|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-415 |
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: 582.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 1 MNVLIVGSGGREHALAWKMKQSPKVKNVIVAPGNGG---HSERIDINSNDLDAVADFCEKHNIHCVLIGPEEPLSNGLAD 77
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGtaqLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 78 HLIRIHpnLMVFGPLKDGAQLETSKSFSKHFMKEYGLPTADFVTVS-----IENVKSLDcvferLPWknsVVKADGLAAG 152
Cdd:COG0151 81 AFRAAG--IPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTdleeaLAYLEEQG-----API---VVKADGLAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 153 KGVIIPRNNAEAVEAARSIL-HGQFGNAGRTVIIEERLEGYEVSALAFTDGISFKRMPLGKDHKRLLESDLGPNTGGMGV 231
Cdd:COG0151 151 KGVVVAETLEEALAAVDDMLaDGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 232 VAPVSV--PKEVDRQIDEIFEKTLKGLADRKIKYCGVLYAGFMIVDQKPLLLEFNCRFGDPETQVLMRLLESDLFEIISS 309
Cdd:COG0151 231 YSPAPVvtEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 310 CVNQTLNTCDINWSTKSVCGVVLASGNYPKSGDKGSPITEIPSPDSTNV-VFHAGTSVINSQIVTNGGRILCVTSLADTL 388
Cdd:COG0151 311 AAEGRLDEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVkVFHAGTALEDGKLVTNGGRVLGVTALGDTL 390
|
410 420
....*....|....*....|....*..
gi 392926330 389 HDAREHANKIAQNIQFTGKQFRKDIGK 415
Cdd:COG0151 391 EEARERAYEAVEKIRFEGMFYRRDIGW 417
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-415 |
2.10e-161 |
|
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: 480.27 E-value: 2.10e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 1 MNVLIVGSGGREHALAWKMKQSPKVKNVIVAPGNGGHS-----ERIDINSNDLDAVADFCEKHNIHCVLIGPEEPLSNGL 75
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTArlaknKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 76 ADHLIRIhpNLMVFGPLKDGAQLETSKSFSKHFMKEYGLPTADFVTVSieNVKSLDCVFERL--PWknsVVKADGLAAGK 153
Cdd:TIGR00877 81 VDALEEA--GIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFT--DPEEAKSYIQEKgaPI---VVKADGLAAGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 154 GVIIPRNNAEAVEAARSILHGQFGNAGRTVIIEERLEGYEVSALAFTDGISFKRMPLGKDHKRLLESDLGPNTGGMGVVA 233
Cdd:TIGR00877 154 GVIVAKTNEEAIKAVEDILEQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 234 PVSV-PKEVDRQI-DEIFEKTLKGLADRKIKYCGVLYAGFMIVDQKPLLLEFNCRFGDPETQVLMRLLESDLFEIISSCV 311
Cdd:TIGR00877 234 PAPVfTEEVERRIaEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 312 NQTLNTCDINWSTKSVCGVVLASGNYPKSGDKGSPITEIPSPDSTNV-VFHAGTSVINSQIVTNGGRILCVTSLADTLHD 390
Cdd:TIGR00877 314 EGKLDEVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVkVFHAGTKADNGKLVTNGGRVLAVTALGKTLEE 393
|
410 420
....*....|....*....|....*
gi 392926330 391 AREHANKIAQNIQFTGKQFRKDIGK 415
Cdd:TIGR00877 394 ARERAYEAVEYIKFEGMFYRKDIGF 418
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
421-768 |
6.59e-147 |
|
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: 439.86 E-value: 6.59e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 421 TPSLSYGSSGVNIDEGNQFVEDIKLLVKKTLLPGA-AQIGGFGAVLDLKKAGFsNDSQLVVGIDGVGTKIEVATHCNNFT 499
Cdd:COG0150 2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVlGGLGGFGGLFDLPAKGY-KEPVLVSGTDGVGTKLKIAQALDKHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 500 GVGYDVVAMCVNDVICHCAKPIAFLDYFVCGKLERSMATQVLTSISEACVEAECSLIGGETAEMPGVYSTHQWDLAGCA- 578
Cdd:COG0150 81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 579 -IAAREStwpMLPlSSEIRDGDVILGLPSSGLHSNGFSLARKILTVNGVKYNDPLPWDSKsTFGTELLRGTKLYVKKVLP 657
Cdd:COG0150 161 gVVEKDK---IID-GSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPELGR-TLGEALLEPTRIYVKPVLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 658 LLSTGLVKGCAHITGGGLTENAIRVLDKNSkdSLVIDCASWKFREIFNWMAAAGPVDTKEMIRTFNCGIGMVLIVSPDNV 737
Cdd:COG0150 236 LLKAVDVHGMAHITGGGLPENLPRVLPEGL--GAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDA 313
|
330 340 350
....*....|....*....|....*....|.
gi 392926330 738 EKVKKQLRKHEEEFYEIGHVEnSKNGEAIKF 768
Cdd:COG0150 314 DAALALLKAAGETAYVIGEVV-AGEGEGVVL 343
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
456-758 |
1.07e-143 |
|
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: 429.59 E-value: 1.07e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 456 AQIGGFGAVLDLKKAGFsNDSQLVVGIDGVGTKIEVATHCNNFTGVGYDVVAMCVNDVICHCAKPIAFLDYFVCGKLERS 535
Cdd:cd02196 1 GGIGGFAGLFDLGLGGY-KDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 536 MATQVLTSISEACVEAECSLIGGETAEMPGVYSTHQWDLAGCAIAARESTWPMLPlsSEIRDGDVILGLPSSGLHSNGFS 615
Cdd:cd02196 80 VAAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG--SKIKPGDVLIGLPSSGLHSNGYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 616 LARKILTVNGVKYNDPLPWDSKsTFGTELLRGTKLYVKKVLPLLSTGLVKGCAHITGGGLTENAIRVLDKNskDSLVIDC 695
Cdd:cd02196 158 LVRKILFEEGLDYDDPEPGLGK-TLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEG--LGAVIDL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926330 696 ASWKFREIFNWMAAAGPVDTKEMIRTFNCGIGMVLIVSPDNVEKVKKQLRKHEEEFYEIGHVE 758
Cdd:cd02196 235 GSWEIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
424-760 |
5.99e-112 |
|
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: 348.55 E-value: 5.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 424 LSYGSSGVNIDEGNQFVEDIKLLVKKTLLPGAAQ-IGGFGAVLDLKkaGFSNDSQLVVGIDGVGTKIEVATHCNNFTGVG 502
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGgLGGFAGLFDLG--DKYKEPVLVSGTDGVGTKLLVAEAMNKHDTIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 503 YDVVAMCVNDVICHCAKPIAFLDYFVCGKLERSMATQVLTSISEACVEAECSLIGGETAEMPGVYSTHQWDLAGCAIAAR 582
Cdd:TIGR00878 79 IDLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 583 ESTWPMLPlsSEIRDGDVILGLPSSGLHSNGFSLARKILTVNGVKYNDPLPWDSKSTFGTELLRGTKLYVKKVLPLLSTG 662
Cdd:TIGR00878 159 EKDEIITG--EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFGKTLGEELLEPTRIYVKPILELIKSV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 663 LVKGCAHITGGGLTENAIRVLDKNSKdsLVIDCASWKFREIFNWMAAAGPVDTKEMIRTFNCGIGMVLIVSPDNVEKVKK 742
Cdd:TIGR00878 237 IVHGLAHITGGGLLENIPRRLPDGLK--AVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALA 314
|
330
....*....|....*...
