|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-422 |
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: 779.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 1 MRVLLIGSGGREHALAWKLSASPSLTKLYCAPGNPGIATIAELVDIGVDDHQALIAFAKDKKIDLVVVGPEAPLVAGLSD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 81 EMRAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPIVVKADGLAAGKGVIVAMTLD 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 161 EALDAVDACFE-GAFGSAGAEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGDGDTGPNTGGMGAYAPAPVMTPE 239
Cdd:COG0151 161 EALAAVDDMLAdGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 240 IVERTMRELIEPTMRGMAEIGAPFSGILFLGLMIGKDGPKLIEYNTRFGDPECQVLMMRLNSDLLALINAAVDGKLDEVS 319
Cdd:COG0151 241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 320 LDWKNQPALTVVMAAEGYPSNVKKGSVIRDLDKLEGiDGVKLFHAGTAEKDGSIVASGGRVLNITAIADTVAEAQARAYE 399
Cdd:COG0151 321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEA-EGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYE 399
|
410 420
....*....|....*....|...
gi 501038859 400 AVKLIDWPEGFYRSDIGWRAVER 422
Cdd:COG0151 400 AVEKIRFEGMFYRRDIGWRALKR 422
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-429 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 650.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 4 LLIGSGGREHALAWKLSASPSLTKLYCAPGNPGIAT---IAELVDIGVDDHQALIAFAKDKKIDLVVVGPEAPLVAGLSD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATsgdATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 81 EMRAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPIVVKADGLAAGKGVIVAMTLD 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 161 EALDAVDACF-EGAFGSAGAEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGDGDTGPNTGGMGAYAPAPVMTPE 239
Cdd:PLN02257 161 EAYEAVDSMLvKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 240 IVERTMRELIEPTMRGMAEIGAPFSGILFLGLMI-GKDG-PKLIEYNTRFGDPECQVLMMRLNSDLLALINAAVDGKLDE 317
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIeKKSGlPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 318 VSLDWKNQPALTVVMAAEGYPSNVKKGSVIRDLDKLEGI-DGVKLFHAGTA-EKDGSIVASGGRVLNITAIADTVAEAQA 395
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVaPGVKVFHAGTAlDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420 430
....*....|....*....|....*....|....
gi 501038859 396 RAYEAVKLIDWPEGFYRSDIGWRAVERETQADKK 429
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQVANKR 434
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-421 |
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: 584.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 1 MRVLLIGSGGREHALAWKLSASPSLTKLYCAPGNPGIATIAE--LVDIGVDDHQALIAFAKDKKIDLVVVGPEAPLVAGL 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKnkNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 79 SDEMRAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPIVVKADGLAAGKGVIVAMT 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 159 LDEALDAVDACFEGAFGSAGAEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGDGDTGPNTGGMGAYAPAPVMTP 238
Cdd:TIGR00877 161 NEEAIKAVEDILEQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 239 EIVERTMRELIEPTMRGMAEIGAPFSGILFLGLMIGKDGPKLIEYNTRFGDPECQVLMMRLNSDLLALINAAVDGKLDEV 318
Cdd:TIGR00877 241 EVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDEV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 319 SLDWKNQPALTVVMAAEGYPSNVKKGSVIRDLDKLEgIDGVKLFHAGTAEKDGSIVASGGRVLNITAIADTVAEAQARAY 398
Cdd:TIGR00877 321 ELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAE-AEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAY 399
|
410 420
....*....|....*....|...
gi 501038859 399 EAVKLIDWPEGFYRSDIGWRAVE 421
Cdd:TIGR00877 400 EAVEYIKFEGMFYRKDIGFRALE 422
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-292 |
6.15e-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: 6.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 101 GSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPI-VVKADGLAAGKGVIVAMTLDEALDAVDACFE-GAFGSAG 178
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEqKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 179 AEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGDGDTGPNTGGMGAYAPAPVMTPEIVERTMRELIEPTMRGMAE 258
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 501038859 259 IGAPFSGILFLGLMIGKDGPKLIEYNTRFGDPEC 292
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-422 |
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: 779.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 1 MRVLLIGSGGREHALAWKLSASPSLTKLYCAPGNPGIATIAELVDIGVDDHQALIAFAKDKKIDLVVVGPEAPLVAGLSD 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 81 EMRAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPIVVKADGLAAGKGVIVAMTLD 160
Cdd:COG0151 81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 161 EALDAVDACFE-GAFGSAGAEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGDGDTGPNTGGMGAYAPAPVMTPE 239
Cdd:COG0151 161 EALAAVDDMLAdGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 240 IVERTMRELIEPTMRGMAEIGAPFSGILFLGLMIGKDGPKLIEYNTRFGDPECQVLMMRLNSDLLALINAAVDGKLDEVS 319
Cdd:COG0151 241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDEVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 320 LDWKNQPALTVVMAAEGYPSNVKKGSVIRDLDKLEGiDGVKLFHAGTAEKDGSIVASGGRVLNITAIADTVAEAQARAYE 399
Cdd:COG0151 321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEA-EGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYE 399
|
410 420
....*....|....*....|...
