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Conserved domains on  [gi|2552310907|ref|WP_302763573|]
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phosphoribosylamine--glycine ligase [Alistipes putredinis]

Protein Classification

phosphoribosylamine--glycine ligase( domain architecture ID 11414962)

phosphoribosylamine--glycine ligase catalyzes the second step of the de novo purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi

CATH:  3.30.1490.20
Gene Ontology:  GO:0005524|GO:0004637|GO:0009113|GO:0006164
PubMed:  2687276

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 1-414 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: 689.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGGGREHAVVDALSRSPQVSKIYCAPGNAGIARQAECVPVKDTDVEGLLSLAREKEIDLTVVGPEAALVAGIVD 80
Cdd:COG0151     1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  81 RFREEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAVLKYDGLAAGKGVVIARTME 160
Cdd:COG0151    81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 161 EADAALRDMLLDDKFGKG--RVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFITPE 238
Cdd:COG0151   161 EALAAVDDMLADGKFGDAgaRVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 239 DEAFALEMVMQRTADALCDEGCPFTGVLYGGLMKTPQGIRVIEFNARFGDPETEVVLPRLKSDIYDIFSAVADGR-DPGE 317
Cdd:COG0151   241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRlDEVE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 318 AEWHDFATLGIVLASKGYPGSYEKGYEITGTEQV---DGVVYHMGTAIKEGRLVTSGGRVMIVVCRGADPEQARCRALEE 394
Cdd:COG0151   321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAeaeGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYEA 400

                         410       420
                  ....*....|....*....|
gi 2552310907 395 VRKIGCENLFYRSDIGMKAL 414
Cdd:COG0151   401 VEKIRFEGMFYRRDIGWRAL 420
 
Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 1-414 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: 689.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGGGREHAVVDALSRSPQVSKIYCAPGNAGIARQAECVPVKDTDVEGLLSLAREKEIDLTVVGPEAALVAGIVD 80
Cdd:COG0151     1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  81 RFREEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAVLKYDGLAAGKGVVIARTME 160
Cdd:COG0151    81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 161 EADAALRDMLLDDKFGKG--RVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFITPE 238
Cdd:COG0151   161 EALAAVDDMLADGKFGDAgaRVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 239 DEAFALEMVMQRTADALCDEGCPFTGVLYGGLMKTPQGIRVIEFNARFGDPETEVVLPRLKSDIYDIFSAVADGR-DPGE 317
Cdd:COG0151   241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRlDEVE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 318 AEWHDFATLGIVLASKGYPGSYEKGYEITGTEQV---DGVVYHMGTAIKEGRLVTSGGRVMIVVCRGADPEQARCRALEE 394
Cdd:COG0151   321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAeaeGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYEA 400

                         410       420
                  ....*....|....*....|
gi 2552310907 395 VRKIGCENLFYRSDIGMKAL 414
Cdd:COG0151   401 VEKIRFEGMFYRRDIGWRAL 420
purD TIGR00877
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ...
 1-414 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: 534.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGGGREHAVVDALSRSPQVSKIYCAPGNAGIARQAEC--VPVKDTDVEGLLSLAREKEIDLTVVGPEAALVAGI 78
Cdd:TIGR00877   1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNknVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  79 VDRFREEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAVLKYDGLAAGKGVVIART 158
Cdd:TIGR00877  81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 159 MEEADAALRDMLlDDKFGKG--RVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFIT 236
Cdd:TIGR00877 161 NEEAIKAVEDIL-EQKFGDAgeRVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 237 PEDEAFALEMVMQRTADALCDEGCPFTGVLYGGLMKTPQGIRVIEFNARFGDPETEVVLPRLKSDIYDIFSAVADGR-DP 315
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKlDE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 316 GEAEWHDFATLGIVLASKGYPGSYEKGYEITG---TEQVDGVVYHMGTAIKEGRLVTSGGRVMIVVCRGADPEQARCRAL 392
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPITGeplAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAY 399

