEGYPGAYPKGVEITGFPEAqalGLQVFHAGTALKDGRVVTSGGRVLTVTAVQENLMSALTEARKGLAALKFE 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA---GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|.
gi 1195504543 414 GAVYRKDIGFR 424
Cdd:pfam02843 78 GMFYRKDIGTR 88
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
809-1002 |
2.77e-37 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 139.06 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDRAERAGIPTRVINHKLYKNRAEFDNAVDRVLEEFSVD 888
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSPDELVDALRGAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 889 IVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKG-----SNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPV 963
Cdd:PLN02331 81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1195504543 964 HRGDTVATLSERVKVAEHKIFPAALQLVASGAVQLQEDG 1002
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
806-984 |
5.65e-37 |
|
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: 140.96 E-value: 5.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 806 KKARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLdrAERAGIPTRVINHKLyKNRAEFDNAVDRVLEEF 885
Cdd:COG0788 85 RRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLLELLEEY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 886 SVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHR 965
Cdd:COG0788 162 DIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDH 241
|
170 180 190
....*....|....*....|....*....|..
gi 1195504543 966 GDTVA------------TLSERVK-VAEHKIF 984
Cdd:COG0788 242 RDTPEdlvrkgrdvekrVLARAVRwHLEDRVL 273
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
607-776 |
7.99e-35 |
|
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: 130.16 E-value: 7.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 607 EGDAVIGVASSGLHSNGFSLVRKIVERSslqysspapgGCGDQTLGDLLLTPTRIYSHSLLPIIrSGHVKAFAHITGGGL 686
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDS----------GLAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 687 LENIPRVLPQ-KFGVDLDActwRVPKIFSWLQqegqlSEEEMARTFNCGIGAALVVSQDqAEQILHDIRQQQEEAWVIGS 765
Cdd:pfam02769 71 AGALAEMAPAsGVGAEIDL---DKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEE-AEAVLAILEKEGLEAAVIGE 141
|
170
....*....|.
gi 1195504543 766 VVACPEDSPRV 776
Cdd:pfam02769 142 VTAGGRLTVIV 152
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
809-996 |
1.03e-33 |
|
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: 128.45 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 809 RVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLdrAERAGIPTRVIN-HKLYKNRAEfdNAVDRVLEEFSV 887
Cdd:cd08648 2 RVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPL--AERFGIPFHHIPvTKDTKAEAE--AEQLELLEEYGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 888 DIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPV-HRg 966
Cdd:cd08648 78 DLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVsHR- 156
|
170 180 190
....*....|....*....|....*....|
gi 1195504543 967 DTVATLSERVKVAEHKIFPAALQLVASGAV 996
Cdd:cd08648 157 DSVEDLVRKGRDIEKQVLARAVKWHLEDRV 186
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
837-972 |
5.13e-31 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 123.68 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 837 IVLVISNKAAVAGLdrAERAGIPTRVINH-KLykNRAEFDNAVDRVLEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIH 915
Cdd:PRK06027 119 IAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIH 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195504543 916 PSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPV-HRgDTVATL 972
Cdd:PRK06027 195 HSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVdHR-DTAEDL 251
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
489-765 |
2.45e-28 |
|
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: 114.03 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 489 LASGTDGVGTKLKIaqlcrKHDSIGQDLVAMCVNDILAQGAEPLFFLDYFSCGK-LDLSTTEAVVAGIAAACQRAGCALL 567
Cdd:cd00396 2 LAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 568 GGETAEMPDMYPPgEYDLAGFAVGamerhqklpqleritegdavigvassglhsngfslvrkIVERSSLQYSSPApggcg 647
Cdd:cd00396 77 GGHTSVSPGTMGH-KLSLAVFAIG--------------------------------------VVEKDRVIDSSGA----- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 648 dqTLGD-LLLTPTRiyshSLLPIIRSGHVKAFAHITGGGLLENIPRVLPQK-FGVDLDACTWRVPKIFSWLQQEgqlsEE 725
Cdd:cd00396 113 --RPGDvLILTGVD----AVLELVAAGDVHAMHDITDGGLLGTLPELAQASgVGAEIDLEAIPLDEVVRWLCVE----HI 182
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1195504543 726 EMARTFNCGIGAALVVSQDQAEQILHDIRQQQEEAWVIGS 765
Cdd:cd00396 183 EEALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
489-593 |
1.70e-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: 95.98 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 489 LASGTDGVGTKLKIAqlcrKHDSIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDL--STTEAVVAGIAAACQRAGCAL 566
Cdd:pfam00586 5 VAVTTDGHGTPSLVD----PYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEveWVLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*..
