|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
5-427 |
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: 703.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 5 VLVIGNGGREHTLAWKLAQSEHVSQVIVAPGNAGTANNGKisNSAVSVNDHTALAQFCKDQKIELVVVGPEAPLADGIVG 84
Cdd:COG0151 3 VLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 85 NLTSAGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNK 164
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 165 EEACKAVQDIMQDKAFGTAGDTVVIEEVLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDHGPNTGGMGAYCPTPQVPK 244
Cdd:COG0151 160 EEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 245 DLLLKIKNTILQRAVDGMKQEGVPYVGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSVLDGQLSNS 324
Cdd:COG0151 240 ELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 325 LPVWREDsAAVTVVMASKGYPANYTKGIEITGIPEAKALGLEVFQAGTTLKEDKtLVTNGGRVLTVTAIQKDLMSALQEA 404
Cdd:COG0151 320 ELEWDDR-AAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGK-LVTNGGRVLGVTALGDTLEEARERA 397
|
410 420
....*....|....*....|...
gi 821472192 405 NKGITVIKFEGAVYRKDIGYRAI 427
Cdd:COG0151 398 YEAVEKIRFEGMFYRRDIGWRAL 420
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
5-427 |
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: 632.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 5 VLVIGNGGREHTLAWKLAQSEHVSQVIVAPGNAGTANNGKISNSAVSVNDHTALAQFCKDQKIELVVVGPEAPLADGIVG 84
Cdd:TIGR00877 3 VLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 85 NLTSAGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPAlVIKASGLAAGKGVIVANNK 164
Cdd:TIGR00877 83 ALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 165 EEACKAVQDIMQDKaFGTAGDTVVIEEVLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDHGPNTGGMGAYCPTPQVPK 244
Cdd:TIGR00877 162 EEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 245 DLLLKIKNTILQRAVDGMKQEGVPYVGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSVLDGQLsNS 324
Cdd:TIGR00877 241 EVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKL-DE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 325 LPVWREDSAAVTVVMASKGYPANYTKGIEITGIPEAKALGLEVFQAGTTLKEDKtLVTNGGRVLTVTAIQKDLMSALQEA 404
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGK-LVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 821472192 405 NKGITVIKFEGAVYRKDIGYRAI 427
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
432-772 |
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: 580.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 432 QSRGLTYKESGVDISAGNELVKKIKPLAKATSRPGSNVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQQCNKHD 511
Cdd:COG0150 1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 512 TIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGMYPPGEYDLAGFAV 591
Cdd:COG0150 81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 592 GAMERNQKLPQlNRITEGDVVIGIASSGVHSNGFSLIRKIVENSSFQFSSLAPDgcGNQTLGELLLKPTKIYSRTLLPVL 671
Cdd:COG0150 161 GVVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLGEALLEPTRIYVKPVLALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 672 RSGHVKAFAHITGGGLLENIPRVLPETLGVDLDARCWKIPRIFSWLQLEGCLSEEEMAKTFNCGIGAVMVVQKDLAEQVL 751
Cdd:COG0150 238 KAVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAAL 317
|
330 340
....*....|....*....|.
gi 821472192 752 KDIHQQEEEAWIIGNVVTCPT 772
Cdd:COG0150 318 ALLKAAGETAYVIGEVVAGEG 338
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
470-768 |
9.42e-173 |
|
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: 505.86 E-value: 9.42e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 470 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQQCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDVSTA 549
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 550 ETVIAGIAKACEKAGCALLGGETAEMPGMYPPGEYDLAGFAVGAMERNQKLPQlNRITEGDVVIGIASSGVHSNGFSLIR 629
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 630 KIVENSSFQFSSLAPDgcGNQTLGELLLKPTKIYSRTLLPVLRSGHVKAFAHITGGGLLENIPRVLPETLGVDLDARCWK 709
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 821472192 710 IPRIFSWLQLEGCLSEEEMAKTFNCGIGAVMVVQKDLAEQVLKDIHQQEEEAWIIGNVV 768
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-431 |
1.69e-166 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 495.03 E-value: 1.69e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 6 LVIGNGGREHTLAWKLAQSEHVSQVIVAPGNAGTANNGKISN-SAVSVNDHTALAQFCKDQKIELVVVGPEAPLADGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 85 NLTSAGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 165 EEACKAVQDIMQDKAFGTAGDTVVIEEVLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDHGPNTGGMGAYCPTPQVPK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 245 DLLLKIKNTILQRAVDGMKQEGVPYVGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSVLDGQLS 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 323 NSLPVWREDSaAVTVVMASKGYPANYTKGIEITGIPEAKAL--GLEVFQAGTTLKEDKTLVTNGGRVLTVTAIQKDLMSA 400
Cdd:PLN02257 320 GVSLTWSPDS-AMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|.
gi 821472192 401 LQEANKGITVIKFEGAVYRKDIGYRAISFLK 431
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
436-768 |
8.66e-148 |
|
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: 442.93 E-value: 8.66e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 436 LTYKESGVDISAGNELVKKIKPLAKATSRPGSNVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQQCNKHDTIGQ 515
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 516 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGMYPPGEYDLAGFAVGAME 595
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 596 RNQKLPQlNRITEGDVVIGIASSGVHSNGFSLIRKIVENSSFQFSSLAPDGCGnQTLGELLLKPTKIYSRTLLPVLRSGH 675
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFG-KTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 676 VKAFAHITGGGLLENIPRVLPETLGVDLDARCWKIPRIFSWLQLEGCLSEEEMAKTFNCGIGAVMVVQKDLAEQVLKDIH 755
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|...
gi 821472192 756 QQEEEAWIIGNVV 768
Cdd:TIGR00878 318 AYGEKAWVIGEVK 330
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
435-768 |
8.99e-130 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 397.64 E-value: 8.99e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 435 GLTYKESGVDISAGNELVKKIKPLAkatsrPGsnvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQQCNKHDTIG 514
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 515 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGMYPPGEYDLAGFAVGAM 594
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 595 ERNqKLPQLNRITEGDVVIGIASSGVHSNGFSLIRKIVENSSFQFSSLAPDgcGNQTLGELLLKPTKIYSRTLLPVLRSG 674
Cdd:PLN02557 204 KKD-AVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPG--ASVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 675 HVKAFAHITGGGLLENIPRVLPETLGVDLDARCWKIPRIFSWLQLEGCLSEEEMAKTFNCGIGAVMVVQKDLAEQVLKDI 754
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEEG 360
|
330
....*....|....
