|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
5-414 |
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: 607.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 5 VLVIGSGGREHVLSWKLSKSPKVSQVYVAPGNAGTCQDkkVENVDLNVKDFNAVVKFCGDKKVSLVVVGPEDPLAAGIAD 84
Cdd:COG0151 3 VLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQL--AECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 85 TLQQHGICCFGPSAAAAQIEASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATYKaLVIKASGLSAGKGVVVAQNR 164
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 165 DQACQAVTDILVNKKYGAAGEEvvveeflegeevSVLAFCDGDTVALMPPAQDHKQLNEGDQGPNTGGMGAICPYPQIST 244
Cdd:COG0151 160 EEALAAVDDMLADGKFGDAGARvvieeflegeeaSLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 245 QELQVIEREIILKTVVGLKSEGRTYKGALYAGLMLTEDGPKVLEFNCRFGDPETQTILPLLESDLYDVCKSCVDGTLKQH 324
Cdd:COG0151 240 ELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 325 QPVFSqDKHVAGVVLVS--------------GIDVAEKTGLQIFHAGTSLKDGSTVTSGGRVLAVIAVDRSLKTACERAT 390
Cdd:COG0151 320 ELEWD-DRAAVCVVLASggypgsyekgdvitGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAY 398
|
410 420
....*....|....*....|....
gi 2054299380 391 EGAKFIQFQNSYFRSDIGFRVLTR 414
Cdd:COG0151 399 EAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
421-761 |
0e+00 |
|
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439920 [Multi-domain] Cd Length: 343 Bit Score: 584.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 421 MTYSDAGVSIETGNSLVQAIKPLAKSTTRPGCDALIGGFGALFDLKAAGFVDPVLVSGTDGVGTKLKIAQEVGRHDTIGI 500
Cdd:COG0150 5 LTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 501 DLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMATDVITGITKGCKEAGCALAGGETAEMPGMYTGSEYDLAGFAVGAVE 580
Cdd:COG0150 85 DLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVVE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 581 RSCIIPRlDQIETGDILIGLPSSGLHSNGFSLVRKVINKLEMTYDMPCPfQRGTTLGDVLLTPTKIYVKELLPLMKEMKV 660
Cdd:COG0150 165 KDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP-ELGRTLGEALLEPTRIYVKPVLALLKAVDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 661 KAFAHITGGGLVENVARVLPSDLTASIDANKWNIPAVFGWLADKGNINAREMSRTFNCGIGGVLVVRSEESKSVLNSLTN 740
Cdd:COG0150 243 HGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKA 322
|
330 340
....*....|....*....|.
gi 2054299380 741 SGVQASIIGEICKKEDKSVTV 761
Cdd:COG0150 323 AGETAYVIGEVVAGEGEGVVL 343
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
5-412 |
2.66e-173 |
|
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: 511.47 E-value: 2.66e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 5 VLVIGSGGREHVLSWKLSKSPKVSQVYVAPGNAGTCQDKKVENVDLNVKDFNAVVKFCGDKKVSLVVVGPEDPLAAGIAD 84
Cdd:TIGR00877 3 VLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 85 TLQQHGICCFGPSAAAAQIEASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATYKAlVIKASGLSAGKGVVVAQNR 164
Cdd:TIGR00877 83 ALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 165 DQACQAVTDILVnKKYGAAGEEVVVEEFLEGEEVSVLAFCDGDTVALMPPAQDHKQLNEGDQGPNTGGMGAICPYPQIST 244
Cdd:TIGR00877 162 EEAIKAVEDILE-QKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 245 QELQVIEREIILKTVVGLKSEGRTYKGALYAGLMLTEDGPKVLEFNCRFGDPETQTILPLLESDLYDVCKSCVDGTLKQH 324
Cdd:TIGR00877 241 EVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDEV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 325 QPVFSqDKHVAGVVLVS--------------GIDVAEKTGLQIFHAGTSLKDGSTVTSGGRVLAVIAVDRSLKTACERAT 390
Cdd:TIGR00877 321 ELRFD-NRAAVTVVLASegypedyrkgdpitGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAY 399
|
410 420
....*....|....*....|..
gi 2054299380 391 EGAKFIQFQNSYFRSDIGFRVL 412
Cdd:TIGR00877 400 EAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
456-751 |
5.55e-170 |
|
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: 497.77 E-value: 5.55e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 456 IGGFGALFDLKAAGFVDPVLVSGTDGVGTKLKIAQEVGRHDTIGIDLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMAT 535
Cdd:cd02196 3 IGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 536 DVITGITKGCKEAGCALAGGETAEMPGMYTGSEYDLAGFAVGAVERSCIIPRlDQIETGDILIGLPSSGLHSNGFSLVRK 615
Cdd:cd02196 83 EIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 616 VINKLEMTYDMPCPFQrGTTLGDVLLTPTKIYVKELLPLMKEMKVKAFAHITGGGLVENVARVLPSDLTASIDANKWNIP 695
Cdd:cd02196 162 ILFEEGLDYDDPEPGL-GKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2054299380 696 AVFGWLADKGNINAREMSRTFNCGIGGVLVVRSEESKSVLNSLTNSGVQASIIGEI 751
Cdd:cd02196 241 PIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEV 296
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
421-753 |
2.02e-156 |
|
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: 464.11 E-value: 2.02e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 421 MTYSDAGVSIETGNSLVQAIKPLAKSTTRPGCDALIGGFGALFDLKAaGFVDPVLVSGTDGVGTKLKIAQEVGRHDTIGI 500
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 501 DLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMATDVITGITKGCKEAGCALAGGETAEMPGMYTGSEYDLAGFAVGAVE 580
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 581 RSCIIPRlDQIETGDILIGLPSSGLHSNGFSLVRKVI-NKLEMTYDmPCPFQRGTTLGDVLLTPTKIYVKELLPLMKEMK 659
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLeDIAGLDYE-DTPEEFGKTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 660 VKAFAHITGGGLVENVARVLPSDLTASIDANKWNIPAVFGWLADKGNINAREMSRTFNCGIGGVLVVRSEESKSVLNSLT 739
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....