gi 1195504543 567 LGGETAEMPDMYPPgeyDLAGFAVGAM 593
Cdd:pfam00586 81 VGGDTSFDPEGGKP---TISVTAVGIV 104
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
800-989 |
7.61e-22 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 96.35 E-value: 7.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 800 NFPVQQKKARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKaavaglDRA---------ERAGIPTRVInHKLYKN 870
Cdd:PLN02828 63 RVPGLDPKYKIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNH------ERGpnthvmrflERHGIPYHYL-PTTKEN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 871 RAEfdnavDRVLEEFS-VDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAED 949
Cdd:PLN02828 136 KRE-----DEILELVKgTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1195504543 950 VDAGQIILQEAVPVHRGDTVATLSERVKVAEHKIFPAALQ 989
Cdd:PLN02828 211 LDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAIK 250
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
837-963 |
7.78e-22 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 96.98 E-value: 7.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 837 IVLVISNKAAVAGLdrAERAGIPTRVInhKLYK-NRAEFDNAVDRVLEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIH 915
Cdd:PRK13011 119 IVGVVSNHPDLEPL--AAWHGIPFHHF--PITPdTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIH 194
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1195504543 916 PSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPV 963
Cdd:PRK13011 195 HSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERV 242
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
56-294 |
5.72e-20 |
|
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: 90.70 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 56 SALAQFCKDEKIELVVVGPEA--PLAAGIVGDLtsaGVRcfGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDA 133
Cdd:COG0439 7 AAAAELARETGIDAVLSESEFavETAAELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 134 CSFIMSANFPaLVVKASGLAAGKGVIVAKSTAEACKAVQEMMQEKSFGAAGETVVVEEFLEGEEVSCLCF-TDGKTV-AE 211
Cdd:COG0439 82 LAFAEEIGYP-VVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLvRDGEVVvCS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 212 MppaqdHKRLLDGDEGPNTGGMgayCPAPqVSKDLLVKIKNTIlQRAVD--GMQqegtpyTGILYAGIMLTKDG-PKVLE 288
Cdd:COG0439 161 I-----TRKHQKPPYFVELGHE---APSP-LPEELRAEIGELV-ARALRalGYR------RGAFHTEFLLTPDGePYLIE 224
|
....*.
gi 1195504543 289 FNCRFG 294
Cdd:COG0439 225 INARLG 230
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
805-984 |
4.82e-19 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 88.70 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 805 QKKARVAVLISGTGSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLdrAERAGIPTRVInhKLYK-NRAEFDNAVDRVLE 883
Cdd:PRK13010 91 GQRPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPL--AVQHDIPFHHL--PVTPdTKAQQEAQILDLIE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 884 EFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPV 963
Cdd:PRK13010 167 TSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERV 246
|
170 180 190
....*....|....*....|....*....|....
