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Conserved domains on  [gi|499271736|ref|WP_010969129|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Sinorhizobium meliloti]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
argC_other super family cl36993
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ...
 2-308 5.66e-146

N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less 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 gap architecture in a multiple sequence alignment. [Amino acid biosynthesis, Glutamate family]


The actual alignment was detected with superfamily member TIGR01851:

Pssm-ID: 273833 [Multi-domain]  Cd Length: 310  Bit Score: 412.70  E-value: 5.66e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736    2 KPKIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAMREDLLNSADIAILCLPDDASREAVAMVAgNNRVRIIDT 81
Cdd:TIGR01851   1 APKVFIDGEAGTTGLQIRERLSGRDDIELLSIAPDRRKDAAERAKLLNAADVAILCLPDDAAREAVSLVD-NPNTCIIDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736   82 STAHRVAPDWAYGFAEMDKAQPQRIRDARHVANPGCYPTGAIALIRPLRQAGILPDGYPVTVNAVSGYTGGGKQMIAQME 161
Cdd:TIGR01851  80 STAYRTADDWAYGFPELAPGQREKIRNSKRIANPGCYPTGFIALMRPLVEAGILPADFPITINAVSGYSGGGKAMIADYE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  162 DDQNPDHIGAPHFLYGLTLKHKHVPEMKMHGLLERAPVFSPSVGKFAQGMIVQVPLYLEDLAAGATLETIHRALVDHYAG 241
Cdd:TIGR01851 160 QGSADNPSLQPFRIYGLALTHKHLPEMRVHSGLALPPIFTPAVGNFAQGMAVTIPLHLQTLASKVSPADIHAALADYYQG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499271736  242 QSIVEVVPLDESAKLAR--IDATELAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLML 308
Cdd:TIGR01851 240 EQFVRVAPLDDVETLDNtfLDPQGLNGTNRLDLFVFGSDDGERALLVARLDNLGKGASGAAVQNLNIML 308
 
Name Accession Description Interval E-value
argC_other TIGR01851
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ...
 2-308 5.66e-146

N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less 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 gap architecture in a multiple sequence alignment. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273833 [Multi-domain]  Cd Length: 310  Bit Score: 412.70  E-value: 5.66e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736    2 KPKIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAMREDLLNSADIAILCLPDDASREAVAMVAgNNRVRIIDT 81
Cdd:TIGR01851   1 APKVFIDGEAGTTGLQIRERLSGRDDIELLSIAPDRRKDAAERAKLLNAADVAILCLPDDAAREAVSLVD-NPNTCIIDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736   82 STAHRVAPDWAYGFAEMDKAQPQRIRDARHVANPGCYPTGAIALIRPLRQAGILPDGYPVTVNAVSGYTGGGKQMIAQME 161
Cdd:TIGR01851  80 STAYRTADDWAYGFPELAPGQREKIRNSKRIANPGCYPTGFIALMRPLVEAGILPADFPITINAVSGYSGGGKAMIADYE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  162 DDQNPDHIGAPHFLYGLTLKHKHVPEMKMHGLLERAPVFSPSVGKFAQGMIVQVPLYLEDLAAGATLETIHRALVDHYAG 241
Cdd:TIGR01851 160 QGSADNPSLQPFRIYGLALTHKHLPEMRVHSGLALPPIFTPAVGNFAQGMAVTIPLHLQTLASKVSPADIHAALADYYQG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499271736  242 QSIVEVVPLDESAKLAR--IDATELAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLML 308
Cdd:TIGR01851 240 EQFVRVAPLDDVETLDNtfLDPQGLNGTNRLDLFVFGSDDGERALLVARLDNLGKGASGAAVQNLNIML 308
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 116-296 1.08e-88

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: 262.54  E-value: 1.08e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 116 GCYPTGAIALIRPLRQAGILPDGYPVTVNAVSGYTGGGKQMIAQMEDDQNPDHigAPHFLYGLTLKHKHVPEMKMHGLLE 195
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPADYPLSIHAVSGYSGGGKKMIEQYEAAEAADL--PPPRPYGLGLEHKHLPEMQKHAGLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 196 RAPVFSPSVGKFAQGMIVQVPLYLEDLAAGATLETIHRALVDHYAGQSIVEVVPLDESAKLARIDATELAGSDAMKLFVF 275
Cdd:cd23935   79 RPPIFTPAVGNFYQGMLVTVPLHLDLLEKGVSAAEVHEALAEHYAGERFVKVMPLDEPDALGFLDPQALNGTNNLELFVF 158

