ID   ARGC_PROM2              Reviewed;         351 AA.
AC   A8G4T4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00150};
DE            Short=AGPR {ECO:0000255|HAMAP-Rule:MF_00150};
DE            EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_00150};
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150};
DE            Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150};
GN   Name=argC {ECO:0000255|HAMAP-Rule:MF_00150}; OrderedLocusNames=P9215_10001;
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC       glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC       {ECO:0000255|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:0000255|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:0000255|HAMAP-
CC       Rule:MF_00150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00150}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00150}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000825; ABV50615.1; -; Genomic_DNA.
DR   RefSeq; WP_012007702.1; NC_009840.1.
DR   AlphaFoldDB; A8G4T4; -.
DR   SMR; A8G4T4; -.
DR   STRING; 93060.P9215_10001; -.
DR   EnsemblBacteria; ABV50615; ABV50615; P9215_10001.
DR   KEGG; pmh:P9215_10001; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_1_3; -.
DR   OMA; PHLTPMI; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002014; Chromosome.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01850; argC; 1.
DR   PROSITE; PS01224; ARGC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW   Oxidoreductase.
FT   CHAIN           1..351
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_1000058153"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   351 AA;  38812 MW;  EE98EC0B0266D801 CRC64;
     MNVAIVGATG YGGIQAVNLL KKNKNYKISF LGGNKTSGSK WNDNFPFIYL DNDPYVEEIS
     VDNISKNSDV ALLCLPNGLS STLTRKLLER GLKVIDLSAD YRYKSLDEWK KVYSKEAAIY
     KRNDDDLCKE AVYGLPEINK EAISKGRLIA CPGCYPTSAL IPLAPYLSQG IIENEGIVID
     SKSGTSGGGR EPNQKLLLSE CGEGLSAYGL INHRHTSEIE QVASLISGNK IELLFTPHLV
     PIPRGMHSTI YGRLRDPGLT SDDCRILLDN YYRNFKNIKV LPVDTFPSTK WVKNTNQIFL
     SVKVDIRNGR IIILSAIDNL LKGQTGQAIQ NLNIMSGFSM DEGLELTNNY P