                         410       420
                  ....*....|....*....|..
gi 2552310907 393 EEVRKIGCENLFYRSDIGMKAL 414
Cdd:TIGR00877 400 EAVEYIKFEGMFYRKDIGFRAL 421
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 4-415 2.01e-152

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 438.40  E-value: 2.01e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   4 LVVGGGGREHAVVDALSRSPQVSKIYCAPGNAGIARQ--AECVP-VKDTDVEGLLSLAREKEIDLTVVGPEAALVAGIVD 80
Cdd:PLN02257    1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSgdATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  81 RFREEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAVLKYDGLAAGKGVVIARTME 160
Cdd:PLN02257   81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 161 EADAALRDMLLDDKFGK--GRVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFITPE 238
Cdd:PLN02257  161 EAYEAVDSMLVKGAFGSagSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 239 DEAFALEMVMQRTADALCDEGCPFTGVLYGGLMKTPQG--IRVIEFNARFGDPETEVVLPRLKSDIYDIFSAVADGR-DP 315
Cdd:PLN02257  241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGElSG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 316 GEAEWHDFATLGIVLASKGYPGSYEKGYEITGTEQVDGV-----VYHMGTAIK-EGRLVTSGGRVMIVVCRGADPEQARC 389
Cdd:PLN02257  321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapgvkVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEARA 400

                         410       420
                  ....*....|....*....|....*.
gi 2552310907 390 RALEEVRKIGCENLFYRSDIGMKALS 415
Cdd:PLN02257  401 RAYDAVDQIDWPGGFFRRDIGWRAVA 426
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 101-291 1.34e-94

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: 282.25  E-value: 1.34e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 101 SSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPA-VLKYDGLAAGKGVVIARTMEEADAALRDMLLDDKFGK-- 177
Cdd:pfam01071   1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEag 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 178 GRVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFITPEDEAFALEMVMQRTADALCD 257
Cdd:pfam01071  81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2552310907 258 EGCPFTGVLYGGLMKTPQGIRVIEFNARFGDPET 291
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
 
Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 1-414 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: 689.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGGGREHAVVDALSRSPQVSKIYCAPGNAGIARQAECVPVKDTDVEGLLSLAREKEIDLTVVGPEAALVAGIVD 80
Cdd:COG0151     1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  81 RFREEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAVLKYDGLAAGKGVVIARTME 160
Cdd:COG0151    81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 161 EADAALRDMLLDDKFGKG--RVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFITPE 238
Cdd:COG0151   161 EALAAVDDMLADGKFGDAgaRVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 239 DEAFALEMVMQRTADALCDEGCPFTGVLYGGLMKTPQGIRVIEFNARFGDPETEVVLPRLKSDIYDIFSAVADGR-DPGE 317
Cdd:COG0151   241 LLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRlDEVE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 318 AEWHDFATLGIVLASKGYPGSYEKGYEITGTEQV---DGVVYHMGTAIKEGRLVTSGGRVMIVVCRGADPEQARCRALEE 394
Cdd:COG0151   321 LEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAeaeGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERAYEA 400

                         410       420
                  ....*....|....*....|
gi 2552310907 395 VRKIGCENLFYRSDIGMKAL 414
Cdd:COG0151   401 VEKIRFEGMFYRRDIGWRAL 420
purD TIGR00877
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ...
 1-414 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: 534.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGGGREHAVVDALSRSPQVSKIYCAPGNAGIARQAEC--VPVKDTDVEGLLSLAREKEIDLTVVGPEAALVAGI 78
Cdd:TIGR00877   1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNknVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  79 VDRFREEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAVLKYDGLAAGKGVVIART 158
Cdd:TIGR00877  81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 159 MEEADAALRDMLlDDKFGKG--RVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFIT 236
Cdd:TIGR00877 161 NEEAIKAVEDIL-EQKFGDAgeRVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 237 PEDEAFALEMVMQRTADALCDEGCPFTGVLYGGLMKTPQGIRVIEFNARFGDPETEVVLPRLKSDIYDIFSAVADGR-DP 315
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKlDE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 316 GEAEWHDFATLGIVLASKGYPGSYEKGYEITG---TEQVDGVVYHMGTAIKEGRLVTSGGRVMIVVCRGADPEQARCRAL 392
Cdd:TIGR00877 320 VELRFDNRAAVTVVLASEGYPEDYRKGDPITGeplAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERAY 399