gi 821472192 755 HqqeEEAWIIGNVV 768
Cdd:PLN02557 361 A---YPAYRIGEVI 371
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
1.97e-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: 365.84 E-value: 1.97e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 105 SSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPALVIKASGLAAGKGVIVANNKEEACKAVQDIMQDKAFGTAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 185 DTVVIEEVLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDHGPNTGGMGAYCPTPQVPKDLLLKIKNTILQRAVDGMKQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 821472192 265 EGVPYVGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
812-993 |
3.77e-103 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 320.10 E-value: 3.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 812 VAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINHKLYKSRSEFDSEIDSVLEEFSVDL 891
Cdd:cd08645 2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 892 VCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTV 971
Cdd:cd08645 82 IVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTP 161
|
170 180
....*....|....*....|..
gi 821472192 972 ATLSERVKIAEHKAFPAALQLV 993
Cdd:cd08645 162 ETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
807-1003 |
1.70e-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: 313.89 E-value: 1.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 807 PKRVqvAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINHKLYKSRSEFDSEIDSVLEE 886
Cdd:COG0299 1 MKRI--AVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 887 FSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVK 966
Cdd:COG0299 79 YGPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 821472192 967 RDDTVATLSERVKIAEHKAFPAALQLVASGTVKLGEN 1003
Cdd:COG0299 159 PDDTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGR 195
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
812-999 |
4.30e-77 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 250.37 E-value: 4.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 812 VAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINHKLYKSRSEFDSEIDSVLEEFSVDL 891
Cdd:TIGR00639 3 IVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 892 VCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTV 971
Cdd:TIGR00639 83 VVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTE 162
|
170 180
....*....|....*....|....*...
gi 821472192 972 ATLSERVKIAEHKAFPAALQLVASGTVK 999
Cdd:TIGR00639 163 ETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
812-990 |
2.76e-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: 245.28 E-value: 2.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 812 VAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINHKLYKSRSEFDSEIDSVLEEFSVDL 891
Cdd:pfam00551 3 IAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAADV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 892 VCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTV 971
Cdd:pfam00551 83 IVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTA 162
|
170
....*....|....*....
gi 821472192 972 ATLSERVKIAEHKAFPAAL 990
Cdd:pfam00551 163 ETLYNRVADLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
811-1011 |
5.93e-40 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 146.76 E-value: 5.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 811 QVAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINhklyKSRSEFD----SEIDSVLEE 886
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYP----KTKGEPDglspDELVDALRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 887 FSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKG-----SNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQE 961
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 821472192 962 AVPVKRDDTVATLSERVKIAEHKAFPAALQLVASGTVKLGENG-KICWSKE 1011
Cdd:PLN02331 157 VVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDGvPLIRSKE 207
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
608-768 |
3.34e-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: 122.45 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 608 EGDVVIGIASSGVHSNGFSLIRKIvenssfqfssLAPDGCGNQTLGELLLKPTKIYSRTLLPVLrSGHVKAFAHITGGGL 687
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKG----------LEDSGLAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 688 LENIPRVLPET-LGVDLDARcwkIPRIFSWLQlegclSEEEMAKTFNCGIGaVMVVQKDLAEQVLKDIHQQEEEAWIIGN 766
Cdd:pfam02769 71 AGALAEMAPASgVGAEIDLD---KVPIFEELM-----LPLEMLLSENQGRG-LVVVAPEEAEAVLAILEKEGLEAAVIGE 141
|
..
gi 821472192 767 VV 768
Cdd:pfam02769 142 VT 143
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
5-427 |
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: 703.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 5 VLVIGNGGREHTLAWKLAQSEHVSQVIVAPGNAGTANNGKisNSAVSVNDHTALAQFCKDQKIELVVVGPEAPLADGIVG 84
Cdd:COG0151 3 VLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 85 NLTSAGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNK 164
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 165 EEACKAVQDIMQDKAFGTAGDTVVIEEVLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDHGPNTGGMGAYCPTPQVPK 244
Cdd:COG0151 160 EEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 245 DLLLKIKNTILQRAVDGMKQEGVPYVGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSVLDGQLSNS 324
Cdd:COG0151 240 ELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 325 LPVWREDsAAVTVVMASKGYPANYTKGIEITGIPEAKALGLEVFQAGTTLKEDKtLVTNGGRVLTVTAIQKDLMSALQEA 404
Cdd:COG0151 320 ELEWDDR-AAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGK-LVTNGGRVLGVTALGDTLEEARERA 397
|
410 420
....*....|....*....|...
gi 821472192 405 NKGITVIKFEGAVYRKDIGYRAI 427
Cdd:COG0151 398 YEAVEKIRFEGMFYRRDIGWRAL 420
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
5-427 |
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: 632.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 5 VLVIGNGGREHTLAWKLAQSEHVSQVIVAPGNAGTANNGKISNSAVSVNDHTALAQFCKDQKIELVVVGPEAPLADGIVG 84
Cdd:TIGR00877 3 VLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 85 NLTSAGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPAlVIKASGLAAGKGVIVANNK 164
Cdd:TIGR00877 83 ALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 165 EEACKAVQDIMQDKaFGTAGDTVVIEEVLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDHGPNTGGMGAYCPTPQVPK 244
Cdd:TIGR00877 162 EEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 245 DLLLKIKNTILQRAVDGMKQEGVPYVGILYAGIMLTKDGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSVLDGQLsNS 324
Cdd:TIGR00877 241 EVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKL-DE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 325 LPVWREDSAAVTVVMASKGYPANYTKGIEITGIPEAKALGLEVFQAGTTLKEDKtLVTNGGRVLTVTAIQKDLMSALQEA 404
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGK-LVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 821472192 405 NKGITVIKFEGAVYRKDIGYRAI 427
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
432-772 |
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: 580.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 432 QSRGLTYKESGVDISAGNELVKKIKPLAKATSRPGSNVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQQCNKHD 511
Cdd:COG0150 1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 512 TIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGMYPPGEYDLAGFAV 591
Cdd:COG0150 81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 592 GAMERNQKLPQlNRITEGDVVIGIASSGVHSNGFSLIRKIVENSSFQFSSLAPDgcGNQTLGELLLKPTKIYSRTLLPVL 671
Cdd:COG0150 161 GVVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPE--LGRTLGEALLEPTRIYVKPVLALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 672 RSGHVKAFAHITGGGLLENIPRVLPETLGVDLDARCWKIPRIFSWLQLEGCLSEEEMAKTFNCGIGAVMVVQKDLAEQVL 751
Cdd:COG0150 238 KAVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAAL 317
|
330 340
....*....|....*....|.