gi 2054299380 740 NSGVQASIIGEICK 753
Cdd:TIGR00878 318 AYGEKAWVIGEVKK 331
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-416 |
4.97e-131 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 402.58 E-value: 4.97e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 6 LVIGSGGREHVLSWKLSKSPKVSQVYVAPGNAGTCQDKKVENV-DLNVKDFNAVVKFCGDKKVSLVVVGPEDPLAAGIAD 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVpDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 85 TLQQHGICCFGPSAAAAQIEASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATyKALVIKASGLSAGKGVVVAQNR 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQG-APIVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 165 DQACQAVTDILVNKKYGAAGEEVVVEEFLEGEEVSVLAFCDGDTVALMPPAQDHKQLNEGDQGPNTGGMGAICPYPqIST 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAP-VLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 245 QELQ-VIEREIILKTVVGLKSEGRTYKGALYAGLMLTEDG--PKVLEFNCRFGDPETQTILPLLESDLYDVCKSCVDGTL 321
Cdd:PLN02257 239 PELEsKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 322 KQHQPVFSQD--------------KHVAGVVlVSGIDVAEK--TGLQIFHAGTSLK-DGSTVTSGGRVLAVIAVDRSLKT 384
Cdd:PLN02257 319 SGVSLTWSPDsamvvvmasngypgSYKKGTV-IKNLDEAEAvaPGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAE 397
|
410 420 430
....*....|....*....|....*....|..
gi 2054299380 385 ACERATEGAKFIQFQNSYFRSDIGFRVLTRNR 416
Cdd:PLN02257 398 ARARAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
421-755 |
6.72e-124 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 381.85 E-value: 6.72e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 421 MTYSDAGVSIETGNSLVQAIKPLAksttrPGcdalIGGFGALFDlkaagFVDPVLVSGTDGVGTKLKIAQEVGRHDTIGI 500
Cdd:PLN02557 59 LTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 501 DLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMATDVITGITKGCKEAGCALAGGETAEMPGMYTGSEYDLAGFAVGAVE 580
Cdd:PLN02557 125 DLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 581 RSCIIPRlDQIETGDILIGLPSSGLHSNGFSLVRKVINKLEMTYDMPCPfQRGTTLGDVLLTPTKIYVKELLPLMKEMKV 660
Cdd:PLN02557 205 KDAVIDG-KNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLP-GASVTIGEALMAPTVIYVKQVLDIISKGGV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 661 KAFAHITGGGLVENVARVLPSDLTASIDANKWNIPAVFGWLADKGNINAREMSRTFNCGIGGVLVVRSEESKSVLNSLTN 740
Cdd:PLN02557 283 KGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEEGAY 362
|
330
....*....|....*
gi 2054299380 741 sgvQASIIGEICKKE 755
Cdd:PLN02557 363 ---PAYRIGEVINGE 374
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
783-967 |
2.00e-102 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 317.41 E-value: 2.00e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 783 RVAVLISGSGTNLQALIDHTteQNSNSSAEIVLVISNKPNVQGLTRAEKAGIATKVISHKDYKSRDDFDEALHASLTSAG 862
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAI--KSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 863 IDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHG 942
Cdd:cd08645 79 VDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPG 158
|
170 180
....*....|....*....|....*
gi 2054299380 943 DTEETLAERVKKVEHTAFPKALELV 967
Cdd:cd08645 159 DTPETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
781-971 |
1.10e-101 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 316.20 E-value: 1.10e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 781 RKRVAVLISGSGTNLQALIDHTTEQNSNssAEIVLVISNKPNVQGLTRAEKAGIATKVISHKDYKSRDDFDEALHASLTS 860
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLP--AEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 861 AGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVY 940
Cdd:COG0299 79 YGPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVL 158
|
170 180 190
....*....|....*....|....*....|.
gi 2054299380 941 HGDTEETLAERVKKVEHTAFPKALELVASEK 971
Cdd:COG0299 159 PDDTEETLAARILEQEHRLYPEAIRLLAEGR 189
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
1.62e-87 |
|
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: 278.40 E-value: 1.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 105 ASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATYKALVIKASGLSAGKGVVVAQNRDQACQAVTDILVNKKYGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 185 EEVVVEEFLEGEEVSVLAFCDGDTVALMPPAQDHKQLNEGDQGPNTGGMGAICPYPQISTQELQVIEREIILKTVVGLKS 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 2054299380 265 EGRTYKGALYAGLMLTEDGPKVLEFNCRFGDPET 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
782-968 |
5.76e-78 |
|
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: 252.68 E-value: 5.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 782 KRVAVLISGSGTNLQALIDHTTEQNSNssAEIVLVISNKPNVQGLTRAEKAGIATKVISHKDYKSRDDFDEALHASLTSA 861
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIP--ASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 862 GIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYH 941
Cdd:TIGR00639 79 EVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILP 158
|
170 180
....*....|....*....|....*..
gi 2054299380 942 GDTEETLAERVKKVEHTAFPKALELVA 968
Cdd:TIGR00639 159 EDTEETLEQRIHKQEHRIYPLAIAWFA 185
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
782-964 |
8.48e-68 |
|
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: 224.48 E-value: 8.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 782 KRVAVLISGSGTNLQALIDHTTEqnSNSSAEIVLVISNKPNVQGLTRAEKAGIATKVISHKDYKSRDDFDEALHASLTSA 861
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRK--GGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 862 GIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYH 941
Cdd:pfam00551 79 AADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILP 158
|
170 180
....*....|....*....|...
gi 2054299380 942 GDTEETLAERVKKVEHTAFPKAL 964
Cdd:pfam00551 159 DDTAETLYNRVADLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
783-983 |
4.24e-38 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 141.37 E-value: 4.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 783 RVAVLISGSGTNLQALIDHTTEQNSNssAEIVLVISNKPNVQGLTRAEKAGIATKVISHKdyKSRDD--FDEALHASLTS 860
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVN--GDVVVVVTNKPGCGGAEYARENGIPVLVYPKT--KGEPDglSPDELVDALRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 861 AGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKG-----HNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQE 935
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2054299380 936 SVPVYHGDTEETLAERVKKVEHTAFPKALELVASEKallnsdafISWR 983
Cdd:PLN02331 157 VVPVLATDTPEELAARVLHEEHQLYVEVVAALCEER--------IVWR 196
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
592-761 |
5.45e-32 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 122.07 E-value: 5.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 592 ETGDILIGLPSSGLHSNGFSLVRKVINKLEmtydmpcpfQRGTTLGDVLLTPTKIYVKELLPLMKEMkVKAFAHITGGGL 671
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSG---------LAAVQLGDPLLEPTLIYVKLLLAALGGL-VKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 672 VENVARVLP-SDLTASIDANKwniPAVFGWLADkgninAREMSRTFNCGIgGVLVVRSEESKSVLNSLTNSGVQASIIGE 750
Cdd:pfam02769 71 AGALAEMAPaSGVGAEIDLDK---VPIFEELML-----PLEMLLSENQGR-GLVVVAPEEAEAVLAILEKEGLEAAVIGE 141
|
170
....*....|.
