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Conserved domains on  [gi|504382656|ref|WP_014569758|]
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phosphoribosylamine--glycine ligase [Lacticaseibacillus rhamnosus]

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]; ...
 3-414 3.33e-161

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: 459.86  E-value: 3.33e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   3 KVLVIGGGARESALALKFSQSPQVDHVYVAPGNPAMELLGvEPIGIKEKEVPALIKFAQTHQIDLTFVGPEVPLAAGIVD 82
Cdd:COG0151    2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA-ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  83 DFQAIGLPIFGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGVVIANDAA 162
Cdd:COG0151   81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 163 TLDDTIEQFYAGHP----DATVLLEEYLAGEEASVMALFNDQKRVILPLSQDHKRRHAADRGPNTGGMGAISPLPQFKPD 238
Cdd:COG0151  161 EALAAVDDMLADGKfgdaGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 239 QVQAAQSLV-DATLAGMHQDGLNGHGVMYIGLIFTKEGPKILEYNMRFGDPETQVLLPQIENDFYQLVSDLLDGQ--QPT 315
Cdd:COG0151  241 LLEKIMEEIiEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRldEVE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 316 LKLNGQAYACFVAVNPDYPRA--------NLKTVP---VIVptnwpigtwLPAGVERTDNGWISDAGRIFSVVAGAVTLP 384
Cdd:COG0151  321 LEWDDRAAVCVVLASGGYPGSyekgdvitGLEEAEaegVKV---------FHAGTALEDGKLVTNGGRVLGVTALGDTLE 391

                        410       420       430
                 ....*....|....*....|....*....|...
gi 504382656 385 EAVAKAKHDLESIQgvLD---YRTDIGFHALKG 414
Cdd:COG0151  392 EARERAYEAVEKIR--FEgmfYRRDIGWRALKR 422
 
Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 3-414 3.33e-161

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: 459.86  E-value: 3.33e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   3 KVLVIGGGARESALALKFSQSPQVDHVYVAPGNPAMELLGvEPIGIKEKEVPALIKFAQTHQIDLTFVGPEVPLAAGIVD 82
Cdd:COG0151    2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA-ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  83 DFQAIGLPIFGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGVVIANDAA 162
Cdd:COG0151   81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 163 TLDDTIEQFYAGHP----DATVLLEEYLAGEEASVMALFNDQKRVILPLSQDHKRRHAADRGPNTGGMGAISPLPQFKPD 238
Cdd:COG0151  161 EALAAVDDMLADGKfgdaGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 239 QVQAAQSLV-DATLAGMHQDGLNGHGVMYIGLIFTKEGPKILEYNMRFGDPETQVLLPQIENDFYQLVSDLLDGQ--QPT 315
Cdd:COG0151  241 LLEKIMEEIiEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRldEVE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 316 LKLNGQAYACFVAVNPDYPRA--------NLKTVP---VIVptnwpigtwLPAGVERTDNGWISDAGRIFSVVAGAVTLP 384
Cdd:COG0151  321 LEWDDRAAVCVVLASGGYPGSyekgdvitGLEEAEaegVKV---------FHAGTALEDGKLVTNGGRVLGVTALGDTLE 391

                        410       420       430
                 ....*....|....*....|....*....|...
gi 504382656 385 EAVAKAKHDLESIQgvLD---YRTDIGFHALKG 414
Cdd:COG0151  392 EARERAYEAVEKIR--FEgmfYRRDIGWRALKR 422
purD TIGR00877
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ...
 3-413 3.29e-126