gi 1195504543 964 HRG----DTVA--------TLSERVKV-AEHKIF 984
Cdd:PRK13010 247 DHSyspeDLVAkgrdveclTLARAVKAfIEHRVF 280
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
821-1007 |
1.16e-18 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 87.85 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 821 LQALIDSTRDpkssshIVLVISNKAAVAGLDR----------AERAGIPtrVIN-HKLykNRAEFDNAvdrvLEEFSVDI 889
Cdd:COG0223 16 LEALLAAGHE------VVAVVTQPDRPAGRGRkltpspvkelALEHGIP--VLQpESL--KDPEFLEE----LRALNPDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 890 VCLAGFMRILSGPFvrkWD---GKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRG 966
Cdd:COG0223 82 IVVVAYGQILPKEV---LDiprLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1195504543 967 DTVATLSERVKVAEHKIFPAALQLVASGAVQLQ---------------EDGKLHWT 1007
Cdd:COG0223 159 DTAGSLHDKLAELGAELLLETLDALEAGTLTPTpqdesgatyapkiskEDGRIDWS 214
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
882-1006 |
3.90e-15 |
|
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 77.44 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 882 LEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:TIGR00460 74 VRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETF 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 962 PVHRGDTVATLSERVKVAEHKIFPAALQLVASGAVQLQ---------------EDGKLHW 1006
Cdd:TIGR00460 154 PIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPEpqdaeeatyapkiskEQERIDW 213
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
806-975 |
7.16e-14 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 73.96 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 806 KKARVAVLisGT----GSNLQALIDSTRDPKSSSHIVLVISNKAAVAGLDR----------AERAGIPTRVInhkLYKNR 871
Cdd:PLN02285 5 RKKRLVFL--GTpevaATVLDALLDASQAPDSAFEVAAVVTQPPARRGRGRklmpspvaqlALDRGFPPDLI---FTPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 872 AEFDNAVDRvLEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVD 951
Cdd:PLN02285 80 AGEEDFLSA-LRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALD 158
|
170 180
....*....|....*....|....
gi 1195504543 952 AGQIILQEAVPVHRGDTVATLSER 975
Cdd:PLN02285 159 AGPVIAQERVEVDEDIKAPELLPL 182
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
821-975 |
1.02e-11 |
|
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 65.16 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 821 LQALIdstrdpKSSSHIVLVISNKAAVAGL----------DRAERAGIPTRVINhKLykNRAEFDNAvdrvLEEFSVDIV 890
Cdd:cd08646 16 LEALL------KSGHEVVAVVTQPDKPRGRgkkltpspvkELALELGLPVLQPE-KL--KDEEFLEE----LKALKPDLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 891 CLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVA 970
Cdd:cd08646 83 VVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAG 162
|
....*
gi 1195504543 971 TLSER 975
Cdd:cd08646 163 ELLDK 167
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
86-290 |
1.94e-11 |
|
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: 66.12 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 86 LTSAGVRCFGPtAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPaLVVKASGLAAGKGVIVAKSTA 165
Cdd:COG0189 77 LEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGP-VVLKPLDGSGGRGVFLVEDED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 166 EACKAVQEMMQEKSfgaagETVVVEEFL---EGEEVSCLCFtDGKTVAEM---PPAQDHKRlldgdegpNT--GGMGAYC 237
Cdd:COG0189 155 ALESILEALTELGS-----EPVLVQEFIpeeDGRDIRVLVV-GGEPVAAIrriPAEGEFRT--------NLarGGRAEPV 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1195504543 238 PAPQVSKDLLVKIkntilqravdgmqqegTPYTGILYAGI--MLTKDGPKVLEFN 290
Cdd:COG0189 221 ELTDEERELALRA----------------APALGLDFAGVdlIEDDDGPLVLEVN 259
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
881-976 |
2.03e-11 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 63.00 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 881 VLEEFSVDIVCLAGfMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAH-EQVLEAGVTITGCTVHFVAEDVDAGQIILQE 959
Cdd:cd08653 42 ALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGfWALANGDPDNVGVTVHLVDAGIDTGDVLAQA 120
|
90
....*....|....*..
gi 1195504543 960 AVPVHRGDTVATLSERV 976
Cdd:cd08653 121 RPPLAAGDTLLSLYLRL 137
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
915-1005 |
6.26e-11 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 62.48 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 915 HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVATLSERVkvaehkIFPAALQLVASG 994
Cdd:cd08822 95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRA------LAPMGVKLLTQV 168
|
90
....*....|.