gi 821472192 752 KDIHQQEEEAWIIGNVVTCPT 772
Cdd:COG0150 318 ALLKAAGETAYVIGEVVAGEG 338
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
470-768 |
9.42e-173 |
|
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: 505.86 E-value: 9.42e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 470 DLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQQCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDVSTA 549
Cdd:cd02196 2 GIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 550 ETVIAGIAKACEKAGCALLGGETAEMPGMYPPGEYDLAGFAVGAMERNQKLPQlNRITEGDVVIGIASSGVHSNGFSLIR 629
Cdd:cd02196 82 AEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 630 KIVENSSFQFSSLAPDgcGNQTLGELLLKPTKIYSRTLLPVLRSGHVKAFAHITGGGLLENIPRVLPETLGVDLDARCWK 709
Cdd:cd02196 161 KILFEEGLDYDDPEPG--LGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 821472192 710 IPRIFSWLQLEGCLSEEEMAKTFNCGIGAVMVVQKDLAEQVLKDIHQQEEEAWIIGNVV 768
Cdd:cd02196 239 IPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-431 |
1.69e-166 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 495.03 E-value: 1.69e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 6 LVIGNGGREHTLAWKLAQSEHVSQVIVAPGNAGTANNGKISN-SAVSVNDHTALAQFCKDQKIELVVVGPEAPLADGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 85 NLTSAGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 165 EEACKAVQDIMQDKAFGTAGDTVVIEEVLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDHGPNTGGMGAYCPTPQVPK 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 245 DLLLKIKNTILQRAVDGMKQEGVPYVGILYAGIMLTKDG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSVLDGQLS 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 323 NSLPVWREDSaAVTVVMASKGYPANYTKGIEITGIPEAKAL--GLEVFQAGTTLKEDKTLVTNGGRVLTVTAIQKDLMSA 400
Cdd:PLN02257 320 GVSLTWSPDS-AMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|.
gi 821472192 401 LQEANKGITVIKFEGAVYRKDIGYRAISFLK 431
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
436-768 |
8.66e-148 |
|
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: 442.93 E-value: 8.66e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 436 LTYKESGVDISAGNELVKKIKPLAKATSRPGSNVDLGGFAGLFDLKAaGFKDPLLASGTDGVGTKLKIAQQCNKHDTIGQ 515
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 516 DLVAMCVNDILAQGAEPLFFLDYFSCGKLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGMYPPGEYDLAGFAVGAME 595
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 596 RNQKLPQlNRITEGDVVIGIASSGVHSNGFSLIRKIVENSSFQFSSLAPDGCGnQTLGELLLKPTKIYSRTLLPVLRSGH 675
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFG-KTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 676 VKAFAHITGGGLLENIPRVLPETLGVDLDARCWKIPRIFSWLQLEGCLSEEEMAKTFNCGIGAVMVVQKDLAEQVLKDIH 755
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|...
gi 821472192 756 QQEEEAWIIGNVV 768
Cdd:TIGR00878 318 AYGEKAWVIGEVK 330
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
435-768 |
8.99e-130 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 397.64 E-value: 8.99e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 435 GLTYKESGVDISAGNELVKKIKPLAkatsrPGsnvdLGGFAGLFDlkaagFKDPLLASGTDGVGTKLKIAQQCNKHDTIG 514
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 515 QDLVAMCVNDILAQGAEPLFFLDYFSCGKLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGMYPPGEYDLAGFAVGAM 594
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 595 ERNqKLPQLNRITEGDVVIGIASSGVHSNGFSLIRKIVENSSFQFSSLAPDgcGNQTLGELLLKPTKIYSRTLLPVLRSG 674
Cdd:PLN02557 204 KKD-AVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPG--ASVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 675 HVKAFAHITGGGLLENIPRVLPETLGVDLDARCWKIPRIFSWLQLEGCLSEEEMAKTFNCGIGAVMVVQKDLAEQVLKDI 754
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILEEG 360
|
330
....*....|....
gi 821472192 755 HqqeEEAWIIGNVV 768
Cdd:PLN02557 361 A---YPAYRIGEVI 371
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
1.97e-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: 365.84 E-value: 1.97e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 105 SSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPALVIKASGLAAGKGVIVANNKEEACKAVQDIMQDKAFGTAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 185 DTVVIEEVLEGEEVSCLCFTDGKTVAPMPPAQDHKRLLDGDHGPNTGGMGAYCPTPQVPKDLLLKIKNTILQRAVDGMKQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 821472192 265 EGVPYVGILYAGIMLTKDGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
812-993 |
3.77e-103 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 320.10 E-value: 3.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 812 VAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINHKLYKSRSEFDSEIDSVLEEFSVDL 891
Cdd:cd08645 2 IAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 892 VCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTV 971
Cdd:cd08645 82 IVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTP 161
|
170 180
....*....|....*....|..
gi 821472192 972 ATLSERVKIAEHKAFPAALQLV 993
Cdd:cd08645 162 ETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
807-1003 |
1.70e-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: 313.89 E-value: 1.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 807 PKRVqvAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINHKLYKSRSEFDSEIDSVLEE 886
Cdd:COG0299 1 MKRI--AVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 887 FSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVK 966
Cdd:COG0299 79 YGPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 821472192 967 RDDTVATLSERVKIAEHKAFPAALQLVASGTVKLGEN 1003
Cdd:COG0299 159 PDDTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGR 195
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
812-999 |
4.30e-77 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 250.37 E-value: 4.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 812 VAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINHKLYKSRSEFDSEIDSVLEEFSVDL 891
Cdd:TIGR00639 3 IVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 892 VCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTV 971
Cdd:TIGR00639 83 VVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTE 162
|
170 180
....*....|....*....|....*...
gi 821472192 972 ATLSERVKIAEHKAFPAALQLVASGTVK 999
Cdd:TIGR00639 163 ETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
812-990 |
2.76e-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: 245.28 E-value: 2.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 812 VAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINHKLYKSRSEFDSEIDSVLEEFSVDL 891
Cdd:pfam00551 3 IAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAADV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 892 VCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTV 971
Cdd:pfam00551 83 IVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTA 162
|
170
....*....|....*....
gi 821472192 972 ATLSERVKIAEHKAFPAAL 990
Cdd:pfam00551 163 ETLYNRVADLEHKALPRVL 181
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
5-104 |
3.63e-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: 166.38 E-value: 3.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 5 VLVIGNGGREHTLAWKLAQSEHVSQVIVAPGNAGTANNGKisNSAVSVNDHTALAQFCKDQKIELVVVGPEAPLADGIVG 84
Cdd:pfam02844 3 VLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 821472192 85 NLTS--AGVRCFGPTAKAAQLE 104
Cdd:pfam02844 81 ALREraAGIPVFGPSKAAAQLE 102
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
814-992 |
1.77e-44 |
|
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: 158.61 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 814 VLISGTGTNLQALIDSTQEPTSCaQIAVVISNKAGVAGLEKAEKAGIptkviNHKLYKSRSEFDSEIDSVLEEFSVDLVC 893
Cdd:cd08369 1 IVILGSGNIGQRVLKALLSKEGH-EIVGVVTHPDSPRGTAQLSLELV-----GGKVYLDSNINTPELLELLKEFAPDLIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 894 LAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVAT 973
Cdd:cd08369 75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154
|
170
....*....|....*....
