|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-425 |
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: 768.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 1 MKLLVIGSGGREHALAWRLARSPRVHKVYVAPGNGGTAQGEQLENVPLTSAEELADFVQREGVSLTVVGPEAPLAAGVVD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 81 VFRARGLKIFGPTKAAAQLESSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKADGLAAGKGVVVAMTLD 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 161 EAHGAIDAMLGDGSLGEAGARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKRLKDGDAGPNTGGMGAYSPAPVVTPE 240
Cdd:COG0151 161 EALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 241 LHHRIMREIILPTVQGMARDGIPYTGFLYAGLMIaagdDPDRPiKTLEYNCRMGDPETQPIMMRVKSDLLDAFEHAVDGT 320
Cdd:COG0151 241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMI----TADGP-KVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 321 LDQADIVWDRRTALGVVLAAHNYPATPRTGDVIAGLPAA-TEDCVVFHAATALDGDATKTTGGRVLCVTALGDSVRIARD 399
Cdd:COG0151 316 LDEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAeAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARE 395
|
410 420
....*....|....*....|....*.
gi 633378321 400 RAYEAVDAIHFDGRQYRTDIGWRALK 425
Cdd:COG0151 396 RAYEAVEKIRFEGMFYRRDIGWRALK 421
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-425 |
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: 589.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 1 MKLLVIGSGGREHALAWRLARSPRVHKVYVAPGNGGTAQGEQLENVPLTSA--EELADFVQREGVSLTVVGPEAPLAAGV 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITdiEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 79 VDVFRARGLKIFGPTKAAAQLESSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKADGLAAGKGVVVAMT 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 159 LDEAHGAIDAMLgDGSLGEAGARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKRLKDGDAGPNTGGMGAYSPAPVVT 238
Cdd:TIGR00877 161 NEEAIKAVEDIL-EQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 239 PELHHRIMREIILPTVQGMARDGIPYTGFLYAGLMIaagdDPDRPiKTLEYNCRMGDPETQPIMMRVKSDLLDAFEHAVD 318
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLML----TKEGP-KVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 319 GTLDQADIVWDRRTALGVVLAAHNYPATPRTGDVIAGLPAA-TEDCVVFHAATALDGDATKTTGGRVLCVTALGDSVRIA 397
Cdd:TIGR00877 315 GKLDEVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAeAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEA 394
|
410 420
....*....|....*....|....*...
gi 633378321 398 RDRAYEAVDAIHFDGRQYRTDIGWRALK 425
Cdd:TIGR00877 395 RERAYEAVEYIKFEGMFYRKDIGFRALE 422
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-433 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 516.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 4 LVIGSGGREHALAWRLARSPRVHKVYVAPGNGGTAQGEQLENVP---LTSAEELADFVQREGVSLTVVGPEAPLAAGVVD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdldISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 81 VFRARGLKIFGPTKAAAQLESSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKADGLAAGKGVVVAMTLD 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 161 EAHGAIDAMLGDGSLGEAGARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKRLKDGDAGPNTGGMGAYSPAPVVTPE 240
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 241 LHHRIMREIILPTVQGMARDGIPYTGFLYAGLMIAA-GDDPdrpiKTLEYNCRMGDPETQPIMMRVKSDLLDAFEHAVDG 319
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKkSGLP----KLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 320 TLDQADIVWDRRTALGVVLAAHNYPATPRTGDVIAGLPAATE--DCV-VFHAATALDGDATKT-TGGRVLCVTALGDSVR 395
Cdd:PLN02257 317 ELSGVSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAvaPGVkVFHAGTALDSDGNVVaAGGRVLGVTAKGKDIA 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 633378321 396 IARDRAYEAVDAIHFDGRQYRTDIGWRALkPSQQKAPK 433
Cdd:PLN02257 397 EARARAYDAVDQIDWPGGFFRRDIGWRAV-ARLQVANK 433
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-298 |
6.82e-98 |
|
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: 291.11 E-value: 6.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 101 SSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPI-VIKADGLAAGKGVVVAMTLDEAHGAIDAMLGDGSLGEAG 179
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 180 ARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKRLKDGDAGPNTGGMGAYSPAPVVTPELHHRIMREIILPTVQGMAR 259
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 633378321 260 DGIPYTGFLYAGLMIAagddPDRPiKTLEYNCRMGDPET 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLT----KDGP-KVLEFNCRFGDPET 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-425 |
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: 768.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 1 MKLLVIGSGGREHALAWRLARSPRVHKVYVAPGNGGTAQGEQLENVPLTSAEELADFVQREGVSLTVVGPEAPLAAGVVD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 81 VFRARGLKIFGPTKAAAQLESSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKADGLAAGKGVVVAMTLD 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 161 EAHGAIDAMLGDGSLGEAGARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKRLKDGDAGPNTGGMGAYSPAPVVTPE 240
Cdd:COG0151 161 EALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 241 LHHRIMREIILPTVQGMARDGIPYTGFLYAGLMIaagdDPDRPiKTLEYNCRMGDPETQPIMMRVKSDLLDAFEHAVDGT 320
Cdd:COG0151 241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMI----TADGP-KVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 321 LDQADIVWDRRTALGVVLAAHNYPATPRTGDVIAGLPAA-TEDCVVFHAATALDGDATKTTGGRVLCVTALGDSVRIARD 399
Cdd:COG0151 316 LDEVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAeAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARE 395
|
410 420
....*....|....*....|....*.
