|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
4-427 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 712.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKisNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 84 DDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQD 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 164 KDEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVS 243
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 244 DELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDS 323
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 324 ASVQWlQDCAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTALkEGGGVITSGGRVLTVTAVRPTLESALQS 403
Cdd:COG0151 319 VELEW-DDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTAL-EDGKLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....
gi 18858729 404 ANEGVGAISFPDAVYRRDIGHRAI 427
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRAL 420
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
4-427 |
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: 618.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKISNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 84 DDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKASGLAAGKGVIVAQD 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 164 KDEACQAVLDIMKDKaFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 244 DELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDS 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 324 ASVQWLQDcAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTAlKEGGGVITSGGRVLTVTAVRPTLESALQS 403
Cdd:TIGR00877 320 VELRFDNR-AAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTK-ADNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....
gi 18858729 404 ANEGVGAISFPDAVYRRDIGHRAI 427
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
433-778 |
0e+00 |
|
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439920 [Multi-domain] Cd Length: 343 Bit Score: 578.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 433 TRGLTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHST 512
Cdd:COG0150 2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 513 LGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVG 592
Cdd:COG0150 82 IGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 593 AVERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPfgRPGQTIGDVLLTPTKIYSRVLQPVLR 672
Cdd:COG0150 162 VVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP--ELGRTLGEALLEPTRIYVKPVLALLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 673 SGAVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLR 752
Cdd:COG0150 239 AVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALA 318
|
330 340
....*....|....*....|....*..
gi 18858729 753 LLQAH-EESWIIGSLThrhPGAESVVV 778
Cdd:COG0150 319 LLKAAgETAYVIGEVV---AGEGEGVV 342
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-430 |
1.04e-179 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 529.31 E-value: 1.04e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 6 LVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKISN-SEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMVD 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 85 DLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 165 DEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSD 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 245 ELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQG--PRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELD 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 323 SASVQWLQDcAAVTVVMASGGYPNAYRKGLEISGLSQASEM--GVQVFHAGTALKEGGGVITSGGRVLTVTAVRPTLESA 400
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|
gi 18858729 401 LQSANEGVGAISFPDAVYRRDIGHRAITYL 430
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARL 428
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
1.16e-172 |
|
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: 505.47 E-value: 1.16e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 469 ADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNV 548
Cdd:cd02196 1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 549 AASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLV 628
Cdd:cd02196 81 AAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 629 RTILERSGLNISSPAPFGrpGQTIGDVLLTPTKIYSRVLQPVLRSGAVKAFAHITGGGLLENIPRVLPADLTADLDACRW 708
Cdd:cd02196 160 RKILFEEGLDYDDPEPGL--GKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSW 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 709 RIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLRLLQAH-EESWIIGSLT 767
Cdd:cd02196 238 EIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLgEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
436-769 |
7.36e-150 |
|
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: 448.32 E-value: 7.36e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 436 LTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAaGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQ 515
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 516 DLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVE 595
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 596 RSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLnISSPAPFGRPGQTIGDVLLTPTKIYSRVLQPVLRSGA 675
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAG-LDYEDTPEEFGKTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 676 VKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLRLLQ 755
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....*
gi 18858729 756 A-HEESWIIGSLTHR 769
Cdd:TIGR00878 318 AyGEKAWVIGEVKKG 332
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
435-764 |
1.24e-124 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 384.54 E-value: 1.24e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 435 GLTYKDSGVDIAAGNRLVDIIKPLAkatsrPGcnadLGGFAGLFDlkaagFTDPILVSGTDGVGTKLKIAQECGVHSTLG 514
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 515 QDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAV 594
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 595 ERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPFGrpGQTIGDVLLTPTKIYSRVLQPVLRSG 674
Cdd:PLN02557 204 KKDAVIDG-KNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGA--SVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 675 AVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLRll 754
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILE-- 358
|
330
....*....|
gi 18858729 755 QAHEESWIIG 764
Cdd:PLN02557 359 EGAYPAYRIG 368
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
6.17e-119 |
|
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: 362.37 E-value: 6.17e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 105 ASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPALVVKASGLAAGKGVIVAQDKDEACQAVLDIMKDKAFGSAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 185 ETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSDELLQEISRSVLQKTVDGMRE 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 18858729 265 EGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
814-996 |
1.83e-97 |
|
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: 305.08 E-value: 1.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 894 LVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDS 973
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 18858729 974 EESLSERIREAEHRAFPAALELV 996
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
812-1005 |
9.64e-97 |
|
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: 303.88 E-value: 9.64e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 812 RTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFS 891
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 892 VELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVT 971
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190
....*....|....*....|....*....|....