gi 821472192 974 LSERVKIAEHKAFPAALQL 992
Cdd:cd08369 155 LYQRLIELGPKLLKEALQK 173
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
811-1011 |
5.93e-40 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 146.76 E-value: 5.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 811 QVAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAGLEKAEKAGIPTKVINhklyKSRSEFD----SEIDSVLEE 886
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYP----KTKGEPDglspDELVDALRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 887 FSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKG-----SNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQE 961
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 821472192 962 AVPVKRDDTVATLSERVKIAEHKAFPAALQLVASGTVKLGENG-KICWSKE 1011
Cdd:PLN02331 157 VVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDGvPLIRSKE 207
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-425 |
9.44e-37 |
|
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: 132.96 E-value: 9.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 334 AVTVVMASKGYPANYTKGIEITGIPEAkalGLEVFQAGTTLKEDKtLVTNGGRVLTVTAIQKDLMSALQEANKGITVIKF 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA---GVKVFHAGTKLKDGK-LVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDF 76
|
90
....*....|..
gi 821472192 414 EGAVYRKDIGYR 425
Cdd:pfam02843 77 EGMFYRKDIGTR 88
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
837-974 |
1.74e-35 |
|
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: 136.33 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 837 AQIAVVISNKAGVAGLekAEKAGIP------TKvinhklyKSRSEFDSEIDSVLEEFSVDLVCLAGFMRILSGPFVQKWN 910
Cdd:COG0788 114 AEIPAVISNHPDLRPL--AEWFGIPfhhipvTK-------ETKAEAEARLLELLEEYDIDLVVLARYMQILSPDFCARLP 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 821472192 911 GKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATL 974
Cdd:COG0788 185 GRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRDTPEDL 248
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
837-998 |
3.32e-32 |
|
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine.
Pssm-ID: 187717 [Multi-domain] Cd Length: 196 Bit Score: 124.21 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 837 AQIAVVISNKAGVAGLekAEKAGIPTKVIN-HKLYKSRSEfdSEIDSVLEEFSVDLVCLAGFMRILSGPFVQKWNGKILN 915
Cdd:cd08648 28 CEIPLVISNHPDLRPL--AERFGIPFHHIPvTKDTKAEAE--AEQLELLEEYGVDLVVLARYMQILSPDFVERYPNRIIN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 916 IHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEHKAFPAALQLVAS 995
Cdd:cd08648 104 IHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSVEDLVRKGRDIEKQVLARAVKWHLE 183
|
...
gi 821472192 996 GTV 998
Cdd:cd08648 184 DRV 186
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
608-768 |
3.34e-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: 122.45 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 608 EGDVVIGIASSGVHSNGFSLIRKIvenssfqfssLAPDGCGNQTLGELLLKPTKIYSRTLLPVLrSGHVKAFAHITGGGL 687
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKG----------LEDSGLAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 688 LENIPRVLPET-LGVDLDARcwkIPRIFSWLQlegclSEEEMAKTFNCGIGaVMVVQKDLAEQVLKDIHQQEEEAWIIGN 766
Cdd:pfam02769 71 AGALAEMAPASgVGAEIDLD---KVPIFEELM-----LPLEMLLSENQGRG-LVVVAPEEAEAVLAILEKEGLEAAVIGE 141
|
..
gi 821472192 767 VV 768
Cdd:pfam02769 142 VT 143
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
837-974 |
7.26e-30 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 120.21 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 837 AQIAVVISNKAGVAGLekAEKAGIPTKVINH-KLykSRSEFDSEIDSVLEEFSVDLVCLAGFMRILSGPFVQKWNGKILN 915
Cdd:PRK06027 117 VEIAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIIN 192
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 821472192 916 IHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATL 974
Cdd:PRK06027 193 IHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHRDTAEDL 251
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
490-765 |
8.94e-30 |
|
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: 118.27 E-value: 8.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 490 LASGTDGVGTKLKIaqqcnKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGK-LDVSTAETVIAGIAKACEKAGCALL 568
Cdd:cd00396 2 LAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 569 GGETAEMPGMYPPgEYDLAGFAVGAMERNqKLPQLNRITEGDVVIgiassgvhsngfslirkIVENSSFQFSSLAPDgcg 648
Cdd:cd00396 77 GGHTSVSPGTMGH-KLSLAVFAIGVVEKD-RVIDSSGARPGDVLI-----------------LTGVDAVLELVAAGD--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 649 nqtlgelllkptkiysrtllpvlrsghVKAFAHITGGGLLENIPRVLPET-LGVDLDARCWKIPRIFSWLqlegCLSEEE 727
Cdd:cd00396 135 ---------------------------VHAMHDITDGGLLGTLPELAQASgVGAEIDLEAIPLDEVVRWL----CVEHIE 183
|
250 260 270
....*....|....*....|....*....|....*...
gi 821472192 728 MAKTFNCGIGAVMVVQKDLAEQVLKDIHQQEEEAWIIG 765
Cdd:cd00396 184 EALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIG 221
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
490-594 |
1.61e-24 |
|
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 98.67 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 490 LASGTDGVGTKLKIaqqcNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGK--LDVSTAETVIAGIAKACEKAGCAL 567
Cdd:pfam00586 5 VAVTTDGHGTPSLV----DPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGgpEVEWVLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*..
gi 821472192 568 LGGETAEMPGMYPPgeyDLAGFAVGAM 594
Cdd:pfam00586 81 VGGDTSFDPEGGKP---TISVTAVGIV 104
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
811-991 |
2.96e-22 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 97.51 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 811 QVAVLISGTGTNLQALIDSTQEPTSCAQIAVVISNKAGVAG---LEKAEKAGIPTkvinHKLYKSRSefDSEIDSVLEEF 887
Cdd:PLN02828 72 KIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNHERGPNthvMRFLERHGIPY----HYLPTTKE--NKREDEILELV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 888 S-VDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVK 966
Cdd:PLN02828 146 KgTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVS 225
|
170 180
....*....|....*....|....*
gi 821472192 967 RDDTVATLSERVKIAEHKAFPAALQ 991
Cdd:PLN02828 226 HRDNLRSFVQKSENLEKQCLAKAIK 250
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
839-965 |
1.11e-21 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 96.21 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 839 IAVVISNKAGVAGLekAEKAGIP------TKvinhklyKSRSEFDSEIDSVLEEFSVDLVCLAGFMRILSGPFVQKWNGK 912
Cdd:PRK13011 119 IVGVVSNHPDLEPL--AAWHGIPfhhfpiTP-------DTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGR 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 821472192 913 ILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPV 965
Cdd:PRK13011 190 AINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERV 242
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
872-986 |
1.10e-19 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 90.63 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 872 SRSEFDSEIDSVLEEFSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQ 951
Cdd:PRK13010 153 TKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDD 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 821472192 952 VDSGQIIVQEAVPVK------------RDDTVATLSERVKI-AEHKAF 986
Cdd:PRK13010 233 LDEGPIIEQDVERVDhsyspedlvakgRDVECLTLARAVKAfIEHRVF 280
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
95-294 |
4.18e-19 |
|
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: 88.39 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 95 GPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNKEEACKAVQDI 174
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYP-VVVKPADGAGSRGVRVVRDEEELEAALAEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 175 MQDKAFGTAGDTVVIEEVLEGEEVSCLCF-TDGKTVapmpPAQDHKRLLDGDHGPNTGGMgaycptpqVPKDLLLKIKNT 253
Cdd:COG0439 122 RAEAKAGSPNGEVLVEEFLEGREYSVEGLvRDGEVV----VCSITRKHQKPPYFVELGHE--------APSPLPEELRAE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 821472192 254 ILQRAVDGMKQEGVPYvGILYAGIMLTKDG-PKVLEFNCRFG 294
Cdd:COG0439 190 IGELVARALRALGYRR-GAFHTEFLLTPDGePYLIEINARLG 230
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
853-1010 |
1.12e-18 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 87.85 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 853 EKAEKAGIPtkvinhkLYKSRSEFDSEIDSVLEEFSVDLVCLAGFMRILSGPFvqkWN---GKILNIHPSLLPSFKGSNA 929
Cdd:COG0223 50 ELALEHGIP-------VLQPESLKDPEFLEELRALNPDLIVVVAYGQILPKEV---LDiprLGCINLHASLLPRYRGAAP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 930 HEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEHKAFPAALQLVASGTV----------- 998
Cdd:COG0223 120 IQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDALEAGTLtptpqdesgat 199
|
170
....*....|....*.