gi 392926330 743 QLRKHEEEFYEIGHVENS 760
Cdd:TIGR00878 315 LLNAYGEKAWVIGEVKKG 332
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-414 |
3.57e-108 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 342.10 E-value: 3.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 4 LIVGSGGREHALAWKMKQSPKVKNVIVAPGNGGHSER------IDINSNDLDAVADFCEKHNIHCVLIGPEEPLSNGLAD 77
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSgdatcvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 78 HLIRIhpNLMVFGPLKDGAQLETSKSFSKHFMKEYGLPTADFVTVS-----IENVKSldcvfERLPwknSVVKADGLAAG 152
Cdd:PLN02257 81 DLVKA--GIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTdpaaaKKYIKE-----QGAP---IVVKADGLAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 153 KGVIIPRNNAEAVEAARSIL-HGQFGNAGRTVIIEERLEGYEVSALAFTDGisFKRMPL--GKDHKRLLESDLGPNTGGM 229
Cdd:PLN02257 151 KGVVVAMTLEEAYEAVDSMLvKGAFGSAGSEVVVEEFLDGEEASFFALVDG--ENAIPLesAQDHKRVGDGDTGPNTGGM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 230 GVV--APVSVPKEVDRQIDEIFEKTLKGLADRKIKYCGVLYAGFMIV--DQKPLLLEFNCRFGDPETQVLMRLLESDLFE 305
Cdd:PLN02257 229 GAYspAPVLTPELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEkkSGLPKLLEYNVRFGDPECQVLMMRLESDLAQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 306 IISSCVNQTLNTCDINWSTKSVCGVVLASGNYPKSGDKGSPITEIPSPD--STNV-VFHAGTSV-INSQIVTNGGRILCV 381
Cdd:PLN02257 309 VLLAACKGELSGVSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEavAPGVkVFHAGTALdSDGNVVAAGGRVLGV 388
|
410 420 430
....*....|....*....|....*....|...
gi 392926330 382 TSLADTLHDAREHANKIAQNIQFTGKQFRKDIG 414
Cdd:PLN02257 389 TAKGKDIAEARARAYDAVDQIDWPGGFFRRDIG 421
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
410-769 |
9.20e-99 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 315.21 E-value: 9.20e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 410 RKDIGKTIDIGTPSLSYGSSGVNIDEGNQFVEDIKllvkkTLLPGaaqIGGFGAVLDLkkagfsNDSQLVVGIDGVGTKI 489
Cdd:PLN02557 45 SKAGRSNKDDSEEGLTYKDAGVDIDAGSELVRRIA-----KMAPG---IGGFGGLFPF------GDSYLVAGTDGVGTKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 490 EVATHCNNFTGVGYDVVAMCVNDVICHCAKPIAFLDYFVCGKLERSMATQVLTSISEACVEAECSLIGGETAEMPGVYST 569
Cdd:PLN02557 111 KLAFETGIHDTIGIDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 570 HQWDLAGCAIAARESTwpMLPLSSEIRDGDVILGLPSSGLHSNGFSLARKILTVNGVKYNDPLPwDSKSTFGTELLRGTK 649
Cdd:PLN02557 191 GEYDLSGFAVGSVKKD--AVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLP-GASVTIGEALMAPTV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 650 LYVKKVLPLLSTGLVKGCAHITGGGLTENAIRVLDKNSkdSLVIDCASWKFREIFNWMAAAGPVDTKEMIRTFNCGIGMV 729
Cdd:PLN02557 268 IYVKQVLDIISKGGVKGIAHITGGGFTDNIPRVFPKGL--GAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMV 345
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 392926330 730 LIVSPDNVEKVkkqLRKHEEEFYEIGHVensKNGEAIKFV 769
Cdd:PLN02557 346 LVVSPEAADRI---LEEGAYPAYRIGEV---INGEGVVYV 379
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
100-292 |
1.26e-97 |
|
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: 304.97 E-value: 1.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 100 TSKSFSKHFMKEYGLPTADFVTVSieNVKSLDCVFERLPWKNSVVKADGLAAGKGVIIPRNNAEAVEAARSILH-GQFGN 178
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFT--DPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEqKKFGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 179 AGRTVIIEERLEGYEVSALAFTDGISFKRMPLGKDHKRLLESDLGPNTGGMGVVAPVSV--PKEVDRQIDEIFEKTLKGL 256
Cdd:pfam01071 79 AGETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVitPELLERIKETIVEPTVDGL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 392926330 257 ADRKIKYCGVLYAGFMIVDQKPLLLEFNCRFGDPET 292
Cdd:pfam01071 159 RKEGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
788-968 |
1.03e-85 |
|
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: 273.11 E-value: 1.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 788 RVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTA--DRVTGDTELAQVLKDFGTE 865
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDfpSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 866 LVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDT 945
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 392926330 946 IETVRQKIQLQEHEMFPNAMIAV 968
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
786-971 |
2.48e-82 |
|
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: 264.59 E-value: 2.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 786 RVRVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHT--ADRVTGDTELAQVLKDFG 863
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKdfPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 864 TELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDT 943
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180
....*....|....*....|....*...
gi 392926330 944 DTIETVRQKIQLQEHEMFPNAMIAVAAK 971
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEG 188
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
788-969 |
1.30e-63 |
|
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: 213.00 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 788 RVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTA--DRVTGDTELAQVLKDFGTE 865
Cdd:TIGR00639 2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDfpSREAFDQAIIEELRAHEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 866 LVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDT 945
Cdd:TIGR00639 82 LVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDT 161
|
170 180
....*....|....*....|....