gi 18858729 972 DSEESLSERIREAEHRAFPAALELVSSGAVKLRD 1005
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDG 194
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
814-1002 |
8.59e-75 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 244.20 E-value: 8.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:TIGR00639 2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 894 LVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDS 973
Cdd:TIGR00639 82 LVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDT 161
|
170 180
....*....|....*....|....*....
gi 18858729 974 EESLSERIREAEHRAFPAALELVSSGAVK 1002
Cdd:TIGR00639 162 EETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
814-993 |
4.74e-72 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 236.42 E-value: 4.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:pfam00551 2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 894 LVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDS 973
Cdd:pfam00551 82 VIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDT 161
|
170 180
....*....|....*....|
gi 18858729 974 EESLSERIREAEHRAFPAAL 993
Cdd:pfam00551 162 AETLYNRVADLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
814-1007 |
5.56e-35 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 132.51 E-value: 5.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKlygsRAEFDG-TIDKVLE---E 889
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKT----KGEPDGlSPDELVDalrG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 890 FSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKG-----VNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQE 964
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18858729 965 AVPVLVTDSEESLSERIREAEHRAFPAALELVSSGAVKLRDDG 1007
Cdd:PLN02331 157 VVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
608-770 |
1.67e-28 |
|
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: 112.05 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 608 EGDLLLGVSSSGIHSNGFSLVRTILERSGLnisspapfgrPGQTIGDVLLTPTKIYSRVLQPVLrSGAVKAFAHITGGGL 687
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGL----------AAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 688 LENIPRVLPA-DLTADLDAcrwRIPPVFSWLQQqggvcEQEFCRTFNCGLGAVLVVsKADAQRVLRLLQAH-EESWIIGS 765
Cdd:pfam02769 71 AGALAEMAPAsGVGAEIDL---DKVPIFEELML-----PLEMLLSENQGRGLVVVA-PEEAEAVLAILEKEgLEAAVIGE 141
|
....*
gi 18858729 766 LTHRH 770
Cdd:pfam02769 142 VTAGG 146
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
4-427 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 712.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKisNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 84 DDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQD 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 164 KDEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVS 243
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 244 DELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDS 323
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 324 ASVQWlQDCAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTALkEGGGVITSGGRVLTVTAVRPTLESALQS 403
Cdd:COG0151 319 VELEW-DDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTAL-EDGKLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....
gi 18858729 404 ANEGVGAISFPDAVYRRDIGHRAI 427
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRAL 420
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
4-427 |
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: 618.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKISNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 84 DDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKASGLAAGKGVIVAQD 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 164 KDEACQAVLDIMKDKaFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 244 DELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDS 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 324 ASVQWLQDcAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTAlKEGGGVITSGGRVLTVTAVRPTLESALQS 403
Cdd:TIGR00877 320 VELRFDNR-AAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTK-ADNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....
gi 18858729 404 ANEGVGAISFPDAVYRRDIGHRAI 427
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
433-778 |
0e+00 |
|
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439920 [Multi-domain] Cd Length: 343 Bit Score: 578.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 433 TRGLTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHST 512
Cdd:COG0150 2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 513 LGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVG 592
Cdd:COG0150 82 IGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 593 AVERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPfgRPGQTIGDVLLTPTKIYSRVLQPVLR 672
Cdd:COG0150 162 VVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP--ELGRTLGEALLEPTRIYVKPVLALLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 673 SGAVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLR 752
Cdd:COG0150 239 AVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALA 318
|
330 340
....*....|....*....|....*..
