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Conserved domains on  [gi|529140837|ref|WP_020931632|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Candidatus Karelsulcia muelleri]

Protein Classification

N-acetyl-gamma-glutamyl-phosphate reductase( domain architecture ID 11414156)

N-acetyl-gamma-glutamyl-phosphate reductase catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to N-acetyl-L-glutamate 5-semialdehyde, as part of the L-arginine biosynthesis

CATH:  3.40.50.720
EC:  1.2.1.38
Gene Ontology:  GO:0051287|GO:0070401|GO:0008652|GO:0016620|GO:0003942
PubMed:  17316682
SCOP:  4000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 12-323 4.12e-123

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


:

Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 356.69  E-value: 4.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  12 YTANELIKILINHPKVEIKTIVSTTYPGLPIEDIHKDLIGEIKNKklFSS----EISDDIDLLFLCIGHGHSKKILKN-I 86
Cdd:COG0002   11 YTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLV--FEPpdpdELAAGCDVVFLALPHGVSMELAPElL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  87 SSKINVIDMSNDFRINQNFFFKK------------RIFHYGLPELNKNIINKYKNIANPGCFATAIQLSILPLAKRKLLK 154
Cdd:COG0002   89 EAGVKVIDLSADFRLKDPAVYEKwygfehaapellGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAPLLKAGLID 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 155 -NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNQyDGKIYFIPYRGGFSRGIISTLYT 233
Cdd:COG0002  169 pDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGE-DVKVSFTPHLVPMVRGILATIYA 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 234 RI--DLSFEEVKNLYDRFYKNNPFIFISEKE--IHLKQVINTNKCILNLKYIK--NKLIITSIIDNLIKGASGQAVQNLN 307
Cdd:COG0002  248 RLkdGVTEEDLRAAYEEFYADEPFVRVLPEGrlPETKSVRGSNFCDIGVAVDErtGRLVVVSAIDNLVKGAAGQAVQNMN 327

                        330
                 ....*....|....*.
gi 529140837 308 LMYNFEETCGLKLKPL 323
Cdd:COG0002  328 LMFGLPETTGLELVPL 343
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 12-323 4.12e-123

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 356.69  E-value: 4.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  12 YTANELIKILINHPKVEIKTIVSTTYPGLPIEDIHKDLIGEIKNKklFSS----EISDDIDLLFLCIGHGHSKKILKN-I 86
Cdd:COG0002   11 YTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLV--FEPpdpdELAAGCDVVFLALPHGVSMELAPElL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  87 SSKINVIDMSNDFRINQNFFFKK------------RIFHYGLPELNKNIINKYKNIANPGCFATAIQLSILPLAKRKLLK 154
Cdd:COG0002   89 EAGVKVIDLSADFRLKDPAVYEKwygfehaapellGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAPLLKAGLID 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 155 -NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNQyDGKIYFIPYRGGFSRGIISTLYT 233
Cdd:COG0002  169 pDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGE-DVKVSFTPHLVPMVRGILATIYA 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 234 RI--DLSFEEVKNLYDRFYKNNPFIFISEKE--IHLKQVINTNKCILNLKYIK--NKLIITSIIDNLIKGASGQAVQNLN 307
Cdd:COG0002  248 RLkdGVTEEDLRAAYEEFYADEPFVRVLPEGrlPETKSVRGSNFCDIGVAVDErtGRLVVVSAIDNLVKGAAGQAVQNMN 327

                        330
                 ....*....|....*.
gi 529140837 308 LMYNFEETCGLKLKPL 323
Cdd:COG0002  328 LMFGLPETTGLELVPL 343
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 12-323 1.99e-96