gi 501038859 400 AVKLIDWPEGFYRSDIGWRAVER 422
Cdd:COG0151 400 AVEKIRFEGMFYRRDIGWRALKR 422
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-429 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 650.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 4 LLIGSGGREHALAWKLSASPSLTKLYCAPGNPGIAT---IAELVDIGVDDHQALIAFAKDKKIDLVVVGPEAPLVAGLSD 80
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATsgdATCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 81 EMRAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPIVVKADGLAAGKGVIVAMTLD 160
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 161 EALDAVDACF-EGAFGSAGAEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGDGDTGPNTGGMGAYAPAPVMTPE 239
Cdd:PLN02257 161 EAYEAVDSMLvKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 240 IVERTMRELIEPTMRGMAEIGAPFSGILFLGLMI-GKDG-PKLIEYNTRFGDPECQVLMMRLNSDLLALINAAVDGKLDE 317
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIeKKSGlPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 318 VSLDWKNQPALTVVMAAEGYPSNVKKGSVIRDLDKLEGI-DGVKLFHAGTA-EKDGSIVASGGRVLNITAIADTVAEAQA 395
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVaPGVKVFHAGTAlDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420 430
....*....|....*....|....*....|....
gi 501038859 396 RAYEAVKLIDWPEGFYRSDIGWRAVERETQADKK 429
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQVANKR 434
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-421 |
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: 584.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 1 MRVLLIGSGGREHALAWKLSASPSLTKLYCAPGNPGIATIAE--LVDIGVDDHQALIAFAKDKKIDLVVVGPEAPLVAGL 78
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKnkNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 79 SDEMRAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPIVVKADGLAAGKGVIVAMT 158
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 159 LDEALDAVDACFEGAFGSAGAEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGDGDTGPNTGGMGAYAPAPVMTP 238
Cdd:TIGR00877 161 NEEAIKAVEDILEQKFGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 239 EIVERTMRELIEPTMRGMAEIGAPFSGILFLGLMIGKDGPKLIEYNTRFGDPECQVLMMRLNSDLLALINAAVDGKLDEV 318
Cdd:TIGR00877 241 EVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDEV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 319 SLDWKNQPALTVVMAAEGYPSNVKKGSVIRDLDKLEgIDGVKLFHAGTAEKDGSIVASGGRVLNITAIADTVAEAQARAY 398
Cdd:TIGR00877 321 ELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAE-AEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAY 399
|
410 420
....*....|....*....|...
gi 501038859 399 EAVKLIDWPEGFYRSDIGWRAVE 421
Cdd:TIGR00877 400 EAVEYIKFEGMFYRKDIGFRALE 422
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
101-292 |
6.15e-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: 6.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 101 GSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPI-VVKADGLAAGKGVIVAMTLDEALDAVDACFE-GAFGSAG 178
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEqKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 179 AEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGDGDTGPNTGGMGAYAPAPVMTPEIVERTMRELIEPTMRGMAE 258
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 501038859 259 IGAPFSGILFLGLMIGKDGPKLIEYNTRFGDPEC 292
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-100 |
8.66e-59 |
|
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: 187.18 E-value: 8.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 1 MRVLLIGSGGREHALAWKLSASPSLTKLYCAPGNPGIATIAELVDIGVDDHQALIAFAKDKKIDLVVVGPEAPLVAGLSD 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80
|
90 100
....*....|....*....|..
gi 501038859 81 --EMRAEGIRVFGPSKAAAQLE 100
Cdd:pfam02844 81 alRERAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
327-418 |
2.01e-40 |
|
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: 139.12 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 327 ALTVVMAAEGYPSNVKKGSVIRDLDKLegidGVKLFHAGTAEKDGSIVASGGRVLNITAIADTVAEAQARAYEAVKLIDW 406
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA----GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDF 76
|
90
....*....|..