                         410       420
                  ....*....|....*....|..
gi 2552310907 393 EEVRKIGCENLFYRSDIGMKAL 414
Cdd:TIGR00877 400 EAVEYIKFEGMFYRKDIGFRAL 421
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 4-415 2.01e-152

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 438.40  E-value: 2.01e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   4 LVVGGGGREHAVVDALSRSPQVSKIYCAPGNAGIARQ--AECVP-VKDTDVEGLLSLAREKEIDLTVVGPEAALVAGIVD 80
Cdd:PLN02257    1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSgdATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  81 RFREEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAVLKYDGLAAGKGVVIARTME 160
Cdd:PLN02257   81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 161 EADAALRDMLLDDKFGK--GRVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFITPE 238
Cdd:PLN02257  161 EAYEAVDSMLVKGAFGSagSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 239 DEAFALEMVMQRTADALCDEGCPFTGVLYGGLMKTPQG--IRVIEFNARFGDPETEVVLPRLKSDIYDIFSAVADGR-DP 315
Cdd:PLN02257  241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGElSG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 316 GEAEWHDFATLGIVLASKGYPGSYEKGYEITGTEQVDGV-----VYHMGTAIK-EGRLVTSGGRVMIVVCRGADPEQARC 389
Cdd:PLN02257  321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapgvkVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEARA 400

                         410       420
                  ....*....|....*....|....*.
gi 2552310907 390 RALEEVRKIGCENLFYRSDIGMKALS 415
Cdd:PLN02257  401 RAYDAVDQIDWPGGFFRRDIGWRAVA 426
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 101-291 1.34e-94

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: 282.25  E-value: 1.34e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 101 SSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPA-VLKYDGLAAGKGVVIARTMEEADAALRDMLLDDKFGK-- 177
Cdd:pfam01071   1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEag 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 178 GRVVVEDFLTGPEFSFMCFVSGRKVLPMVLAQDHKRAFDGDEGPNTGGMGAYSPLPFITPEDEAFALEMVMQRTADALCD 257
Cdd:pfam01071  81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2552310907 258 EGCPFTGVLYGGLMKTPQGIRVIEFNARFGDPET 291
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
GARS_N pfam02844
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ...
 1-100 2.23e-54

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: 175.62  E-value: 2.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGGGREHAVVDALSRSPQVSKIYCAPGNAGIARQAECVPVKDTDVEGLLSLAREKEIDLTVVGPEAALVAGIVD 80
Cdd:pfam02844   1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80

                          90       100
                  ....*....|....*....|..
gi 2552310907  81 RFREE--GLRIFGPTKAAVRIE 100
Cdd:pfam02844  81 ALRERaaGIPVFGPSKAAAQLE 102
GARS_C pfam02843
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ...
 325-410 2.26e-35

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: 125.64  E-value: 2.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 325 TLGIVLASKGYPGSYEKGYEITGTEQVDGVVYHMGTAIKEGRLVTSGGRVMIVVCRGADPEQARCRALEEVRKIGCENLF 404
Cdd:pfam02843   1 AVCVVLASGGYPGSYEKGDVITGLDEAGVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFEGMF 80