gi 1195504543 995 AVQLQEDGKLH 1005
Cdd:cd08822 169 IDALLRGGNLP 179
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
86-269 |
2.96e-10 |
|
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: 62.43 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 86 LTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPA-LVVKASGLAAGKGVIVAKST 164
Cdd:COG1181 75 LELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLpLFVKPAREGSSVGVSKVKNA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 165 AEACKAVQEMMQEksfgaaGETVVVEEFLEGEEVSCLCFTDGKTVAeMPPAQ----------DHKRLLDGDEgpntggmg 234
Cdd:COG1181 155 EELAAALEEAFKY------DDKVLVEEFIDGREVTVGVLGNGGPRA-LPPIEivpengfydyEAKYTDGGTE-------- 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1195504543 235 AYCPAPqVSKDLLVKIKNTILQ--RAVDG---------MQQEGTPY 269
Cdd:COG1181 220 YICPAR-LPEELEERIQELALKafRALGCrgyarvdfrLDEDGEPY 264
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
817-1006 |
5.82e-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: 63.08 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 817 TGSNLQALIDSTRDPKSSSHIvlvisnkAAVAGLdrAERAGIPTRV---INHKLYknraefdnaVDRvLEEFSVDIVCLA 893
Cdd:PRK08125 22 AGYEIAAVFTHTDNPGENHFF-------GSVARL--AAELGIPVYApedVNHPLW---------VER-IRELAPDVIFSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 894 GFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVATLS 973
Cdd:PRK08125 83 YYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLH 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1195504543 974 ERVKVAEHKIFPAALQLVASGAVQLQ---------------EDGKLHW 1006
Cdd:PRK08125 163 HKLCHAARQLLEQTLPAIKHGNIPEIpqdesqatyfgrrtpADGLIDW 210
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
65-292 |
1.12e-09 |
|
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: 62.71 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 65 EKIELVVVGPEAPLAAGIVGDLTSAGVRCFGPTAQAA-QLESSKKFAkEFMDRHGIPTAQWRAFTNPEDACSFIMSANFP 143
Cdd:TIGR01369 628 EKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIdRAEDREKFS-ELLDELGIPQPKWKTATSVEEAVEFASEIGYP 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 144 ALvVKASGLAAGKGVIVAKSTAEackaVQEMMQEKSFGAAGETVVVEEFLEGE---EVSCLCftDGKTVAeMPPAQDHKR 220
Cdd:TIGR01369 707 VL-VRPSYVLGGRAMEIVYNEEE----LRRYLEEAVAVSPEHPVLIDKYLEDAvevDVDAVS--DGEEVL-IPGIMEHIE 778
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195504543 221 lldgDEGPNTGGMGAYCPAPQVSKDLLVKIKNtILQRAVDGMQqegtpYTGILYAGIMLTKDGPKVLEFNCR 292
Cdd:TIGR01369 779 ----EAGVHSGDSTCVLPPQTLSAEIVDRIKD-IVRKIAKELN-----VKGLMNIQFAVKDGEVYVIEVNPR 840
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
833-989 |
2.06e-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: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 833 SSSHIVLVISN--KAAVAGLDRAERAGIPTRVINHKLyknraefdnavDRVLEEFSVDIVCLAGFMRILSGPFVRKWDGK 910
Cdd:cd08820 25 GSFEIIAVLTNtsPADVWEGSEPLYDIGSTERNLHKL-----------LEILENKGVDILISVQYHWILPGSILEKAKEI 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195504543 911 MLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVATLSERVKVAEHKIFPAALQ 989
Cdd:cd08820 94 AFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYILAHYAAIALFGEHIT 172
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
882-992 |
2.74e-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: 187725 [Multi-domain] Cd Length: 177 Bit Score: 57.46 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 882 LEEFSVDIVCLAGFMRILSGPFVRKWDGKMLNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:cd08823 67 LRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFT 146
|
90 100 110
....*....|....*....|....*....|.