N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273832 [Multi-domain]  Cd Length: 346  Bit Score: 289.10  E-value: 1.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837   12 YTANELIKILINHPKVEIKTIV-STTYPGLPIEDIHKDLIGEIkNKKLFS---SEISDDIDLLFLCIGHGHSKKI-LKNI 86
Cdd:TIGR01850  11 YTGGELLRLLLNHPEVEITYLVsSRESAGKPVSEVHPHLRGLV-DLNLEPidvEEILEDADVVFLALPHGVSAELaPELL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837   87 SSKINVIDMSNDFRINQNFFFKK--RIFH----------YGLPELNKNIINKYKNIANPGCFATAIQLSILPLAKRKLLK 154
Cdd:TIGR01850  90 AAGVKVIDLSADFRLKDPELYEKwyGFEHagpellqkavYGLPELHREEIKGARLIANPGCYPTATLLALAPLLKEGLID 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  155 -NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNQyDGKIYFIPYRGGFSRGIISTLYT 233
Cdd:TIGR01850 170 pTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGG-KVKVSFTPHLVPMTRGILATIYA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  234 RI--DLSFEEVKNLYDRFYKNNPFIFISEKEI--HLKQVINTNKCILNLKYIK--NKLIITSIIDNLIKGASGQAVQNLN 307
Cdd:TIGR01850 249 KLkdGLTEEDLRALYEEFYADEPFVRVLPEGGypSTKAVIGSNFCDIGFAVDErtGRVVVVSAIDNLVKGAAGQAVQNMN 328

                         330
                  ....*....|....*.
gi 529140837  308 LMYNFEETCGLKLKPL 323
Cdd:TIGR01850 329 LMFGFDETTGLPFPPL 344
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 134-298 7.58e-61

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both, the arginine and lysine, biosynthetic pathways.


Pssm-ID: 467683  Cd Length: 171  Bit Score: 191.92  E-value: 7.58e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 134 GCFATAIQLSILPLAKRKLLK-NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNQyDG 212
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEpDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGE-DV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 213 KIYFIPYRGGFSRGIISTLYTRI--DLSFEEVKNLYDRFYKNNPFIFISEKEI--HLKQVINTNKCILNLKY--IKNKLI 286
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLkdGVTAEDVRALYEEFYADEPFVRVLPEGQlpSTKAVRGSNFCDIGVAVdgRTGRLI 159

                        170
                 ....*....|..
gi 529140837 287 ITSIIDNLIKGA 298
Cdd:cd23934  160 VVSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 12-323 1.12e-57

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 190.42  E-value: 1.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  12 YTANELIKILINHPKVEIKTI---------VSTTYPGLPIEDIHKDLigEIKnKKLFSseisdDIDLLFLCIGHGHSKKI 82
Cdd:PLN02968  49 YTGAEVRRLLANHPDFEITVMtadrkagqsFGSVFPHLITQDLPNLV--AVK-DADFS-----DVDAVFCCLPHGTTQEI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  83 LKNISSKINVIDMSNDFRINQNFFFKKRIFH------------YGLPELNKNIINKYKNIANPGCFATAIQLSILPLAKR 150
Cdd:PLN02968 121 IKALPKDLKIVDLSADFRLRDIAEYEEWYGHphrapelqkeavYGLTELQREEIKSARLVANPGCYPTGIQLPLVPLVKA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 151 KLLK-NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKlQNQYDGKIYFIPYRGGFSRGIIS 229
Cdd:PLN02968 201 GLIEpDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLAD-AAGSKVTPSFTPHLMPMSRGMQS 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 230 TLYTRIDlSFEEVKNLYDRF---YKNNPFIFISEKEI--HLKQVINTNKCILNL--KYIKNKLIITSIIDNLIKGASGQA 302
Cdd:PLN02968 280 TVYVHYA-PGVTAEDLHQHLkerYEGEEFVKVLERGAvpHTDHVRGSNYCELNVfaDRIPGRAIIISVIDNLVKGASGQA 358

                        330       340
                 ....*....|....*....|.
gi 529140837 303 VQNLNLMYNFEETCGLKLKPL 323
Cdd:PLN02968 359 VQNLNLMMGLPETTGLLQQPL 379
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 9-127 3.36e-16

Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 73.74  E-value: 3.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837     9 GAGYTANELIKILINHPKVEIKTIVST-TYPGLPIEDIHKDLIGEIKNKKLFSSEISDDIDLLFLCIGHGHSKKI----L 83
Cdd:smart00859   7 ATGYVGQELLRLLAEHPDFELTALAASsRSAGKKVSEAGPHLKGEVVLELDPPDFEELAVDIVFLALPHGVSKESapllP 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 529140837    84 KNISSKINVIDMSNDFRINQNfffkkriFHYGLPELNKNIINKY 127
Cdd:smart00859  87 RAAAAGAVVIDLSSAFRMDDD-------VPYGLPEVNPEAIKKA 123
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 9-120 3.98e-16

Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 73.33  E-value: 3.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837    9 GAGYTANELIKILINHPKVEIKTIVSTTYP-GLPIEDIHKDLIGeIKNKKL--FSSEISDDIDLLFLCIGHGHSKKILKN 85
Cdd:pfam01118   7 ATGYVGQELLRLLEEHPPVELVVLFASSRSaGKKLAFVHPILEG-GKDLVVedVDPEDFKDVDIVFFALPGGVSKEIAPK 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 529140837   86 I-SSKINVIDMSNDFRINQNFFfkkrifhYGLPELN 120
Cdd:pfam01118  86 LaEAGAKVIDLSSDFRMDDDVP-------YGLPEVN 114
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 12-323 4.12e-123

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 356.69  E-value: 4.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  12 YTANELIKILINHPKVEIKTIVSTTYPGLPIEDIHKDLIGEIKNKklFSS----EISDDIDLLFLCIGHGHSKKILKN-I 86
Cdd:COG0002   11 YTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLV--FEPpdpdELAAGCDVVFLALPHGVSMELAPElL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  87 SSKINVIDMSNDFRINQNFFFKK------------RIFHYGLPELNKNIINKYKNIANPGCFATAIQLSILPLAKRKLLK 154
Cdd:COG0002   89 EAGVKVIDLSADFRLKDPAVYEKwygfehaapellGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAPLLKAGLID 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 155 -NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNQyDGKIYFIPYRGGFSRGIISTLYT 233
Cdd:COG0002  169 pDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGE-DVKVSFTPHLVPMVRGILATIYA 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 234 RI--DLSFEEVKNLYDRFYKNNPFIFISEKE--IHLKQVINTNKCILNLKYIK--NKLIITSIIDNLIKGASGQAVQNLN 307
Cdd:COG0002  248 RLkdGVTEEDLRAAYEEFYADEPFVRVLPEGrlPETKSVRGSNFCDIGVAVDErtGRLVVVSAIDNLVKGAAGQAVQNMN 327

                        330
                 ....*....|....*.
gi 529140837 308 LMYNFEETCGLKLKPL 323
Cdd:COG0002  328 LMFGLPETTGLELVPL 343
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 12-323 1.99e-96

N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273832 [Multi-domain]  Cd Length: 346  Bit Score: 289.10  E-value: 1.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837   12 YTANELIKILINHPKVEIKTIV-STTYPGLPIEDIHKDLIGEIkNKKLFS---SEISDDIDLLFLCIGHGHSKKI-LKNI 86
Cdd:TIGR01850  11 YTGGELLRLLLNHPEVEITYLVsSRESAGKPVSEVHPHLRGLV-DLNLEPidvEEILEDADVVFLALPHGVSAELaPELL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837   87 SSKINVIDMSNDFRINQNFFFKK--RIFH----------YGLPELNKNIINKYKNIANPGCFATAIQLSILPLAKRKLLK 154
Cdd:TIGR01850  90 AAGVKVIDLSADFRLKDPELYEKwyGFEHagpellqkavYGLPELHREEIKGARLIANPGCYPTATLLALAPLLKEGLID 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  155 -NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNQyDGKIYFIPYRGGFSRGIISTLYT 233
Cdd:TIGR01850 170 pTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGG-KVKVSFTPHLVPMTRGILATIYA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  234 RI--DLSFEEVKNLYDRFYKNNPFIFISEKEI--HLKQVINTNKCILNLKYIK--NKLIITSIIDNLIKGASGQAVQNLN 307
Cdd:TIGR01850 249 KLkdGLTEEDLRALYEEFYADEPFVRVLPEGGypSTKAVIGSNFCDIGFAVDErtGRVVVVSAIDNLVKGAAGQAVQNMN 328

                         330
                  ....*....|....*.
gi 529140837  308 LMYNFEETCGLKLKPL 323
Cdd:TIGR01850 329 LMFGFDETTGLPFPPL 344
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 134-298 7.58e-61

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both, the arginine and lysine, biosynthetic pathways.