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: 371.26  E-value: 3.29e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656    3 KVLVIGGGARESALALKFSQSPQVDHVYVAPGNPAMELLG-VEPIGIKEKEVPALIKFAQTHQIDLTFVGPEVPLAAGIV 81
Cdd:TIGR00877   2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAkNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   82 DDFQAIGLPIFGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGVVIANDA 161
Cdd:TIGR00877  82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  162 ----ATLDDTIEQ--FYAGHPdatVLLEEYLAGEEASVMAlFNDQKRVI-LPLSQDHKRRHAADRGPNTGGMGAISPLPQ 234
Cdd:TIGR00877 162 eeaiKAVEDILEQkfGDAGER---VVIEEFLDGEEFSLLA-FVDGKTVIpMPPAQDHKRALEGDKGPNTGGMGAYSPAPV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  235 FKPDQVQAAQS-LVDATLAGMHQDGLNGHGVMYIGLIFTKEGPKILEYNMRFGDPETQVLLPQIENDFYQLVSDLLDGQ- 312
Cdd:TIGR00877 238 FTEEVERRIAEeIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKl 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  313 -QPTLKLNGQAYACFVAVNPDYPRANLKTVPVivpTNWPI-----GTWLPAGVERTDNGWISDAGRIFSVVAGAVTLPEA 386
Cdd:TIGR00877 318 dEVELRFDNRAAVTVVLASEGYPEDYRKGDPI---TGEPLaeaegVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEA 394

                         410       420
                  ....*....|....*....|....*...
gi 504382656  387 VAKAKHDLESIQG-VLDYRTDIGFHALK 413
Cdd:TIGR00877 395 RERAYEAVEYIKFeGMFYRKDIGFRALE 422
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 5-413 4.21e-88

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 273.92  E-value: 4.21e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   5 LVIGGGARESALALKFSQSPQVDHVYVAPGNPAMELLG-VEPIG-IKEKEVPALIKFAQTHQIDLTFVGPEVPLAAGIVD 82
Cdd:PLN02257   1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGdATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  83 DFQAIGLPIFGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGVVIANDA- 161
Cdd:PLN02257  81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 162 ---ATLDDTIEQFYAGHPDATVLLEEYLAGEEASVMALFNDQKRVILPLSQDHKRRHAADRGPNTGGMGAISPLPQFKPD 238
Cdd:PLN02257 161 eayEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 239 -QVQAAQSLVDATLAGMHQDGLNGHGVMYIGLIFTKEG--PKILEYNMRFGDPETQVLLPQIENDFYQLVSDLLDGQQPT 315
Cdd:PLN02257 241 lESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 316 LKLN---GQAYACFVAVNpDYPRA--------NLKTVPVIVPTN--WPIGTWLPAgvertDNGWISDAGRIFSVVAGAVT 382
Cdd:PLN02257 321 VSLTwspDSAMVVVMASN-GYPGSykkgtvikNLDEAEAVAPGVkvFHAGTALDS-----DGNVVAAGGRVLGVTAKGKD 394

                        410       420       430
                 ....*....|....*....|....*....|....
gi 504382656 383 LPEAVAKAKHDLESIQ---GVldYRTDIGFHALK 413
Cdd:PLN02257 395 IAEARARAYDAVDQIDwpgGF--FRRDIGWRAVA 426
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 103-290 7.09e-62

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: 198.27  E-value: 7.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  103 SSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLP-LVLKKDGLAAGKGVVIANDAA----TLDDTIEQFYAGHPD 177
Cdd:pfam01071   1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPaIVVKADGLAAGKGVIVASSNEeaikAVDEILEQKKFGEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  178 ATVLLEEYLAGEEASVMAlFNDQKRVI-LPLSQDHKRRHAADRGPNTGGMGAISPLPQFKPDQVQAAQ-SLVDATLAGMH 255
Cdd:pfam01071  81 ETVVIEEFLEGEEVSVLA-FVDGKTVKpLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKeTIVEPTVDGLR 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 504382656  256 QDGLNGHGVMYIGLIFTKEGPKILEYNMRFGDPET 290
Cdd:pfam01071 160 KEGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
 
Name Accession Description Interval E-value
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 3-414 3.33e-161