gi 392926330 946 IETVRQKIQLQEHEMFPNAMIAVA 969
Cdd:TIGR00639 162 EETLEQRIHKQEHRIYPLAIAWFA 185
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
787-964 |
3.27e-57 |
|
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: 194.82 E-value: 3.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 787 VRVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTA--DRVTGDTELAQVLKDFGT 864
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGltPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 865 ELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTD 944
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|
gi 392926330 945 TIETVRQKIQLQEHEMFPNA 964
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRV 180
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
788-968 |
1.42e-40 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 148.69 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 788 RVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTADRVTGDT--ELAQVLKDFGTE 865
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSpdELVDALRGAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 866 LVCLGGYMRILSPCFISQFPSRIINIHPSLLPAF--KGAHAL---QDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVV 940
Cdd:PLN02331 81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggKGYYGIkvhKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160
|
170 180
....*....|....*....|....*...
gi 392926330 941 EDTDTIETVRQKIQLQEHEMFPNAMIAV 968
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAAL 188
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
596-766 |
3.78e-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: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 596 RDGDVILGLPSSGLHSNGFSLARKILTVNGvkyndplpwDSKSTFGTELLRGTKLYVKKVLPLLsTGLVKGCAHITGGGL 675
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSG---------LAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 676 TENAIRVLDKnSKDSLVIDcasWKFREIFNWMAaagpvDTKEMIRTFNCGIGMVlIVSPDNVEKVKKQLRKHEEEFYEIG 755
Cdd:pfam02769 71 AGALAEMAPA-SGVGAEID---LDKVPIFEELM-----LPLEMLLSENQGRGLV-VVAPEEAEAVLAILEKEGLEAAVIG 140
|
170
....*....|.
gi 392926330 756 HVENSKNGEAI 766
Cdd:pfam02769 141 EVTAGGRLTVI 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-415 |
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: 582.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 1 MNVLIVGSGGREHALAWKMKQSPKVKNVIVAPGNGG---HSERIDINSNDLDAVADFCEKHNIHCVLIGPEEPLSNGLAD 77
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGtaqLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 78 HLIRIHpnLMVFGPLKDGAQLETSKSFSKHFMKEYGLPTADFVTVS-----IENVKSLDcvferLPWknsVVKADGLAAG 152
Cdd:COG0151 81 AFRAAG--IPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTdleeaLAYLEEQG-----API---VVKADGLAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 153 KGVIIPRNNAEAVEAARSIL-HGQFGNAGRTVIIEERLEGYEVSALAFTDGISFKRMPLGKDHKRLLESDLGPNTGGMGV 231
Cdd:COG0151 151 KGVVVAETLEEALAAVDDMLaDGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 232 VAPVSV--PKEVDRQIDEIFEKTLKGLADRKIKYCGVLYAGFMIVDQKPLLLEFNCRFGDPETQVLMRLLESDLFEIISS 309
Cdd:COG0151 231 YSPAPVvtEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 310 CVNQTLNTCDINWSTKSVCGVVLASGNYPKSGDKGSPITEIPSPDSTNV-VFHAGTSVINSQIVTNGGRILCVTSLADTL 388
Cdd:COG0151 311 AAEGRLDEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVkVFHAGTALEDGKLVTNGGRVLGVTALGDTL 390
|
410 420
....*....|....*....|....*..
gi 392926330 389 HDAREHANKIAQNIQFTGKQFRKDIGK 415
Cdd:COG0151 391 EEARERAYEAVEKIRFEGMFYRRDIGW 417
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-415 |
2.10e-161 |
|
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: 480.27 E-value: 2.10e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 1 MNVLIVGSGGREHALAWKMKQSPKVKNVIVAPGNGGHS-----ERIDINSNDLDAVADFCEKHNIHCVLIGPEEPLSNGL 75
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTArlaknKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 76 ADHLIRIhpNLMVFGPLKDGAQLETSKSFSKHFMKEYGLPTADFVTVSieNVKSLDCVFERL--PWknsVVKADGLAAGK 153
Cdd:TIGR00877 81 VDALEEA--GIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFT--DPEEAKSYIQEKgaPI---VVKADGLAAGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 154 GVIIPRNNAEAVEAARSILHGQFGNAGRTVIIEERLEGYEVSALAFTDGISFKRMPLGKDHKRLLESDLGPNTGGMGVVA 233
Cdd:TIGR00877 154 GVIVAKTNEEAIKAVEDILEQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 234 PVSV-PKEVDRQI-DEIFEKTLKGLADRKIKYCGVLYAGFMIVDQKPLLLEFNCRFGDPETQVLMRLLESDLFEIISSCV 311
Cdd:TIGR00877 234 PAPVfTEEVERRIaEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 312 NQTLNTCDINWSTKSVCGVVLASGNYPKSGDKGSPITEIPSPDSTNV-VFHAGTSVINSQIVTNGGRILCVTSLADTLHD 390
Cdd:TIGR00877 314 EGKLDEVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVkVFHAGTKADNGKLVTNGGRVLAVTALGKTLEE 393
|
410 420
....*....|....*....|....*
gi 392926330 391 AREHANKIAQNIQFTGKQFRKDIGK 415
Cdd:TIGR00877 394 ARERAYEAVEYIKFEGMFYRKDIGF 418
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
421-768 |
6.59e-147 |
|
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: 439.86 E-value: 6.59e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 421 TPSLSYGSSGVNIDEGNQFVEDIKLLVKKTLLPGA-AQIGGFGAVLDLKKAGFsNDSQLVVGIDGVGTKIEVATHCNNFT 499
Cdd:COG0150 2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVlGGLGGFGGLFDLPAKGY-KEPVLVSGTDGVGTKLKIAQALDKHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 500 GVGYDVVAMCVNDVICHCAKPIAFLDYFVCGKLERSMATQVLTSISEACVEAECSLIGGETAEMPGVYSTHQWDLAGCA- 578
Cdd:COG0150 81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 579 -IAAREStwpMLPlSSEIRDGDVILGLPSSGLHSNGFSLARKILTVNGVKYNDPLPWDSKsTFGTELLRGTKLYVKKVLP 657
Cdd:COG0150 161 gVVEKDK---IID-GSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVPELGR-TLGEALLEPTRIYVKPVLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 658 LLSTGLVKGCAHITGGGLTENAIRVLDKNSkdSLVIDCASWKFREIFNWMAAAGPVDTKEMIRTFNCGIGMVLIVSPDNV 737
Cdd:COG0150 236 LLKAVDVHGMAHITGGGLPENLPRVLPEGL--GAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDA 313
|
330 340 350
....*....|....*....|....*....|.
