ARGC_AGRFC
ID ARGC_AGRFC Reviewed; 310 AA.
AC Q8UG00;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=Atu1244;
GN ORFNames=AGR_C_2293;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007869; AAK87041.2; -; Genomic_DNA.
DR PIR; AG2729; AG2729.
DR PIR; H97510; H97510.
DR RefSeq; NP_354256.2; NC_003062.2.
DR RefSeq; WP_010971495.1; NC_003062.2.
DR AlphaFoldDB; Q8UG00; -.
DR SMR; Q8UG00; -.
DR STRING; 176299.Atu1244; -.
DR EnsemblBacteria; AAK87041; AAK87041; Atu1244.
DR KEGG; atu:Atu1244; -.
DR PATRIC; fig|176299.10.peg.1265; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_077118_0_0_5; -.
DR OMA; FSWRNNN; -.
DR PhylomeDB; Q8UG00; -.
DR BioCyc; AGRO:ATU1244-MON; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000813; Chromosome circular.
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; Reference proteome.
FT CHAIN 1..310
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112502"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ SEQUENCE 310 AA; 33271 MW; 60A2AAA320903317 CRC64;
MTAKIFIDGE HGTTGLQIRT RLAGRRDIEL LSIPETERRN AAMREDLLNN ADISILCLPD
DASKEAVSMV AGNNNVRIID TSTAYRVHQD WAYGFAEMDR DQGEKVRSAR FVANPGCYPT
GAIGLIRPLR ASGILPDGYP VSVNAVSGYT GGGKQMIAQM EDQSRDDAIS ANNFLYGLTL
KHKHVPEMTI HGQLDRAPLF APSVGRFPQG MIVQVPLFAA DLAEGTTIET IHAALTAHYA
GQDIVSVVPL AESKGISRID AEELAGKDTM KLFVFGTPGG EHINLVALLD NLGKGASGAA
VQNMELMLSA