gi 1195504543 962 PVHRGDTVATLSERVKVAEHKIFPAALQLVA 992
Cdd:cd08823 147 PIHPDDTYGLLCSRLAMLAVGLLEELYQNLA 177
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
912-996 |
4.46e-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: 57.36 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 912 LNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVATLSERVKVAEHKIFPAALQLV 991
Cdd:cd08644 101 FNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLARTLPAL 180
|
....*
gi 1195504543 992 ASGAV 996
Cdd:cd08644 181 KAGKA 185
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
912-1007 |
1.44e-08 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 57.40 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 912 LNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVATLSERVKVAEHKIFPAAL-QL 990
Cdd:PRK06988 103 YNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVTVAAEQTLWRVLpAL 182
|
90 100 110
....*....|....*....|....*....|.
gi 1195504543 991 VASGAVQLQ--------------EDGKLHWT 1007
Cdd:PRK06988 183 LAGEAPHLPndlaqgsyfggrkpEDGRIDWS 213
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
821-979 |
2.28e-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: 187720 [Multi-domain] Cd Length: 180 Bit Score: 54.96 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 821 LQALIDSTRdpksssHIVLVISNKAAVAG--------LDRAERAGIP---TRVINhklyknraefDNAVDRVLEEFSVDI 889
Cdd:cd08651 15 LEAILEAGG------EVVGVITLDDSSSNndsdyldlDSFARKNGIPyykFTDIN----------DEEIIEWIKEANPDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 890 VCLAGFMRILSGPFvrkwdgkmLNI--------HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAV 961
Cdd:cd08651 79 IFVFGWSQLLKPEI--------LAIprlgvigfHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPF 150
|
170
....*....|....*...
gi 1195504543 962 PVHRGDTVATLSERVKVA 979
Cdd:cd08651 151 PIDKDDTANSLYDKIMEA 168
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
88-294 |
3.35e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 56.86 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 88 SAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPaLVVKAS--------GLAAGKGVI 159
Cdd:COG3919 99 EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFP-VVVKPAdsvgydelSFPGKKKVF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 160 VAKSTAEACKAVQEMmqeksfGAAGETVVVEEFLEGEE-----VSCLCFTDGKTVAEMppaqDHKRLLdgdEGPNTGGMG 234
Cdd:COG3919 178 YVDDREELLALLRRI------AAAGYELIVQEYIPGDDgemrgLTAYVDRDGEVVATF----TGRKLR---HYPPAGGNS 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195504543 235 AYC---PAPQV---SKDLLvkikntilqRAVDgmqqegtpYTGILYAGIMLT-KDG-PKVLEFNCRFG 294
Cdd:COG3919 245 AAResvDDPELeeaARRLL---------EALG--------YHGFANVEFKRDpRDGeYKLIEINPRFW 295
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
111-283 |
5.24e-08 |
|
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: 56.24 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 111 KEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPAlVVKasglAA-----GKGVIVAKSTAEACKAVQEMmqeksfgaAGE 185
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPA-VLK----TRrggydGKGQVVIKSAADLEAAWAAL--------GGG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 186 TVVVEEFLEGE-EVSCLC--FTDGKTVAeMPPAQDHKRllDG--DEgpntggmgAYCPApQVSKDLLVKIKNtILQRAVD 260
Cdd:COG0026 161 PCILEEFVPFErELSVIVarSPDGEVAT-YPVVENVHR--NGilDE--------SIAPA-RISEALAAEAEE-IAKRIAE 227
|
170 180
....*....|....*....|....*
gi 1195504543 261 GMQqegtpYTGILyaGI--MLTKDG 283
Cdd:COG0026 228 ALD-----YVGVL--AVefFVTKDG 245
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
115-283 |
6.47e-08 |
|
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: 53.41 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 115 DRHGIPTAQWRAFTNPEDACSFIMSANFPAlVVKASGLA-AGKGVIVAKSTAEACKAVQEmmqeksfgAAGETVVVEEFL 193
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPC-VVKARRGGyDGKGQYVVRSEADLPQAWEE--------LGDGPVIVEEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 194 EGE-EVSCLC--FTDGKTVAeMPPAQDHKRllDGDEGPNtggmgaYCPAPqVSKDLLVKIKnTILQRAVDGMqqegtPYT 270
Cdd:pfam02222 72 PFDrELSVLVvrSVDGETAF-YPVVETIQE--DGICRLS------VAPAR-VPQAIQAEAQ-DIAKRLVDEL-----GGV 135
|
170
....*....|...