gi 2054299380 751 ICKKEDKSVTV 761
Cdd:pfam02769 142 VTAGGRLTVIV 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
5-414 |
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: 607.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 5 VLVIGSGGREHVLSWKLSKSPKVSQVYVAPGNAGTCQDkkVENVDLNVKDFNAVVKFCGDKKVSLVVVGPEDPLAAGIAD 84
Cdd:COG0151 3 VLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQL--AECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 85 TLQQHGICCFGPSAAAAQIEASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATYKaLVIKASGLSAGKGVVVAQNR 164
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 165 DQACQAVTDILVNKKYGAAGEEvvveeflegeevSVLAFCDGDTVALMPPAQDHKQLNEGDQGPNTGGMGAICPYPQIST 244
Cdd:COG0151 160 EEALAAVDDMLADGKFGDAGARvvieeflegeeaSLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 245 QELQVIEREIILKTVVGLKSEGRTYKGALYAGLMLTEDGPKVLEFNCRFGDPETQTILPLLESDLYDVCKSCVDGTLKQH 324
Cdd:COG0151 240 ELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 325 QPVFSqDKHVAGVVLVS--------------GIDVAEKTGLQIFHAGTSLKDGSTVTSGGRVLAVIAVDRSLKTACERAT 390
Cdd:COG0151 320 ELEWD-DRAAVCVVLASggypgsyekgdvitGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAY 398
|
410 420
....*....|....*....|....
gi 2054299380 391 EGAKFIQFQNSYFRSDIGFRVLTR 414
Cdd:COG0151 399 EAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
421-761 |
0e+00 |
|
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439920 [Multi-domain] Cd Length: 343 Bit Score: 584.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 421 MTYSDAGVSIETGNSLVQAIKPLAKSTTRPGCDALIGGFGALFDLKAAGFVDPVLVSGTDGVGTKLKIAQEVGRHDTIGI 500
Cdd:COG0150 5 LTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 501 DLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMATDVITGITKGCKEAGCALAGGETAEMPGMYTGSEYDLAGFAVGAVE 580
Cdd:COG0150 85 DLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGVVE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 581 RSCIIPRlDQIETGDILIGLPSSGLHSNGFSLVRKVINKLEMTYDMPCPfQRGTTLGDVLLTPTKIYVKELLPLMKEMKV 660
Cdd:COG0150 165 KDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP-ELGRTLGEALLEPTRIYVKPVLALLKAVDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 661 KAFAHITGGGLVENVARVLPSDLTASIDANKWNIPAVFGWLADKGNINAREMSRTFNCGIGGVLVVRSEESKSVLNSLTN 740
Cdd:COG0150 243 HGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKA 322
|
330 340
....*....|....*....|.
gi 2054299380 741 SGVQASIIGEICKKEDKSVTV 761
Cdd:COG0150 323 AGETAYVIGEVVAGEGEGVVL 343
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
5-412 |
2.66e-173 |
|
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: 511.47 E-value: 2.66e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 5 VLVIGSGGREHVLSWKLSKSPKVSQVYVAPGNAGTCQDKKVENVDLNVKDFNAVVKFCGDKKVSLVVVGPEDPLAAGIAD 84
Cdd:TIGR00877 3 VLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 85 TLQQHGICCFGPSAAAAQIEASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATYKAlVIKASGLSAGKGVVVAQNR 164
Cdd:TIGR00877 83 ALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 165 DQACQAVTDILVnKKYGAAGEEVVVEEFLEGEEVSVLAFCDGDTVALMPPAQDHKQLNEGDQGPNTGGMGAICPYPQIST 244
Cdd:TIGR00877 162 EEAIKAVEDILE-QKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 245 QELQVIEREIILKTVVGLKSEGRTYKGALYAGLMLTEDGPKVLEFNCRFGDPETQTILPLLESDLYDVCKSCVDGTLKQH 324
Cdd:TIGR00877 241 EVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDEV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 325 QPVFSqDKHVAGVVLVS--------------GIDVAEKTGLQIFHAGTSLKDGSTVTSGGRVLAVIAVDRSLKTACERAT 390
Cdd:TIGR00877 321 ELRFD-NRAAVTVVLASegypedyrkgdpitGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAY 399
|
410 420
....*....|....*....|..
gi 2054299380 391 EGAKFIQFQNSYFRSDIGFRVL 412
Cdd:TIGR00877 400 EAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
456-751 |
5.55e-170 |
|
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: 497.77 E-value: 5.55e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 456 IGGFGALFDLKAAGFVDPVLVSGTDGVGTKLKIAQEVGRHDTIGIDLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMAT 535
Cdd:cd02196 3 IGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 536 DVITGITKGCKEAGCALAGGETAEMPGMYTGSEYDLAGFAVGAVERSCIIPRlDQIETGDILIGLPSSGLHSNGFSLVRK 615
Cdd:cd02196 83 EIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 616 VINKLEMTYDMPCPFQrGTTLGDVLLTPTKIYVKELLPLMKEMKVKAFAHITGGGLVENVARVLPSDLTASIDANKWNIP 695
Cdd:cd02196 162 ILFEEGLDYDDPEPGL-GKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2054299380 696 AVFGWLADKGNINAREMSRTFNCGIGGVLVVRSEESKSVLNSLTNSGVQASIIGEI 751
Cdd:cd02196 241 PIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEV 296
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
421-753 |
2.02e-156 |
|
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: 464.11 E-value: 2.02e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 421 MTYSDAGVSIETGNSLVQAIKPLAKSTTRPGCDALIGGFGALFDLKAaGFVDPVLVSGTDGVGTKLKIAQEVGRHDTIGI 500
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 501 DLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMATDVITGITKGCKEAGCALAGGETAEMPGMYTGSEYDLAGFAVGAVE 580
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 581 RSCIIPRlDQIETGDILIGLPSSGLHSNGFSLVRKVI-NKLEMTYDmPCPFQRGTTLGDVLLTPTKIYVKELLPLMKEMK 659
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLeDIAGLDYE-DTPEEFGKTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 660 VKAFAHITGGGLVENVARVLPSDLTASIDANKWNIPAVFGWLADKGNINAREMSRTFNCGIGGVLVVRSEESKSVLNSLT 739
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....