gi 501038859 407 PEGFYRSDIGWR 418
Cdd:pfam02843 77 EGMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
53-288 |
8.67e-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: 79.92 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 53 ALIAFAKDKKIDLVVVGPEA--PLVAGLSDEMraeGIRvfGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAK 130
Cdd:COG0439 8 AAAELARETGIDAVLSESEFavETAAELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 131 AYIRQQGAPIVVKADGLAAGKGVIVAMTLDEALDAVDACFEGAF-GSAGAEVVVEEFLDGEEASFFCICDGKTALPLGSA 209
Cdd:COG0439 83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKaGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 210 QDHKrvgdgdTGPNTGGMGAYAPAPvMTPEIVERtMRELIEptmRGMAEIGAPFsGILFLGLMIGKDG-PKLIEYNTRFG 288
Cdd:COG0439 163 RKHQ------KPPYFVELGHEAPSP-LPEELRAE-IGELVA---RALRALGYRR-GAFHTEFLLTPDGePYLIEINARLG 230
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
52-288 |
1.82e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 56.09 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 52 QALIAFAKDKKIDLVV-VGPEAPLVAGLSDEMRAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAK 130
Cdd:COG3919 66 DALLELAERHGPDVLIpTGDEYVELLSRHRDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 131 AYIRQQGAPIVVK-ADGLAA-------GKGVIVAMTLDEALDAVDACFEgafgsAGAEVVVEEFL---DGEEASFFCICD 199
Cdd:COG3919 146 ALAEDLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRIAA-----AGYELIVQEYIpgdDGEMRGLTAYVD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 200 --GKtalPLGSAQDHKRVGDgdtgPNTGGMGAYapapvmtpeIVERTMRELIEPTMRGMAEIGapFSGILFLGLMI-GKD 276
Cdd:COG3919 221 rdGE---VVATFTGRKLRHY----PPAGGNSAA---------RESVDDPELEEAARRLLEALG--YHGFANVEFKRdPRD 282
|
250
....*....|...
gi 501038859 277 G-PKLIEYNTRFG 288
Cdd:COG3919 283 GeYKLIEINPRFW 295
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
83-288 |
1.38e-07 |
|
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: 52.64 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 83 RAEGIRVFGPSkAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPIVVK-ADGlAAGKGVIVAMTLDE 161
Cdd:COG0189 78 EAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGVFLVEDEDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 162 ALDAVDAcfegAFGSAGAEVVVEEFL---DGEEASFFCIcDGKtalPLGSaqdHKRVG-DGDTGPNTGGMGAYAPAPVmT 237
Cdd:COG0189 156 LESILEA----LTELGSEPVLVQEFIpeeDGRDIRVLVV-GGE---PVAA---IRRIPaEGEFRTNLARGGRAEPVEL-T 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501038859 238 PE---IVERTMRELieptmrgmaeigapfsGILFLG--LMIGKDGPKLIEYNTRFG 288
Cdd:COG0189 224 DEereLALRAAPAL----------------GLDFAGvdLIEDDDGPLVLEVNVTPG 263
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
139-290 |
3.28e-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: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 139 PIVVK-ADGlAAGKGVIVAMTLDEALdavdacfegafgSAGAEVVVEEFLDGEEASFFCICDGKTALPLGSAQDHKRVGd 217
Cdd:pfam02655 33 KYVVKpRDG-CGGEGVRKVENGREDE------------AFIENVLVQEFIEGEPLSVSLLSDGEKALPLSVNRQYIDNG- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501038859 218 GDTGPNTGGMGayaPAPVMTPEIVERTMRELIE--PTMRGMAeigapfsGIlflGLMIGKDGPKLIEYNTRFGDP 290
Cdd:pfam02655 99 GSGFVYAGNVT---PSRTELKEEIIELAEEVVEclPGLRGYV-------GV---DLVLKDNEPYVIEVNPRITTS 160
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
53-288 |
5.02e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 47.96 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 53 ALIAFAKDKKIDLVVVG--PEAPLVAGLSDEMRAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIPTGAYGRFNNAPKAK 130
Cdd:PRK12767 60 RLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 131 AYIR--QQGAPIVVKADGLAAGKGVIVAMTLDEALDAVDACfegafgsagAEVVVEEFLDGEE--ASFFCICDGKtalPL 206
Cdd:PRK12767 140 AALAkgELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV---------PNLIIQEFIEGQEytVDVLCDLNGE---VI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 207 GSAQDHK---RVGD---GDTGPNtggmgayapapvmtPEIvertmRELIEPTMRGMAEIGApfsgiLFLGLMIGKDGPKL 280
Cdd:PRK12767 208 SIVPRKRievRAGEtskGVTVKD--------------PEL-----FKLAERLAEALGARGP-----LNIQCFVTDGEPYL 263
|
....*...