gi 1195504543 271 GILYAGIMLTKDG 283
Cdd:pfam02222 136 GVFGVELFVTEDG 148
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
86-290 |
4.60e-07 |
|
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: 52.35 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 86 LTSAGVRCFGPTaQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPAlVVKASGLAAGKGVIVAKSTA 165
Cdd:TIGR00768 69 LESLGVPVINSS-DAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPV-VLKPVFGSWGRGVSLARDRQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 166 EACKAvqeMMQEKSFGAAGETVVVEEFL---EGEEVSCLCfTDGKTVAEMppaqdhKRLLDGDEGPNT--GGMGAYCPAP 240
Cdd:TIGR00768 147 AAESL---LEHFEQLNGPQNLFLVQEYIkkpGGRDIRVFV-VGDEVVAAI------YRITSGHWRSNLarGGKAEPCSLT 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1195504543 241 QVSKDLLVKIKNTIlqravdgmqqegtpytGILYAGIML--TKDGPKVLEFN 290
Cdd:TIGR00768 217 EEIEELAIKAAKAL----------------GLDVAGVDLleSEDGLLVNEVN 252
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
836-972 |
8.78e-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: 49.95 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 836 HIVLVISNKAAVAglDRAERAGIPtrvinhklyknRAEFDNAVDRVLEEFSVD----IVCLagfmRILSGPFVRKWDGKM 911
Cdd:cd08649 24 RIAAVVSTDPAIR--AWAAAEGIA-----------VLEPGEALEELLSDEPFDwlfsIVNL----RILPSEVLALPRKGA 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195504543 912 LNIHPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVATL 972
Cdd:cd08649 87 INFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-194 |
1.04e-06 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 50.34 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 110 AKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPALVVKASGLAAGK----GVIVAKSTAEACKAVQEM----MQEKSFG 181
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMlgknLVTKQTG 86
|
90
....*....|....*.
gi 1195504543 182 AAGETV---VVEEFLE 194
Cdd:pfam08442 87 PDGQPVnkvLVEEALD 102
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
915-1003 |
1.46e-06 |
|
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: 50.14 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 915 HPSLLPSFKGSNAHEQVLEAGVTITGCTVHFVAEDVDAGQIILQEAVPVHRGDTVATLSERVkvaehkIFPAALQLVASg 994
Cdd:cd08647 106 HPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPEGIKAMVE- 178
|
....*....
gi 1195504543 995 AVQLQEDGK 1003
Cdd:cd08647 179 AVRLIAEGK 187
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
51-294 |
1.57e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 51.42 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 51 SVNDHS---ALAQFCKDEKIELVVVG--PEAPLAAGIVGDLTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWR 125
Cdd:PRK12767 51 KVTDPNyidRLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 126 AFTNPED--ACSFIMSANFPaLVVKASGLAAGKGVIVAKSTAEAckavqemmqeKSFGAAGETVVVEEFLEGEE--VSCL 201
Cdd:PRK12767 131 LPESLEDfkAALAKGELQFP-LFVKPRDGSASIGVFKVNDKEEL----------EFLLEYVPNLIIQEFIEGQEytVDVL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 202 CFTDGKTVAEMPpaqdHKRL--LDGDegpntggmgaycpapqVSKDllVKIKNTILQRAVDGMQQEgTPYTGILYAGIML 279
Cdd:PRK12767 200 CDLNGEVISIVP----RKRIevRAGE----------------TSKG--VTVKDPELFKLAERLAEA-LGARGPLNIQCFV 256
|
250
....*....|....*
gi 1195504543 280 TKDGPKVLEFNCRFG 294
Cdd:PRK12767 257 TDGEPYLFEINPRFG 271
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
111-199 |
2.37e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 50.92 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 111 KEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPAlVVKasglAA-----GKGVIVAKSTAEACKAVQEMmqeksfgaAGE 185
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPA-VLK----TRrggydGKGQWVIRSAEDLEAAWALL--------GSV 171
|
90
....*....|....*
gi 1195504543 186 TVVVEEFLEGE-EVS 199
Cdd:PRK06019 172 PCILEEFVPFErEVS 186
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
512-599 |
3.37e-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: 49.86 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 512 IGQDLVAMCVNDILAQGAEPLFFLdyFSCG---KLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDMYppgeydLAGF 588
Cdd:cd02194 59 IGWKALAVNLSDLAAMGARPLGFL--LSLGlppDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELV------ISVT 130
|
90
....*....|.