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: 459.86  E-value: 3.33e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   3 KVLVIGGGARESALALKFSQSPQVDHVYVAPGNPAMELLGvEPIGIKEKEVPALIKFAQTHQIDLTFVGPEVPLAAGIVD 82
Cdd:COG0151    2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA-ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  83 DFQAIGLPIFGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGVVIANDAA 162
Cdd:COG0151   81 AFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 163 TLDDTIEQFYAGHP----DATVLLEEYLAGEEASVMALFNDQKRVILPLSQDHKRRHAADRGPNTGGMGAISPLPQFKPD 238
Cdd:COG0151  161 EALAAVDDMLADGKfgdaGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVTEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 239 QVQAAQSLV-DATLAGMHQDGLNGHGVMYIGLIFTKEGPKILEYNMRFGDPETQVLLPQIENDFYQLVSDLLDGQ--QPT 315
Cdd:COG0151  241 LLEKIMEEIiEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRldEVE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 316 LKLNGQAYACFVAVNPDYPRA--------NLKTVP---VIVptnwpigtwLPAGVERTDNGWISDAGRIFSVVAGAVTLP 384
Cdd:COG0151  321 LEWDDRAAVCVVLASGGYPGSyekgdvitGLEEAEaegVKV---------FHAGTALEDGKLVTNGGRVLGVTALGDTLE 391

                        410       420       430
                 ....*....|....*....|....*....|...
gi 504382656 385 EAVAKAKHDLESIQgvLD---YRTDIGFHALKG 414
Cdd:COG0151  392 EARERAYEAVEKIR--FEgmfYRRDIGWRALKR 422
purD TIGR00877
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ...
 3-413 3.29e-126

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: 371.26  E-value: 3.29e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656    3 KVLVIGGGARESALALKFSQSPQVDHVYVAPGNPAMELLG-VEPIGIKEKEVPALIKFAQTHQIDLTFVGPEVPLAAGIV 81
Cdd:TIGR00877   2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAkNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   82 DDFQAIGLPIFGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGVVIANDA 161
Cdd:TIGR00877  82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  162 ----ATLDDTIEQ--FYAGHPdatVLLEEYLAGEEASVMAlFNDQKRVI-LPLSQDHKRRHAADRGPNTGGMGAISPLPQ 234
Cdd:TIGR00877 162 eeaiKAVEDILEQkfGDAGER---VVIEEFLDGEEFSLLA-FVDGKTVIpMPPAQDHKRALEGDKGPNTGGMGAYSPAPV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  235 FKPDQVQAAQS-LVDATLAGMHQDGLNGHGVMYIGLIFTKEGPKILEYNMRFGDPETQVLLPQIENDFYQLVSDLLDGQ- 312
Cdd:TIGR00877 238 FTEEVERRIAEeIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKl 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  313 -QPTLKLNGQAYACFVAVNPDYPRANLKTVPVivpTNWPI-----GTWLPAGVERTDNGWISDAGRIFSVVAGAVTLPEA 386
Cdd:TIGR00877 318 dEVELRFDNRAAVTVVLASEGYPEDYRKGDPI---TGEPLaeaegVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEA 394

                         410       420
                  ....*....|....*....|....*...
gi 504382656  387 VAKAKHDLESIQG-VLDYRTDIGFHALK 413
Cdd:TIGR00877 395 RERAYEAVEYIKFeGMFYRKDIGFRALE 422
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 5-413 4.21e-88

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 273.92  E-value: 4.21e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   5 LVIGGGARESALALKFSQSPQVDHVYVAPGNPAMELLG-VEPIG-IKEKEVPALIKFAQTHQIDLTFVGPEVPLAAGIVD 82
Cdd:PLN02257   1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGdATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  83 DFQAIGLPIFGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGVVIANDA- 161
Cdd:PLN02257  81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 162 ---ATLDDTIEQFYAGHPDATVLLEEYLAGEEASVMALFNDQKRVILPLSQDHKRRHAADRGPNTGGMGAISPLPQFKPD 238
Cdd:PLN02257 161 eayEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 239 -QVQAAQSLVDATLAGMHQDGLNGHGVMYIGLIFTKEG--PKILEYNMRFGDPETQVLLPQIENDFYQLVSDLLDGQQPT 315
Cdd:PLN02257 241 lESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 316 LKLN---GQAYACFVAVNpDYPRA--------NLKTVPVIVPTN--WPIGTWLPAgvertDNGWISDAGRIFSVVAGAVT 382
Cdd:PLN02257 321 VSLTwspDSAMVVVMASN-GYPGSykkgtvikNLDEAEAVAPGVkvFHAGTALDS-----DGNVVAAGGRVLGVTAKGKD 394