gi 392926330 738 EKVKKQLRKHEEEFYEIGHVEnSKNGEAIKF 768
Cdd:COG0150 314 DAALALLKAAGETAYVIGEVV-AGEGEGVVL 343
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
456-758 |
1.07e-143 |
|
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: 429.59 E-value: 1.07e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 456 AQIGGFGAVLDLKKAGFsNDSQLVVGIDGVGTKIEVATHCNNFTGVGYDVVAMCVNDVICHCAKPIAFLDYFVCGKLERS 535
Cdd:cd02196 1 GGIGGFAGLFDLGLGGY-KDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 536 MATQVLTSISEACVEAECSLIGGETAEMPGVYSTHQWDLAGCAIAARESTWPMLPlsSEIRDGDVILGLPSSGLHSNGFS 615
Cdd:cd02196 80 VAAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG--SKIKPGDVLIGLPSSGLHSNGYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 616 LARKILTVNGVKYNDPLPWDSKsTFGTELLRGTKLYVKKVLPLLSTGLVKGCAHITGGGLTENAIRVLDKNskDSLVIDC 695
Cdd:cd02196 158 LVRKILFEEGLDYDDPEPGLGK-TLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEG--LGAVIDL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926330 696 ASWKFREIFNWMAAAGPVDTKEMIRTFNCGIGMVLIVSPDNVEKVKKQLRKHEEEFYEIGHVE 758
Cdd:cd02196 235 GSWEIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
424-760 |
5.99e-112 |
|
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: 348.55 E-value: 5.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 424 LSYGSSGVNIDEGNQFVEDIKLLVKKTLLPGAAQ-IGGFGAVLDLKkaGFSNDSQLVVGIDGVGTKIEVATHCNNFTGVG 502
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGgLGGFAGLFDLG--DKYKEPVLVSGTDGVGTKLLVAEAMNKHDTIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 503 YDVVAMCVNDVICHCAKPIAFLDYFVCGKLERSMATQVLTSISEACVEAECSLIGGETAEMPGVYSTHQWDLAGCAIAAR 582
Cdd:TIGR00878 79 IDLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 583 ESTWPMLPlsSEIRDGDVILGLPSSGLHSNGFSLARKILTVNGVKYNDPLPWDSKSTFGTELLRGTKLYVKKVLPLLSTG 662
Cdd:TIGR00878 159 EKDEIITG--EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFGKTLGEELLEPTRIYVKPILELIKSV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 663 LVKGCAHITGGGLTENAIRVLDKNSKdsLVIDCASWKFREIFNWMAAAGPVDTKEMIRTFNCGIGMVLIVSPDNVEKVKK 742
Cdd:TIGR00878 237 IVHGLAHITGGGLLENIPRRLPDGLK--AVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALA 314
|
330
....*....|....*...
gi 392926330 743 QLRKHEEEFYEIGHVENS 760
Cdd:TIGR00878 315 LLNAYGEKAWVIGEVKKG 332
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-414 |
3.57e-108 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 342.10 E-value: 3.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 4 LIVGSGGREHALAWKMKQSPKVKNVIVAPGNGGHSER------IDINSNDLDAVADFCEKHNIHCVLIGPEEPLSNGLAD 77
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSgdatcvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 78 HLIRIhpNLMVFGPLKDGAQLETSKSFSKHFMKEYGLPTADFVTVS-----IENVKSldcvfERLPwknSVVKADGLAAG 152
Cdd:PLN02257 81 DLVKA--GIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTdpaaaKKYIKE-----QGAP---IVVKADGLAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 153 KGVIIPRNNAEAVEAARSIL-HGQFGNAGRTVIIEERLEGYEVSALAFTDGisFKRMPL--GKDHKRLLESDLGPNTGGM 229
Cdd:PLN02257 151 KGVVVAMTLEEAYEAVDSMLvKGAFGSAGSEVVVEEFLDGEEASFFALVDG--ENAIPLesAQDHKRVGDGDTGPNTGGM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 230 GVV--APVSVPKEVDRQIDEIFEKTLKGLADRKIKYCGVLYAGFMIV--DQKPLLLEFNCRFGDPETQVLMRLLESDLFE 305
Cdd:PLN02257 229 GAYspAPVLTPELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEkkSGLPKLLEYNVRFGDPECQVLMMRLESDLAQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 306 IISSCVNQTLNTCDINWSTKSVCGVVLASGNYPKSGDKGSPITEIPSPD--STNV-VFHAGTSV-INSQIVTNGGRILCV 381
Cdd:PLN02257 309 VLLAACKGELSGVSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEavAPGVkVFHAGTALdSDGNVVAAGGRVLGV 388
|
410 420 430
....*....|....*....|....*....|...
gi 392926330 382 TSLADTLHDAREHANKIAQNIQFTGKQFRKDIG 414
Cdd:PLN02257 389 TAKGKDIAEARARAYDAVDQIDWPGGFFRRDIG 421
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
410-769 |
9.20e-99 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 315.21 E-value: 9.20e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 410 RKDIGKTIDIGTPSLSYGSSGVNIDEGNQFVEDIKllvkkTLLPGaaqIGGFGAVLDLkkagfsNDSQLVVGIDGVGTKI 489
Cdd:PLN02557 45 SKAGRSNKDDSEEGLTYKDAGVDIDAGSELVRRIA-----KMAPG---IGGFGGLFPF------GDSYLVAGTDGVGTKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 490 EVATHCNNFTGVGYDVVAMCVNDVICHCAKPIAFLDYFVCGKLERSMATQVLTSISEACVEAECSLIGGETAEMPGVYST 569
Cdd:PLN02557 111 KLAFETGIHDTIGIDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 570 HQWDLAGCAIAARESTwpMLPLSSEIRDGDVILGLPSSGLHSNGFSLARKILTVNGVKYNDPLPwDSKSTFGTELLRGTK 649
Cdd:PLN02557 191 GEYDLSGFAVGSVKKD--AVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLP-GASVTIGEALMAPTV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 650 LYVKKVLPLLSTGLVKGCAHITGGGLTENAIRVLDKNSkdSLVIDCASWKFREIFNWMAAAGPVDTKEMIRTFNCGIGMV 729
Cdd:PLN02557 268 IYVKQVLDIISKGGVKGIAHITGGGFTDNIPRVFPKGL--GAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMV 345
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 392926330 730 LIVSPDNVEKVkkqLRKHEEEFYEIGHVensKNGEAIKFV 769
Cdd:PLN02557 346 LVVSPEAADRI---LEEGAYPAYRIGEV---INGEGVVYV 379
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
100-292 |
1.26e-97 |
|
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: 304.97 E-value: 1.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 100 TSKSFSKHFMKEYGLPTADFVTVSieNVKSLDCVFERLPWKNSVVKADGLAAGKGVIIPRNNAEAVEAARSILH-GQFGN 178
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFT--DPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEqKKFGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 179 AGRTVIIEERLEGYEVSALAFTDGISFKRMPLGKDHKRLLESDLGPNTGGMGVVAPVSV--PKEVDRQIDEIFEKTLKGL 256
Cdd:pfam01071 79 AGETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVitPELLERIKETIVEPTVDGL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 392926330 257 ADRKIKYCGVLYAGFMIVDQKPLLLEFNCRFGDPET 292
Cdd:pfam01071 159 RKEGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
788-968 |
1.03e-85 |
|
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: 273.11 E-value: 1.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 788 RVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTA--DRVTGDTELAQVLKDFGTE 865
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDfpSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 866 LVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDT 945
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 392926330 946 IETVRQKIQLQEHEMFPNAMIAV 968
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
786-971 |
2.48e-82 |
|
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: 264.59 E-value: 2.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 786 RVRVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHT--ADRVTGDTELAQVLKDFG 863
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKdfPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 864 TELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDT 943
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180
....*....|....*....|....*...