gi 633378321 400 RAYEAVDAIHFDGRQYRTDIGWRALK 425
Cdd:COG0151 396 RAYEAVEKIRFEGMFYRRDIGWRALK 421
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-425 |
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: 589.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 1 MKLLVIGSGGREHALAWRLARSPRVHKVYVAPGNGGTAQGEQLENVPLTSA--EELADFVQREGVSLTVVGPEAPLAAGV 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITdiEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 79 VDVFRARGLKIFGPTKAAAQLESSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKADGLAAGKGVVVAMT 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 159 LDEAHGAIDAMLgDGSLGEAGARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKRLKDGDAGPNTGGMGAYSPAPVVT 238
Cdd:TIGR00877 161 NEEAIKAVEDIL-EQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 239 PELHHRIMREIILPTVQGMARDGIPYTGFLYAGLMIaagdDPDRPiKTLEYNCRMGDPETQPIMMRVKSDLLDAFEHAVD 318
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLML----TKEGP-KVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 319 GTLDQADIVWDRRTALGVVLAAHNYPATPRTGDVIAGLPAA-TEDCVVFHAATALDGDATKTTGGRVLCVTALGDSVRIA 397
Cdd:TIGR00877 315 GKLDEVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAeAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEA 394
|
410 420
....*....|....*....|....*...
gi 633378321 398 RDRAYEAVDAIHFDGRQYRTDIGWRALK 425
Cdd:TIGR00877 395 RERAYEAVEYIKFEGMFYRKDIGFRALE 422
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-433 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 516.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 4 LVIGSGGREHALAWRLARSPRVHKVYVAPGNGGTAQGEQLENVP---LTSAEELADFVQREGVSLTVVGPEAPLAAGVVD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdldISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 81 VFRARGLKIFGPTKAAAQLESSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKADGLAAGKGVVVAMTLD 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 161 EAHGAIDAMLGDGSLGEAGARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKRLKDGDAGPNTGGMGAYSPAPVVTPE 240
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 241 LHHRIMREIILPTVQGMARDGIPYTGFLYAGLMIAA-GDDPdrpiKTLEYNCRMGDPETQPIMMRVKSDLLDAFEHAVDG 319
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKkSGLP----KLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 320 TLDQADIVWDRRTALGVVLAAHNYPATPRTGDVIAGLPAATE--DCV-VFHAATALDGDATKT-TGGRVLCVTALGDSVR 395
Cdd:PLN02257 317 ELSGVSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAvaPGVkVFHAGTALDSDGNVVaAGGRVLGVTAKGKDIA 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 633378321 396 IARDRAYEAVDAIHFDGRQYRTDIGWRALkPSQQKAPK 433
Cdd:PLN02257 397 EARARAYDAVDQIDWPGGFFRRDIGWRAV-ARLQVANK 433
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-298 |
6.82e-98 |
|
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: 291.11 E-value: 6.82e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 101 SSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPI-VIKADGLAAGKGVVVAMTLDEAHGAIDAMLGDGSLGEAG 179
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 180 ARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKRLKDGDAGPNTGGMGAYSPAPVVTPELHHRIMREIILPTVQGMAR 259
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 633378321 260 DGIPYTGFLYAGLMIAagddPDRPiKTLEYNCRMGDPET 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLT----KDGP-KVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-100 |
1.56e-53 |
|
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: 173.70 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 1 MKLLVIGSGGREHALAWRLARSPRVHKVYVAPGNGGTAQGEQLENVPLTSAEELADFVQREGVSLTVVGPEAPLAAGVVD 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 633378321 81 VF--RARGLKIFGPTKAAAQLE 100
Cdd:pfam02844 81 ALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
333-422 |
1.59e-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: 134.11 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 333 ALGVVLAAHNYPATPRTGDVIAGLPAAteDCVVFHAATALDGDATKTTGGRVLCVTALGDSVRIARDRAYEAVDAIHFDG 412
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA--GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEG 78
|
90
....*....|
gi 633378321 413 RQYRTDIGWR 422
Cdd:pfam02843 79 MFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
84-294 |
2.91e-16 |
|