gi 821472192 999 ---KLG-ENGKICWSK 1010
Cdd:COG0223 200 yapKISkEDGRIDWSR 215
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
811-977 |
1.27e-16 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 82.43 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 811 QVAVLIsgtgtnLQALIDSTQEPTSCAQIAVVISNKAGVAG----------LEKAEKAGIPTKVINHKLYKSRSEFDSEi 880
Cdd:PLN02285 16 EVAATV------LDALLDASQAPDSAFEVAAVVTQPPARRGrgrklmpspvAQLALDRGFPPDLIFTPEKAGEEDFLSA- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 881 dsvLEEFSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQ 960
Cdd:PLN02285 89 ---LRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQ 165
|
170
....*....|....*..
gi 821472192 961 EAVPVKRDDTVATLSER 977
Cdd:PLN02285 166 ERVEVDEDIKAPELLPL 182
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
855-1009 |
1.47e-16 |
|
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 81.68 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 855 AEKAGIPTkvinhkLYKSRSEFDSEIDSVlEEFSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVL 934
Cdd:TIGR00460 52 AEEKGIPV------FQPEKQRQLEELPLV-RELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 935 EAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEHKAFPAALQLVASGTVKL-------------- 1000
Cdd:TIGR00460 125 LNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPepqdaeeatyapki 204
|
170
....*....|
gi 821472192 1001 -GENGKICWS 1009
Cdd:TIGR00460 205 sKEQERIDWN 214
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
853-977 |
4.51e-13 |
|
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 69.01 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 853 EKAEKAGIPtkvinhkLYKSRSEFDSEIDSVLEEFSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQ 932
Cdd:cd08646 50 ELALELGLP-------VLQPEKLKDEEFLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQR 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 821472192 933 VLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSER 977
Cdd:cd08646 123 AILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
86-290 |
8.21e-12 |
|
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: 67.27 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 86 LTSAGVRCFGPtAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNKE 165
Cdd:COG0189 77 LEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGP-VVLKPLDGSGGRGVFLVEDED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 166 EAckavQDIMqDKAFGTAGDTVVIEEVL---EGEEVSCLCFtDGKTVAPMP--PAQDHKRlldgdHGPNTGGMGAYCP-T 239
Cdd:COG0189 155 AL----ESIL-EALTELGSEPVLVQEFIpeeDGRDIRVLVV-GGEPVAAIRriPAEGEFR-----TNLARGGRAEPVElT 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 821472192 240 PQVpKDLLLKIkntilqravdgmkqegVPYVGILYAGI--MLTKDGPKVLEFN 290
Cdd:COG0189 224 DEE-RELALRA----------------APALGLDFAGVdlIEDDDGPLVLEVN 259
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
838-991 |
8.48e-12 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 64.77 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 838 QIAVVISNKAGVAGLEKAEkagiPTKVINHKLYKSrsefdSEIDSVLEEFSVDLVCLAGFMRILSGPFVQKWNGKILNIH 917
Cdd:cd08820 28 EIIAVLTNTSPADVWEGSE----PLYDIGSTERNL-----HKLLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLH 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 821472192 918 PSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEHKAFPAALQ 991
Cdd:cd08820 99 NAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYILAHYAAIALFGEHIT 172
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
823-981 |
1.53e-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: 187720 [Multi-domain] Cd Length: 180 Bit Score: 64.21 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 823 LQALIDSTQEptscaqIAVVISNKAGVAG--------LEKAEKAGIPtkvinhkLYKSRSEFDSEIDSVLEEFSVDLVCL 894
Cdd:cd08651 15 LEAILEAGGE------VVGVITLDDSSSNndsdyldlDSFARKNGIP-------YYKFTDINDEEIIEWIKEANPDIIFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 895 AGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATL 974
Cdd:cd08651 82 FGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSL 161
|
....*..
gi 821472192 975 SERVKIA 981
Cdd:cd08651 162 YDKIMEA 168
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
883-978 |
1.66e-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: 187721 [Multi-domain] Cd Length: 152 Bit Score: 60.30 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 883 VLEEFSVDLVCLAGfMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAH-EQVLEAGVKITGCTVHFVAEQVDSGQIIVQE 961
Cdd:cd08653 42 ALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGfWALANGDPDNVGVTVHLVDAGIDTGDVLAQA 120
|
90
....*....|....*..
gi 821472192 962 AVPVKRDDTVATLSERV 978
Cdd:cd08653 121 RPPLAAGDTLLSLYLRL 137
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
884-994 |
1.44e-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: 58.23 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 884 LEEFSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAV 963
Cdd:cd08823 67 LRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFT 146
|
90 100 110
....*....|....*....|....*....|.
gi 821472192 964 PVKRDDTVATLSERVKIAEHKAFPAALQLVA 994
Cdd:cd08823 147 PIHPDDTYGLLCSRLAMLAVGLLEELYQNLA 177
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
853-999 |
2.77e-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: 58.13 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 853 EKAEKAGIPT---KVINHKLYKSRsefdseidsvLEEFSVDLVCLAGFMRILSGPFVQKWNGKILNIHPSLLPSFKGSNA 929
Cdd:cd08644 47 QLAREHGIPVftpDDINHPEWVER----------LRALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAP 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 930 HEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEHKAFPAALQLVASGTVK 999
Cdd:cd08644 117 LNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLARTLPALKAGKAR 186
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
89-194 |
5.92e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 59.61 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 89 AGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKW--KAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNKEE 166
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYP-VIIKASAGGGGIGMRVVYSEEE 176
|
90 100 110
....*....|....*....|....*....|
gi 821472192 167 ACKAVQDIMQ--DKAFGTAgdTVVIEEVLE 194
Cdd:PRK08654 177 LEDAIESTQSiaQSAFGDS--TVFIEKYLE 204
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
914-1010 |
3.18e-08 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 57.69 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 914 LNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEHKAFPAALQLV 993
Cdd:PRK08125 101 FNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAI 180
|
90 100 110
....*....|....*....|....*....|..