gi 392926330 944 DTIETVRQKIQLQEHEMFPNAMIAVAAK 971
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEG 188
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
788-969 |
1.30e-63 |
|
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: 213.00 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 788 RVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTA--DRVTGDTELAQVLKDFGTE 865
Cdd:TIGR00639 2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDfpSREAFDQAIIEELRAHEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 866 LVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDT 945
Cdd:TIGR00639 82 LVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDT 161
|
170 180
....*....|....*....|....
gi 392926330 946 IETVRQKIQLQEHEMFPNAMIAVA 969
Cdd:TIGR00639 162 EETLEQRIHKQEHRIYPLAIAWFA 185
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
787-964 |
3.27e-57 |
|
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: 194.82 E-value: 3.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 787 VRVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTA--DRVTGDTELAQVLKDFGT 864
Cdd:pfam00551 1 MKIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGltPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 865 ELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTD 944
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|
gi 392926330 945 TIETVRQKIQLQEHEMFPNA 964
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRV 180
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-99 |
1.79e-45 |
|
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: 158.29 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 1 MNVLIVGSGGREHALAWKMKQSPKVKNVIVAPGNGG---HSERIDINSNDLDAVADFCEKHNIHCVLIGPEEPLSNGLAD 77
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGtaqLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 392926330 78 HLIRIHPNLMVFGPLKDGAQLE 99
Cdd:pfam02844 81 ALRERAAGIPVFGPSKAAAQLE 102
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
784-952 |
1.02e-40 |
|
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: 151.36 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 784 RKRVRVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLtiAASYGIPTKVVPHTAD-RVTGDTELAQVLKDF 862
Cdd:COG0788 84 DRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTKEtKAEAEARLLELLEEY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 863 GTELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFV-DELvDHGDIIAQRPVVVE 941
Cdd:COG0788 162 DIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVtADL-DEGPIIEQDVERVD 240
|
170
....*....|.
gi 392926330 942 DTDTIETVRQK 952
Cdd:COG0788 241 HRDTPEDLVRK 251
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
788-968 |
1.42e-40 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 148.69 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 788 RVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTADRVTGDT--ELAQVLKDFGTE 865
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKTKGEPDGLSpdELVDALRGAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 866 LVCLGGYMRILSPCFISQFPSRIINIHPSLLPAF--KGAHAL---QDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVV 940
Cdd:PLN02331 81 FVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggKGYYGIkvhKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVPV 160
|
170 180
....*....|....*....|....*...
gi 392926330 941 EDTDTIETVRQKIQLQEHEMFPNAMIAV 968
Cdd:PLN02331 161 LATDTPEELAARVLHEEHQLYVEVVAAL 188
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
788-952 |
5.72e-39 |
|
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: 143.47 E-value: 5.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 788 RVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAggLTIAASYGIPTKVVPHTAD-RVTGDTELAQVLKDFGTEL 866
Cdd:cd08648 2 RVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDL--RPLAERFGIPFHHIPVTKDtKAEAEAEQLELLEEYGVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 867 VCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTI 946
Cdd:cd08648 80 VVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDSV 159
|
....*.
gi 392926330 947 ETVRQK 952
Cdd:cd08648 160 EDLVRK 165
|
|
| PurU |
TIGR00655 |
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ... |
788-952 |
3.02e-37 |
|
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273199 [Multi-domain] Cd Length: 280 Bit Score: 141.41 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 788 RVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLtiAASYGIPTKVVPHTAD-RVTGDTELAQVLKDFGTEL 866
Cdd:TIGR00655 86 RVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSL--VERFGIPFHYIPATKDnRVEHEKRQLELLKQYQVDL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 867 VCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTI 946
Cdd:TIGR00655 164 VVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHTDNV 243
|
....*.
gi 392926330 947 ETVRQK 952
Cdd:TIGR00655 244 EDLIRA 249
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
771-947 |
5.38e-36 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 137.93 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 771 EEKMFQREKYTTQRKRVrvAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLtiAASYGIPTKVVPHTAD-RV 849
Cdd:PRK06027 76 EFEMDWRLLDSAERKRV--VILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVTKEtKA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 850 TGDTELAQVLKDFGTELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDH 929
Cdd:PRK06027 152 EAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDE 231
|
170
....*....|....*...
gi 392926330 930 GDIIAQRPVVVEDTDTIE 947
Cdd:PRK06027 232 GPIIEQDVIRVDHRDTAE 249
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
791-965 |
2.12e-34 |
|
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: 129.72 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 791 ILISGTGTNMQKLIERSKTpDSNCDVVLVVSNKEGAGGLTIAASYGIPTKVVPHTADRvtgDTELAQVLKDFGTELVCLG 870
Cdd:cd08369 1 IVILGSGNIGQRVLKALLS-KEGHEIVGVVTHPDSPRGTAQLSLELVGGKVYLDSNIN---TPELLELLKEFAPDLIVSI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 871 GYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETVR 950
Cdd:cd08369 77 NFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLY 156
|
170
....*....|....*
gi 392926330 951 QKIQLQEHEMFPNAM 965
Cdd:cd08369 157 QRLIELGPKLLKEAL 171
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
328-415 |
1.49e-33 |
|
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: 124.10 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 328 CGVVLASGNYPKSGDKGSPITEIPSPDStnVVFHAGTSVINSQIVTNGGRILCVTSLADTLHDAREHANKIAQNIQFTGK 407
Cdd:pfam02843 2 VCVVLASGGYPGSYEKGDVITGLDEAGV--KVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEGM 79
|
....*...