                        410       420       430
                 ....*....|....*....|....*....|....
gi 504382656 383 LPEAVAKAKHDLESIQ---GVldYRTDIGFHALK 413
Cdd:PLN02257 395 IAEARARAYDAVDQIDwpgGF--FRRDIGWRAVA 426
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 103-290 7.09e-62

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: 198.27  E-value: 7.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  103 SSKTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLP-LVLKKDGLAAGKGVVIANDAA----TLDDTIEQFYAGHPD 177
Cdd:pfam01071   1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPaIVVKADGLAAGKGVIVASSNEeaikAVDEILEQKKFGEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  178 ATVLLEEYLAGEEASVMAlFNDQKRVI-LPLSQDHKRRHAADRGPNTGGMGAISPLPQFKPDQVQAAQ-SLVDATLAGMH 255
Cdd:pfam01071  81 ETVVIEEFLEGEEVSVLA-FVDGKTVKpLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKeTIVEPTVDGLR 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 504382656  256 QDGLNGHGVMYIGLIFTKEGPKILEYNMRFGDPET 290
Cdd:pfam01071 160 KEGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
GARS_N pfam02844
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ...
 3-102 3.65e-45

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: 151.35  E-value: 3.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656    3 KVLVIGGGARESALALKFSQSPQVDHVYVAPGNPAMELLGvEPIGIKEKEVPALIKFAQTHQIDLTFVGPEVPLAAGIVD 82
Cdd:pfam02844   2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLA-ECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIVD 80

                          90       100
                  ....*....|....*....|..
gi 504382656   83 DF--QAIGLPIFGVTQKLAQLE 102
Cdd:pfam02844  81 ALreRAAGIPVFGPSKAAAQLE 102
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 55-286 2.02e-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: 78.76  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  55 ALIKFAQTHQID--LTFVGPEVPLAAGIVDDFqaiGLPifGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHSAIEAH 132
Cdd:COG0439    8 AAAELARETGIDavLSESEFAVETAAELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 133 AEATLMGLPLVLKKDGLAAGKGVVIANDAATLDDTIEQF----YAGHPDATVLLEEYLAGEEASVMALFNDQKRVILPLS 208
Cdd:COG0439   83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAraeaKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSIT 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504382656 209 qdhkRRHaaDRGPNTGGMGAISPLPqFKPDQVQAAQSLVDATLAGMhqdGLNgHGVMYIGLIFTKEG-PKILEYNMRFG 286
Cdd:COG0439  163 ----RKH--QKPPYFVELGHEAPSP-LPEELRAEIGELVARALRAL---GYR-RGAFHTEFLLTPDGePYLIEINARLG 230
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 1-286 1.13e-09

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 59.13  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   1 MKKVLVIGGGARESAL-ALKFSQSPqvDHVYVA---PGNPAMELlGVEPI---GIKEKE-VPALIKFAQTHQIDLTFVG- 71
Cdd:PRK12767   1 MMNILVTSAGRRVQLVkALKKSLLK--GRVIGAdisELAPALYF-ADKFYvvpKVTDPNyIDRLLDICKKEKIDLLIPLi 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  72 -PEVPLAAGIVDDFQAIGLPIFGVTQKLAQLESSKTFAKAFMHRHHLPTAASKTVHS--AIEAHAEATLMGLPLVLKKDG 148
Cdd:PRK12767  78 dPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESleDFKAALAKGELQFPLFVKPRD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 149 LAAGKGVVIANDAATLddtiEQFYAGHPDatVLLEEYLAGEEASVMALFNDQKRV--ILPLSQDHKRRHAADRG---PNt 223
Cdd:PRK12767 158 GSASIGVFKVNDKEEL----EFLLEYVPN--LIIQEFIEGQEYTVDVLCDLNGEVisIVPRKRIEVRAGETSKGvtvKD- 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504382656 224 ggmgaisplpqfkPDQVQAAQSLVDAtlagmhqdgLNGHGVMYIGLIFTKEGPKILEYNMRFG 286
Cdd:PRK12767 231 -------------PELFKLAERLAEA---------LGARGPLNIQCFVTDGEPYLFEINPRFG 271
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 105-282 1.22e-06

