ARGC_BRUC2
ID ARGC_BRUC2 Reviewed; 310 AA.
AC A9MAG5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_01110};
DE Short=AGPR {ECO:0000255|HAMAP-Rule:MF_01110};
DE EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_01110};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01110};
DE Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01110};
GN Name=argC {ECO:0000255|HAMAP-Rule:MF_01110}; OrderedLocusNames=BCAN_A0801;
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) 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:0000255|HAMAP-Rule:MF_01110}.
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_01110};
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_01110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01110}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01110}.
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DR EMBL; CP000872; ABX61868.1; -; Genomic_DNA.
DR RefSeq; WP_002963923.1; NC_010103.1.
DR AlphaFoldDB; A9MAG5; -.
DR SMR; A9MAG5; -.
DR EnsemblBacteria; ABX61868; ABX61868; BCAN_A0801.
DR GeneID; 45051859; -.
DR GeneID; 55590501; -.
DR KEGG; bcs:BCAN_A0801; -.
DR HOGENOM; CLU_077118_0_0_5; -.
DR OMA; FSWRNNN; -.
DR PhylomeDB; A9MAG5; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000001385; Chromosome I.
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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01110; ArgC_type2; 1.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR010136; AGPR_type-2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01851; argC_other; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW Oxidoreductase.
FT CHAIN 1..310
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_1000084868"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ SEQUENCE 310 AA; 33797 MW; 48864AD69488DE5E CRC64;
MKPKIFIDGE HGTTGLQIRT RLAERDDLEV ISIPEAERRN KDLRADYLRA ADIAILCLPD
DASKEAVSLL EGHNSTRIID TSTAHRVHPD WAYGFAELAK GQRERIAEAR LVANPGCYPT
GAIALVRPLR DAGLLPADYP VSVNAVSGYT GGGKQLIAQM EDRNHPDYLA ANNFLYGLPL
KHKHVPELQL HGRLDRRPIF SPSVGRFPQG MIVQVPLFLS ELEGSPSLAK VHAVLTEHYA
GQDIVEVVPL EESAKLPRVD AEELAGKDGM KLFVFGTEDH GQVNLVALLD NLGKGASGAA
VQNMNLMLGK