gi 392926330 408 QFRKDIGK 415
Cdd:pfam02843 80 FYRKDIGT 87
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
596-766 |
3.78e-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: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 596 RDGDVILGLPSSGLHSNGFSLARKILTVNGvkyndplpwDSKSTFGTELLRGTKLYVKKVLPLLsTGLVKGCAHITGGGL 675
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSG---------LAAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 676 TENAIRVLDKnSKDSLVIDcasWKFREIFNWMAaagpvDTKEMIRTFNCGIGMVlIVSPDNVEKVKKQLRKHEEEFYEIG 755
Cdd:pfam02769 71 AGALAEMAPA-SGVGAEID---LDKVPIFEELM-----LPLEMLLSENQGRGLV-VVAPEEAEAVLAILEKEGLEAAVIG 140
|
170
....*....|.
gi 392926330 756 HVENSKNGEAI 766
Cdd:pfam02769 141 EVTAGGRLTVI 151
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
785-947 |
3.98e-27 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 112.38 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 785 KRVRVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGGLtiAASYGIPTKVVPHTAD-RVTGDTELAQVLKDFG 863
Cdd:PRK13011 88 ARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPL--AAWHGIPFHHFPITPDtKPQQEAQVLDVVEESG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 864 TELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDT 943
Cdd:PRK13011 166 AELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHA 245
|
....
gi 392926330 944 DTIE 947
Cdd:PRK13011 246 YSPE 249
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
786-947 |
2.34e-22 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 98.33 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 786 RVRVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAggLTIAASYGIPTKVVPHTAD-RVTGDTELAQVLKDFGT 864
Cdd:PRK13010 93 RPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDL--QPLAVQHDIPFHHLPVTPDtKAQQEAQILDLIETSGA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 865 ELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTD 944
Cdd:PRK13010 171 ELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSY 250
|
...
gi 392926330 945 TIE 947
Cdd:PRK13010 251 SPE 253
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
478-755 |
1.18e-21 |
|
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: 94.39 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 478 LVVGIDGVGTkievATHCNNFTGvGYDVVAMCVNDVICHCAKPIAFLDYFVCGK-LERSMATQVLTSISEACVEAECSLI 556
Cdd:cd00396 2 LAMSTDGINP----PLAINPWAG-GRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 557 GGETAEMPGvYSTHQWDLAGCAIAAREStwPMLPLSSEIRDGDVILglpssglhsngfslarkiltVNGVKYndplpwds 636
Cdd:cd00396 77 GGHTSVSPG-TMGHKLSLAVFAIGVVEK--DRVIDSSGARPGDVLI--------------------LTGVDA-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 637 kstfgtellrgtklyvkkVLPLLSTGLVKGCAHITGGGLTENAIRVLDKnSKDSLVIDCASWKFREIFNWMAAAGPvdtk 716
Cdd:cd00396 126 ------------------VLELVAAGDVHAMHDITDGGLLGTLPELAQA-SGVGAEIDLEAIPLDEVVRWLCVEHI---- 182
|
250 260 270
....*....|....*....|....*....|....*....
gi 392926330 717 EMIRTFNCGIGMVLIVSPDNVEKVKKQLRKHEEEFYEIG 755
Cdd:cd00396 183 EEALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIG 221
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
768-965 |
5.76e-20 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 90.96 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 768 FVNEEKMFQREKYTTQ----RKRVRVAILISGTGTNMQKLIERSKTPDSNCDVVLVVSNKEGAGG---LTIAASYGIPTK 840
Cdd:PLN02828 48 FQEISKHFKALKSVVRvpglDPKYKIAVLASKQDHCLIDLLHRWQDGRLPVDITCVISNHERGPNthvMRFLERHGIPYH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 841 VVPhTADRVTGDTELAQVLKdfGTELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTA 920
Cdd:PLN02828 128 YLP-TTKENKREDEILELVK--GTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392926330 921 HFVDELVDHGDIIAQRPVVVEDTDTIETVRQKIQLQEHEMFPNAM 965
Cdd:PLN02828 205 HFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENLEKQCLAKAI 249
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
475-566 |
6.12e-17 |
|
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: 77.10 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 475 DSQLVVGIDGVGTKIEVathcNNFTGVGYDVVAMCVNDVICHCAKPIAFLDYFVCGK--LERSMATQVLTSISEACVEAE 552
Cdd:pfam00586 2 DAAVAVTTDGHGTPSLV----DPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGgpEVEWVLEEIVEGIAEACREAG 77
|
90
....*....|....
gi 392926330 553 CSLIGGETAEMPGV 566
Cdd:pfam00586 78 VPLVGGDTSFDPEG 91
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
811-974 |
4.83e-16 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 80.15 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 811 DSNCDVVLVVSNKEGAGG----LT------IAASYGIPTkvvpHTADRVTgDTELAQVLKDFGTELVCLGGYMRILSPCF 880
Cdd:COG0223 21 AAGHEVVAVVTQPDRPAGrgrkLTpspvkeLALEHGIPV----LQPESLK-DPEFLEELRALNPDLIVVVAYGQILPKEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 881 ISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETVRQKIqlqeHEM 960
Cdd:COG0223 96 LDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKL----AEL 171
|
170
....*....|....
gi 392926330 961 FPNAMIAVAAKILE 974
Cdd:COG0223 172 GAELLLETLDALEA 185
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
811-952 |
6.90e-16 |
|
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: 77.10 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 811 DSNCDVVLVVSN---KEGAGGLTI-------AASYGIPtkvvPHTADRVTGDTELAQvLKDFGTELVCLGGYMRILSPCF 880
Cdd:cd08646 21 KSGHEVVAVVTQpdkPRGRGKKLTpspvkelALELGLP----VLQPEKLKDEEFLEE-LKALKPDLIVVVAYGQILPKEI 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926330 881 ISQFPSRIINIHPSLLPAFKGA----HALqdaLNfGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETVRQK 952
Cdd:cd08646 96 LDLPPYGCINVHPSLLPKYRGAapiqRAI---LN-GDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
800-953 |
1.63e-13 |
|
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: 69.60 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 800 MQKLIERSKTpdsncdVVLVVSNKEGAGG--------LTIAASYGIPtkvVPHTADrvTGDTELAQVLKDFGTELVCLGG 871
Cdd:cd08651 15 LEAILEAGGE------VVGVITLDDSSSNndsdyldlDSFARKNGIP---YYKFTD--INDEEIIEWIKEANPDIIFVFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 872 YMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETVRQ 951
Cdd:cd08651 84 WSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYD 163
|
..