                        170       180
                 ....*....|....*....|.
gi 499271736 276 GTKGGaHVNLVALLDNLGKGA 296
Cdd:cd23935  159 GNDKG-QALLVARLDNLGKGA 178
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 4-308 5.55e-81

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 250.13  E-value: 5.55e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736   4 KIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAM------------------REDLLNSADIAILCLPDDASRE 65
Cdd:PLN02968  40 RIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFgsvfphlitqdlpnlvavKDADFSDVDAVFCCLPHGTTQE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  66 AVAMVAgnNRVRIIDTSTAHRVA-----PDW--------------AYGFAEMdkaQPQRIRDARHVANPGCYPTGAIALI 126
Cdd:PLN02968 120 IIKALP--KDLKIVDLSADFRLRdiaeyEEWyghphrapelqkeaVYGLTEL---QREEIKSARLVANPGCYPTGIQLPL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 127 RPLRQAGILPDGyPVTVNAVSGYTGGGKQMIAQMEDDQNPDHIGAphflYGLTlKHKHVPEMKmHGLLE-----RAPVFS 201
Cdd:PLN02968 195 VPLVKAGLIEPD-NIIIDAKSGVSGAGRGAKEANLYTEIAEGIGA----YGVT-RHRHVPEIE-QGLADaagskVTPSFT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 202 PSVGKFAQGMIVQVPLyleDLAAGATLETIHRALVDHYAGQSIVEVvpLDESAKLaRIDAteLAGSDAMKLFVFGTKGGA 281
Cdd:PLN02968 268 PHLMPMSRGMQSTVYV---HYAPGVTAEDLHQHLKERYEGEEFVKV--LERGAVP-HTDH--VRGSNYCELNVFADRIPG 339

                        330       340
                 ....*....|....*....|....*..
gi 499271736 282 HVNLVALLDNLGKGASGAAVQNMDLML 308
Cdd:PLN02968 340 RAIIISVIDNLVKGASGQAVQNLNLMM 366
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 22-308 4.91e-38

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: 137.51  E-value: 4.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  22 MAGRTDLELLSIPEAErrnaamredLLNSADIAILCLPDDASREAVAMVAGNNrVRIIDTSTAHRV-------------- 87
Cdd:COG0002   48 LRGLTDLVFEPPDPDE---------LAAGCDVVFLALPHGVSMELAPELLEAG-VKVIDLSADFRLkdpavyekwygfeh 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  88 -APD----WAYGFAEMdkaQPQRIRDARHVANPGCYPTGAI-ALIrPLRQAGILpDGYPVTVNAVSGYTGGGKQmiaqme 161
Cdd:COG0002  118 aAPEllgeAVYGLPEL---NREEIKGARLIANPGCYPTAVLlALA-PLLKAGLI-DPDDIIIDAKSGVSGAGRK------ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 162 ddqnpdhiGAPHFL----------YGLTlKHKHVPEMKMH-GLLERAPV---FSPSVGKFAQGMIVQVplYLEdLAAGAT 227
Cdd:COG0002  187 --------ASEGTHfsevnenfraYKVG-GHRHTPEIEQElSRLAGEDVkvsFTPHLVPMVRGILATI--YAR-LKDGVT 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 228 LETIHRALVDHYAGQSIVEVVPLDESAKLAridatELAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLM 307
Cdd:COG0002  255 EEDLRAAYEEFYADEPFVRVLPEGRLPETK-----SVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAGQAVQNMNLM 329


                 .
gi 499271736 308 L 308
Cdd:COG0002  330 F 330
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-109 2.29e-13

