|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-423 |
2.88e-169 |
|
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: 481.44 E-value: 2.88e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 1 MKVLVVGTGAREHAICDALKDD--VD-LYAymSKNNPGISKISTFKKGDEGEVDEVAKFAKENEIELAVIGPEAPLGKGI 77
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSprVDkLYV--APGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 78 VNALEAVGVPCVGPAQESARIETDKSFMRNLFEKYQIKgSLTYKVFDNYEDISAFLDTYEKDVVVKPVGLTGGKGVKIVG 157
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIP-TAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 158 DHlkdnQDAKAYAKEVM-DNAMGG-FAQVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDHPHAFENDQGLITGGMGSYSD 235
Cdd:COG0151 158 TL----EEALAAVDDMLaDGKFGDaGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 236 VggllPFLTQEDYDEAVD-IMKETLKAIAKETTPYKGILYGQFMLSKDGPKLIEYNARFGDPEAMNVLPLLKTPMVDVCK 314
Cdd:COG0151 234 A----PVVTEELLEKIMEeIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 315 AIVDGKLEDV--EFEDKASVCKYIVPDGYPDTPHAGELIEIDEEAiEALGAKVFYAAVSQEDDGVHLSGSRALGIVAQGD 392
Cdd:COG0151 310 AAAEGRLDEVelEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEA-EAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGD 388
|
410 420 430
....*....|....*....|....*....|..
gi 889008271 393 TIAEAEKIAEEACGLVEG-NVYHRRDVGTEAL 423
Cdd:COG0151 389 TLEEARERAYEAVEKIRFeGMFYRRDIGWRAL 420
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-424 |
4.06e-164 |
|
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: 468.33 E-value: 4.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 1 MKVLVVGTGAREHAICDAL-KDDVDLYAYMSKNNPGISKISTFKKG--DEGEVDEVAKFAKENEIELAVIGPEAPLGKGI 77
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLaQSPLVKYVYVAPGNAGTARLAKNKNVaiEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 78 VNALEAVGVPCVGPAQESARIETDKSFMRNLFEKYQIKgSLTYKVFDNYEDISAFLDTYEKDVVVKPVGLTGGKGVKIVg 157
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIP-TAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 158 dhlKDNQDAKAYAKEVMD-NAMGGFAQVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDHPHAFENDQGLITGGMGSYSDV 236
Cdd:TIGR00877 159 ---KTNEEAIKAVEDILEqKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 237 GgllPFLTQEDYDEAVDIMKETLKAIAKETTPYKGILYGQFMLSKDGPKLIEYNARFGDPEAMNVLPLLKTPMVDVCKAI 316
Cdd:TIGR00877 236 P---VFTEEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 317 VDGKLEDVE--FEDKASVCKYIVPDGYPDTPHAGELIEiDEEAIEALGAKVFYAAVSQEDDGVHLSGSRALGIVAQGDTI 394
Cdd:TIGR00877 313 VEGKLDEVElrFDNRAAVTVVLASEGYPEDYRKGDPIT-GEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTL 391
|
410 420 430
....*....|....*....|....*....|.