Pssm-ID: 467683  Cd Length: 171  Bit Score: 191.92  E-value: 7.58e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 134 GCFATAIQLSILPLAKRKLLK-NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNQyDG 212
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEpDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGE-DV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 213 KIYFIPYRGGFSRGIISTLYTRI--DLSFEEVKNLYDRFYKNNPFIFISEKEI--HLKQVINTNKCILNLKY--IKNKLI 286
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLkdGVTAEDVRALYEEFYADEPFVRVLPEGQlpSTKAVRGSNFCDIGVAVdgRTGRLI 159

                        170
                 ....*....|..
gi 529140837 287 ITSIIDNLIKGA 298
Cdd:cd23934  160 VVSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 12-323 1.12e-57

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 190.42  E-value: 1.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  12 YTANELIKILINHPKVEIKTI---------VSTTYPGLPIEDIHKDLigEIKnKKLFSseisdDIDLLFLCIGHGHSKKI 82
Cdd:PLN02968  49 YTGAEVRRLLANHPDFEITVMtadrkagqsFGSVFPHLITQDLPNLV--AVK-DADFS-----DVDAVFCCLPHGTTQEI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  83 LKNISSKINVIDMSNDFRINQNFFFKKRIFH------------YGLPELNKNIINKYKNIANPGCFATAIQLSILPLAKR 150
Cdd:PLN02968 121 IKALPKDLKIVDLSADFRLRDIAEYEEWYGHphrapelqkeavYGLTELQREEIKSARLVANPGCYPTGIQLPLVPLVKA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 151 KLLK-NNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKlQNQYDGKIYFIPYRGGFSRGIIS 229
Cdd:PLN02968 201 GLIEpDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLAD-AAGSKVTPSFTPHLMPMSRGMQS 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 230 TLYTRIDlSFEEVKNLYDRF---YKNNPFIFISEKEI--HLKQVINTNKCILNL--KYIKNKLIITSIIDNLIKGASGQA 302
Cdd:PLN02968 280 TVYVHYA-PGVTAEDLHQHLkerYEGEEFVKVLERGAvpHTDHVRGSNYCELNVfaDRIPGRAIIISVIDNLVKGASGQA 358

                        330       340
                 ....*....|....*....|.
gi 529140837 303 VQNLNLMYNFEETCGLKLKPL 323
Cdd:PLN02968 359 VQNLNLMMGLPETTGLLQQPL 379
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 9-133 3.14e-31

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both the arginine and lysine biosynthetic pathways.


Pssm-ID: 467521 [Multi-domain]  Cd Length: 170  Bit Score: 115.22  E-value: 3.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837   9 GAGYTANELIKILINHPKVEIKTIVSTTYPGLPIEDIHKDLIGEI--KNKKLFSSEISDDIDLLFLCIGHGHSKKILKN- 85
Cdd:cd17895    8 ASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTdlTFEPDDDEEIAEDADVVFLALPHGVSMELAPKl 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  86 ISSKINVIDMSNDFRINQNFFFKK------------RIFHYGLPELNKNIINKYKNIANP 133
Cdd:cd17895   88 LEAGVKVIDLSADFRLKDPETYEKwygfehaapellKEAVYGLPELNREEIKKARLVANP 147
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 134-298 2.27e-26

C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY; EC 1.2.1.103/EC 1.2.1.106) is involved in both, the arginine and lysine, biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LysY is the third enzyme in lysine biosynthesis from AAA. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor.


Pssm-ID: 467688  Cd Length: 174  Bit Score: 102.70  E-value: 2.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 134 GCFATAIQLSILPLAKRKLLKNN-LHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNQydG 212
Cdd:cd23939    1 GCNATASILALYPLVKAGLLDDErIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGLLARE--I 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 213 KIYFIPYRGGFSRGIISTLYTRI--DLSFEEVKNLYDRFYKNNPFI-FISEKE-IH----LKQVINTNKCILNLKY--IK 282
Cdd:cd23939   79 SVSFTAHSVDMVRGILATAHVFLkeGVTEKDLWKAYRKAYGNEPFVrIVKDRKgIYrypdPKLVIGSNFCDIGFELdeDN 158

                        170
                 ....*....|....*.
gi 529140837 283 NKLIITSIIDNLIKGA 298
Cdd:cd23939  159 GRLVVFSAIDNLMKGA 174
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 135-298 5.88e-26

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways.