gi 2054299380 740 NSGVQASIIGEICK 753
Cdd:TIGR00878 318 AYGEKAWVIGEVKK 331
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-416 |
4.97e-131 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 402.58 E-value: 4.97e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 6 LVIGSGGREHVLSWKLSKSPKVSQVYVAPGNAGTCQDKKVENV-DLNVKDFNAVVKFCGDKKVSLVVVGPEDPLAAGIAD 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVpDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 85 TLQQHGICCFGPSAAAAQIEASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATyKALVIKASGLSAGKGVVVAQNR 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQG-APIVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 165 DQACQAVTDILVNKKYGAAGEEVVVEEFLEGEEVSVLAFCDGDTVALMPPAQDHKQLNEGDQGPNTGGMGAICPYPqIST 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAP-VLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 245 QELQ-VIEREIILKTVVGLKSEGRTYKGALYAGLMLTEDG--PKVLEFNCRFGDPETQTILPLLESDLYDVCKSCVDGTL 321
Cdd:PLN02257 239 PELEsKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 322 KQHQPVFSQD--------------KHVAGVVlVSGIDVAEK--TGLQIFHAGTSLK-DGSTVTSGGRVLAVIAVDRSLKT 384
Cdd:PLN02257 319 SGVSLTWSPDsamvvvmasngypgSYKKGTV-IKNLDEAEAvaPGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAE 397
|
410 420 430
....*....|....*....|....*....|..
gi 2054299380 385 ACERATEGAKFIQFQNSYFRSDIGFRVLTRNR 416
Cdd:PLN02257 398 ARARAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
421-755 |
6.72e-124 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 381.85 E-value: 6.72e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 421 MTYSDAGVSIETGNSLVQAIKPLAksttrPGcdalIGGFGALFDlkaagFVDPVLVSGTDGVGTKLKIAQEVGRHDTIGI 500
Cdd:PLN02557 59 LTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 501 DLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMATDVITGITKGCKEAGCALAGGETAEMPGMYTGSEYDLAGFAVGAVE 580
Cdd:PLN02557 125 DLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 581 RSCIIPRlDQIETGDILIGLPSSGLHSNGFSLVRKVINKLEMTYDMPCPfQRGTTLGDVLLTPTKIYVKELLPLMKEMKV 660
Cdd:PLN02557 205 KDAVIDG-KNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLP-GASVTIGEALMAPTVIYVKQVLDIISKGGV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 661 KAFAHITGGGLVENVARVLPSDLTASIDANKWNIPAVFGWLADKGNINAREMSRTFNCGIGGVLVVRSEESKSVLNSLTN 740
Cdd:PLN02557 283 KGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEEGAY 362
|
330
....*....|....*
gi 2054299380 741 sgvQASIIGEICKKE 755
Cdd:PLN02557 363 ---PAYRIGEVINGE 374
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
783-967 |
2.00e-102 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 317.41 E-value: 2.00e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 783 RVAVLISGSGTNLQALIDHTteQNSNSSAEIVLVISNKPNVQGLTRAEKAGIATKVISHKDYKSRDDFDEALHASLTSAG 862
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAI--KSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 863 IDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHG 942
Cdd:cd08645 79 VDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPG 158
|
170 180
....*....|....*....|....*
gi 2054299380 943 DTEETLAERVKKVEHTAFPKALELV 967
Cdd:cd08645 159 DTPETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
781-971 |
1.10e-101 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 316.20 E-value: 1.10e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 781 RKRVAVLISGSGTNLQALIDHTTEQNSNssAEIVLVISNKPNVQGLTRAEKAGIATKVISHKDYKSRDDFDEALHASLTS 860
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLP--AEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 861 AGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVY 940
Cdd:COG0299 79 YGPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVL 158
|
170 180 190
....*....|....*....|....*....|.
gi 2054299380 941 HGDTEETLAERVKKVEHTAFPKALELVASEK 971
Cdd:COG0299 159 PDDTEETLAARILEQEHRLYPEAIRLLAEGR 189
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
1.62e-87 |
|
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: 278.40 E-value: 1.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 105 ASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATYKALVIKASGLSAGKGVVVAQNRDQACQAVTDILVNKKYGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 185 EEVVVEEFLEGEEVSVLAFCDGDTVALMPPAQDHKQLNEGDQGPNTGGMGAICPYPQISTQELQVIEREIILKTVVGLKS 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 2054299380 265 EGRTYKGALYAGLMLTEDGPKVLEFNCRFGDPET 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
782-968 |
5.76e-78 |
|
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: 252.68 E-value: 5.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 782 KRVAVLISGSGTNLQALIDHTTEQNSNssAEIVLVISNKPNVQGLTRAEKAGIATKVISHKDYKSRDDFDEALHASLTSA 861
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIP--ASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 862 GIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYH 941
Cdd:TIGR00639 79 EVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILP 158
|
170 180
....*....|....*....|....*..
gi 2054299380 942 GDTEETLAERVKKVEHTAFPKALELVA 968
Cdd:TIGR00639 159 EDTEETLEQRIHKQEHRIYPLAIAWFA 185
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
782-964 |
8.48e-68 |
|
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: 224.48 E-value: 8.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 782 KRVAVLISGSGTNLQALIDHTTEqnSNSSAEIVLVISNKPNVQGLTRAEKAGIATKVISHKDYKSRDDFDEALHASLTSA 861
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRK--GGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 862 GIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYH 941
Cdd:pfam00551 79 AADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILP 158
|
170 180
....*....|....*....|...