gi 18858729 753 LLQAH-EESWIIGSLThrhPGAESVVV 778
Cdd:COG0150 319 LLKAAgETAYVIGEVV---AGEGEGVV 342
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-430 |
1.04e-179 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 529.31 E-value: 1.04e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 6 LVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKISN-SEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMVD 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCvPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 85 DLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 165 DEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSD 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 245 ELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQG--PRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELD 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 323 SASVQWLQDcAAVTVVMASGGYPNAYRKGLEISGLSQASEM--GVQVFHAGTALKEGGGVITSGGRVLTVTAVRPTLESA 400
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|
gi 18858729 401 LQSANEGVGAISFPDAVYRRDIGHRAITYL 430
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARL 428
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
1.16e-172 |
|
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: 505.47 E-value: 1.16e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 469 ADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNV 548
Cdd:cd02196 1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 549 AASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLV 628
Cdd:cd02196 81 AAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 629 RTILERSGLNISSPAPFGrpGQTIGDVLLTPTKIYSRVLQPVLRSGAVKAFAHITGGGLLENIPRVLPADLTADLDACRW 708
Cdd:cd02196 160 RKILFEEGLDYDDPEPGL--GKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSW 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 709 RIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLRLLQAH-EESWIIGSLT 767
Cdd:cd02196 238 EIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLgEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
436-769 |
7.36e-150 |
|
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: 448.32 E-value: 7.36e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 436 LTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAaGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQ 515
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 516 DLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVE 595
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 596 RSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLnISSPAPFGRPGQTIGDVLLTPTKIYSRVLQPVLRSGA 675
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAG-LDYEDTPEEFGKTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 676 VKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLRLLQ 755
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....*
gi 18858729 756 A-HEESWIIGSLTHR 769
Cdd:TIGR00878 318 AyGEKAWVIGEVKKG 332
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
435-764 |
1.24e-124 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 384.54 E-value: 1.24e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 435 GLTYKDSGVDIAAGNRLVDIIKPLAkatsrPGcnadLGGFAGLFDlkaagFTDPILVSGTDGVGTKLKIAQECGVHSTLG 514
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 515 QDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVNVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAV 594
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 595 ERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPFGrpGQTIGDVLLTPTKIYSRVLQPVLRSG 674
Cdd:PLN02557 204 KKDAVIDG-KNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGA--SVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 675 AVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKADAQRVLRll 754
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILE-- 358
|
330
....*....|
gi 18858729 755 QAHEESWIIG 764
Cdd:PLN02557 359 EGAYPAYRIG 368
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
6.17e-119 |
|
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: 362.37 E-value: 6.17e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 105 ASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPALVVKASGLAAGKGVIVAQDKDEACQAVLDIMKDKAFGSAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 185 ETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSDELLQEISRSVLQKTVDGMRE 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 18858729 265 EGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
814-996 |
1.83e-97 |
|
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: 305.08 E-value: 1.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 894 LVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDS 973
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDT 160
|
170 180
....*....|....*....|...
gi 18858729 974 EESLSERIREAEHRAFPAALELV 996
Cdd:cd08645 161 PETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
812-1005 |
9.64e-97 |
|
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: 303.88 E-value: 9.64e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 812 RTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFS 891
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 892 VELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVT 971
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPD 160
|
170 180 190
....*....|....*....|....*....|....
gi 18858729 972 DSEESLSERIREAEHRAFPAALELVSSGAVKLRD 1005
Cdd:COG0299 161 DTEETLAARILEQEHRLYPEAIRLLAEGRLTLDG 194
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
814-1002 |
8.59e-75 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 244.20 E-value: 8.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:TIGR00639 2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 894 LVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDS 973
Cdd:TIGR00639 82 LVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDT 161
|
170 180
....*....|....*....|....*....
gi 18858729 974 EESLSERIREAEHRAFPAALELVSSGAVK 1002
Cdd:TIGR00639 162 EETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
814-993 |
4.74e-72 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 236.42 E-value: 4.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:pfam00551 2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 894 LVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDS 973
Cdd:pfam00551 82 VIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDT 161
|
170 180
....*....|....*....|
gi 18858729 974 EESLSERIREAEHRAFPAAL 993
Cdd:pfam00551 162 AETLYNRVADLEHKALPRVL 181
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
4-104 |
2.65e-48 |
|
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam00289). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460723 [Multi-domain] Cd Length: 102 Bit Score: 166.76 E-value: 2.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKISNseVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:pfam02844 2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVD--IDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 18858729 84 DDLT--AAGVLCFGPSARAAQLE 104
Cdd:pfam02844 80 DALRerAAGIPVFGPSKAAAQLE 102
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
817-995 |
4.80e-40 |
|
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: 145.89 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 817 VLISGSGTNLQALMDQARKpSSSAEIVLVISNRPgvmglKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVELVC 896
Cdd:cd08369 1 IVILGSGNIGQRVLKALLS-KEGHEIVGVVTHPD-----SPRGTAQLSLELVGGKVYLDSNINTPELLELLKEFAPDLIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 897 LAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEES 976
Cdd:cd08369 75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154
|
170
....*....|....*....
gi 18858729 977 LSERIREAEHRAFPAALEL 995
Cdd:cd08369 155 LYQRLIELGPKLLKEALQK 173
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-425 |
6.50e-38 |
|
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: 136.42 E-value: 6.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 334 AVTVVMASGGYPNAYRKGLEISGLSQAsemGVQVFHAGTALKeGGGVITSGGRVLTVTAVRPTLESALQSANEGVGAISF 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA---GVKVFHAGTKLK-DGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDF 76
|
90
....*....|..