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: 78.38 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 84 ARGLKIFGPTKAAAQLESSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKADGLAAGKGVVVAMTLDEAH 163
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 164 GAIDAMLGDGSLGEAGARVVIEEFLTGEEASFIVMCDGRHVLALATSQDHKrlkdgdAGPNTGGMGAYSPAPvVTPELHH 243
Cdd:COG0439 116 AALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELRA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 633378321 244 RIMREiilpTVQGMARDGIPYtGFLYAGLMIaagdDPDRPIKTLEYNCRMG 294
Cdd:COG0439 189 EIGEL----VARALRALGYRR-GAFHTEFLL----TPDGEPYLIEINARLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
75-208 |
1.25e-08 |
|
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: 56.10 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 75 AAGVVDVFRARGLKIFGPTkAAAQLESSKDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIK-ADGlAAGKGV 153
Cdd:COG0189 70 GLALLRQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGV 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 633378321 154 VVAMTLDEAHGAIDAMLGDGSlgeagARVVIEEFLTGEEASF--IVMCDGRHVLALA 208
Cdd:COG0189 148 FLVEDEDALESILEALTELGS-----EPVLVQEFIPEEDGRDirVLVVGGEPVAAIR 199
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
107-197 |
1.26e-08 |
|
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: 56.24 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 107 KAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKA-----DglaaGKGVVVAMTLDEAHGAIDAMlgdgslgeAGAR 181
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90
....*....|....*..
gi 633378321 182 VVIEEFLTGE-EASFIV 197
Cdd:COG0026 162 CILEEFVPFErELSVIV 178
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
107-197 |
4.81e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 48.23 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 107 KAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKA-----DglaaGKGVVVAMTLDEAHGAIDAMlgdgslgeAGAR 181
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrggyD----GKGQWVIRSAEDLEAAWALL--------GSVP 172
|
90
....*....|....*..
gi 633378321 182 VVIEEFLTGE-EASFIV 197
Cdd:PRK06019 173 CILEEFVPFErEVSVIV 189
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
108-309 |
2.66e-03 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 38.64 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 108 AFMVRHAIPTARYETFTDPAQAHAYVDQ--HGAPIVIKADGLAAGKGVVVAMTLDEAHGAIDAMlgdgslgeaGARVVIE 185
Cdd:pfam08443 9 QLLAKHGIGPPNTRLAWYPEDAEQFIEQikRQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSAT---------NEQILVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 186 EFL--TGEEASFIVMCDGRHVLALatsqdHKRLKDGDAGPNTGGMGAYSPAPvVTPELhhrimREIILPTVQGMARDgip 263
Cdd:pfam08443 80 EFIaeANNEDIRCLVVGDQVVGAL-----HRQSNEGDFRSNLHRGGVGEKYQ-LSQEE-----TELAIKAAQAMQLD--- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 633378321 264 ytgflYAGLMIAagdDPDRPIKTLEYNcrmGDPETQPIMMRVKSDL 309
Cdd:pfam08443 146 -----VAGVDLL---RQKRGLLVCEVN---SSPGLEGIEKTLGINI 180
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
112-187 |
2.72e-03 |
|
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: 38.39 E-value: 2.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 633378321 112 RHAIPTARYETFTDPAQAHAYVDQHGAPIVIKADGLA-AGKGVVVAMTLDEAHGAIDAmLGDGslgeagaRVVIEEF 187
Cdd:pfam02222 2 KLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEE-LGDG-------PVIVEEF 70
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
79-155 |
6.67e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 38.57 E-value: 6.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 633378321 79 VDVFRARGLKIFGPTKAAAQLESSKDYAKAFMVRHAIPTARYET--FTDPAQAHAYVDQHGAPIVIKADGLAAGKGVVV 155
Cdd:PRK08462 94 VEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDgaLKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRV 172
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
103-192 |
9.88e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 37.78 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633378321 103 KDYAKAFMVRHAIPTARYETFTDPAQAHAYVDQHGAPIVIKadglAAGKGVVVAMTLDEAHGAIDAMLGDGSlgEAGARV 182
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKVKEEDELQAALELAF--KYDDEV 172
|
90
....*....|
gi 633378321 183 VIEEFLTGEE 192
Cdd:PRK01372 173 LVEKYIKGRE 182
|
|
| |