gi 2054299380 942 GDTEETLAERVKKVEHTAFPKAL 964
Cdd:pfam00551 159 DDTAETLYNRVADLEHKALPRVL 181
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
5-104 |
2.44e-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: 166.76 E-value: 2.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 5 VLVIGSGGREHVLSWKLSKSPKVSQVYVAPGNAGTCQDkkVENVDLNVKDFNAVVKFCGDKKVSLVVVGPEDPLAAGIAD 84
Cdd:pfam02844 3 VLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQL--AECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 2054299380 85 TLQQH--GICCFGPSAAAAQIE 104
Cdd:pfam02844 81 ALRERaaGIPVFGPSKAAAQLE 102
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
786-966 |
1.07e-39 |
|
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: 144.74 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 786 VLISGSGTNLQALIDHTTeqnSNSSAEIVLVISNKPNVQGLTRAEKAGIatkviSHKDYKSRDDFDEALHASLTSAGIDI 865
Cdd:cd08369 1 IVILGSGNIGQRVLKALL---SKEGHEIVGVVTHPDSPRGTAQLSLELV-----GGKVYLDSNINTPELLELLKEFAPDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 866 VCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHGDTE 945
Cdd:cd08369 73 IVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTA 152
|
170 180
....*....|....*....|.
gi 2054299380 946 ETLAERVKKVEHTAFPKALEL 966
Cdd:cd08369 153 GTLYQRLIELGPKLLKEALQK 173
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
783-983 |
4.24e-38 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 141.37 E-value: 4.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 783 RVAVLISGSGTNLQALIDHTTEQNSNssAEIVLVISNKPNVQGLTRAEKAGIATKVISHKdyKSRDD--FDEALHASLTS 860
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVN--GDVVVVVTNKPGCGGAEYARENGIPVLVYPKT--KGEPDglSPDELVDALRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 861 AGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKG-----HNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQE 935
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2054299380 936 SVPVYHGDTEETLAERVKKVEHTAFPKALELVASEKallnsdafISWR 983
Cdd:PLN02331 157 VVPVLATDTPEELAARVLHEEHQLYVEVVAALCEER--------IVWR 196
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
780-975 |
1.34e-33 |
|
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: 130.94 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 780 QRKRVAVLISGSGTNLQALIDhttEQNSNS-SAEIVLVISNKPNVQGLtrAEKAGIATKVISHKDyKSRDDFDEALHASL 858
Cdd:COG0788 85 RRKRVAILVSKEDHCLNDLLY---RWRSGElPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLLELL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 859 TSAGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKG----HNAHEqvikANVRISGCTVHFVAEEVDGGAIIVQ 934
Cdd:COG0788 159 EEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGakpyHQAYE----RGVKLIGATAHYVTADLDEGPIIEQ 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2054299380 935 ESVPVYHGDTEETLAERVKKVEHTAFPKALELVASEKALLN 975
Cdd:COG0788 235 DVERVDHRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVN 275
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
782-977 |
3.43e-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: 126.91 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 782 KRVAVLISGSGTNLQALIDHTTEQNSNssAEIVLVISNKPNVQGLtrAEKAGIATKVIS-HKDYKSRDDfdEALHASLTS 860
Cdd:cd08648 1 KRVAIFVSKEDHCLYDLLHRWREGELP--CEIPLVISNHPDLRPL--AERFGIPFHHIPvTKDTKAEAE--AEQLELLEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 861 AGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVY 940
Cdd:cd08648 75 YGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVS 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2054299380 941 HGDTEETLAERVKKVEHTAFPKALELVASEKALLNSD 977
Cdd:cd08648 155 HRDSVEDLVRKGRDIEKQVLARAVKWHLEDRVLVYGN 191
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
592-761 |
5.45e-32 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 122.07 E-value: 5.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 592 ETGDILIGLPSSGLHSNGFSLVRKVINKLEmtydmpcpfQRGTTLGDVLLTPTKIYVKELLPLMKEMkVKAFAHITGGGL 671
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSG---------LAAVQLGDPLLEPTLIYVKLLLAALGGL-VKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 672 VENVARVLP-SDLTASIDANKwniPAVFGWLADkgninAREMSRTFNCGIgGVLVVRSEESKSVLNSLTNSGVQASIIGE 750
Cdd:pfam02769 71 AGALAEMAPaSGVGAEIDLDK---VPIFEELML-----PLEMLLSENQGR-GLVVVAPEEAEAVLAILEKEGLEAAVIGE 141
|
170
....*....|.
gi 2054299380 751 ICKKEDKSVTV 761
Cdd:pfam02769 142 VTAGGRLTVIV 152
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
474-750 |
2.05e-31 |
|
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: 122.89 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 474 VLVSGTDGVGTKLKIaqevgRHDTIGIDLVAMCVNDILAHGAEPLFFLDYFSTGQ-LSVSMATDVITGITKGCKEAGCAL 552
Cdd:cd00396 1 SLAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 553 AGGETAEMPGMyTGSEYDLAGFAVGAVERSCIIPrldqietgdiliglpssglhsngfslvrkvinklemtydmpcpfQR 632
Cdd:cd00396 76 VGGHTSVSPGT-MGHKLSLAVFAIGVVEKDRVID--------------------------------------------SS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 633 GTTLGDVLLTPTKIYVKEllpLMKEMKVKAFAHITGGGLVENVARVLP-SDLTASIDANKWNIPAVFGWLADkgniNARE 711
Cdd:cd00396 111 GARPGDVLILTGVDAVLE---LVAAGDVHAMHDITDGGLLGTLPELAQaSGVGAEIDLEAIPLDEVVRWLCV----EHIE 183
|
250 260 270
....*....|....*....|....*....|....*....
