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Database: UniProt
Entry: A0A1R1ST35_9ACTN
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ID   A0A1R1ST35_9ACTN        Unreviewed;       342 AA.
AC   A0A1R1ST35;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00150};
DE            Short=AGPR {ECO:0000256|HAMAP-Rule:MF_00150};
DE            EC=1.2.1.38 {ECO:0000256|HAMAP-Rule:MF_00150};
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00150};
DE            Short=NAGSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00150};
GN   Name=argC {ECO:0000256|HAMAP-Rule:MF_00150,
GN   ECO:0000313|EMBL:OMI41438.1};
GN   ORFNames=SPAR_00874 {ECO:0000313|EMBL:OMI41438.1};
OS   Streptomyces sparsogenes DSM 40356.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI41438.1, ECO:0000313|Proteomes:UP000186168};
RN   [1] {ECO:0000313|EMBL:OMI41438.1, ECO:0000313|Proteomes:UP000186168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI41438.1,
RC   ECO:0000313|Proteomes:UP000186168};
RA   Coyne S., Seebeck F.P.;
RT   "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC       glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC       {ECO:0000256|HAMAP-Rule:MF_00150}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC         H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00150};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 3/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00150}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMI41438.1}.
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DR   EMBL; ASQP01000011; OMI41438.1; -; Genomic_DNA.
DR   RefSeq; WP_065966015.1; NZ_ASQP01000011.1.
DR   AlphaFoldDB; A0A1R1ST35; -.
DR   STRING; 67365.GCA_001704635_01116; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000186168; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0070401; F:NADP+ binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00150; ArgC_type1; 1.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR000706; AGPR_type-1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   NCBIfam; TIGR01850; argC; 1.
DR   PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01224; ARGC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00150};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00150}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00150};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00150}; Reference proteome {ECO:0000313|Proteomes:UP000186168}.
FT   DOMAIN          4..136
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT                   ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   342 AA;  34554 MW;  20277397A13AEDFA CRC64;
     MAVRVAVAGA SGYAGGEVLR LLLAHPRAEI GALTGNSNAG GRLGALQPHL LPLADRVLEP
     TGPEALAGHD VVFLALPHGQ SAAVAEQLGD EVLIIDCGAD FRLEDAGEWE RFYGSPHAGT
     WPYGLPELPG ARAALEGSKR VAVPGCYPTA VSLALFPAYA AGLVEPEAVI VAASGTSGAG
     KAPKPHLLGS EVMGAMSPYG VGGGHRHTPE MIQNLSAVAG EPVSVSFTPT LAPMPRGILA
     TCSAKARPGV TAEAVRAAYE KALQDEPFVH LLPEGQWPST AAVYGSNAAL IQVAHDPAAG
     RVIAISAIDN LTKGTAGGAV QSMNVALGLP EGLGLPTTGI AP
//
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