gi 889008271 395 AEAEKIAEEACGLVEG-NVYHRRDVGTEALI 424
Cdd:TIGR00877 392 EEARERAYEAVEYIKFeGMFYRKDIGFRALE 422
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
100-298 |
2.72e-77 |
|
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: 238.72 E-value: 2.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 100 TDKSFMRNLFEKYQIKGSlTYKVFDNYEDISAFLDTY-EKDVVVKPVGLTGGKGVKIVgdhlKDNQDAKAYAKEVMDNAM 178
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTA-EYETFTDPEEAKSYIQEAgFPAIVVKADGLAAGKGVIVA----SSNEEAIKAVDEILEQKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 179 GGFA--QVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDHPHAFENDQGLITGGMGSYSdvggLLPFLTQEDYDEAVD-IM 255
Cdd:pfam01071 76 FGEAgeTVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYS----PAPVITPELLERIKEtIV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 889008271 256 KETLKAIAKETTPYKGILYGQFMLSKDGPKLIEYNARFGDPEA 298
Cdd:pfam01071 152 EPTVDGLRKEGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-427 |
7.59e-76 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 243.11 E-value: 7.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 4 LVVGTGAREHAICDALK-----DDVdlyaYMSKNNPGISK---ISTFKKGDEGEVDEVAKFAKENEIELAVIGPEAPLGK 75
Cdd:PLN02257 1 LVIGGGGREHALCYALQrspscDAV----FCAPGNAGIATsgdATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 76 GIVNALEAVGVPCVGPAQESARIETDKSFMRNLFEKYQIKgSLTYKVFDNYEDISAFLDTYEKDVVVKPVGLTGGKGVkI 155
Cdd:PLN02257 77 GLADDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIP-TAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGV-V 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 156 VGDHLkdnQDAKAYAKEVMDNAMGGFA--QVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDHPHAFENDQGLITGGMGSY 233
Cdd:PLN02257 155 VAMTL---EEAYEAVDSMLVKGAFGSAgsEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 234 SDVggllPFLTQEDYDEAVD-IMKETLKAIAKETTPYKGILYGQFMLSKDG--PKLIEYNARFGDPEAMNVLPLLKTPMV 310
Cdd:PLN02257 232 SPA----PVLTPELESKVMEtIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 311 DVCKAIVDGKLEDVEFE--DKASVCKYIVPDGYPDTPHAGELIE-IDEEAIEALGAKVFYAAVSQEDDG-VHLSGSRALG 386
Cdd:PLN02257 308 QVLLAACKGELSGVSLTwsPDSAMVVVMASNGYPGSYKKGTVIKnLDEAEAVAPGVKVFHAGTALDSDGnVVAAGGRVLG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 889008271 387 IVAQGDTIAEAEKIAEEACGLVE-GNVYHRRDVGTEALIQKR 427
Cdd:PLN02257 388 VTAKGKDIAEARARAYDAVDQIDwPGGFFRRDIGWRAVARLQ 429
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-423 |
2.88e-169 |
|
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: 481.44 E-value: 2.88e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 1 MKVLVVGTGAREHAICDALKDD--VD-LYAymSKNNPGISKISTFKKGDEGEVDEVAKFAKENEIELAVIGPEAPLGKGI 77
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSprVDkLYV--APGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 78 VNALEAVGVPCVGPAQESARIETDKSFMRNLFEKYQIKgSLTYKVFDNYEDISAFLDTYEKDVVVKPVGLTGGKGVKIVG 157
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIP-TAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 158 DHlkdnQDAKAYAKEVM-DNAMGG-FAQVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDHPHAFENDQGLITGGMGSYSD 235
Cdd:COG0151 158 TL----EEALAAVDDMLaDGKFGDaGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 236 VggllPFLTQEDYDEAVD-IMKETLKAIAKETTPYKGILYGQFMLSKDGPKLIEYNARFGDPEAMNVLPLLKTPMVDVCK 314
Cdd:COG0151 234 A----PVVTEELLEKIMEeIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 315 AIVDGKLEDV--EFEDKASVCKYIVPDGYPDTPHAGELIEIDEEAiEALGAKVFYAAVSQEDDGVHLSGSRALGIVAQGD 392
Cdd:COG0151 310 AAAEGRLDEVelEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEA-EAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGD 388
|
410 420 430
....*....|....*....|....*....|..