gi 2054299380 712 MSRTFNCGIGGVLVVRSEESKSVLNSLTNSGVQASIIGE 750
Cdd:cd00396 184 EALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
780-975 |
2.15e-29 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 118.67 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 780 QRKRVAVLISGSGtnlQALID-----HTTEQNsnssAEIVLVISNKPNVQGLtrAEKAGIATKVISH-KDykSRDDFDEA 853
Cdd:PRK06027 88 ERKRVVILVSKED---HCLGDllwrwRSGELP----VEIAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEAR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 854 LHASLTSAGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKG----HNAHEQvikaNVRISGCTVHFVAEEVDGG 929
Cdd:PRK06027 157 LLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGakpyHQAYER----GVKLIGATAHYVTADLDEG 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2054299380 930 AIIVQESVPVYHGDTEETLAERVKKVEHTAFPKALELVASEKALLN 975
Cdd:PRK06027 233 PIIEQDVIRVDHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVY 278
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
335-410 |
3.78e-25 |
|
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: 99.83 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 335 AGVVLVSG-----------IDVAEKTGLQIFHAGTSLKDGSTVTSGGRVLAVIAVDRSLKTACERATEGAKFIQFQNSYF 403
Cdd:pfam02843 2 VCVVLASGgypgsyekgdvITGLDEAGVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEGMFY 81
|
....*..
gi 2054299380 404 RSDIGFR 410
Cdd:pfam02843 82 RKDIGTR 88
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
475-579 |
6.70e-21 |
|
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: 88.27 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 475 LVSGTDGVGTKLKiaqeVGRHDTIGIDLVAMCVNDILAHGAEPLFFLDYFSTGQLSVSMAT--DVITGITKGCKEAGCAL 552
Cdd:pfam00586 5 VAVTTDGHGTPSL----VDPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWVleEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*..
gi 2054299380 553 AGGETAEMPGmytGSEYDLAGFAVGAV 579
Cdd:pfam00586 81 VGGDTSFDPE---GGKPTISVTAVGIV 104
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
774-976 |
7.20e-21 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 93.66 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 774 RTPVLLQRKRVAVLISGSGtnlQALID--HTTeQNSNSSAEIVLVISNK---PNVQGLTRAEKAGIATKVISHKDYKSRD 848
Cdd:PLN02828 63 RVPGLDPKYKIAVLASKQD---HCLIDllHRW-QDGRLPVDITCVISNHergPNTHVMRFLERHGIPYHYLPTTKENKRE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 849 DfdEALhaSLTSaGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDG 928
Cdd:PLN02828 139 D--EIL--ELVK-GTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDA 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2054299380 929 GAIIVQESVPVYHGDTEETLAERVKKVEHTAFPKALELVASEKALLNS 976
Cdd:PLN02828 214 GPIIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAIKSYCELRVLPYG 261
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
812-977 |
1.34e-19 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 90.04 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 812 EIVLVISNKPNVQGLtrAEKAGIATKVIS-HKDYKSRDdfdEA-LHASLTSAGIDIVCLAGFMRILTGGFVSKWHGKMLN 889
Cdd:PRK13011 118 DIVGVVSNHPDLEPL--AAWHGIPFHHFPiTPDTKPQQ---EAqVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAIN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 890 IHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAERVKKVEHTAFPKALELVAS 969
Cdd:PRK13011 193 IHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDLVAKGRDVECLTLARAVKAHIE 272
|
....*...
gi 2054299380 970 EKALLNSD 977
Cdd:PRK13011 273 RRVFLNGN 280
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
812-977 |
7.04e-19 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 88.31 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 812 EIVLVISNKPNVQGLtrAEKAGIATKVIS-HKDYKSRDdfdEA-LHASLTSAGIDIVCLAGFMRILTGGFVSKWHGKMLN 889
Cdd:PRK13010 122 DIVGIISNHPDLQPL--AVQHDIPFHHLPvTPDTKAQQ---EAqILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAIN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 890 IHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAERVKKVEHTAFPKALELVAS 969
Cdd:PRK13010 197 IHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDLVAKGRDVECLTLARAVKAFIE 276
|
....*...
gi 2054299380 970 EKALLNSD 977
Cdd:PRK13010 277 HRVFINGD 284
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
795-983 |
7.22e-13 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 70.52 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 795 LQALIDhtteqnsnSSAEIVLVISNKPNVQGLTR----------AEKAGIatKVISHKDYKsrddfDEALHASLTSAGID 864
Cdd:COG0223 16 LEALLA--------AGHEVVAVVTQPDRPAGRGRkltpspvkelALEHGI--PVLQPESLK-----DPEFLEELRALNPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 865 IVCLAGFMRILtggfvSKW------HGkMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVP 938
Cdd:COG0223 81 LIVVVAYGQIL-----PKEvldiprLG-CINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 939 VYHGDTEETLAERVKKVEHTAFPKALELVASEKA---------------LLNSDAFISWR 983
Cdd:COG0223 155 IGPDDTAGSLHDKLAELGAELLLETLDALEAGTLtptpqdesgatyapkISKEDGRIDWS 214
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
864-954 |
5.77e-10 |
|
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: 61.65 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 864 DIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHGD 943
Cdd:TIGR00460 80 DVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEED 159
|
90
....*....|.
gi 2054299380 944 TEETLAERVKK 954
Cdd:TIGR00460 160 NSGTLSDKLSE 170
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
891-952 |
7.37e-10 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 59.40 E-value: 7.37e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2054299380 891 HPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAERV 952
Cdd:cd08822 95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRA 156
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
795-951 |
2.05e-09 |
|
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: 58.22 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 795 LQALIDhtteqnsnSSAEIVLVISNKPNVQG----LT------RAEKAGIatKVisHKDYKSRDdfdEALHASLTSAGID 864
Cdd:cd08646 16 LEALLK--------SGHEVVAVVTQPDKPRGrgkkLTpspvkeLALELGL--PV--LQPEKLKD---EEFLEELKALKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 865 IVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKG----HNAheqvIKANVRISGCTVHFVAEEVDGGAIIVQESVPVY 940
Cdd:cd08646 81 LIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGaapiQRA----ILNGDKETGVTIMKMDEGLDTGDILAQEEVPID 156
|
170
....*....|.
gi 2054299380 941 HGDTEETLAER 951
Cdd:cd08646 157 PDDTAGELLDK 167
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
804-950 |
4.21e-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: 56.68 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 804 EQNSNSSAEIVLVISNkpnvqgltrAEKAGIATKVISHKDYKSRDDFDEALHASLTSAGIDIVCLAGFMRILTGGFVSKW 883
Cdd:cd08820 20 RLQDRGSFEIIAVLTN---------TSPADVWEGSEPLYDIGSTERNLHKLLEILENKGVDILISVQYHWILPGSILEKA 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2054299380 884 HGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAE 950
Cdd:cd08820 91 KEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYI 157
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
887-965 |
4.91e-09 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 56.07 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 887 MLNIHPSLLPSFKG---------HNAHEQVikanvrisGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAERVKKVEH 957
Cdd:cd08653 71 VLNLHGGILPDYRGvhtgfwalaNGDPDNV--------GVTVHLVDAGIDTGDVLAQARPPLAAGDTLLSLYLRLYRAGV 142
|
....*...