gi 18858729 414 PDAVYRRDIGHR 425
Cdd:pfam02843 77 EGMFYRKDIGTR 88
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
814-1007 |
5.56e-35 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 132.51 E-value: 5.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKlygsRAEFDG-TIDKVLE---E 889
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKT----KGEPDGlSPDELVDalrG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 890 FSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKG-----VNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQE 964
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyygIKVHKAVIASGARYSGPTVHFVDEHYDTGRILAQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18858729 965 AVPVLVTDSEESLSERIREAEHRAFPAALELVSSGAVKLRDDG 1007
Cdd:PLN02331 157 VVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIVWREDG 199
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
809-985 |
1.87e-32 |
|
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: 127.86 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 809 SRRRTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLkrAALAGIQTRVVDHKLyGSRAEFDGTIDKVLE 888
Cdd:COG0788 83 SDRRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTK-ETKAEAEARLLELLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 889 EFSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPV 968
Cdd:COG0788 160 EYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERV 239
|
170
....*....|....*..
gi 18858729 969 LVTDSEESLSERIREAE 985
Cdd:COG0788 240 DHRDTPEDLVRKGRDVE 256
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
814-996 |
2.02e-29 |
|
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: 116.12 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLkrAALAGIQTRVV----DHKLYGSRAEFDgtidkVLEE 889
Cdd:cd08648 2 RVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDLRPL--AERFGIPFHHIpvtkDTKAEAEAEQLE-----LLEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 890 FSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVL 969
Cdd:cd08648 75 YGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVS 154
|
170 180
....*....|....*....|....*..
gi 18858729 970 VTDSEESLSERIREAEHRAFPAALELV 996
Cdd:cd08648 155 HRDSVEDLVRKGRDIEKQVLARAVKWH 181
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
608-770 |
1.67e-28 |
|
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: 112.05 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 608 EGDLLLGVSSSGIHSNGFSLVRTILERSGLnisspapfgrPGQTIGDVLLTPTKIYSRVLQPVLrSGAVKAFAHITGGGL 687
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGL----------AAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 688 LENIPRVLPA-DLTADLDAcrwRIPPVFSWLQQqggvcEQEFCRTFNCGLGAVLVVsKADAQRVLRLLQAH-EESWIIGS 765
Cdd:pfam02769 71 AGALAEMAPAsGVGAEIDL---DKVPIFEELML-----PLEMLLSENQGRGLVVVA-PEEAEAVLAILEKEgLEAAVIGE 141
|
....*
gi 18858729 766 LTHRH 770
Cdd:pfam02769 142 VTAGG 146
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
809-977 |
4.26e-26 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 109.43 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 809 SRRRTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLkrAALAGIQTRVVDH-KLygSRAEFDGTIDKVL 887
Cdd:PRK06027 86 SAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEARLLELI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 888 EEFSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVP 967
Cdd:PRK06027 162 DEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIR 241
|
170
....*....|
gi 18858729 968 VLVTDSEESL 977
Cdd:PRK06027 242 VDHRDTAEDL 251
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
490-765 |
4.67e-26 |
|
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: 107.48 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 490 LVSGTDGVGTKLKIAqecgvHSTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGR-LDVNVAASVIGGIADACQMAGCALL 568
Cdd:cd00396 2 LAMSTDGINPPLAIN-----PWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 569 GGETAEMPGVYPPgEYDLAGFCVGAVERSAllprlkdisegdlllGVSSSGIhsngfslvrtilersglnisspapfgRP 648
Cdd:cd00396 77 GGHTSVSPGTMGH-KLSLAVFAIGVVEKDR---------------VIDSSGA--------------------------RP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 649 GQTIgdvLLTPTkiysRVLQPVLRSGAVKAFAHITGGGLLENIPRVLPA-DLTADLDACRWRIPPVFSWLQQQGGvceqE 727
Cdd:cd00396 115 GDVL---ILTGV----DAVLELVAAGDVHAMHDITDGGLLGTLPELAQAsGVGAEIDLEAIPLDEVVRWLCVEHI----E 183
|
250 260 270
....*....|....*....|....*....|....*....
gi 18858729 728 FCRTFNCGLGAVLVVSKADAQRVLRLLQAH-EESWIIGS 765
Cdd:cd00396 184 EALLFNSSGGLLIAVPAEEADAVLLLLNGNgIDAAVIGR 222
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
487-594 |
1.92e-22 |
|
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: 92.89 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 487 DPILVSGTDGVGTKLKIAqecGVHsTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVN--VAASVIGGIADACQMAG 564
Cdd:pfam00586 2 DAAVAVTTDGHGTPSLVD---PYH-FPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVewVLEEIVEGIAEACREAG 77
|
90 100 110
....*....|....*....|....*....|
gi 18858729 565 CALLGGETAEMPGVYPPgeyDLAGFCVGAV 594
Cdd:pfam00586 78 VPLVGGDTSFDPEGGKP---TISVTAVGIV 104
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
811-993 |
6.20e-22 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 96.98 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 811 RRTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLkrAALAGIQTRVV----DHKlygsrAEFDGTIDKV 886
Cdd:PRK13011 88 ARPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNHPDLEPL--AAWHGIPFHHFpitpDTK-----PQQEAQVLDV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 887 LEEFSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAV 966
Cdd:PRK13011 161 VEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVE 240
|
170 180
....*....|....*....|....*..