gi 392926330 952 KI 953
Cdd:cd08651 164 KI 165
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
48-288 |
3.21e-13 |
|
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: 70.67 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 48 LDAVADFCEKHNIHCVLIGPEEPLSN--GLADHLirihpNLMVFGPlkDGAQLETSKSFSKHFMKEYGLPTADFVTVSie 125
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVETaaELAEEL-----GLPGPSP--EAIRAMRDKVLMREALAAAGVPVPGFALVD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 126 NVKSLDCVFERL--PWknsVVKADGLAAGKGVIIPRNNAEAVEAARSIL-HGQFGNAGRTVIIEERLEGYEVSAlaftDG 202
Cdd:COG0439 77 SPEEALAFAEEIgyPV---VVKPADGAGSRGVRVVRDEEELEAALAEARaEAKAGSPNGEVLVEEFLEGREYSV----EG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 203 ISFKRMPLgkdHKRLLESDLGPNTGG-MGVVAPVSVPKEVDRQIDEIFEKTLKGLadrKIKYcGVLYAGFMIV-DQKPLL 280
Cdd:COG0439 150 LVRDGEVV---VCSITRKHQKPPYFVeLGHEAPSPLPEELRAEIGELVARALRAL---GYRR-GAFHTEFLLTpDGEPYL 222
|
....*...
gi 392926330 281 LEFNCRFG 288
Cdd:COG0439 223 IEINARLG 230
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
872-975 |
6.51e-13 |
|
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: 70.89 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 872 YMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETVrq 951
Cdd:TIGR00460 87 FGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTL-- 164
|
90 100
....*....|....*....|....
gi 392926330 952 KIQLQEHEmfPNAMIAVAAKILEK 975
Cdd:TIGR00460 165 SDKLSELG--AQLLIETLKELPEG 186
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
852-949 |
1.09e-12 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 66.47 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 852 DTELAQVLKDFGTELVCLGGyMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDAL-NFGVRIVGCTAHFVDELVDHG 930
Cdd:cd08653 36 GPEVVAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALaNGDPDNVGVTVHLVDAGIDTG 114
|
90
....*....|....*....
gi 392926330 931 DIIAQRPVVVEDTDTIETV 949
Cdd:cd08653 115 DVLAQARPPLAAGDTLLSL 133
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
781-945 |
5.86e-10 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 62.02 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 781 TTQRKRV------RVAILIsgtgtnMQKLIERSKTPDSNCDVVLVVSN---KEGAGGLTI-------AASYGIPTKVV-- 842
Cdd:PLN02285 3 SGRKKRLvflgtpEVAATV------LDALLDASQAPDSAFEVAAVVTQppaRRGRGRKLMpspvaqlALDRGFPPDLIft 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 843 PHTAdrvtGDTELAQVLKDFGTELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHF 922
Cdd:PLN02285 77 PEKA----GEEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAF 152
|
170 180
....*....|....*....|...
gi 392926330 923 VDELVDHGDIIAQRPVVVEDTDT 945
Cdd:PLN02285 153 TVRALDAGPVIAQERVEVDEDIK 175
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
847-943 |
1.81e-08 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 55.14 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 847 DRVTGDTELAQVLKDFGTELVCLGGYMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDEL 926
Cdd:cd08823 55 DTANLKEQLAEWLRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAE 134
|
90
....*....|....*....
gi 392926330 927 VDHGDIIAQR--PVVVEDT 943
Cdd:cd08823 135 IDRGPIVLEQftPIHPDDT 153
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
817-969 |
2.21e-07 |
|
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.
Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 52.45 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 817 VLVVSNKEG-AGGLTIAASY-GIPTKVVPHTadRVTGDT--ELAQVLKDFGTELVCLggymrilsPcFISQF-PSRIIN- 890
Cdd:cd08647 29 VFTIPDKDGkADPLALEAEKdGVPVFKFPRW--RAKGQAipEVVAKYKALGAELNVL--------P-FCSQFiPMEVIDa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 891 -------IHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETVRQKIqlqeheMFPN 963
Cdd:cd08647 98 pkhgsiiYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRF------LYPE 171
|
....*.
gi 392926330 964 AMIAVA 969
Cdd:cd08647 172 GIKAMV 177
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
887-961 |
2.24e-07 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 52.98 E-value: 2.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926330 887 RIINIHPSLLPAFKGAHALQDALNFGVRIvGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETVRQKIQLQEHEMF 961
Cdd:PRK07579 87 RCINIHPGFNPYNRGWFPQVFSIINGLKI-GATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELV 160
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
67-267 |
1.20e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 51.69 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 67 PEEPLSNgLADHlIRIHPNLMVFGPLKDgaqletsKSFSKHFMKEYGLPTADFvtVSIENVKSLDCVFERLPWKnSVVKA 146
Cdd:PRK06019 75 PAEALDA-LAAR-VPVPPGPDALAIAQD-------RLTEKQFLDKLGIPVAPF--AVVDSAEDLEAALADLGLP-AVLKT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 147 -----DglaaGKGVIIPRNNAEAVEAARSILHGQfgnagrtVIIEERLE-GYEVSALA--FTDGiSFKRMPLGKDHKR-- 216
Cdd:PRK06019 143 rrggyD----GKGQWVIRSAEDLEAAWALLGSVP-------CILEEFVPfEREVSVIVarGRDG-EVVFYPLVENVHRng 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392926330 217 -LLESdlgpntggmgvVAPVSVPKEVDRQIDEIFEKtlkgLADrKIKYCGVL 267
Cdd:PRK06019 211 iLRTS-----------IAPARISAELQAQAEEIASR----IAE-ELDYVGVL 246
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
816-962 |
1.47e-06 |
|
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: 49.77 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 816 VVLVVSNKEGAGGLTIAASYGIPtkVVPHTADRVTGDTELAQvlkdfGTELVCLGGYMRILSPCFISQFPSRIINIHPSL 895
Cdd:cd08822 26 LLGVAAPEEGDRLAAAARTAGSR--GLPRAGVAVLPADAIPP-----GTDLIVAAHCHAFISAKTRARARLGAIGYHPSL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926330 896 LPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETvrqkiqLQEHEMFP 962
Cdd:cd08822 99 LPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAE------LWRRALAP 159
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
25-288 |
1.52e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 51.47 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 25 VKNVIVAPGNGGHSERIdinsndLDAVADFCEKHNIHcVLIGPEEPLSNGLADHLIRIHPNLMVfgPLKDGAQLET--SK 102
Cdd:COG3919 48 VDEVVVVPDPGDDPEAF------VDALLELAERHGPD-VLIPTGDEYVELLSRHRDELEEHYRL--PYPDADLLDRllDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 103 SfskHFMK---EYGLPTADfvTVSIENVKSLDCVFERLPWkNSVVK-ADGLAA-------GKGVIIPRNNAEAVEAARSI 171
Cdd:COG3919 119 E---RFYElaeELGVPVPK--TVVLDSADDLDALAEDLGF-PVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 172 LHgqfgnAGRTVIIEERLEG-----YEVSALAFTDGisfkRMPLGKDHKRLLESdlgPNTGGMGVVApVSVPkevdrqID 246
Cdd:COG3919 193 AA-----AGYELIVQEYIPGddgemRGLTAYVDRDG----EVVATFTGRKLRHY---PPAGGNSAAR-ESVD------DP 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 392926330 247 EIFEKTLKGLadRKIKYCGVLYAGFMI--VDQKPLLLEFNCRFG 288
Cdd:COG3919 254 ELEEAARRLL--EALGYHGFANVEFKRdpRDGEYKLIEINPRFW 295
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
872-953 |
2.05e-06 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 51.52 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 872 YMRILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIETVRQ 951
Cdd:PRK08125 84 YRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHH 163
|
..