gi 1195504543 589 AVGAMERHQKL 599
Cdd:cd02194 131 ALGEVEKGKPL 141
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
62-209 |
8.97e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 49.97 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 62 CKDEKIELVVVGPEAPLAAGIVGDLTSAGVRCFGPTAQAA-QLESSKKFaKEFMDRHGIPTAQWRAFTNPEDACSFIMSA 140
Cdd:PRK12815 626 AEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIdRLEDRDRF-YQLLDELGLPHVPGLTATDEEEAFAFAKRI 704
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195504543 141 NFPALvVKASGLAAGKGVIVAKSTAeackAVQEMMQEKSfgAAGETVVVEEFLEGEEVSCLCFTDGKTV 209
Cdd:PRK12815 705 GYPVL-IRPSYVIGGQGMAVVYDEP----ALEAYLAENA--SQLYPILIDQFIDGKEYEVDAISDGEDV 766
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
89-194 |
2.09e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 48.44 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 89 AGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWR--AFTNPEDACSFIMSANFPaLVVKASGLAAGKGVIVAKSTAE 166
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTeeGIEDIEEAKEIAEEIGYP-VIIKASAGGGGIGMRVVYSEEE 176
|
90 100 110
....*....|....*....|....*....|
gi 1195504543 167 ACKAVQEMMQ--EKSFGAAgeTVVVEEFLE 194
Cdd:PRK08654 177 LEDAIESTQSiaQSAFGDS--TVFIEKYLE 204
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
113-200 |
9.43e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 44.61 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 113 FMDRHGIPTAQWRAFT------NPEDACSFIMSAN-FPaLVVKASGLAAGKGVIVAKSTAEACKAVQEMMQEKsfgaagE 185
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTradwklNPKEWCAQVEEALgYP-VFVKPARLGSSVGVSKVESREELQAAIEEAFQYD------E 73
|
90
....*....|....*
gi 1195504543 186 TVVVEEFLEGEEVSC 200
Cdd:pfam07478 74 KVLVEEGIEGREIEC 88
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
116-290 |
1.07e-04 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 44.41 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 116 RHGIPTAQWRAFTNPEDACSFI--MSANFPaLVVKASGLAAGKGVIVAKSTAEAckavqemmqEKSFGAAGETVVVEEFL 193
Cdd:pfam08443 13 KHGIGPPNTRLAWYPEDAEQFIeqIKRQFP-VIVKSIYGSQGIGVFLAEDEQKL---------RQTLSATNEQILVQEFI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 194 ---EGEEVSCLCfTDGKTVAEMppaqdHKRLLDGDEGPN--TGGMGAYCPAPQVSKDLLVKIKNTIlqravdgmqqegtp 268
Cdd:pfam08443 83 aeaNNEDIRCLV-VGDQVVGAL-----HRQSNEGDFRSNlhRGGVGEKYQLSQEETELAIKAAQAM-------------- 142
|
170 180
....*....|....*....|....
gi 1195504543 269 ytGILYAGIML--TKDGPKVLEFN 290
Cdd:pfam08443 143 --QLDVAGVDLlrQKRGLLVCEVN 164
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
521-612 |
1.91e-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: 44.36 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 521 VNDILAQGAEPLffldYFSCG-----KLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDmyppGEYD-----LAGfaV 590
Cdd:cd02197 67 VNDLAMMGAKPL----YLSLGfileeGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPK----GKADgifinTTG--I 136
|
90 100
....*....|....*....|..