gi 889008271 393 TIAEAEKIAEEACGLVEG-NVYHRRDVGTEAL 423
Cdd:COG0151 389 TLEEARERAYEAVEKIRFeGMFYRRDIGWRAL 420
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-424 |
4.06e-164 |
|
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: 468.33 E-value: 4.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 1 MKVLVVGTGAREHAICDAL-KDDVDLYAYMSKNNPGISKISTFKKG--DEGEVDEVAKFAKENEIELAVIGPEAPLGKGI 77
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLaQSPLVKYVYVAPGNAGTARLAKNKNVaiEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 78 VNALEAVGVPCVGPAQESARIETDKSFMRNLFEKYQIKgSLTYKVFDNYEDISAFLDTYEKDVVVKPVGLTGGKGVKIVg 157
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIP-TAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 158 dhlKDNQDAKAYAKEVMD-NAMGGFAQVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDHPHAFENDQGLITGGMGSYSDV 236
Cdd:TIGR00877 159 ---KTNEEAIKAVEDILEqKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 237 GgllPFLTQEDYDEAVDIMKETLKAIAKETTPYKGILYGQFMLSKDGPKLIEYNARFGDPEAMNVLPLLKTPMVDVCKAI 316
Cdd:TIGR00877 236 P---VFTEEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 317 VDGKLEDVE--FEDKASVCKYIVPDGYPDTPHAGELIEiDEEAIEALGAKVFYAAVSQEDDGVHLSGSRALGIVAQGDTI 394
Cdd:TIGR00877 313 VEGKLDEVElrFDNRAAVTVVLASEGYPEDYRKGDPIT-GEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTL 391
|
410 420 430
....*....|....*....|....*....|.
gi 889008271 395 AEAEKIAEEACGLVEG-NVYHRRDVGTEALI 424
Cdd:TIGR00877 392 EEARERAYEAVEYIKFeGMFYRKDIGFRALE 422
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
100-298 |
2.72e-77 |
|
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: 238.72 E-value: 2.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 100 TDKSFMRNLFEKYQIKGSlTYKVFDNYEDISAFLDTY-EKDVVVKPVGLTGGKGVKIVgdhlKDNQDAKAYAKEVMDNAM 178
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTA-EYETFTDPEEAKSYIQEAgFPAIVVKADGLAAGKGVIVA----SSNEEAIKAVDEILEQKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 179 GGFA--QVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDHPHAFENDQGLITGGMGSYSdvggLLPFLTQEDYDEAVD-IM 255
Cdd:pfam01071 76 FGEAgeTVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYS----PAPVITPELLERIKEtIV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 889008271 256 KETLKAIAKETTPYKGILYGQFMLSKDGPKLIEYNARFGDPEA 298
Cdd:pfam01071 152 EPTVDGLRKEGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-427 |
7.59e-76 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 243.11 E-value: 7.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 4 LVVGTGAREHAICDALK-----DDVdlyaYMSKNNPGISK---ISTFKKGDEGEVDEVAKFAKENEIELAVIGPEAPLGK 75
Cdd:PLN02257 1 LVIGGGGREHALCYALQrspscDAV----FCAPGNAGIATsgdATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 76 GIVNALEAVGVPCVGPAQESARIETDKSFMRNLFEKYQIKgSLTYKVFDNYEDISAFLDTYEKDVVVKPVGLTGGKGVkI 155
Cdd:PLN02257 77 GLADDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIP-TAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGV-V 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 156 VGDHLkdnQDAKAYAKEVMDNAMGGFA--QVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDHPHAFENDQGLITGGMGSY 233
Cdd:PLN02257 155 VAMTL---EEAYEAVDSMLVKGAFGSAgsEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 234 SDVggllPFLTQEDYDEAVD-IMKETLKAIAKETTPYKGILYGQFMLSKDG--PKLIEYNARFGDPEAMNVLPLLKTPMV 310
Cdd:PLN02257 232 SPA----PVLTPELESKVMEtIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 311 DVCKAIVDGKLEDVEFE--DKASVCKYIVPDGYPDTPHAGELIE-IDEEAIEALGAKVFYAAVSQEDDG-VHLSGSRALG 386
Cdd:PLN02257 308 QVLLAACKGELSGVSLTwsPDSAMVVVMASNGYPGSYKKGTVIKnLDEAEAVAPGVKVFHAGTALDSDGnVVAAGGRVLG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 889008271 387 IVAQGDTIAEAEKIAEEACGLVE-GNVYHRRDVGTEALIQKR 427
Cdd:PLN02257 388 VTAKGKDIAEARARAYDAVDQIDwPGGFFRRDIGWRAVARLQ 429
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-99 |
6.13e-33 |
|
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: 119.77 E-value: 6.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 1 MKVLVVGTGAREHAICDALKDD--VD-LYAYMskNNPGISKISTFKKGDEGEVDEVAKFAKENEIELAVIGPEAPLGKGI 77
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSplVEkLYVAP--GNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 889008271 78 VNAL--EAVGVPCVGPAQESARIE 99
Cdd:pfam02844 79 VDALreRAAGIPVFGPSKAAAQLE 102
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
82-294 |
4.87e-19 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 86.46 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 82 EAVGVPCVGPaqESARIETDKSFMRNLFEKYQIKgSLTYKVFDNYEDISAFLDTYEKDVVVKPVGLTGGKGVKIVgdhlK 161
Cdd:COG0439 37 EELGLPGPSP--EAIRAMRDKVLMREALAAAGVP-VPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVV----R 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 162 DNQDAKAYAKEVMDNAMGGF--AQVIIEEKVVGEEFTIQAFCDGENLaampaaqdHPHAFendQGLITGGMgSYSDVGGL 239
Cdd:COG0439 110 DEEELEAALAEARAEAKAGSpnGEVLVEEFLEGREYSVEGLVRDGEV--------VVCSI---TRKHQKPP-YFVELGHE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 889008271 240 LP-FLTQEDYDEAVDIMKETLKAIakettpykGILYG----QFMLSKDG-PKLIEYNARFG 294
Cdd:COG0439 178 APsPLPEELRAEIGELVARALRAL--------GYRRGafhtEFLLTPDGePYLIEINARLG 230
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-420 |
7.69e-14 |
|
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: 66.70 E-value: 7.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 331 SVCKYIVPDGYPDTPHAGELIEideeAIEALGAKVFYAAVSQEDDGVHLSGSRALGIVAQGDTIAEAEKIAEEACGLVE- 409
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVIT----GLDEAGVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDf 76
|
90
....*....|.
gi 889008271 410 GNVYHRRDVGT 420
Cdd:pfam02843 77 EGMFYRKDIGT 87
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-294 |
2.89e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 67.22 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 1 MKVLVVGTGAReHAICDALKDDVDLY----AYMSKNNPGISKISTF----KKGDEGEVDEVAKFAKENEIELAVIGPEAP 72
Cdd:PRK12767 2 MNILVTSAGRR-VQLVKALKKSLLKGrvigADISELAPALYFADKFyvvpKVTDPNYIDRLLDICKKEKIDLLIPLIDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 73 LGKGIVN--ALEAVGVPCVGPAQESARIETDKSFMRNLFEKYQIKGSLTYKVfDNYEDISAFLDTYEKD--VVVKPVGLT 148
Cdd:PRK12767 81 LPLLAQNrdRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLP-ESLEDFKAALAKGELQfpLFVKPRDGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 149 GGKGVKIVGDHlKDNQDAKAYAKEVmdnamggfaqvIIEEKVVGEEFTIQAFCD--GENLAAMPAAQDHPHAFENDQGlI 226