gi 392926330 952 KI 953
Cdd:PRK08125 164 KL 165
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
46-267 |
2.15e-06 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 50.84 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 46 NDLDAVADFCEK-------H-NIhcvligPEEPLsNGLADHlIRIHPNLMVfgplkdgaqLETS--KSFSKHFMKEYGLP 115
Cdd:COG0026 41 DDEEALREFAERcdvvtfeFeNV------PAEAL-EALEAE-VPVRPGPEA---------LEIAqdRLLEKAFLAELGIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 116 TADFVTVsiENVKSLDCVFERLPWKnSVVKA-----DglaaGKGVIIPRNNAEAVEAARSILHGQFgnagrtvIIEERLE 190
Cdd:COG0026 104 VAPFAAV--DSLEDLEAAIAELGLP-AVLKTrrggyD----GKGQVVIKSAADLEAAWAALGGGPC-------ILEEFVP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 191 -GYEVSALA-----------------FTDGIsfkrmplgkdhkrLLESdlgpntggmgvVAPVSVPKEVDRQIDEIFEKT 252
Cdd:COG0026 170 fERELSVIVarspdgevatypvvenvHRNGI-------------LDES-----------IAPARISEALAAEAEEIAKRI 225
|
250
....*....|....*
gi 392926330 253 LKGLadrkiKYCGVL 267
Cdd:COG0026 226 AEAL-----DYVGVL 235
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
811-948 |
2.19e-06 |
|
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: 48.98 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 811 DSNCDVVLVVSNKEGAGGLTIAAS-YGIPTKVVPhtadrvtgDTELAQVLKDFGTELVCLGGYMRILSPCFISQFPSRII 889
Cdd:cd08820 24 RGSFEIIAVLTNTSPADVWEGSEPlYDIGSTERN--------LHKLLEILENKGVDILISVQYHWILPGSILEKAKEIAF 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 392926330 890 NIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDTIET 948
Cdd:cd08820 96 NLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVIS 154
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
871-953 |
1.09e-05 |
|
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: 47.34 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 871 GYMRILSPCFISQFPSRII--------------NIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQR 936
Cdd:cd08644 69 ERLRALKPDLIFSFYYRHMisedileiarlgafNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQE 148
|
90
....*....|....*..
gi 392926330 937 PVVVEDTDTIETVRQKI 953
Cdd:cd08644 149 KVPILPDDTAKSLFHKL 165
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
874-945 |
5.08e-05 |
|
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: 44.56 E-value: 5.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926330 874 RILSPCFISQFPSRIINIHPSLLPAFKGAHALQDALNFGVRIVGCTAHFVDELVDHGDIIAQRPVVVEDTDT 945
Cdd:cd08649 72 RILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDT 143
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-288 |
1.48e-04 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 44.87 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 1 MNVLIVGSGGReHALAWKMKQSPKVKNVIVA---PGNGGHSE--------RIDiNSNDLDAVADFCEKHNIHCVLIGPEE 69
Cdd:PRK12767 2 MNILVTSAGRR-VQLVKALKKSLLKGRVIGAdisELAPALYFadkfyvvpKVT-DPNYIDRLLDICKKEKIDLLIPLIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 70 PLSnGLADHLIRIHpNLMVFGPLKDGAQLETS--KSFSKHFMKEYGLPTADFVTV-SIENVKSLDCVFE-RLPWknsVVK 145
Cdd:PRK12767 80 ELP-LLAQNRDRFE-EIGVKVLVSSKEVIEICndKWLTYEFLKENGIPTPKSYLPeSLEDFKAALAKGElQFPL---FVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 146 ADGLAAGKGVIIPRNNAEAVEAARSILhgqfgnagrTVIIEERLEGYEVSALAFTDgisfkrmplgKDHKrllesdlgpn 225
Cdd:PRK12767 155 PRDGSASIGVFKVNDKEELEFLLEYVP---------NLIIQEFIEGQEYTVDVLCD----------LNGE---------- 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926330 226 tggmgVVAPVSVPK------EVDRQI---DEIFEKTLKGLAdRKIKYCGVLYAGFMIVDQKPLLLEFNCRFG 288
Cdd:PRK12767 206 -----VISIVPRKRievragETSKGVtvkDPELFKLAERLA-EALGARGPLNIQCFVTDGEPYLFEINPRFG 271
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
105-190 |
1.50e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 41.09 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 105 SKHFMKEYGLPTAD-FVTVSIENVKSldcVFERLPWKNSVVKADGLAAGK----GVIIPRNNAEAVEAARSIL-----HG 174
Cdd:pfam08442 7 AKEIFAKYGIPVPRgEVATSPEEAEE---IAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMLgknlvTK 83
|
90
....*....|....*....
gi 392926330 175 QFGNAGRTV---IIEERLE 190
Cdd:pfam08442 84 QTGPDGQPVnkvLVEEALD 102
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
106-187 |
8.46e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 39.69 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926330 106 KHFMKEYGLPTAD-FVTVSIENVKSldcVFERLPWKNSVVKADGLAAGK----GVIIPRNNAEAVEAARSILH-----GQ 175
Cdd:PRK00696 9 KELFAKYGVPVPRgIVATTPEEAVE---AAEELGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQILGmtlvtHQ 85
|
90
....*....|....*
gi 392926330 176 FGNAGRTV---IIEE 187
Cdd:PRK00696 86 TGPKGQPVnkvLVEE 100
|
|
| |