gi 18858729 967 PVLVTDSEESLSERIREAEHRAFPAAL 993
Cdd:PRK13011 241 RVDHAYSPEDLVAKGRDVECLTLARAV 267
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
812-995 |
1.13e-20 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 93.71 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 812 RTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLkrAALAGIQTrvvdHKL---YGSRAEFDGTIDKVLE 888
Cdd:PRK13010 93 RPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPL--AVQHDIPF----HHLpvtPDTKAQQEAQILDLIE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 889 EFSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPV 968
Cdd:PRK13010 167 TSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERV 246
|
170 180
....*....|....*....|....*..
gi 18858729 969 LVTDSEESLSERIREAEHRAFPAALEL 995
Cdd:PRK13010 247 DHSYSPEDLVAKGRDVECLTLARAVKA 273
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
884-994 |
2.44e-17 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 83.26 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 884 DKVLEEFS-VELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVV 962
Cdd:PLN02828 139 DEILELVKgTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIE 218
|
90 100 110
....*....|....*....|....*....|..
gi 18858729 963 QEAVPVLVTDSEESLSERIREAEHRAFPAALE 994
Cdd:PLN02828 219 QMVERVSHRDNLRSFVQKSENLEKQCLAKAIK 250
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
95-294 |
6.28e-17 |
|
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: 81.84 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 95 GPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDKDEACQAVLDI 174
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYP-VVVKPADGAGSRGVRVVRDEEELEAALAEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 175 MKDKAFGSAGETVVVEELLDGQEVSCLCFS-DGVTVapmpPAQDHKRLLDGDMGPNTGGMgayCPTPqVSDELLQEIsRS 253
Cdd:COG0439 122 RAEAKAGSPNGEVLVEEFLEGREYSVEGLVrDGEVV----VCSITRKHQKPPYFVELGHE---APSP-LPEELRAEI-GE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18858729 254 VLQKTVD--GMREegapyvGVLYAGLMLTAQG-PRVLEFNCRFG 294
Cdd:COG0439 193 LVARALRalGYRR------GAFHTEFLLTPDGePYLIEINARLG 230
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
807-968 |
6.14e-16 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 80.12 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 807 QNSRRRTRVAVLISG--SGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKR-------AALAGIQTRVVDHKLYGSRA 877
Cdd:PLN02285 1 AGSGRKKRLVFLGTPevAATVLDALLDASQAPDSAFEVAAVVTQPPARRGRGRklmpspvAQLALDRGFPPDLIFTPEKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 878 EFDGTIDKvLEEFSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDA 957
Cdd:PLN02285 81 GEEDFLSA-LRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDA 159
|
170
....*....|.
gi 18858729 958 GAIVVQEAVPV 968
Cdd:PLN02285 160 GPVIAQERVEV 170
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
917-1012 |
3.15e-12 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 68.59 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 917 LNIHPSLLPSFKG---VNaqkQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSERIREAEHRAFPAAL 993
Cdd:COG0223 104 INLHASLLPRYRGaapIQ---WAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETL 180
|
90 100 110
....*....|....*....|....*....|....
gi 18858729 994 ELVSSGAVKL---------------RDDGHIVWS 1012
Cdd:COG0223 181 DALEAGTLTPtpqdesgatyapkisKEDGRIDWS 214
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
887-1004 |
3.97e-12 |
|
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: 68.58 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 887 LEEFSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAV 966
Cdd:TIGR00460 74 VRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETF 153
|
90 100 110
....*....|....*....|....*....|....*...
gi 18858729 967 PVLVTDSEESLSERIREAEHRAFPAALELVSSGAVKLR 1004
Cdd:TIGR00460 154 PIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPE 191
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
885-994 |
7.35e-11 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 61.46 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 885 KVLEEFSVELVCLAGfMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAG-VRVTGCSVHFVAEDVDAGAIVVQ 963
Cdd:cd08653 41 AALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGdPDNVGVTVHLVDAGIDTGDVLAQ 119
|
90 100 110
....*....|....*....|....*....|.