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: 49.55  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 105 KTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGVVIANDAATLDDTIEQFyAGHPDATVLLEE 184
Cdd:COG0189   97 KLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEAL-TELGSEPVLVQE 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 185 YLAGEEASvmalfnDqKRVIL----PL-------SQDHKRRHAADrgpntGGMGAISPLPqfkPDQVQAAQSLVDATlag 253
Cdd:COG0189  176 FIPEEDGR------D-IRVLVvggePVaairripAEGEFRTNLAR-----GGRAEPVELT---DEERELALRAAPAL--- 237

                        170       180       190
                 ....*....|....*....|....*....|.
gi 504382656 254 mhqdglnghGVMYIG--LIFTKEGPKILEYN 282
Cdd:COG0189  238 ---------GLDFAGvdLIEDDDGPLVLEVN 259
GARS_C pfam02843
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ...
 357-409 1.25e-06

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: 46.29  E-value: 1.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 504382656  357 AGVERTDNGWISDAGRIFSVVAGAVTLPEAVAKAKHDLESIQgvLD---YRTDIGF 409
Cdd:pfam02843  34 AGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKID--FEgmfYRKDIGT 87
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 76-188 2.02e-06

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 49.88  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  76 LAAGIVDDFQAIGLPIFGVTQK-LAQLESSKTFaKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKkdglAA--- 151
Cdd:COG0458   86 LAVELEEAGILEGVKILGTSPDaIDLAEDRELF-KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVR----PSyvl 160

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504382656 152 -GKGVVIANDAATLDDTIEQFYAGHPDATVLLEEYLAG 188
Cdd:COG0458  161 gGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLG 198
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 105-207 6.35e-06

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 47.80  E-value: 6.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 105 KTFAKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKdgLAAGK--GVVIANDAATLDDTIEqfYAGHPDATVLL 182
Cdd:PRK01372  99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALE--LAFKYDDEVLV 174

                         90       100
                 ....*....|....*....|....*
gi 504382656 183 EEYLAGEEASVmALFNDQkrvILPL 207
Cdd:PRK01372 175 EKYIKGRELTV-AVLGGK---ALPV 195
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 88-195 7.12e-06

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 47.84  E-value: 7.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  88 GLPIFGVTQ-KLAQlessktfaKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKkdglAA-----GKGVVIANDA 161
Cdd:PRK06019  91 GPDALAIAQdRLTE--------KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLK----TRrggydGKGQWVIRSA 158

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504382656 162 ATLDDTIEQFyaghPDATVLLEEYLAGE-EASVMA 195
Cdd:PRK06019 159 EDLEAAWALL----GSVPCILEEFVPFErEVSVIV 189
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 78-188 1.93e-05

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 46.92  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656    78 AGIVDDF--QAIGLPIfgvtQKLAQLESSKTFaKAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLAAGKGV 155
Cdd:TIGR01369  104 SGVLEKYgvEVLGTPV----EAIKKAEDRELF-REAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGG 178

                           90       100       110
                   ....*....|....*....|....*....|...
gi 504382656   156 VIANDAATLDDTIEQFYAGHPDATVLLEEYLAG 188
Cdd:TIGR01369  179 GIAYNREELKEIAERALSASPINQVLVEKSLAG 211
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 109-195 1.97e-05

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 46.22  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656 109 KAFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKkdglAA-----GKGVVIANDAatldDTIEQFYAGHPDATVLLE 183
Cdd:COG0026   94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLK----TRrggydGKGQVVIKSA----ADLEAAWAALGGGPCILE 165

