(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NX53_YERPA

ID   A0A0E1NX53_YERPA        Unreviewed;       334 AA.
AC   A0A0E1NX53;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 28.
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   OrderedLocusNames=YPA_0097 {ECO:0000313|EMBL:ABG12066.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12066.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12066.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12066.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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, ECO:0000256|SAAS:SAAS01081944}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate
CC         = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH;
CC         Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936,
CC         ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00150, ECO:0000256|SAAS:SAAS01127949};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 3/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00150, ECO:0000256|SAAS:SAAS01096212}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150,
CC       ECO:0000256|SAAS:SAAS01087196}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00150,
CC       ECO:0000256|SAAS:SAAS00591558}.
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; CP000308; ABG12066.1; -; Genomic_DNA.
DR   RefSeq; WP_002209489.1; NZ_CP009906.1.
DR   SMR; A0A0E1NX53; -.
DR   EnsemblBacteria; ABG12066; ABG12066; YPA_0097.
DR   EnsemblBacteria; AJJ81554; AJJ81554; CH58_2932.
DR   KEGG; ypa:YPA_0097; -.
DR   PATRIC; fig|360102.15.peg.3086; -.
DR   KO; K00145; -.
DR   OMA; PHLTPMI; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000001971; 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;
DR   PRODOM; A0A0E1NX53.
DR   SWISS-2DPAGE; A0A0E1NX53.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS00333562};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS01096209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS01087102};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00150, ECO:0000256|SAAS:SAAS00333569};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00150,
KW   ECO:0000256|SAAS:SAAS00333583, ECO:0000313|EMBL:ABG12066.1}.
FT   ACT_SITE    154    154       {ECO:0000256|HAMAP-Rule:MF_00150}.
SQ   SEQUENCE   334 AA;  35870 MW;  00AC62A772F45CCF CRC64;
     MLNTLIVGAS GYAGAELTAY LNRHPHMNIT GLAVSAQSAD AGKLLSDLHP QLKGILDLPL
     QPLVDVAQAA KGIDVVFLAT AHEVSHDLAP QFLAAGCVVF DLSGAFRVRD AAFYSQYYGF
     EHQHPDWLDK AVYGLAEWQS EDIKQAQLIA VPGCYPTASQ LALKPLVDGQ LLNDAQWPVI
     NAVSGVSGAG RKASMGNSFC EVSLQPYGLF THRHQPEIVT HLGTPVIFTP HLGNFARGIL
     ATITCRLKAG VTAQNIADAY HHAYQNKPLV RLYQQGVPAL KAVVGLPFCD IGFSVQGEHL
     IIVATEDNLL KGAAAQAVQC MNIRFGFPET QSLL
//

If you have problems or comments...

PBIL Back to PBIL home page