gi 2054299380 958 TAFPKALE 965
Cdd:cd08653 143 ELMVEAIA 150
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
795-967 |
1.47e-07 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 52.27 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 795 LQALIDhtteqnsnSSAEIVLVISNKPNVQG--------LTRAEKAGIATkvishkdYKSRDDFDEALHASLTSAGIDIV 866
Cdd:cd08651 15 LEAILE--------AGGEVVGVITLDDSSSNndsdyldlDSFARKNGIPY-------YKFTDINDEEIIEWIKEANPDII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 867 CLAGFMRILTGGFvskwhgkmLNI--------HPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVP 938
Cdd:cd08651 80 FVFGWSQLLKPEI--------LAIprlgvigfHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFP 151
|
170 180
....*....|....*....|....*....
gi 2054299380 939 VYHGDTEETLAERVKKVEHTAFPKALELV 967
Cdd:cd08651 152 IDKDDTANSLYDKIMEAAKQQIDKFLPRL 180
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
780-939 |
1.93e-07 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 54.31 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 780 QRKRVAVLISG--SGTNLQALIDhtTEQNSNSSAEIVLVISNKPNVQGLTR----------AEKAGIATKVISHKDYKSR 847
Cdd:PLN02285 5 RKKRLVFLGTPevAATVLDALLD--ASQAPDSAFEVAAVVTQPPARRGRGRklmpspvaqlALDRGFPPDLIFTPEKAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 848 DDFDEALHAsltsAGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVD 927
Cdd:PLN02285 83 EDFLSALRE----LQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALD 158
|
170
....*....|..
gi 2054299380 928 GGAIIVQESVPV 939
Cdd:PLN02285 159 AGPVIAQERVEV 170
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
852-952 |
4.88e-07 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 50.91 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 852 EALHASLTSAGIDIVCLAGFMRILTGGFVSKWHGKMLNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAI 931
Cdd:cd08823 61 EQLAEWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPI 140
|
90 100
....*....|....*....|.
gi 2054299380 932 IVQESVPVYHGDTEETLAERV 952
Cdd:cd08823 141 VLEQFTPIHPDDTYGLLCSRL 161
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
502-606 |
2.78e-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: 50.24 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 502 LVAMCVNDILAHGAEPLFFLdyFSTG---QLSVSMATDVITGITKGCKEAGCALAGGETAEmpgmytGSEYDLAGFAVGA 578
Cdd:cd02194 63 ALAVNLSDLAAMGARPLGFL--LSLGlppDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTS------GSELVISVTALGE 134
|
90 100 110
....*....|....*....|....*....|...
gi 2054299380 579 VERSCIIPRlDQIETGDIL-----IGLPSSGLH 606
Cdd:cd02194 135 VEKGKPLRR-SGAKPGDLLyvtgtLGDAAAGLA 166
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
509-762 |
1.17e-05 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 48.53 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 509 DILAHGAEPLFFLDY--FSTGQLSVSMATDVITGITKGCKEAGCALAGGETAEmpgmytGSE--YdlaGFAV-GAVERSC 583
Cdd:COG0709 89 DVYAMGGRPLTALAIvgFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSID------DPEpkY---GLAVtGLVHPDK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 584 IIpRLDQIETGDILI-----GlpsSGLHSNGF-------SLVRKVInklemtydmpcpfqrgttlgDVLLTPTKIYVKel 651
Cdd:COG0709 160 VL-RNAGARPGDVLIltkplG---TGILTTAIkagladgEDIAAAI--------------------ASMTTLNKAAAE-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 652 lpLMKEMKVKAFAHITGGGL----VEnVARvlPSDLTASIDANKwnIPAVFG--WLADKG--------NINAREMSRTFN 717
Cdd:COG0709 214 --LARLYGVHACTDVTGFGLlghlLE-MAR--GSGVSAEIDLDA--VPLLPGalELAEQGivpggtyrNRASYGAKVEFA 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 718 CGI--------------GGVLV-VRSEESKSVLNSLTNSGVQASIIGEICKKEDKSVTVH 762
Cdd:COG0709 287 EGLdeaqrdllfdpqtsGGLLIaVPPEAAEELLAALRAAGYAAAIIGEVTAGEGGAIEVR 346
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
506-751 |
2.11e-05 |
|
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100031 [Multi-domain] Cd Length: 287 Bit Score: 47.52 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 506 CVNDILAHGAEPLFFLDY--FSTG--QLSVSMATDVITGITKGCKEAGCALAGGETAEMPGMytgseydLAGFAV-GAVE 580
Cdd:cd02195 80 ALSDIYAMGAKPLSALAIvtLPRKlpALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEP-------KYGLSVtGLVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 581 RSCIIpRLDQIETGDILI-----GlpsSGlhsngfslvrkVINKLEMtydmpcpfqRGTTLGDVLLTPTKIYV---KELL 652
Cdd:cd02195 153 PNKIL-RNSGAKPGDVLIltkplG---TG-----------ILFAAEM---------AGLARGEDIDAALESMArlnRAAA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 653 PLMKEMKVKAFAHITGGGLV---ENVARvlPSDLTASIDANKwnIPAVfgwladkgninarEMSrtfncgiGGVLV-VRS 728
Cdd:cd02195 209 ELLRKYGAHACTDVTGFGLLghlLEMAR--ASGVSAEIDLDK--LPLL-------------QTS-------GGLLAaVPP 264
|
250 260
....*....|....*....|...
