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Entry: D1BNM9_VEIPT
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ID   D1BNM9_VEIPT            Unreviewed;       316 AA.
AC   D1BNM9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   11-JUN-2014, entry version 33.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase;
DE            Short=AGPR;
DE            EC=1.2.1.38;
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase;
GN   Name=argC; OrderedLocusNames=Vpar_1307;
OS   Veillonella parvula (strain ATCC 10790 / DSM 2008 / JCM 12972 / Te3)
OS   (Veillonella alcalescens).
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=479436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10790 / DSM 2008 / JCM 12972 / Te3;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Wellnitz S., Schneider S., Gronow S.,
RA   Klenk H.P., Eisen J.A.;
RT   "The complete genome of Veillonella parvula DSM 2008.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+)
CC       + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2
CC       subfamily.
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DR   EMBL; CP001820; ACZ24986.1; -; Genomic_DNA.
DR   RefSeq; YP_003312266.1; NC_013520.1.
DR   EnsemblBacteria; ACZ24986; ACZ24986; Vpar_1307.
DR   GeneID; 8636779; -.
DR   KEGG; vpr:Vpar_1307; -.
DR   PATRIC; 32531904; VBIVeiPar80537_1279.
DR   HOGENOM; HOG000254903; -.
DR   KO; K00145; -.
DR   OMA; IAQMENP; -.
DR   OrthoDB; EOG6XSZS3; -.
DR   BioCyc; VPAR479436:GHOS-1340-MONOMER; -.
DR   UniPathway; UPA00068; UER00108.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_01110; ArgC_type2; 1.
DR   InterPro; IPR010136; AGPR_type-2.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   TIGRFAMs; TIGR01851; argC_other; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; NADP; Oxidoreductase.
FT   ACT_SITE    117    117       By similarity{EA3}.
SQ   SEQUENCE   316 AA;  34391 MW;  5DEABA79236FF33A CRC64;
     MTPHRVFIVG HEGTTGLRIH ERLSDRKDIE LLATADEDRK NVEAIKVVAK KADLVFLCLP
     DVASKEIMAA IGDFPCKVID TSTAFRTTAG WAYGFPELGE SYKTAIATKK HIANPGCHAS
     GMIACIAPLV KAGLVPVDYP FTITSLTGYS GGGKKMIGQY ESNPKDYFLY APRQYGLGQE
     HKHLPEVQHV CGIIEAPIFM PIVDDYYSGM EVTVGIHSRL CHKPVCIDKV QQTLEYFYKD
     STIVTVAPFT ENSNSGMLNA NQLSNTDSMK IYVTGNDERI MVHAIFDNLG KGASGAAVQC
     MNIALGLPED TGLVLG
//
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