Pssm-ID: 467675  Cd Length: 166  Bit Score: 101.42  E-value: 5.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 135 CFATAIQLSILPLAKRKLLKNN-LHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNqydgk 213
Cdd:cd18125    1 CYATAALLALYPLLKAGLLKPTpITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNLGGKHN----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 214 IYFIPYRGGFSRGIISTLYTRID--LSFEEVKNLYDRFYKNNPFIFISEKEIHL--KQVINTNKCILNLKYIKN--KLII 287
Cdd:cd18125   76 VHFTPHVGPWVRGILMTIQCFTQkgWSLRQLHEAYREAYAGEPFVRVMPQGKGPdpKFVQGTNYADIGVELEEDtgRLVV 155

                        170
                 ....*....|.
gi 529140837 288 TSIIDNLIKGA 298
Cdd:cd18125  156 MSAIDNLVKGA 166
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 134-298 3.50e-19

C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. This model corresponds to the AGPR C-terminal catalytic domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467685  Cd Length: 161  Bit Score: 83.07  E-value: 3.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 134 GCFATAIQLSILPLAkrKLLKNNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIqtikklqNQYDGK 213
Cdd:cd23936    1 GCYATGAQLALAPLL--DDLDGPPSVFGVSGYSGAGTKPSPKNDPEVLADNLIPYSLVGHIHEREVS-------RHLGTP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 214 IYFIPYRGGFSRGIISTLYTRID--LSFEEVKNLYDRFYKNNPFIFISEKEIHLKQVINTNKCIL---NLKYIKNKLIIT 288
Cdd:cd23936   72 VAFMPHVAPWFQGITLTISIPLKksMTADEIRELYQEAYAGEPLIKVTKEIPLVRDNAGKHGVVVggfTVHPDGKRVVVV 151

                        170
                 ....*....|
gi 529140837 289 SIIDNLIKGA 298
Cdd:cd23936  152 ATIDNLLKGA 161
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 9-133 1.27e-17

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467515 [Multi-domain]  Cd Length: 160  Bit Score: 78.76  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837   9 GAGYTANELIKILINHPKVEIKTIVSTTYPGLPIEDIHKDLIGEIKNKKLFSSEISDDIDLLFLCIGHGHSKKILKNISS 88
Cdd:cd02280    8 ASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIISLQIQEFRPCEVLNSADILVLALPHGASAELVAAISN 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 529140837  89 -KINVIDMSNDFRINQNFFFKKRI-------FHYGLPELNKNI-INKYKNIANP 133
Cdd:cd02280   88 pQVKIIDLSADFRFTDPEVYRRHPrpdleggWVYGLPELDREQrIANATRIANP 141
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 9-127 3.36e-16

Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 73.74  E-value: 3.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837     9 GAGYTANELIKILINHPKVEIKTIVST-TYPGLPIEDIHKDLIGEIKNKKLFSSEISDDIDLLFLCIGHGHSKKI----L 83
Cdd:smart00859   7 ATGYVGQELLRLLAEHPDFELTALAASsRSAGKKVSEAGPHLKGEVVLELDPPDFEELAVDIVFLALPHGVSKESapllP 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 529140837    84 KNISSKINVIDMSNDFRINQNfffkkriFHYGLPELNKNIINKY 127
Cdd:smart00859  87 RAAAAGAVVIDLSSAFRMDDD-------VPYGLPEVNPEAIKKA 123
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 9-120 3.98e-16

Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 73.33  E-value: 3.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837    9 GAGYTANELIKILINHPKVEIKTIVSTTYP-GLPIEDIHKDLIGeIKNKKL--FSSEISDDIDLLFLCIGHGHSKKILKN 85
Cdd:pfam01118   7 ATGYVGQELLRLLEEHPPVELVVLFASSRSaGKKLAFVHPILEG-GKDLVVedVDPEDFKDVDIVFFALPGGVSKEIAPK 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 529140837   86 I-SSKINVIDMSNDFRINQNFFfkkrifhYGLPELN 120
Cdd:pfam01118  86 LaEAGAKVIDLSSDFRMDDDVP-------YGLPEVN 114
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 12-131 1.38e-14