gi 18858729 964 EAVPVLVTDSEESLSERIREAEHRAFPAALE 994
Cdd:cd08653 120 ARPPLAAGDTLLSLYLRLYRAGVELMVEAIA 150
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
916-980 |
6.14e-10 |
|
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: 60.15 E-value: 6.14e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18858729 916 MLNIHPSLLPSFKG---VNAqkqALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSER 980
Cdd:cd08646 103 CINVHPSLLPKYRGaapIQR---AILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
86-290 |
7.01e-10 |
|
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: 61.11 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 86 LTAAGVLCFgPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDKD 165
Cdd:COG0189 77 LEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGP-VVLKPLDGSGGRGVFLVEDED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 166 EAcQAVLDIMkdkaFGSAGETVVVEELL---DGQEVSCLCFsDGVTVAPM---PPAQDHKRlldgdmgpNT--GGMGAYC 237
Cdd:COG0189 155 AL-ESILEAL----TELGSEPVLVQEFIpeeDGRDIRVLVV-GGEPVAAIrriPAEGEFRT--------NLarGGRAEPV 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18858729 238 PtpqVSDELLqEISRSVlqktvdgmreegAPYVGVLYAG--LMLTAQGPRVLEFN 290
Cdd:COG0189 221 E---LTDEER-ELALRA------------APALGLDFAGvdLIEDDDGPLVLEVN 259
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
62-294 |
5.65e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 58.74 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 62 CKDHKVGLVVVG--PEVPLAAGMVDDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARwsSFTDPQQACAYIRD 139
Cdd:PRK12767 65 CKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPK--SYLPESLEDFKAAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 140 A----DFPaLVVKASGLAAGKGVIVAQDKDE---ACQAVLDIMkdkafgsagetvvVEELLDGQE--VSCLCFSDGVTVA 210
Cdd:PRK12767 143 AkgelQFP-LFVKPRDGSASIGVFKVNDKEElefLLEYVPNLI-------------IQEFIEGQEytVDVLCDLNGEVIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 211 PMPpaqdHKRLldgdmgpntgGM--GAYCPTPQVSDELLQEISRSVLQKTvdgmreegaPYVGVLYAGLMLTAQGPRVLE 288
Cdd:PRK12767 209 IVP----RKRI----------EVraGETSKGVTVKDPELFKLAERLAEAL---------GARGPLNIQCFVTDGEPYLFE 265
|
....*.
gi 18858729 289 FNCRFG 294
Cdd:PRK12767 266 INPRFG 271
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
917-1005 |
1.59e-08 |
|
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: 55.81 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 917 LNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSERIREAEHRAFPAALELV 996
Cdd:cd08644 101 FNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLARTLPAL 180
|
....*....
gi 18858729 997 SSGAVKLRD 1005
Cdd:cd08644 181 KAGKARERP 189
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
920-1010 |
1.86e-08 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 55.54 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 920 HPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSERIreaehrAFPAALELVSSG 999
Cdd:cd08822 95 HPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTAAELWRRA------LAPMGVKLLTQV 168
|
90
....*....|.
gi 18858729 1000 AVKLRDDGHIV 1010
Cdd:cd08822 169 IDALLRGGNLP 179
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
887-997 |
8.86e-08 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 53.22 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 887 LEEFSVELVCLAGFMRILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAV 966
Cdd:cd08823 67 LRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFT 146
|
90 100 110
....*....|....*....|....*....|.
gi 18858729 967 PVLVTDSEESLSERIREAEHRAFPAALELVS 997
Cdd:cd08823 147 PIHPDDTYGLLCSRLAMLAVGLLEELYQNLA 177
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
86-290 |
1.29e-06 |
|
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: 51.19 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 86 LTAAGVLCFGPSAraAQLEAS-KSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDK 164
Cdd:TIGR00768 69 LESLGVPVINSSD--AILNAGdKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFP-VVLKPVFGSWGRGVSLARDR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 165 DEAcQAVLDIMkdKAFGSAGETVVVEELLD---GQEVSCLCFSDGVtVAPMppaqdhKRLLDGDMGPNT--GGMGAYCP- 238
Cdd:TIGR00768 146 QAA-ESLLEHF--EQLNGPQNLFLVQEYIKkpgGRDIRVFVVGDEV-VAAI------YRITSGHWRSNLarGGKAEPCSl 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18858729 239 TPQVsDELLQEISRSVlqktvdgmreeGAPYVGVlyaGLMLTAQGPRVLEFN 290
Cdd:TIGR00768 216 TEEI-EELAIKAAKAL-----------GLDVAGV---DLLESEDGLLVNEVN 252
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
65-292 |
1.37e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 51.95 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 65 HKVGLVVV--GPE--VPLAagmvDDLTAAGVLCFG-----PSARAAQLEASKSFSKAfmdrhNIPTARWSSFTDPQQACA 135
Cdd:PRK07206 67 RKLGPEAIiaGAEsgVELA----DRLAEILTPQYSndpalSSARRNKAEMINALAEA-----GLPAARQINTADWEEAEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 136 YIRDADFPA--LVVKASGLAAGKGVIVAQDKDEACQAVLDIM-KDKAFGSAGETVVVEELLDGQEVSCLCFS-DG-VTVA 210
Cdd:PRK07206 138 WLRENGLIDrpVVIKPLESAGSDGVFICPAKGDWKHAFNAILgKANKLGLVNETVLVQEYLIGTEYVVNFVSlDGnHLVT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 211 PMppAQDHKRlldgdmgPNTGGMGAYcptpqVSDELL-------QEISRSVlQKTVD--GMREegapyvGVLYAGLMLTA 281
Cdd:PRK07206 218 EI--VRYHKT-------SLNSGSTVY-----DYDEFLdysepeyQELVDYT-KQALDalGIKN------GPAHAEVMLTA 276
|
250
....*....|.