gi 501038859 281 IEYNTRFG 288
Cdd:PRK12767 264 FEINPRFG 271
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
41-191 |
3.46e-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: 45.48 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 41 AELVDIGVDDhqaLIAFAKDKKIDLVVV---GP--EAPLVAGLSDEMraeGIRVFGPSKAAAQLEGSKGFTKDLCARFDI 115
Cdd:COG1181 35 VVPIGIDVED---LPAALKELKPDVVFPalhGRggEDGTIQGLLELL---GIPYTGSGVLASALAMDKALTKRVLAAAGL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501038859 116 PTGAYGRFN--NAPKAKAYIRQQGAPIVVKADGLAAGKGVIVAMTLDEALDAVDACFEGafgsaGAEVVVEEFLDGEE 191
Cdd:COG1181 109 PTPPYVVLRrgELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY-----DDKVLVEEFIDGRE 181
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
49-404 |
9.49e-05 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 44.14 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 49 DDHQALIAFAKDKKIDLVVVGPEAPLVAGLSDEMrAEGIRVFGPSKAAAQLEGSKGFTKDLCARFDIP---TgaygRFNN 125
Cdd:COG2232 60 DLPAALLELAAADDPDGLVYGSGFENFPELLERL-ARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPhpeT----RFEP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 126 APKAKAYIrqqgapivVKADGLAAGKGVIVAmtldealdavdacfeGAFGSAGAEVVVEEFLDGEEASFFCICDGKTALP 205
Cdd:COG2232 135 PPDPGPWL--------VKPIGGAGGWHIRPA---------------DSEAPPAPGRYFQRYVEGTPASVLFLADGSDARV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 206 LG-SAQDhkrvgdgdTGPNTGGMGAYAPA--PVMTPEIVERTMRELIEptmrgmaEIGAPFS--GILFLGLMIGKDGPKL 280
Cdd:COG2232 192 LGfNRQL--------IGPAGERPFRYGGNigPLALPPALAEEMRAIAE-------ALVAALGlvGLNGVDFILDGDGPYV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 281 IEYNTRFGdPECQVLMMRLNSDLLALINAAVDGKLDEVSLDWKNQPALTVVMAAEgypsnvkkgsviRDLDklegIDGVK 360
Cdd:COG2232 257 LEVNPRPQ-ASLDLYEDATGGNLFDAHLRACRGELPEVPRPKPRRVAAKAILYAP------------RDLT----IPDDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 501038859 361 LFHAGTAekD----GSIVASGGRVLNITAIADTVAEAQARAYEAVKLI 404
Cdd:COG2232 320 SWPPWVA--DipapGTRIEKGEPVCTVLAEGPTAEAARALLERRAEEV 365
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
103-218 |
5.31e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 42.22 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 103 KGFTKDLCARFDIPTGAYGRFNNAPKAKAYIRQ-QGAPIVVKADGLAAGKGVIVAMTLDEALDAVDAcFEGAFgSAGAEV 181
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIFKEPASLEDYEKA-LEIAF-REDSSV 566
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 501038859 182 VVEEFLDGEEASFFCIcDGKTALPLgsaqdhKRV-----GDG 218
Cdd:PRK02471 567 LVEEFIVGTEYRFFVL-DGKVEAVL------LRVpanvvGDG 601
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
107-188 |
7.48e-04 |
|
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: 41.60 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 107 KDLCARFDIPTGAYGRFNNAPKAKAYIRQQGAPIVVKA-----DglaaGKGVIVAMTLDEALDAVDAcfegafgSAGAEV 181
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAA-------LGGGPC 162
|
....*..
gi 501038859 182 VVEEFLD 188
Cdd:COG0026 163 ILEEFVP 169
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
107-189 |
2.67e-03 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 38.82 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501038859 107 KDLCARFDIPT--GAYGRFNNAPKAKAYIRQQGAPIVVKADGLAAGKGVIVAMTLDEALDAVDACFEGAFGSAG-AEVVV 183
Cdd:pfam02786 6 KAAMKEAGVPTvpGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGnPQVLV 85
|
....*.
gi 501038859 184 EEFLDG 189
Cdd:pfam02786 86 EKSLKG 91
|
|
| |
