SWISSPROT: Q2IMB5_ANADE

ID   Q2IMB5_ANADE            Unreviewed;       354 AA.
AC   Q2IMB5;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 106.
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=Adeh_0171 {ECO:0000313|EMBL:ABC79948.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79948.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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: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}.
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DR   EMBL; CP000251; ABC79948.1; -; Genomic_DNA.
DR   RefSeq; WP_011419231.1; NC_007760.1.
DR   STRING; 290397.Adeh_0171; -.
DR   EnsemblBacteria; ABC79948; ABC79948; Adeh_0171.
DR   KEGG; ade:Adeh_0171; -.
DR   eggNOG; ENOG4105C0N; Bacteria.
DR   eggNOG; COG0002; LUCA.
DR   HOGENOM; HOG000254904; -.
DR   KO; K00145; -.
DR   OMA; THHPTRA; -.
DR   BioCyc; ADEH290397:G1G5W-175-MONOMER; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000001935; 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; Q2IMB5.
DR   SWISS-2DPAGE; Q2IMB5.
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:UP000001935};
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:ABC79948.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   DOMAIN        8    148       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   ACT_SITE    156    156       {ECO:0000256|HAMAP-Rule:MF_00150,
FT                                ECO:0000256|PROSITE-ProRule:PRU10010}.
SQ   SEQUENCE   354 AA;  37283 MW;  ED2DE7F4C30C47F4 CRC64;
     MATGKRFKAA VIGGSGYGGA EMIRRLLVHP EVELVRVASI DFVGEPLSAA DPALEAVTDL
     TFEGIPPAEA AAGMDVVLLG LPHTVAASKV PELAALPGVK VVDMSGDFRL KDAAAYQRWY
     KHVHPCPERL ADFVYGLPEL NRERIRGARF VASPGCFATT IELALLPLAR AGLLEGVVHV
     QGITGSSGSG VAPSAGTHHP VRAGNLKTYK PLEHQHVPEI TETLAAAGAR DLALRFVPVS
     APLSRGILAT AFVELPEAWT QDRLDRLYRE AYAGEPFVRV PRKRLPEVAA VSGSNYAEVG
     VAVGPALGGR RTVTLFGATD NLVKGGAGQA IQNMNLVLGL DEKASLADPG PWPP
//