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: 65.65  E-value: 2.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736     4 KIFIDGEHGTTGLQIRVRMAGRTDLELLSIPeAERRNAAMR------------------EDLLNSA-DIAILCLPDDASR 64
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALA-ASSRSAGKKvseagphlkgevvleldpPDFEELAvDIVFLALPHGVSK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 499271736    65 EAVAM--VAGNNRVRIIDTSTAHRVAPDWAYGFAEMdkaQPQRIRDA 109
Cdd:smart00859  80 ESAPLlpRAAAAGAVVIDLSSAFRMDDDVPYGLPEV---NPEAIKKA 123
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 45-109 3.46e-05

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: 42.51  E-value: 3.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271736   45 EDLLNSADIAILCLPDDASREAVAMVAGNNrVRIIDTSTAHRVAPDWAYGFAEMdkaQPQRIRDA 109
Cdd:pfam01118  61 PEDFKDVDIVFFALPGGVSKEIAPKLAEAG-AKVIDLSSDFRMDDDVPYGLPEV---NREAIKQA 121
 
Name Accession Description Interval E-value
argC_other TIGR01851
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ...
 2-308 5.66e-146

N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less 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 gap architecture in a multiple sequence alignment. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273833 [Multi-domain]  Cd Length: 310  Bit Score: 412.70  E-value: 5.66e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736    2 KPKIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAMREDLLNSADIAILCLPDDASREAVAMVAgNNRVRIIDT 81
Cdd:TIGR01851   1 APKVFIDGEAGTTGLQIRERLSGRDDIELLSIAPDRRKDAAERAKLLNAADVAILCLPDDAAREAVSLVD-NPNTCIIDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736   82 STAHRVAPDWAYGFAEMDKAQPQRIRDARHVANPGCYPTGAIALIRPLRQAGILPDGYPVTVNAVSGYTGGGKQMIAQME 161
Cdd:TIGR01851  80 STAYRTADDWAYGFPELAPGQREKIRNSKRIANPGCYPTGFIALMRPLVEAGILPADFPITINAVSGYSGGGKAMIADYE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  162 DDQNPDHIGAPHFLYGLTLKHKHVPEMKMHGLLERAPVFSPSVGKFAQGMIVQVPLYLEDLAAGATLETIHRALVDHYAG 241
Cdd:TIGR01851 160 QGSADNPSLQPFRIYGLALTHKHLPEMRVHSGLALPPIFTPAVGNFAQGMAVTIPLHLQTLASKVSPADIHAALADYYQG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499271736  242 QSIVEVVPLDESAKLAR--IDATELAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLML 308
Cdd:TIGR01851 240 EQFVRVAPLDDVETLDNtfLDPQGLNGTNRLDLFVFGSDDGERALLVARLDNLGKGASGAAVQNLNIML 308
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 116-296 1.08e-88

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: 262.54  E-value: 1.08e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 116 GCYPTGAIALIRPLRQAGILPDGYPVTVNAVSGYTGGGKQMIAQMEDDQNPDHigAPHFLYGLTLKHKHVPEMKMHGLLE 195
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPADYPLSIHAVSGYSGGGKKMIEQYEAAEAADL--PPPRPYGLGLEHKHLPEMQKHAGLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 196 RAPVFSPSVGKFAQGMIVQVPLYLEDLAAGATLETIHRALVDHYAGQSIVEVVPLDESAKLARIDATELAGSDAMKLFVF 275
Cdd:cd23935   79 RPPIFTPAVGNFYQGMLVTVPLHLDLLEKGVSAAEVHEALAEHYAGERFVKVMPLDEPDALGFLDPQALNGTNNLELFVF 158

                        170       180
                 ....*....|....*....|.
gi 499271736 276 GTKGGaHVNLVALLDNLGKGA 296
Cdd:cd23935  159 GNDKG-QALLVARLDNLGKGA 178
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 4-308 5.55e-81