gi 2054299380 729 EESKSVLNSLTNSGVQASIIGEI 751
Cdd:cd02195 265 EDAAALLALLKAGGPPAAIIGEV 287
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
503-751 |
4.78e-05 |
|
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100037 [Multi-domain] Cd Length: 298 Bit Score: 46.44 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 503 VAMCVNDILAHGAEPLFFLDyfsTGQLSVSMATD----VITGITKGCKEAGCALAGGETaempGMYTGSEYDLAG-FAVG 577
Cdd:cd06061 64 VHIAANDIATSGARPRWLLV---TLLLPPGTDEEelkaIMREINEAAKELGVSIVGGHT----EVTPGVTRPIISvTAIG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 578 AVERSCIIpRLDQIETGDILI-----GLPSSGLHSNGFSLvrKVINKLEMTYdmpcpFQRGTTLGDVLLTptkiyVKELL 652
Cdd:cd06061 137 KGEKDKLV-TPSGAKPGDDIVmtkgaGIEGTAILANDFEE--ELKKRLSEEE-----LREAAKLFYKISV-----VKEAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 653 pLMKEMKVKAFAHITGGG----LVEnVARVlpSDLTASIDANKWNIPAVFGWLADKGNINAREMSrtfncGIGGVL-VVR 727
Cdd:cd06061 204 -IAAEAGVTAMHDATEGGilgaLWE-VAEA--SGVGLRIEKDKIPIRQETKEICEALGIDPLRLI-----SSGTLLiTVP 274
|
250 260
....*....|....*....|....
gi 2054299380 728 SEESKSVLNSLTNSGVQASIIGEI 751
Cdd:cd06061 275 PEKGDELVDALEEAGIPASVIGKI 298
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
888-952 |
1.39e-04 |
|
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: 44.26 E-value: 1.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2054299380 888 LNIHPSLLPSFKGHNA-HEQVIKANVRIsGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAERV 952
Cdd:cd08644 101 FNLHGSLLPKYRGRAPlNWALINGETET-GVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKL 165
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
77-294 |
5.07e-04 |
|
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: 42.94 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 77 PLAAGIADtlqQHGIccFGPSAAAAQIEASKSFSKKFMERHNIPTARFQTFTCPDAATKHIKSATYKaLVIKASGLSAGK 156
Cdd:COG0439 30 ETAAELAE---ELGL--PGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYP-VVVKPADGAGSR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 157 GVVVAQNRDQACQAVTDILVNKKYGAAGEEVVVEEFLEGEEVSVLAFC-DGDTVALMppAQDHKQLnegdqGPNTGGMGA 235
Cdd:COG0439 104 GVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVrDGEVVVCS--ITRKHQK-----PPYFVELGH 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2054299380 236 ICPYPqISTQELQVIeREIILKTV--VGLKSegrtykGALYAGLMLTEDG-PKVLEFNCRFG 294
Cdd:COG0439 177 EAPSP-LPEELRAEI-GELVARALraLGYRR------GAFHTEFLLTPDGePYLIEINARLG 230
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
782-962 |
6.16e-04 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 42.58 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 782 KRVAVLISgsgtNLQALIDHTTEQNSNSSAEIVLVISNKPnvqgltraekagiaTKVISHKDYKSR----------DDFD 851
Cdd:PRK07579 2 KTILVLTD----NVHAHALAVDLIARKNDMDVDYFCSFKS--------------QTSFAKEIYQSPikqldvaervAEIV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 852 EALHAsltsaGIDIVCLAGFMRILTGGFvskwhgKMLNIHPSLLPSFKGHNAHEQVIKANVRIsGCTVHFVAEEVDGGAI 931
Cdd:PRK07579 64 ERYDL-----VLSFHCKQRFPAKLVNGV------RCINIHPGFNPYNRGWFPQVFSIINGLKI-GATIHEMDEQLDHGPI 131
|
170 180 190
....*....|....*....|....*....|.
gi 2054299380 932 IVQESVPVYHGDTEETLAERVKKVEHTAFPK 962
Cdd:PRK07579 132 IAQREVEIESWDSSGSVYARVMDIERELVLE 162
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
884-972 |
1.35e-03 |
|
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: 41.28 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 884 HGKMLnIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAERVKKVEHT-AFPK 962
Cdd:cd08647 100 HGSII-YHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPEGIkAMVE 178
|
90
....*....|
gi 2054299380 963 ALELVASEKA 972
Cdd:cd08647 179 AVRLIAEGKA 188
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
888-952 |
1.63e-03 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 41.60 E-value: 1.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2054299380 888 LNIHPSLLPSFKGH-NAHEQVIKANVRIsGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAERV 952
Cdd:PRK06988 103 YNMHGSLLPKYRGRvPVNWAVLNGETET-GATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKV 167
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
57-294 |
4.45e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 40.25 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 57 AVVKFCGDKKVSLVVVG--PEDPLAAGIADTLQQHGICCFGPSAAAAQIEASKSFSKKFMERHNIPTARfqTFTCPDAAT 134
Cdd:PRK12767 60 RLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPK--SYLPESLED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 135 KHIKSATYKA---LVIKASGLSAGKGVVVAQNRDQ---ACQAVTDILVNKkygaageevvveeFLEGEEVSVLAFCD--G 206
Cdd:PRK12767 138 FKAALAKGELqfpLFVKPRDGSASIGVFKVNDKEElefLLEYVPNLIIQE-------------FIEGQEYTVDVLCDlnG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 207 DTVALMPpaqdHKQL----NEGDQgpntggmGAICPYPQIstqelqvieREIILKTVVGLKSegrtyKGALYAGLMLTED 282
Cdd:PRK12767 205 EVISIVP----RKRIevraGETSK-------GVTVKDPEL---------FKLAERLAEALGA-----RGPLNIQCFVTDG 259
|
250
....*....|..
gi 2054299380 283 GPKVLEFNCRFG 294
Cdd:PRK12767 260 EPYLFEINPRFG 271
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-184 |
5.77e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 39.17 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 110 SKKFMERHNIPTARFQTFTCPDAATKHIKSATYKALVIKASGLSAGK----GVVVAQNRDQACQAVTDI----LVNKKYG 181
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMlgknLVTKQTG 86
|
...
gi 2054299380 182 AAG 184
Cdd:pfam08442 87 PDG 89
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
888-969 |
7.38e-03 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 40.35 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054299380 888 LNIHPSLLPSFKGHNAHEQVIKANVRISGCTVHFVAEEVDGGAIIVQESVPVYHGDTEETLAERVKKVEHTAFPKALELV 967
Cdd:PRK08125 101 FNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAI 180
|
..
gi 2054299380 968 AS 969
Cdd:PRK08125 181 KH 182
|
|
| |