gi 18858729 282 QGPRVLEFNCR 292
Cdd:PRK07206 277 DGPRLIEIGAR 287
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
917-993 |
1.41e-06 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 51.23 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 917 LNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSERIREAEH----RAFPAA 992
Cdd:PRK06988 103 YNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVTVAAEqtlwRVLPAL 182
|
.
gi 18858729 993 L 993
Cdd:PRK06988 183 L 183
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
902-996 |
3.22e-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: 48.41 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 902 RILTGPFVRKWSGKMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSERI 981
Cdd:cd08649 72 RILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSLNLKC 151
|
90
....*....|....*
gi 18858729 982 REAEHRAFPAALELV 996
Cdd:cd08649 152 YEAGIEGFGELIDEL 166
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
917-1012 |
3.93e-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: 50.75 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 917 LNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSERIREAEHRAFPAALELV 996
Cdd:PRK08125 101 FNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPAI 180
|
90 100 110
....*....|....*....|....*....|.
gi 18858729 997 SSGAVKLRD---------------DGHIVWS 1012
Cdd:PRK08125 181 KHGNIPEIPqdesqatyfgrrtpaDGLIDWH 211
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
837-977 |
6.01e-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: 47.82 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 837 SSSAEIVLVISNRPGVMGLK-RAALAGIQ-TRVVDHKLygsraefdgtiDKVLEEFSVELVCLAGFMRILTGPFVRKWSG 914
Cdd:cd08820 24 RGSFEIIAVLTNTSPADVWEgSEPLYDIGsTERNLHKL-----------LEILENKGVDILISVQYHWILPGSILEKAKE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18858729 915 KMLNIHPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESL 977
Cdd:cd08820 93 IAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISL 155
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
920-984 |
1.10e-05 |
|
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: 46.88 E-value: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18858729 920 HPSLLPSFKGVNAQKQALQAGVRVTGCSVHFVAEDVDAGAIVVQEAVPVLVTDSEESLSERIREA 984
Cdd:cd08651 104 HPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKIMEA 168
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
508-612 |
1.76e-05 |
|
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).
Pssm-ID: 100030 [Multi-domain] Cd Length: 291 Bit Score: 47.93 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 508 GVH-------STLGQDLVAMCVNDVLAQGAEPLFFLdyFSCG---RLDVNVAASVIGGIADACQMAGCALLGGETAEMPG 577
Cdd:cd02194 47 GVHfppdttpEDIGWKALAVNLSDLAAMGARPLGFL--LSLGlppDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSE 124
|
90 100 110
....*....|....*....|....*....|....*
gi 18858729 578 VYppgeydLAGFCVGAVERSALLPRlKDISEGDLL 612
Cdd:cd02194 125 LV------ISVTALGEVEKGKPLRR-SGAKPGDLL 152
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
105-296 |
1.98e-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: 45.84 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 105 ASKSFSKAFMDRHNIPTarwssftdPQQACAYIRDADFPALVVKASGLAAGKGVIVAQDKDEACqavldimkdkafgSAG 184
Cdd:pfam02655 2 SDKLKTYKALKNAGVPT--------PETLQAEELLREEKKYVVKPRDGCGGEGVRKVENGREDE-------------AFI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 185 ETVVVEELLDGQEVSCLCFSDGVTVAPMPPaqdHKRLLDgdmgpNTGGMGAYC----PTPQVSDELLQEISRSVLQKtVD 260
Cdd:pfam02655 61 ENVLVQEFIEGEPLSVSLLSDGEKALPLSV---NRQYID-----NGGSGFVYAgnvtPSRTELKEEIIELAEEVVEC-LP 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 18858729 261 GMREegapYVGVlyaGLMLTAQGPRVLEFNCRFGDP 296
Cdd:pfam02655 132 GLRG----YVGV---DLVLKDNEPYVIEVNPRITTS 160
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
115-286 |
3.17e-05 |
|
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: 45.32 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 115 DRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKASGLA-AGKGVIVAQDKDEACQAVldimkdKAFGsaGETVVVEELL 193
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPC-VVKARRGGyDGKGQYVVRSEADLPQAW------EELG--DGPVIVEEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 194 D-GQEVSCLC--FSDGVTVAPmPPAQDHKRllDGDMgpntggmgAYCPTPQVSDELLQEISRSVLQKTVDGMreegaPYV 270
Cdd:pfam02222 72 PfDRELSVLVvrSVDGETAFY-PVVETIQE--DGIC--------RLSVAPARVPQAIQAEAQDIAKRLVDEL-----GGV 135
|
170 180
....*....|....*....|....