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 250.13  E-value: 5.55e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736   4 KIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAM------------------REDLLNSADIAILCLPDDASRE 65
Cdd:PLN02968  40 RIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFgsvfphlitqdlpnlvavKDADFSDVDAVFCCLPHGTTQE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  66 AVAMVAgnNRVRIIDTSTAHRVA-----PDW--------------AYGFAEMdkaQPQRIRDARHVANPGCYPTGAIALI 126
Cdd:PLN02968 120 IIKALP--KDLKIVDLSADFRLRdiaeyEEWyghphrapelqkeaVYGLTEL---QREEIKSARLVANPGCYPTGIQLPL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 127 RPLRQAGILPDGyPVTVNAVSGYTGGGKQMIAQMEDDQNPDHIGAphflYGLTlKHKHVPEMKmHGLLE-----RAPVFS 201
Cdd:PLN02968 195 VPLVKAGLIEPD-NIIIDAKSGVSGAGRGAKEANLYTEIAEGIGA----YGVT-RHRHVPEIE-QGLADaagskVTPSFT 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 202 PSVGKFAQGMIVQVPLyleDLAAGATLETIHRALVDHYAGQSIVEVvpLDESAKLaRIDAteLAGSDAMKLFVFGTKGGA 281
Cdd:PLN02968 268 PHLMPMSRGMQSTVYV---HYAPGVTAEDLHQHLKERYEGEEFVKV--LERGAVP-HTDH--VRGSNYCELNVFADRIPG 339

                        330       340
                 ....*....|....*....|....*..
gi 499271736 282 HVNLVALLDNLGKGASGAAVQNMDLML 308
Cdd:PLN02968 340 RAIIISVIDNLVKGASGQAVQNLNLMM 366
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 3-116 2.81e-69

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: 211.31  E-value: 2.81e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736   3 PKIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAMREDLLNSADIAILCLPDDASREAVAMVAgNNRVRIIDTS 82
Cdd:cd17896    1 PKVFIDGEAGTTGLQIRERLAGRSDIELLSIPEDKRKDPAARAELLNAADIAILCLPDDAAREAVALVT-NPRTRIIDAS 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499271736  83 TAHRVAPDWAYGFAEMDKAQPQRIRDARHVANPG 116
Cdd:cd17896   80 TAHRTAPGWAYGFPELSPEQREKIATSKRVANPG 113
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 22-308 4.91e-38

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: 137.51  E-value: 4.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  22 MAGRTDLELLSIPEAErrnaamredLLNSADIAILCLPDDASREAVAMVAGNNrVRIIDTSTAHRV-------------- 87
Cdd:COG0002   48 LRGLTDLVFEPPDPDE---------LAAGCDVVFLALPHGVSMELAPELLEAG-VKVIDLSADFRLkdpavyekwygfeh 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  88 -APD----WAYGFAEMdkaQPQRIRDARHVANPGCYPTGAI-ALIrPLRQAGILpDGYPVTVNAVSGYTGGGKQmiaqme 161
Cdd:COG0002  118 aAPEllgeAVYGLPEL---NREEIKGARLIANPGCYPTAVLlALA-PLLKAGLI-DPDDIIIDAKSGVSGAGRK------ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 162 ddqnpdhiGAPHFL----------YGLTlKHKHVPEMKMH-GLLERAPV---FSPSVGKFAQGMIVQVplYLEdLAAGAT 227
Cdd:COG0002  187 --------ASEGTHfsevnenfraYKVG-GHRHTPEIEQElSRLAGEDVkvsFTPHLVPMVRGILATI--YAR-LKDGVT 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 228 LETIHRALVDHYAGQSIVEVVPLDESAKLAridatELAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLM 307
Cdd:COG0002  255 EEDLRAAYEEFYADEPFVRVLPEGRLPETK-----SVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAGQAVQNMNLM 329


                 .
gi 499271736 308 L 308
Cdd:COG0002  330 F 330
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 45-308 1.29e-34

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: 128.47  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736   45 EDLLNSADIAILCLPDDASREAVAMVAGNNrVRIIDTSTAHRV---------------APD----WAYGFAEMdkaQPQR 105
Cdd:TIGR01850  63 EEILEDADVVFLALPHGVSAELAPELLAAG-VKVIDLSADFRLkdpelyekwygfehaGPEllqkAVYGLPEL---HREE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  106 IRDARHVANPGCYPTGAIALIRPLRQAGILpDGYPVTVNAVSGYTGGGKQ-----MIAQMEDDQNPdhigaphflYGLTl 180
Cdd:TIGR01850 139 IKGARLIANPGCYPTATLLALAPLLKEGLI-DPTSIIVDAKSGVSGAGRKaseanHFPEVNENLRP---------YKVT- 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  181 KHKHVPEMKMH-GLLERAPV---FSPSVGKFAQGMIVQVplYLEdLAAGATLETIHRALVDHYAGQSIVEVVPLDESAKL 256
Cdd:TIGR01850 208 GHRHTPEIEQElGRLAGGKVkvsFTPHLVPMTRGILATI--YAK-LKDGLTEEDLRALYEEFYADEPFVRVLPEGGYPST 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499271736  257 ARIdatelAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLML 308
Cdd:TIGR01850 285 KAV-----IGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAAGQAVQNMNLMF 331
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 117-296 1.90e-32