                  ....*.
gi 2552310907 405 YRSDIG 410
Cdd:pfam02843  81 YRKDIG 86
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 50-287 1.75e-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: 87.62  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  50 DVEGLLSLARE--KEIDLTVVGPEAALVAGIVDRFREEgLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYR 127
Cdd:COG0439     1 DIDAIIAAAAElaRETGIDAVLSESEFAVETAAELAEE-LGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 128 KASEYVHSRPLPAVLKYDGLAAGKGVVIARTMEEADAALRDMLLDDKFGK--GRVVVEDFLTGPEFSFMCFVSGRKVLPM 205
Cdd:COG0439    80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSpnGEVLVEEFLEGREYSVEGLVRDGEVVVC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 206 VLAQDHKRAFDGDEGPNTggmgayspLPFITPEDEAFALEMVMQRTADALcdegcpftGVLYGG----LMKTPQG-IRVI 280
Cdd:COG0439   160 SITRKHQKPPYFVELGHE--------APSPLPEELRAEIGELVARALRAL--------GYRRGAfhteFLLTPDGePYLI 223


                  ....*..
gi 2552310907 281 EFNARFG 287
Cdd:COG0439   224 EINARLG 230
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 50-187 6.27e-09

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: 57.39  E-value: 6.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  50 DVEGLLSLAREkeidlTVVGPEAALVAGIVDRFREeglrifgptkaavriessKEFAKDLmgryGIPTAGYRAFDDYRKA 129
Cdd:COG0026    64 PAEALEALEAE-----VPVRPGPEALEIAQDRLLE------------------KAFLAEL----GIPVAPFAAVDSLEDL 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2552310907 130 SEYVHSRPLPAVLK-----YDglaaGKGVVIARTMEEADAALRDMllddkfGKGRVVVEDFLT 187
Cdd:COG0026   117 EAAIAELGLPAVLKtrrggYD----GKGQVVIKSAADLEAAWAAL------GGGPCILEEFVP 169
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
1-287 4.14e-07

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 51.85  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGG----------GREHAVVDALSRSP----QVSKIycapgnagIARQAECVPVKDTD---VEGLLSLAREKEI 63
Cdd:COG3919     6 FRVVVLGGDinalavarslGEAGVRVIVVDRDPlgpaARSRY--------VDEVVVVPDPGDDPeafVDALLELAERHGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  64 DLTVVG--PEAALVAGIVDRFrEEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAV 141
Cdd:COG3919    78 DVLIPTgdEYVELLSRHRDEL-EEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 142 LK--------YDGLAAGKGVVIARTMEEADAALRDMLLDDkfgkGRVVVEDFLTGP---EFSFMCFVSGR-KVLPMVLAQ 209
Cdd:COG3919   157 VKpadsvgydELSFPGKKKVFYVDDREELLALLRRIAAAG----YELIVQEYIPGDdgeMRGLTAYVDRDgEVVATFTGR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 210 DHKRAfdgdegPNTGGMGAYsplpFITPEDEAfalemvMQRTADALCDE-GcpFTGVLYGGLMKTPQG--IRVIEFNARF 286
Cdd:COG3919   233 KLRHY------PPAGGNSAA----RESVDDPE------LEEAARRLLEAlG--YHGFANVEFKRDPRDgeYKLIEINPRF 294


                  .
gi 2552310907 287 G 287
Cdd:COG3919   295 W 295
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 1-287 8.26e-07

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 50.65  E-value: 8.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGGGReHAVVDALSRSPQVSKIYCA---PGNAGI--ARQAECVP-VKDTD-VEGLLSLAREKEIDLTVVG--PE 71
Cdd:PRK12767    2 MNILVTSAGRR-VQLVKALKKSLLKGRVIGAdisELAPALyfADKFYVVPkVTDPNyIDRLLDICKKEKIDLLIPLidPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  72 AALVAGIVDRFREEGLRIFGPTKAAVRIESSK----EFAKDLmgryGIPTAgyRAFD----DYRKASEYVHSRPLPAVLK 143
Cdd:PRK12767   81 LPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKwltyEFLKEN----GIPTP--KSYLpeslEDFKAALAKGELQFPLFVK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 144 -YDGlAAGKGVVIARTMEEADAALRDMLLddkfgkgrVVVEDFLTGPEFSFMCFV--SGRKVLPMVLAQDHKRAFDGDEG 220
Cdd:PRK12767  155 pRDG-SASIGVFKVNDKEELEFLLEYVPN--------LIIQEFIEGQEYTVDVLCdlNGEVISIVPRKRIEVRAGETSKG 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2552310907 221 pntggmgaysplpfITPEDEafALEMVMQRTADALcdegcPFTGVLYGGLMKTPQGIRVIEFNARFG 287
Cdd:PRK12767  226 --------------VTVKDP--ELFKLAERLAEAL-----GARGPLNIQCFVTDGEPYLFEINPRFG 271
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 1-192 8.37e-07

