ARGC_SULMW
ID ARGC_SULMW Reviewed; 325 AA.
AC A8Z5X3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=SMGWSS_110;
OS Sulcia muelleri (strain GWSS).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Candidatus Sulcia.
OX NCBI_TaxID=444179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GWSS;
RX PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA McCutcheon J.P., Moran N.A.;
RT "Parallel genomic evolution and metabolic interdependence in an ancient
RT symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(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}.
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DR EMBL; CP000770; ABS30524.1; -; Genomic_DNA.
DR AlphaFoldDB; A8Z5X3; -.
DR SMR; A8Z5X3; -.
DR STRING; 444179.SMGWSS_110; -.
DR EnsemblBacteria; ABS30524; ABS30524; SMGWSS_110.
DR KEGG; smg:SMGWSS_110; -.
DR HOGENOM; CLU_006384_0_1_10; -.
DR OMA; FSWRNNN; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000781; 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; Reference proteome.
FT CHAIN 1..325
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_1000076748"
FT ACT_SITE 135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ SEQUENCE 325 AA; 37075 MW; BE5846FFD301E40D CRC64;
MIKIGIIGGA GYTANELIKI LINHPKVEIK TIVSTTYPGI PIEYIHKDLI GEIKSNKLFS
SEITDDIDLL FLCIGHGHSK KILKNISYKI NVIDFSNDFR INKNFFFKKR IFNYGLPELN
KNIINKYNNI ANPGCFATAI QLSILPLAKI KLLKNNIHIS AITGSTGAGR INNSKLNFSF
RNNNISTYNL FNHNHINEVI QTINKLQNKY DGKIYFIPYR GGFSRGIIST LYTRIDLSFE
EIKNIYDKFY KNDPFIFLSE KEIHLKQVIN TNKCILNLKY IKNKLIITSI IDNLIKGASG
QAVQNMNIMY NFEETCGLKL KPLGL