gi 18858729 271 GVLYAGLMLTAQG--------PRV 286
Cdd:pfam02222 136 GVFGVELFVTEDGdllinelaPRP 159
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
111-199 |
4.39e-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: 46.99 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 111 KAFMDRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKasglAA-----GKGVIVAQDKDEAcqavldimkDKAFGSAGE 185
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPA-VLK----TRrggydGKGQVVIKSAADL---------EAAWAALGG 159
|
90
....*....|....*.
gi 18858729 186 T-VVVEELLD-GQEVS 199
Cdd:COG0026 160 GpCILEEFVPfERELS 175
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
68-292 |
6.48e-05 |
|
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: 46.92 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 68 GLVV-VGPEVPLaaGMVDDLTAAGVLCFGPSARAA-QLEASKSFSKaFMDRHNIPTARWSSFTDPQQACAYIRDADFPAL 145
Cdd:TIGR01369 632 GVIVqFGGQTPL--NLAKALEEAGVPILGTSPESIdRAEDREKFSE-LLDELGIPQPKWKTATSVEEAVEFASEIGYPVL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 146 vVKASGLAAGKGVIVAQDKDEacqaVLDIMKDKAFGSAGETVVVEELL-DGQEVSCLCFSDGVTVApMPPAQDHKRlldg 224
Cdd:TIGR01369 709 -VRPSYVLGGRAMEIVYNEEE----LRRYLEEAVAVSPEHPVLIDKYLeDAVEVDVDAVSDGEEVL-IPGIMEHIE---- 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18858729 225 DMGPNTGGMGAYCPTPQVSDELLQEISRSVlQKTVDGMReegapYVGVLYAGLMLTAQGPRVLEFNCR 292
Cdd:TIGR01369 779 EAGVHSGDSTCVLPPQTLSAEIVDRIKDIV-RKIAKELN-----VKGLMNIQFAVKDGEVYVIEVNPR 840
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
89-193 |
2.34e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 44.97 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 89 AGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWS--SFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDKDE 166
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTeeGIEDIEEAKEIAEEIGYP-VIIKASAGGGGIGMRVVYSEEE 176
|
90 100
....*....|....*....|....*....
gi 18858729 167 ACQAVLDIMK--DKAFGSAgeTVVVEELL 193
Cdd:PRK08654 177 LEDAIESTQSiaQSAFGDS--TVFIEKYL 203
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
96-199 |
4.56e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.60 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 96 PSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKasglAA-----GKGVIVAQDKDEAcqa 170
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPA-VLK----TRrggydGKGQWVIRSAEDL--- 161
|
90 100 110
....*....|....*....|....*....|.
gi 18858729 171 vldimkDKAFGSAGET-VVVEELLD-GQEVS 199
Cdd:PRK06019 162 ------EAAWALLGSVpCILEEFVPfEREVS 186
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-194 |
6.36e-04 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 42.25 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 110 SKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPALVVKASGLAAGK----GVIVAQDKDEACQAVLDI----MKDKAFG 181
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMlgknLVTKQTG 86
|
90
....*....|....*.
gi 18858729 182 SAGETV---VVEELLD 194
Cdd:pfam08442 87 PDGQPVnkvLVEEALD 102
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
80-209 |
2.21e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 41.55 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858729 80 AGMVDDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFT--DPQQACAYIRDADFPaLVVKASGLAAGKG 157
Cdd:PRK06111 89 ASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNleDAEEAIAIARQIGYP-VMLKASAGGGGIG 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18858729 158 VIVAQDKDEACQAvLDIMKDKA---FGSAgeTVVVEELLDGQ---EVSCLCFSDGVTV 209
Cdd:PRK06111 168 MQLVETEQELTKA-FESNKKRAanfFGNG--EMYIEKYIEDPrhiEIQLLADTHGNTV 222
|
|
| |