N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; LysY (EC 1.2.1.103/EC 1.2.1.106) is involved in both the arginine and lysine biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LysY is the third enzyme in lysine biosynthesis from AAA. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor. Members in this subfamily belong to the type 1 AGPR family. They contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467527 [Multi-domain]  Cd Length: 170  Bit Score: 70.38  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  12 YTANELIKILINHPKVEIKTIVSTTYPGLPIEDIHKDLIGeIKNKKLFSSEISDDIDLLFLCIGHGHSKKILKNISSKIN 91
Cdd:cd24151   11 YTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNLRG-RTLLKFVPPEELESCDVLFLALPHGESMKRIDRFAELAP 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 529140837  92 -VIDMSNDFRIN-----QNFFFKKRI-------FHYGLPELNKNIINKYKNIA 131
Cdd:cd24151   90 rIIDLSADFRLKdpaayDRWYGGPHPrpellerFVYGLPELHREELRGARYIA 142
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 9-134 5.11e-14

N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. The model corresponds to the AGPR N-terminal NAD(P)-binding domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467525 [Multi-domain]  Cd Length: 154  Bit Score: 68.29  E-value: 5.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837   9 GAGYTANELIKILINHPKVEIKTIVSTTYPGLPIEDIHKDLIGE--IKNKKLFSSEISDDIDLLFLCIGHGHSKKILKNI 86
Cdd:cd24149    8 ARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVSGYTKSPIDYlnLSVEDIPEEVAAREVDAWVLALPNGVAKPFVDAI 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 529140837  87 ---SSKINVIDMSNDFRINQNfffkkriFHYGLPELNKNIINKYKNIANPG 134
Cdd:cd24149   88 dkaNPKSVIVDLSADYRFDDA-------WTYGLPELNRRRIAGAKRISNPG 131
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 134-298 1.56e-12

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family.


Pssm-ID: 467684  Cd Length: 178  Bit Score: 64.93  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 134 GCFATAIQLSILPLAKRKLLKNNLHIS--AITGSTGAGR-------INNSKLNFSFRnnnisTYNL-FNHNHINEvIQTI 203
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPADYPLSihAVSGYSGGGKkmieqyeAAEAADLPPPR-----PYGLgLEHKHLPE-MQKH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 204 KKLqnqyDGKIYFIPYRGGFSRGIISTLYTRIDL-----SFEEVKNLYDRFYKNNPFIFI-----SEKEIHLK--QVINT 271
Cdd:cd23935   75 AGL----ARPPIFTPAVGNFYQGMLVTVPLHLDLlekgvSAAEVHEALAEHYAGERFVKVmpldePDALGFLDpqALNGT 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 529140837 272 NKCILnlkYI----KNKLIITSIIDNLIKGA 298
Cdd:cd23935  151 NNLEL---FVfgndKGQALLVARLDNLGKGA 178
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 12-141 1.50e-11

N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate reductase (actinobacAGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC). There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The family includes N-acetyl-gamma-glutamyl-phosphate reductases mainly from actinobacteria. They belong to the type 1 AGPR family. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467524 [Multi-domain]  Cd Length: 164  Bit Score: 61.92  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  12 YTANELIKILINHPKVEIKTIVSTTYPGLPIEDIHKDLiGEIKNKKL--FSSEISDDIDLLFLCIGHGHSKKILKNISSK 89
Cdd:cd24148   11 YAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHL-PPLADRVLepTTPAVLAGHDVVFLALPHGASAAIAAQLPPD 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529140837  90 INVIDMSNDFRIN-----QNFFFKKRIFH--YGLPEL--NKNIINKYKNIANP----GCFATAIQ 141
Cdd:cd24148   90 VLVVDCGADHRLEdaaawEKFYGGEHAGGwtYGLPELpgAREALAGARRIAVPnlgkGTAGQAVQ 154
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 8-133 1.08e-10