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: 117.99  E-value: 1.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 117 CYPTGAIALIRPLRQAGILPDGyPVTVNAVSGYTGGGKqmiAQMEDDQNPDHIGaPHFLYGLTlKHKHVPEMKMHGLLER 196
Cdd:cd18125    1 CYATAALLALYPLLKAGLLKPT-PITVTGVSGTSGAGR---AASPASLHPEVAG-SLRPYALS-GHRHTPEIAQNLGGKH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 197 APVFSPSVGKFAQGMIVQVPLYLEDlaaGATLETIHRALVDHYAGQSIVEVVPLDESaklarIDATELAGSDAMKLFVFG 276
Cdd:cd18125   75 NVHFTPHVGPWVRGILMTIQCFTQK---GWSLRQLHEAYREAYAGEPFVRVMPQGKG-----PDPKFVQGTNYADIGVEL 146

                        170       180
                 ....*....|....*....|
gi 499271736 277 TKGGAHVNLVALLDNLGKGA 296
Cdd:cd18125  147 EEDTGRLVVMSAIDNLVKGA 166
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 3-115 5.12e-20

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: 84.93  E-value: 5.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736   3 PKIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAMRE-----------------DLLNSADIAILCLPDDASRE 65
Cdd:cd02280    1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREyhpsliislqiqefrpcEVLNSADILVLALPHGASAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271736  66 AVAMVAgNNRVRIIDTSTAHRV--------------APDWAYGFAEMDKAqpQRIRDARHVANP 115
Cdd:cd02280   81 LVAAIS-NPQVKIIDLSADFRFtdpevyrrhprpdlEGGWVYGLPELDRE--QRIANATRIANP 141
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 116-296 5.20e-16

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: 74.05  E-value: 5.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 116 GCYPTGAI-ALIrPLRQAG-ILPDGypVTVNAVSGYTGGGKQ-----MIAQMEDDQNPdhigaphflYGLTlKHKHVPEM 188
Cdd:cd23934    1 GCYPTAALlALA-PLLKAGlIEPDD--IIIDAKSGVSGAGRKasettHFSEVNENLKA---------YKVG-GHRHTPEI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 189 KMH-GLLERAPV---FSPSVGKFAQGMIVQVplYLEdLAAGATLETIHRALVDHYAGQSIVEVVPLDESAKLARIdatel 264
Cdd:cd23934   68 EQElSKLAGEDVevsFTPHLVPMTRGILATI--YAK-LKDGVTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAV----- 139

                        170       180       190
                 ....*....|....*....|....*....|..
gi 499271736 265 AGSDAMKLFVFGTKGGAHVNLVALLDNLGKGA 296
Cdd:cd23934  140 RGSNFCDIGVAVDGRTGRLIVVSAIDNLVKGA 171
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-109 2.29e-13

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: 65.65  E-value: 2.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736     4 KIFIDGEHGTTGLQIRVRMAGRTDLELLSIPeAERRNAAMR------------------EDLLNSA-DIAILCLPDDASR 64
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALA-ASSRSAGKKvseagphlkgevvleldpPDFEELAvDIVFLALPHGVSK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 499271736    65 EAVAM--VAGNNRVRIIDTSTAHRVAPDWAYGFAEMdkaQPQRIRDA 109
Cdd:smart00859  80 ESAPLlpRAAAAGAVVIDLSSAFRMDDDVPYGLPEV---NPEAIKKA 123
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 116-296 3.00e-09