gi 821472192 994 ASGTVKL---------------GENGKICWSK 1010
Cdd:PRK08125 181 KHGNIPEipqdesqatyfgrrtPADGLIDWHK 212
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
913-978 |
3.20e-08 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 54.77 E-value: 3.20e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 821472192 913 ILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERV 978
Cdd:cd08822 91 AIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRA 156
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
855-997 |
5.85e-08 |
|
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: 53.99 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 855 AEKAGIPtkVINHKLYKSRSEFDSEIDSVLEEFSVDLVCL---AGF--MRILSGPfvqkWNGKILnIHPSLLPSFKGSNA 929
Cdd:cd08647 46 AEKDGVP--VFKFPRWRAKGQAIPEVVAKYKALGAELNVLpfcSQFipMEVIDAP----KHGSII-YHPSILPRHRGASA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821472192 930 HEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEH-KAFPAALQLVASGT 997
Cdd:cd08647 119 INWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPEGiKAMVEAVRLIAEGK 187
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
65-292 |
5.97e-08 |
|
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: 56.93 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 65 QKIELVVVGPEAPLADGIVGNLTSAGVRCFGPTAKAA-QLESSKKFAkEFMDRHGIPTAKWKAFSNPEEACSFIMSADFP 143
Cdd:TIGR01369 628 EKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIdRAEDREKFS-ELLDELGIPQPKWKTATSVEEAVEFASEIGYP 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 144 ALViKASGLAAGKGVIVANNKEEackaVQDIMQDKAFGTAGDTVVIEEVLEGE---EVSCLCftDGKTVApMPPAQDHKR 220
Cdd:TIGR01369 707 VLV-RPSYVLGGRAMEIVYNEEE----LRRYLEEAVAVSPEHPVLIDKYLEDAvevDVDAVS--DGEEVL-IPGIMEHIE 778
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821472192 221 lldgDHGPNTGGMGAYCPTPQVPKDLLLKIKNtILQRAVDGMKqegvpYVGILYAGIMLTKDGPKVLEFNCR 292
Cdd:TIGR01369 779 ----EAGVHSGDSTCVLPPQTLSAEIVDRIKD-IVRKIAKELN-----VKGLMNIQFAVKDGEVYVIEVNPR 840
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
107-214 |
6.99e-08 |
|
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: 55.11 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 107 KKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPA-LVIKASGLAAGKGVIVANNKEEACKAVQDIMQdkafgtAGD 185
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLpLFVKPAREGSSVGVSKVKNAEELAAALEEAFK------YDD 169
|
90 100
....*....|....*....|....*....
gi 821472192 186 TVVIEEVLEGEEVSCLCFTDGKTVApMPP 214
Cdd:COG1181 170 KVLVEEFIDGREVTVGVLGNGGPRA-LPP 197
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
86-290 |
2.00e-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: 53.50 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 86 LTSAGVRCFGPTAkaAQLESSKKFAK-EFMDRHGIPTAKWKAFSNPEEACSFIMSADFPALVIKASGlAAGKGVIVANNK 164
Cdd:TIGR00768 69 LESLGVPVINSSD--AILNAGDKFLShQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFG-SWGRGVSLARDR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 165 EEACKAvqdIMQDKAFGTAGDTVVIEEVL---EGEEVSCLCfTDGKTVAPMppaqdhKRLLDGDHGPNT--GGMGAYCP- 238
Cdd:TIGR00768 146 QAAESL---LEHFEQLNGPQNLFLVQEYIkkpGGRDIRVFV-VGDEVVAAI------YRITSGHWRSNLarGGKAEPCSl 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 821472192 239 TPQVpKDLLLKIKNTIlqravdgmkqeGVPYVGIlyaGIMLTKDGPKVLEFN 290
Cdd:TIGR00768 216 TEEI-EELAIKAAKAL-----------GLDVAGV---DLLESEDGLLVNEVN 252
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
115-283 |
2.24e-07 |
|
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: 51.87 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 115 DRHGIPTAKWKAFSNPEEACSFIMSADFPAlVIKASGLA-AGKGVIVANNKEEACKAVqdimqdKAFGtaGDTVVIEEVL 193
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPC-VVKARRGGyDGKGQYVVRSEADLPQAW------EELG--DGPVIVEEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 194 EGE-EVSCLC--FTDGKTVAPmPPAQDHKRllDGDHGPNtggmgaYCPTPqVPKDLLLKIKnTILQRAVDgmkqeGVPYV 270
Cdd:pfam02222 72 PFDrELSVLVvrSVDGETAFY-PVVETIQE--DGICRLS------VAPAR-VPQAIQAEAQ-DIAKRLVD-----ELGGV 135
|
170
....*....|...
gi 821472192 271 GILYAGIMLTKDG 283
Cdd:pfam02222 136 GVFGVELFVTEDG 148
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
57-294 |
8.99e-07 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 52.24 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 57 ALAQFCKDQKIELVVvgpeaPLADGIVGNLT------SAGVRCFGPTAKA-AQLESSKKFAkEFMDRHGIPTAKWKAFSN 129
Cdd:COG3919 67 ALLELAERHGPDVLI-----PTGDEYVELLSrhrdelEEHYRLPYPDADLlDRLLDKERFY-ELAEELGVPVPKTVVLDS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 130 PEEACSFIMSADFPaLVIKAS--------GLAAGKGVIVANNKEEACKAVQDImqdkafGTAGDTVVIEEVLEGEE---- 197
Cdd:COG3919 141 ADDLDALAEDLGFP-VVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRI------AAAGYELIVQEYIPGDDgemr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 198 -VSCLCFTDGKTVApmppAQDHKRLLdgdHGPNTGGMGAYCPTpqVPKDLLLKIKNTILqRAVDgmkqegvpYVGILYAG 276
Cdd:COG3919 214 gLTAYVDRDGEVVA----TFTGRKLR---HYPPAGGNSAARES--VDDPELEEAARRLL-EALG--------YHGFANVE 275
|
250 260
....*....|....*....|
gi 821472192 277 IMLT-KDG-PKVLEFNCRFG 294
Cdd:COG3919 276 FKRDpRDGeYKLIEINPRFW 295
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
914-1010 |
1.11e-06 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 51.62 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 914 LNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEHKAFPAALQLV 993
Cdd:PRK06988 103 YNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVTVAAEQTLWRVLPAL 182
|
90 100 110
....*....|....*....|....*....|..
gi 821472192 994 ASGTVK-----LG----------ENGKICWSK 1010
Cdd:PRK06988 183 LAGEAPhlpndLAqgsyfggrkpEDGRIDWSK 214
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
513-600 |
2.18e-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: 50.63 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 513 IGQDLVAMCVNDILAQGAEPLFFLdyFSCG---KLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGMYppgeydLAGF 589
Cdd:cd02194 59 IGWKALAVNLSDLAAMGARPLGFL--LSLGlppDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELV------ISVT 130
|
90
....*....|.
gi 821472192 590 AVGAMERNQKL 600
Cdd:cd02194 131 ALGEVEKGKPL 141
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
826-974 |
3.56e-06 |
|
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.