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: 50.49  E-value: 8.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907   1 MKVLVVGGGGR-EH--------AVVDALSRspqvskiycapgnAGIarqaECVPVkDTDVEGLLSLAREKEIDltVV--- 68
Cdd:COG1181     1 MRVAVLFGGRSaERevslksgrAVAAALDK-------------AGY----DVVPI-GIDVEDLPAALKELKPD--VVfpa 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  69 --GP--EAALVAGIVDRFreeGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPTAGYRAF--DDYRKASEYVHSRPLPAVL 142
Cdd:COG1181    61 lhGRggEDGTIQGLLELL---GIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLrrGELADLEAIEEELGLPLFV 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2552310907 143 KYDGLAAGKGVVIARTMEEADAALRDMLlddKFGkGRVVVEDFLTGPEFS 192
Cdd:COG1181   138 KPAREGSSVGVSKVKNAEELAAALEEAF---KYD-DKVLVEEFIDGREVT 183
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 92-186 1.47e-05

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 46.68  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  92 PTKAAVRIESSKEFAKDLMGRYGIPTAGYRA---FDDYRKASEYVHsrpLPAVLK-----YDglaaGKGVVIARTMEEAD 163
Cdd:PRK06019   90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFAVvdsAEDLEAALADLG---LPAVLKtrrggYD----GKGQWVIRSAEDLE 162

                          90       100
                  ....*....|....*....|...
gi 2552310907 164 AALrdmlldDKFGKGRVVVEDFL 186
Cdd:PRK06019  163 AAW------ALLGSVPCILEEFV 179
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 103-204 5.99e-05

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 44.72  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907 103 KEFAKDLMGRYGIPTAGYRAFDDYRKASEYVHSRPLPAVLKydGLAAGK--GVVIARTMEEADAALRdmlLDDKFGKgRV 180
Cdd:PRK01372   99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK--PAREGSsvGVSKVKEEDELQAALE---LAFKYDD-EV 172

                          90       100
                  ....*....|....*....|....
gi 2552310907 181 VVEDFLTGPEFSfmCFVSGRKVLP 204
Cdd:PRK01372  173 LVEKYIKGRELT--VAVLGGKALP 194
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 76-189 3.80e-03

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 39.24  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552310907  76 AGIVDRFREEGLRIFGPTKAAVRIESSKEFAKDLMGRYGIPT--AGYRAFDDYRKASEYVHSRPLPAVLKYDGLAAGKGV 153
Cdd:PRK06111   89 ASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGM 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2552310907 154 VIARTMEEADAALRdmlLDDK-----FGKGRVVVEDFLTGP 189
Cdd:PRK06111  169 QLVETEQELTKAFE---SNKKraanfFGNGEMYIEKYIEDP 206
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 114-185 7.85e-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: 37.23  E-value: 7.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2552310907 114 GIPTAGYRAFDDYRKASEYVHSRPLPAVLK-----YDglaaGKGVVIARTMEEADAALRDmllddkFGKGRVVVEDF 185
Cdd:pfam02222   4 GLPTPRFMAAESLEELIEAGQELGYPCVVKarrggYD----GKGQYVVRSEADLPQAWEE------LGDGPVIVEEF 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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