                         90
                 ....*....|...
gi 504382656 184 EYLAGE-EASVMA 195
Cdd:COG0026  166 EFVPFErELSVIV 178
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 2-188 2.12e-05

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 46.89  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656    2 KKVLVIGGG-------------ARESALALKfSQSPQVdhVYVAPgNPA-------------MELLGVEPIG-IKEKEVP 54
Cdd:PRK12815    8 QKILVIGSGpivigqaaefdysGTQACLALK-EEGYQV--VLVNP-NPAtimtdpapadtvyFEPLTVEFVKrIIAREKP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   55 -ALI-KFAQTHQIDLTFvgpEVpLAAGIVDDF--QAIGLPIfgvtQKLAQLESSKTFaKAFMHRHHLPTAASKTVHSAIE 130
Cdd:PRK12815   84 dALLaTLGGQTALNLAV---KL-HEDGILEQYgvELLGTNI----EAIQKGEDRERF-RALMKELGEPVPESEIVTSVEE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 504382656  131 AHAEATLMGLPLVLKKDGLAAGKGVVIANDAATLDDTIEQFYAGHPDATVLLEEYLAG 188
Cdd:PRK12815  155 ALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAG 212
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 133-288 2.49e-05

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 44.30  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  133 AEATLMGLPLVLKKDGLAAGKGVVIANDAATLDDTIEQfyaghpdatVLLEEYLAGEEASVMALFNDQKRVILPLSqdhk 212
Cdd:pfam02655  25 EELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIEN---------VLVQEFIEGEPLSVSLLSDGEKALPLSVN---- 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504382656  213 RRHAADRGPNTGGMGAISPLPQFKPDQVQAAQSLVDATLAGMHqdGLNGhgvmyIGLIFTKEGPKILEYNMRFGDP 288
Cdd:pfam02655  92 RQYIDNGGSGFVYAGNVTPSRTELKEEIIELAEEVVECLPGLR--GYVG-----VDLVLKDNEPYVIEVNPRITTS 160
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 68-284 2.61e-04

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: 43.45  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656    68 TFVGPEVPLaaGIVDDFQAIGLPIFGVTQK-LAQLESSKTFAKaFMHRHHLPTAASKTVHSAIEAHAEATLMGLPLVLKK 146
Cdd:TIGR01369  635 VQFGGQTPL--NLAKALEEAGVPILGTSPEsIDRAEDREKFSE-LLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRP 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656   147 DGLAAGKGVVIANDAATLDDTIEQFYAGHPDATVLLEEYL-AGEEASVMALFNDQKRVILPLSQdhkrrHAADRGPNTGG 225
Cdd:TIGR01369  712 SYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGIME-----HIEEAGVHSGD 786

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 504382656   226 MGAISPLPQFKPDQVQAAQSLVDAtLAgmhqDGLNGHGVMYIGLIFTKEGPKILEYNMR 284
Cdd:TIGR01369  787 STCVLPPQTLSAEIVDRIKDIVRK-IA----KELNVKGLMNIQFAVKDGEVYVIEVNPR 840
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 139-205 6.65e-04

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: 39.96  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  139 GLPLVLKKDGLAAGKGVVIANDA-------ATLDDTIEQFYAGHPDATV-----LLEEYLAGEEASVMALFNDQ-KRVIL 205
Cdd:pfam13535   2 PYPCVIKPSVGFFSVGVYKINNReewkaafAAIREEIEQWKEMYPEAVVdggsfLVEEYIEGEEFAVDAYFDENgEPVIL 81
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 114-195 7.67e-04

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: 39.93  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504382656  114 RHHLPTAASKTVHSAIEAHAEATLMGLPLVLKKDGLA-AGKGVVIANDAAtlddTIEQFYAGHPDATVLLEEYLAGE-EA 191
Cdd:pfam02222   2 KLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEA----DLPQAWEELGDGPVIVEEFVPFDrEL 77


                  ....
gi 504382656  192 SVMA 195
Cdd:pfam02222  78 SVLV 81
 
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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