Cdd:PRK12767 160 ASIGVFKVNDK-EELEFLLEYVPNL-----------IIQEFIEGQEYTVDVLCDlnGEVISIVPRKRIEVRAGETSKG-V 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889008271 227 TGGmgsysdvggllpfltQEDYDEAVDIMKETLKAIakettpykGILYGQFMLSKDGPKLIEYNARFG 294
Cdd:PRK12767 227 TVK---------------DPELFKLAERLAEALGAR--------GPLNIQCFVTDGEPYLFEINPRFG 271
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
76-318 |
3.80e-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: 60.72 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 76 GIVNALEAVGVPCVGPAQeSARIETDKSFMRNLFEKYQIKGSLTYkVFDNYEDISAFLDTYEKDVVVKPVGLTGGKGVKI 155
Cdd:COG0189 72 ALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPPTL-VTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 156 VgdhlKDNQDAKAYAKEVMDNamgGFAQVIIEEKVVGEE-FTIQAFC-DGENLAAM---PAAQDHPHAFENdqglitGGM 230
Cdd:COG0189 150 V----EDEDALESILEALTEL---GSEPVLVQEFIPEEDgRDIRVLVvGGEPVAAIrriPAEGEFRTNLAR------GGR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 231 GsysdvggllpfltqedydEAVDIMKEtLKAIAKETTPYKGILYG--QFMLSKDGPKLIEYNARFGDPEAMNVLpllktp 308
Cdd:COG0189 217 A------------------EPVELTDE-ERELALRAAPALGLDFAgvDLIEDDDGPLVLEVNVTPGFRGLERAT------ 271
|
250
....*....|
gi 889008271 309 MVDVCKAIVD 318
Cdd:COG0189 272 GVDIAEAIAD 281
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
48-292 |
4.20e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 55.03 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 48 GEVDEVAKFAKENEIElAVIgPEAPLGKGIVNALEAVGVPCV--GPAQESARieTDKSFMRNLFEKYQIKGSLTYKVfDN 125
Cdd:PRK07206 57 GDIDDLVEFLRKLGPE-AII-AGAESGVELADRLAEILTPQYsnDPALSSAR--RNKAEMINALAEAGLPAARQINT-AD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 126 YEDISAFLDT---YEKDVVVKPVGLTGGKGVKIVGDHlkdnQDAKAYAKEVMD--NAMGGFAQ-VIIEEKVVGEEFTIQA 199
Cdd:PRK07206 132 WEEAEAWLREnglIDRPVVIKPLESAGSDGVFICPAK----GDWKHAFNAILGkaNKLGLVNEtVLVQEYLIGTEYVVNF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 200 FCDGENLAAMPAAQDHPHAFENdqglitgGMGSYsDVGGLLPFlTQEDYDEAVDIMKETLKAIakettpykGILYG---- 275
Cdd:PRK07206 208 VSLDGNHLVTEIVRYHKTSLNS-------GSTVY-DYDEFLDY-SEPEYQELVDYTKQALDAL--------GIKNGpaha 270
|
250
....*....|....*..
gi 889008271 276 QFMLSKDGPKLIEYNAR 292
Cdd:PRK07206 271 EVMLTADGPRLIEIGAR 287
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
137-296 |
3.52e-06 |
|
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: 46.99 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 137 EKDVVVKPVGLTGGKGVKIVGDHLKDNQdakayakevmdnamgGFAQVIIEEKVVGEEFTIQAFCDGEnlaampaaQDHP 216
Cdd:pfam02655 31 EKKYVVKPRDGCGGEGVRKVENGREDEA---------------FIENVLVQEFIEGEPLSVSLLSDGE--------KALP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 217 HAFeNDQGLITGGMGsYSDVGGLLPFLTQEDyDEAVDIMKETLKAIaKETTPYKGIlygQFMLSKDGPKLIEYNARFGDP 296
Cdd:pfam02655 88 LSV-NRQYIDNGGSG-FVYAGNVTPSRTELK-EEIIELAEEVVECL-PGLRGYVGV---DLVLKDNEPYVIEVNPRITTS 160
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
81-211 |