gi 1195504543 591 GAMERHQKLPqLERITEGDAVI 612
Cdd:cd02197 137 GVIPRGVIIS-PSNIRPGDKII 157
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
78-207 |
3.32e-04 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 44.48 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 78 LAAGIVGDLTSAGVRCFGPTAQAAQL-ESSKKFaKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPaLVVKAS---Gla 153
Cdd:COG0458 86 LAVELEEAGILEGVKILGTSPDAIDLaEDRELF-KELLDKLGIPQPKSGTATSVEEALAIAEEIGYP-VIVRPSyvlG-- 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195504543 154 aGKGVIVAKSTAEackaVQEMMqEKSFGAAGET-VVVEEFLEG--E-EVSCLCftDGK 207
Cdd:COG0458 162 -GRGMGIVYNEEE----LEEYL-ERALKVSPDHpVLIDESLLGakEiEVDVVR--DGE 211
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
141-209 |
1.18e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 40.73 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195504543 141 NFPaLVVKASGLAAGKGVIVAKSTAE---ACKAVQEMMQEKS-----FGAAGETVVVEEFLEGEEVSCLCF--TDGKTV 209
Cdd:pfam13535 2 PYP-CVIKPSVGFFSVGVYKINNREEwkaAFAAIREEIEQWKemypeAVVDGGSFLVEEYIEGEEFAVDAYfdENGEPV 79
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
110-191 |
1.46e-03 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 41.96 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 110 AKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPALVVKASGLAAGK----GVIVAKSTAEACKAVQEMM----QEKSFG 181
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEILgmtlVTHQTG 87
|
90
....*....|...
gi 1195504543 182 AAGETV---VVEE 191
Cdd:COG0045 88 PKGKPVnkvLVEE 100
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
518-577 |
1.55e-03 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 41.74 E-value: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195504543 518 AMCVN--DILAQGAEPLFFLdyFSCG---KLDLSTTEAVVAGIAAACQRAGCALLGGETAEMPDM 577
Cdd:PRK05731 66 ALAVNlsDLAAMGARPAAFL--LALAlpkDLDEAWLEALADGLFELADRYGAELIGGDTTRGPDL 128
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
110-191 |
1.79e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 42.00 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 110 AKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPALVVKASGLAAGKG----VIVAKSTAEACKAVQEM--MQEKSF--G 181
Cdd:PRK00696 8 AKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGkaggVKLAKSPEEAREFAKQIlgMTLVTHqtG 87
|
90
....*....|...
gi 1195504543 182 AAGETV---VVEE 191
Cdd:PRK00696 88 PKGQPVnkvLVEE 100
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
95-194 |
2.61e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 41.62 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 95 GPTAQAAQLESSKKFAKEFMDRHGIPT--AQWRAFTNPEDACSFIMSANFPaLVVKASGLAAGKGVIVAKSTAEACKAVQ 172
Cdd:PRK05586 104 GPDSETIELMGNKSNAREIMIKAGVPVvpGSEGEIENEEEALEIAKEIGYP-VMVKASAGGGGRGIRIVRSEEELIKAFN 182
|
90 100
....*....|....*....|..
gi 1195504543 173 EMMQEKSFGAAGETVVVEEFLE 194
Cdd:PRK05586 183 TAKSEAKAAFGDDSMYIEKFIE 204
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
78-198 |
6.04e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 40.72 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195504543 78 LAAGIvgdLTSAGVRCFGPTAQAAQLESSKKFAKEFMDRHGIPTAQWRAFTNPEDACSFIMSANFPALVVKASGLaAGKG 157
Cdd:PRK12815 103 HEDGI---LEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTL-GGTG 178
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1195504543 158 VIVAKSTAEACKAVQEMMQEKSFgaagETVVVEEFLEG-EEV 198
Cdd:PRK12815 179 GGIAENLEELEQLFKQGLQASPI----HQCLLEESIAGwKEI 216
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
523-573 |
9.89e-03 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 39.29 E-value: 9.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1195504543 523 DILAQGAEPLFFLDY--FSCGKLDLSTTEAVVAGIAAACQRAGCALLGGETAE 573
Cdd:COG0709 89 DVYAMGGRPLTALAIvgFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSID 141
|
|
| |