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: 54.95  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 116 GCYPTGAIALIRPLRQagiLPDGYPvTVNAVSGYTGGGKqmiaqmeddqNPDHIGAPHFL------YGLTlKHKHVPEMK 189
Cdd:cd23936    1 GCYATGAQLALAPLLD---DLDGPP-SVFGVSGYSGAGT----------KPSPKNDPEVLadnlipYSLV-GHIHEREVS 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736 190 MHglLERAPVFSPSVGKFAQG--MIVQVPLyledlAAGATLETIHRALVDHYAGQSIVEVVpldESAKLARidatELAGS 267
Cdd:cd23936   66 RH--LGTPVAFMPHVAPWFQGitLTISIPL-----KKSMTADEIRELYQEAYAGEPLIKVT---KEIPLVR----DNAGK 131

                        170       180       190
                 ....*....|....*....|....*....|
gi 499271736 268 DAMKLFVFGT-KGGAHVNLVALLDNLGKGA 296
Cdd:cd23936  132 HGVVVGGFTVhPDGKRVVVVATIDNLLKGA 161
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 27-116 2.83e-08

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: 52.11  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  27 DLELLSIPEAERrnaamredlLNSADIAILCLPDDASREAVAMV-AGNNRVRIIDTSTAHRVAPDWAYGFAEMDKAqpqR 105
Cdd:cd24149   53 NLSVEDIPEEVA---------AREVDAWVLALPNGVAKPFVDAIdKANPKSVIVDLSADYRFDDAWTYGLPELNRR---R 120

                         90
                 ....*....|.
gi 499271736 106 IRDARHVANPG 116
Cdd:cd24149  121 IAGAKRISNPG 131
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 45-109 3.46e-05

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: 42.51  E-value: 3.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271736   45 EDLLNSADIAILCLPDDASREAVAMVAGNNrVRIIDTSTAHRVAPDWAYGFAEMdkaQPQRIRDA 109
Cdd:pfam01118  61 PEDFKDVDIVFFALPGGVSKEIAPKLAEAG-AKVIDLSSDFRMDDDVPYGLPEV---NREAIKQA 121
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 22-115 2.18e-04

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: 41.26  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  22 MAGRTDLELLSIPEaerrnaamrEDLLNSADIAILCLPDDASREAVAMVAGNNrVRIIDTSTAHRV-------------- 87
Cdd:cd17895   48 LRGLTDLTFEPDDD---------EEIAEDADVVFLALPHGVSMELAPKLLEAG-VKVIDLSADFRLkdpetyekwygfeh 117

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499271736  88 -APDW----AYGFAEMDKAQpqrIRDARHVANP 115
Cdd:cd17895  118 aAPELlkeaVYGLPELNREE---IKKARLVANP 147
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 11-115 2.83e-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: 40.73  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271736  11 HGTTGLQIRVRMAGRTDLellsipeAERRNAAMREDLLNSADIAILCLPDDASREAVAMVAGNnrVRIIDTSTAHRV--- 87
Cdd:cd24148   34 HSNAGQRLGELHPHLPPL-------ADRVLEPTTPAVLAGHDVVFLALPHGASAAIAAQLPPD--VLVVDCGADHRLeda 104

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499271736  88 -----------APDWAYGFAEMDKAQpQRIRDARHVANP 115
Cdd:cd24148  105 aawekfyggehAGGWTYGLPELPGAR-EALAGARRIAVP 142
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 291-308 7.29e-04

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: 39.72  E-value: 7.29e-04
                         10
                 ....*....|....*...
gi 499271736 291 NLGKGASGAAVQNMDLML 308
Cdd:cd17895  148 NLVKGAAGQAVQNMNLMF 165
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 291-308 1.73e-03

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: 38.42  E-value: 1.73e-03
                         10
                 ....*....|....*...
gi 499271736 291 NLGKGASGAAVQNMDLML 308
Cdd:cd24148  143 NLGKGTAGQAVQSANLAL 160
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 45-115 2.48e-03

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: 37.73  E-value: 2.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499271736  45 EDLLNSADIAILCLPDDASREaVAMVAGNNRVRIIDTSTAHRVAPDWAYGFAEMDKAQPQRIRDARHVANP 115
Cdd:cd02281   60 EEVLEQVDIVFTALPGGVSAK-LAPELSEAGVLVIDNASDFRLDKDVPLVVPEVNREHIGELKGTKIIANP 129
 
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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