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Entry: A0A1E8E081_9GAMM
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ID   A0A1E8E081_9GAMM        Unreviewed;       349 AA.
AC   A0A1E8E081;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ORFNames=BJN41_13375 {ECO:0000313|EMBL:OFE42623.1};
OS   Acinetobacter towneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=202956 {ECO:0000313|EMBL:OFE42623.1, ECO:0000313|Proteomes:UP000186931};
RN   [1] {ECO:0000313|EMBL:OFE42623.1, ECO:0000313|Proteomes:UP000186931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-2Ac02 {ECO:0000313|EMBL:OFE42623.1,
RC   ECO:0000313|Proteomes:UP000186931};
RA   Barbosa B., Fernandez-Garcia L., Gato E., Leao R., Albano R., Fernandez B.,
RA   Fernandez-Cuenca F., Marques E., Tomas M.;
RT   "Genome of airborne Acinetobacter sp. 5-2Ac02 in the hospital environment:
RT   Species near to Acinetobacter towneri.";
RL   Submitted (OCT-2016) 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:OFE42623.1}.
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DR   EMBL; MKQS01000032; OFE42623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E8E081; -.
DR   STRING; 202956.BJN41_13375; -.
DR   eggNOG; COG0002; Bacteria.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000186931; 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}.
FT   DOMAIN          3..141
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT                   ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   349 AA;  38185 MW;  80BEA7F3976B5DB5 CRC64;
     MISVGIVGGT GYTGVELLRL LLRHPNVKVN VLTSRTEAGR RVDDMFPSLR GHTDLCYSDL
     NIEELKKCDV VFFATPHGVA MQHAAELVAA NTKVVDLAAD FRLQDLSQFE KWYGMQHACP
     EILKDSVYGL SELNREQIKQ AQVIGNPGCY PTTVQLGLAP LFKQTEALVK PESIIIDAKS
     GVSGAGRKAS LGMIYSENAD NFKAYGVAGH RHHPEIVEAL ENISGQKDVF NHIIFVPHLV
     PMIRGMLSTI YADLTDAGDA VDLQSLYEQF YANEQFVDVM PANSSPETRS VRGANQLRIA
     LYKPQPKKLV LLVAQDNLVK GAAGQAVQNM NLMFGFAEHA GLEVIGLLP
//
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