N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and N-acetyl-gamma-glutamyl-phosphate reductase (AGPR); Aspartate-beta-semialdehyde dehydrogenase (ASADH, EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the second step of the aspartate biosynthetic pathway, an essential enzyme found in bacteria, fungi, and higher plants. ASADH catalyses the formation of L-aspartate-beta-semialdehyde (ASA) by the reductive dephosphorylation of L-beta-aspartyl phosphate (BAP), utilizing the reducing power of NADPH. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. N-acetyl-gamma-glutamyl-phosphate reductase (AGPR, EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, reversibly catalyses the NADPH-dependent reduction of N-acetyl-gamma-glutamyl phosphate; the third step of arginine biosynthesis. ASADH and AGPR proteins contain an N-terminal Rossmann fold NAD(P)H binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467516 [Multi-domain]  Cd Length: 145  Bit Score: 58.91  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837   8 GGAGYTANELIKILINHP-KVEIKTIVSTTYPGLPIEDIHKDLIGEIkNKKLFSSEISDDIDLLFLCIGHGHSKKILKNI 86
Cdd:cd02281    7 GATGYVGGEFLRLLLEHPfPLFEIVLLAASSAGAKKKYFHPKLWGRV-LVEFTPEEVLEQVDIVFTALPGGVSAKLAPEL 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 529140837  87 SS-KINVIDMSNDFRINqnfffKKRIfhYGLPELNKNIINKYKN---IANP 133
Cdd:cd02281   86 SEaGVLVIDNASDFRLD-----KDVP--LVVPEVNREHIGELKGtkiIANP 129
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 146-296 1.37e-07

Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase.


Pssm-ID: 397067 [Multi-domain]  Cd Length: 167  Bit Score: 50.39  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  146 PLAKRKLLKNNLHISAITGSTGAGRINNSKLNFSFRNNNISTYNL-FNHNHINEVIQTIKKLQN-----QYDGKIYFIPY 219
Cdd:pfam02774   3 PLRDALGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDgEEHNGTPETREELKMVNEtkkilGFTPKVSATCV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837  220 RGGFSRGIISTLYTRIDLSFEEVKNLYDRFYK-NNPFIFISEKEIHLKQVINTNK-------CILNLKYIKNKLIITSII 291
Cdd:pfam02774  83 RVPVFRGHSETVTVKLKLKPIDVEEVYEAFYAaPGVFVVVRPEEDYPTPRAVRGGtnfvyvgRVRKDPDGDRGLKLVSVI 162


                  ....*
gi 529140837  292 DNLIK 296
Cdd:pfam02774 163 DNLRK 167
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 143-256 1.95e-05

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 44.43  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529140837 143 SILPLAKRKLLKNNLH---ISAITGSTGAGRINNSKLNFSFRNNNISTYNLFNHNHINEVIQTIKKLQNqyDGKIYFIPY 219
Cdd:cd18122    5 GLIPAAKALNDKFGIEeilVVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGEIGK--PIKVDGIAV 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 529140837 220 RGGFSRGIISTLYTRID--LSFEEVKNLYDRFYKNNPFI 256
Cdd:cd18122   83 RVPATLGHLVTVTVKLEktATLEQIAEAVAEAVEEVQIS 121
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 293-309 6.45e-04

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family.


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 39.12  E-value: 6.45e-04
                         10
                 ....*....|....*..
gi 529140837 293 NLIKGASGQAVQNLNLM 309
Cdd:cd17896  114 NLGKGASGAAVQNMNLM 130
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 293-314 7.00e-04

N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate reductase (actinobacAGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC). There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The family includes N-acetyl-gamma-glutamyl-phosphate reductases mainly from actinobacteria. They belong to the type 1 AGPR family. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467524 [Multi-domain]  Cd Length: 164  Bit Score: 39.58  E-value: 7.00e-04
                         10        20
                 ....*....|....*....|..
gi 529140837 293 NLIKGASGQAVQNLNLMYNFEE 314
Cdd:cd24148  143 NLGKGTAGQAVQSANLALGLPE 164
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 68-134 1.80e-03

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family.


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 37.97  E-value: 1.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529140837  68 DLLFLCIGHGHSKKILKNISS-KINVIDMSNDFRINQNFFfkkrifhYGLPELNK---NIINKYKNIANPG 134
Cdd:cd17896   50 DIAILCLPDDAAREAVALVTNpRTRIIDASTAHRTAPGWA-------YGFPELSPeqrEKIATSKRVANPG 113
 
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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