Pssm-ID: 187718 [Multi-domain] Cd Length: 166 Bit Score: 48.02 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 826 LIDSTQEPTSCAQ--------IAVVISNKAGVAglEKAEKAGIPtkVINHKlyksrsefdSEIDSVLEEFSVD-LVCLAG 896
Cdd:cd08649 4 IIGGGTLLIQCAEqllaaghrIAAVVSTDPAIR--AWAAAEGIA--VLEPG---------EALEELLSDEPFDwLFSIVN 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821472192 897 FmRILSGPFVQKWNGKILNIHPSLLPSFKGSNAHEQVLEAGVKITGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATL 974
Cdd:cd08649 71 L-RILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-193 |
4.77e-06 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 48.41 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 110 AKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPALVIKASGLAAGK----GVIVANNKEEACKAVQDI--MQDKAFGTA 183
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMlgKNLVTKQTG 86
|
90
....*....|
gi 821472192 184 GDTVVIEEVL 193
Cdd:pfam08442 87 PDGQPVNKVL 96
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
78-207 |
2.05e-05 |
|
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: 48.34 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 78 LADGIVGNLTSAGVRCFGPTAKAAQL-ESSKKFaKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPaLVIKAS---Gla 153
Cdd:COG0458 86 LAVELEEAGILEGVKILGTSPDAIDLaEDRELF-KELLDKLGIPQPKSGTATSVEEALAIAEEIGYP-VIVRPSyvlG-- 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 821472192 154 aGKGVIVANNKEEackaVQDIMQdKAFGTAGDT-VVIEEVLEG--E-EVSCLCftDGK 207
Cdd:COG0458 162 -GRGMGIVYNEEE----LEEYLE-RALKVSPDHpVLIDESLLGakEiEVDVVR--DGE 211
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
57-294 |
2.18e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 47.57 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 57 ALAQFCKDQKIELVVVG--PEAPLADGIVGNLTSAGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPE--E 132
Cdd:PRK12767 60 RLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEdfK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 133 ACSFIMSADFPaLVIKASGLAAGKGVIVANNKEE---ACKAVQDIMqdkafgtagdtvvIEEVLEGEE--VSCLCFTDGK 207
Cdd:PRK12767 140 AALAKGELQFP-LFVKPRDGSASIGVFKVNDKEElefLLEYVPNLI-------------IQEFIEGQEytVDVLCDLNGE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 208 TVAPMPpaqdHKRLldgdhgpntgGM--GAYCPTPQVPKDLLLKIKNTILQRavdgmkqegVPYVGILYAGIMLTKDGPK 285
Cdd:PRK12767 206 VISIVP----RKRI----------EVraGETSKGVTVKDPELFKLAERLAEA---------LGARGPLNIQCFVTDGEPY 262
|
....*....
gi 821472192 286 VLEFNCRFG 294
Cdd:PRK12767 263 LFEINPRFG 271
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
111-199 |
2.22e-05 |
|
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: 47.76 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 111 KEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPAlVIKasglAA-----GKGVIVANNKEEACKAVQDImqdkafgtAGD 185
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPA-VLK----TRrggydGKGQVVIKSAADLEAAWAAL--------GGG 160
|
90
....*....|....*
gi 821472192 186 TVVIEEVLEGE-EVS 199
Cdd:COG0026 161 PCILEEFVPFErELS 175
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
105-296 |
7.93e-05 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 43.91 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 105 SSKKFAKEFMDRHGIPTakwkafsnPEEACSFIMSADFPALVIKASGLAAGKGVIVANNKEEACKAVQDimqdkafgtag 184
Cdd:pfam02655 2 SDKLKTYKALKNAGVPT--------PETLQAEELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIEN----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 185 dtVVIEEVLEGEEVSCLCFTDGKTVAPMPPaqdHKRLLDgdhgpNTGGMGAYC----PTPQVPKDLLLkiknTILQRAVD 260
Cdd:pfam02655 63 --VLVQEFIEGEPLSVSLLSDGEKALPLSV---NRQYID-----NGGSGFVYAgnvtPSRTELKEEII----ELAEEVVE 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 821472192 261 GMkQEGVPYVGIlyaGIMLTKDGPKVLEFNCRFGDP 296
Cdd:pfam02655 129 CL-PGLRGYVGV---DLVLKDNEPYVIEVNPRITTS 160
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
522-613 |
1.68e-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: 44.75 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 522 VNDILAQGAEPLffldYFSCG-----KLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGmyppGEYD-----LAGfaV 591
Cdd:cd02197 67 VNDLAMMGAKPL----YLSLGfileeGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPK----GKADgifinTTG--I 136
|
90 100
....*....|....*....|..