1.60e-05 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 46.64 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 81 LEAVGVPCVGPAQESARIETDKSFMRNLFEKYQIKgslT--YKVF--DNYEDISAFLDTYEKDVVVKPVGLTGGKGVKIV 156
Cdd:COG1181 75 LELLGIPYTGSGVLASALAMDKALTKRVLAAAGLP---TppYVVLrrGELADLEAIEEELGLPLFVKPAREGSSVGVSKV 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 889008271 157 gdhlKDNQDAKAyakeVMDNAMGGFAQVIIEEKVVGEEFTIqAFCDGENLAAMPA 211
Cdd:COG1181 152 ----KNAEELAA----ALEEAFKYDDKVLVEEFIDGREVTV-GVLGNGGPRALPP 197
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
140-392 |
3.35e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 46.38 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 140 VVVKPVGLTGGKGVKIVgdhlkDNQDAKAYAKEVMDNAMGGfaQVIIEEKVVGEEFTIQAFCDGENLAAMPAAQDH---- 215
Cdd:PRK02186 145 VVVKPRMGSGSVGVRLC-----ASVAEAAAHCAALRRAGTR--AALVQAYVEGDEYSVETLTVARGHQVLGITRKHlgpp 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 216 PHAFEndqglitggmgsysdVGGLLPF-LTQEDYDEAVDIMKETLKAIAKETTPykgiLYGQFMLSKDGPKLIEYNARFg 294
Cdd:PRK02186 218 PHFVE---------------IGHDFPApLSAPQRERIVRTVLRALDAVGYAFGP----AHTELRVRGDTVVIIEINPRL- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 295 dpeAMNVLPLLKTPM--VDVCKAIVDGKLEDVEFED----KASVCKYIVPdgypdtPHAGELIEID-EEAIEALGAKVFY 367
Cdd:PRK02186 278 ---AGGMIPVLLEEAfgVDLLDHVIDLHLGVAAFADptakRYGAIRFVLP------ARSGVLRGLLfLPDDIAARPELRF 348
|
250 260
....*....|....*....|....*...
gi 889008271 368 AAVSQEDDGVHLSGS---RALGIVAQGD 392
Cdd:PRK02186 349 HPLKQPGDALRLEGDfrdRIAAVVCAGD 376
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
140-295 |
1.63e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 39.19 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 140 VVVKPVGLTGGKGVKIV------GDHLKDNQDAKAYAKEVMDNAMGGFAQVIIEEKVVGEEFTIQAFCDGENLAAMPAAQ 213
Cdd:pfam13535 5 CVIKPSVGFFSVGVYKInnreewKAAFAAIREEIEQWKEMYPEAVVDGGSFLVEEYIEGEEFAVDAYFDENGEPVILNIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 214 DHPHAFENDqglitggmgsYSDVGGLLPFLTQEDYDEAvdiMKETLKAIAKETTPYKGILYGQFMLSKDGP-KLIEYNA- 291
Cdd:pfam13535 85 KHDFASSED----------VSDRIYVTSASIIRETQAA---FTEFLKRINALLGLKNFPVHIELRVDEDGQiIPIEVNPl 151
|
....
gi 889008271 292 RFGD 295
Cdd:pfam13535 152 RFAG 155
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
73-324 |
6.38e-03 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 39.21 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 73 LGKGIVNALEAVGVPCVGPAQESARIETDksfmRNLFEKY-------QIKGSLTYKVfdnyEDISAFLDTYEKDVVVKPV 145
Cdd:TIGR01369 641 TPLNLAKALEEAGVPILGTSPESIDRAED----REKFSELldelgipQPKWKTATSV----EEAVEFASEIGYPVLVRPS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 146 GLTGGKGVKIVgdhlKDNQDAKAYAKEVMDNAMGgfAQVIIEEKV-VGEEFTIQAFCDGENLAAmPAAQDHphaFENdQG 224
Cdd:TIGR01369 713 YVLGGRAMEIV----YNEEELRRYLEEAVAVSPE--HPVLIDKYLeDAVEVDVDAVSDGEEVLI-PGIMEH---IEE-AG 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889008271 225 LITGgmgsysDVGGLLPFltQEDYDEAVDIMKETLKAIAKETTpYKGILYGQFMLSKDGPKLIEYNARfgdpeAMNVLPL 304
Cdd:TIGR01369 782 VHSG------DSTCVLPP--QTLSAEIVDRIKDIVRKIAKELN-VKGLMNIQFAVKDGEVYVIEVNPR-----ASRTVPF 847
|
250 260
....*....|....*....|....*
gi 889008271 305 ----LKTPMVDVC-KAIVDGKLEDV 324
Cdd:TIGR01369 848 vskaTGVPLAKLAvRVMLGKKLEEL 872
|
|
| |