gi 821472192 592 GAMERNQKLPqLNRITEGDVVI 613
Cdd:cd02197 137 GVIPRGVIIS-PSNIRPGDKII 157
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
62-209 |
2.06e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 45.35 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 62 CKDQKIELVVVGPEAPLADGIVGNLTSAGVRCFGPTAKAA-QLESSKKFaKEFMDRHGIPTAKWKAFSNPEEACSFIMSA 140
Cdd:PRK12815 626 AEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIdRLEDRDRF-YQLLDELGLPHVPGLTATDEEEAFAFAKRI 704
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821472192 141 DFPALvIKASGLAAGKGVIVANNKeeacKAVQDIMQDKAFGTagDTVVIEEVLEGEEVSCLCFTDGKTV 209
Cdd:PRK12815 705 GYPVL-IRPSYVIGGQGMAVVYDE----PALEAYLAENASQL--YPILIDQFIDGKEYEVDAISDGEDV 766
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
78-198 |
5.01e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 44.19 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 78 LADGIvgnLTSAGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPALVIKASGLaAGKG 157
Cdd:PRK12815 103 HEDGI---LEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTL-GGTG 178
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 821472192 158 VIVANNKEEACKAVQDIMQDKAFgtagDTVVIEEVLEG-EEV 198
Cdd:PRK12815 179 GGIAENLEELEQLFKQGLQASPI----HQCLLEESIAGwKEI 216
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
111-174 |
5.12e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.60 E-value: 5.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821472192 111 KEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPAlVIKasglAA-----GKGVIVANNKEEACKAVQDI 174
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPA-VLK----TRrggydGKGQWVIRSAEDLEAAWALL 168
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
142-209 |
5.81e-04 |
|
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: 41.50 E-value: 5.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821472192 142 FPaLVIKASGLAAGKGVIVANNKEE---ACKAVQDIMQD-----KAFGTAGDTVVIEEVLEGEEVSCLCF--TDGKTV 209
Cdd:pfam13535 3 YP-CVIKPSVGFFSVGVYKINNREEwkaAFAAIREEIEQwkemyPEAVVDGGSFLVEEYIEGEEFAVDAYfdENGEPV 79
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
521-767 |
8.39e-04 |
|
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100031 [Multi-domain] Cd Length: 287 Bit Score: 42.51 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 521 CVNDILAQGAEPLFFLDYFSC----GKLDVSTAETVIAGIAKACEKAGCALLGGETAEMPGMyppgeydLAGFAVGAMER 596
Cdd:cd02195 80 ALSDIYAMGAKPLSALAIVTLprklPALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEP-------KYGLSVTGLVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 597 NQKLPQLNRITEGDVVI-------GIASSGvHSNGfSLIRKIVENSSFQFSSLapdgcgNQTLGELllkptkiysrtllp 669
Cdd:cd02195 153 PNKILRNSGAKPGDVLIltkplgtGILFAA-EMAG-LARGEDIDAALESMARL------NRAAAEL-------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 670 vLRSGHVKAFAHITGGGL---LENIPRVLPETLGVDLDarcwKIPrifsWLQlegclseeemakTfnCGiGAVMVVQKDL 746
Cdd:cd02195 211 -LRKYGAHACTDVTGFGLlghLLEMARASGVSAEIDLD----KLP----LLQ------------T--SG-GLLAAVPPED 266
|
250 260
....*....|....*....|.
gi 821472192 747 AEQVLKDIHQQEEEAWIIGNV 767
Cdd:cd02195 267 AAALLALLKAGGPPAAIIGEV 287
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
95-194 |
1.77e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 42.01 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 95 GPTAKAAQLESSKKFAKEFMDRHGIPTAKW--KAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNKEEACKAVQ 172
Cdd:PRK05586 104 GPDSETIELMGNKSNAREIMIKAGVPVVPGseGEIENEEEALEIAKEIGYP-VMVKASAGGGGRGIRIVRSEEELIKAFN 182
|
90 100
....*....|....*....|....
gi 821472192 173 DIMQDK--AFGTagDTVVIEEVLE 194
Cdd:PRK05586 183 TAKSEAkaAFGD--DSMYIEKFIE 204
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
519-572 |
1.78e-03 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 41.74 E-value: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 821472192 519 AMCVN--DILAQGAEPLFFLdyFSCG---KLDVSTAETVIAGIAKACEKAGCALLGGET 572
Cdd:PRK05731 66 ALAVNlsDLAAMGARPAAFL--LALAlpkDLDEAWLEALADGLFELADRYGAELIGGDT 122
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
110-175 |
1.86e-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: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 110 AKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPALVIKASGLAAGK----GVIVANNKEEACKAVQDIM 175
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEIL 77
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
914-986 |
1.91e-03 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 41.04 E-value: 1.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821472192 914 LNIHPSLLPSFKGsnAHEQVLEA--GVKItGCTVHFVAEQVDSGQIIVQEAVPVKRDDTVATLSERVKIAEHKAF 986
Cdd:PRK07579 89 INIHPGFNPYNRG--WFPQVFSIinGLKI-GATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELV 160
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
95-194 |
2.28e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 41.71 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 95 GPTAKAAQLESSKKFAKEFMDRHGIPT--AKWKAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNKEEACKAVQ 172
Cdd:PRK08591 104 GPSAETIRLMGDKVTAKATMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYP-VIIKATAGGGGRGMRVVRTEAELEKAFS 182
|
90 100
....*....|....*....|....
gi 821472192 173 DIMQD--KAFGTAGdtVVIEEVLE 194
Cdd:PRK08591 183 MARAEakAAFGNPG--VYMEKYLE 204
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
89-209 |
2.97e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 41.17 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 89 AGVRCFGPTAKAAQLESSKKFAKEFMDRHGIPTAKW--KAFSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNKEE 166
Cdd:PRK06111 98 EGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGitTNLEDAEEAIAIARQIGYP-VMLKASAGGGGIGMQLVETEQE 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 821472192 167 ACKAVqDIMQDKAFGTAGD-TVVIEEVLEGE---EVSCLCFTDGKTV 209
Cdd:PRK06111 177 LTKAF-ESNKKRAANFFGNgEMYIEKYIEDPrhiEIQLLADTHGNTV 222
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
110-174 |
3.44e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 40.84 E-value: 3.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821472192 110 AKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPALVIKASGLAAGK----GVIVANNKEEACKAVQDI 174
Cdd:PRK00696 8 AKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQI 76
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
522-572 |
5.53e-03 |
|
AIR synthase (PurM) related protein, subgroup 3 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: 100028 [Multi-domain] Cd Length: 283 Bit Score: 39.89 E-value: 5.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 821472192 522 VNDILAQGAEPLFFLDYFSCGklDVSTAETVIAGIAKACEKAGCALLGGET 572
Cdd:cd02192 76 VSDIAAMGGRPLAMVDALWSP--SAEAAAQVLEGMRDAAEKFGVPIVGGHT 124
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
107-195 |
5.71e-03 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 39.21 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 107 KKFAKEFMDRHGIPTAKWKA--FSNPEEACSFIMSADFPaLVIKASGLAAGKGVIVANNKEEACKAVQDIMQDKAFGTAG 184
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYP-VIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90
....*....|.
gi 821472192 185 DTVVIEEVLEG 195
Cdd:pfam02786 81 PQVLVEKSLKG 91
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
84-166 |
6.33e-03 |
|
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: 40.75 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821472192 84 GNLTSAGVRCFGPTAKAAQL-ESSKKFaKEFMDRHGIPTAKWKAFSNPEEACSFIMSADFPALVIKASGLaAGKGVIVAN 162
Cdd:TIGR01369 105 GVLEKYGVEVLGTPVEAIKKaEDRELF-REAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTL-GGTGGGIAY 182
|
....
gi 821472192 163 NKEE 166
Cdd:TIGR01369 183 NREE 186
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
524-574 |
1.00e-02 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 39.29 E-value: 1.00e-02
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 821472192 524 DILAQGAEPLFFLDY--FSCGKLDVSTAETVIAGIAKACEKAGCALLGGETAE 574
Cdd:COG0709 89 DVYAMGGRPLTALAIvgFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSID 141
|
|
| |
