(data stored in SCRATCH zone)

SWISSPROT: D3VH71_XENNA

ID   D3VH71_XENNA            Unreviewed;       334 AA.
AC   D3VH71;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
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   ECO:0000313|EMBL:CBJ88356.1};
GN   OrderedLocusNames=XNC1_0268 {ECO:0000313|EMBL:CBJ88356.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88356.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88356.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88356.1; -; Genomic_DNA.
DR   RefSeq; WP_013183206.1; NC_014228.1.
DR   STRING; 406817.XNC1_0268; -.
DR   EnsemblBacteria; CBJ88356; CBJ88356; XNC1_0268.
DR   KEGG; xne:XNC1_0268; -.
DR   eggNOG; ENOG4105C0N; Bacteria.
DR   eggNOG; COG0002; LUCA.
DR   HOGENOM; HOG000254902; -.
DR   KO; K00145; -.
DR   OMA; PHLTPMI; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000008075; 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; D3VH71.
DR   SWISS-2DPAGE; D3VH71.
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:UP000008075};
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:CBJ88356.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN        3    146       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   ACT_SITE    154    154       {ECO:0000256|HAMAP-Rule:MF_00150,
FT                                ECO:0000256|PROSITE-ProRule:PRU10010}.
SQ   SEQUENCE   334 AA;  36493 MW;  AADE1DD9A8156321 CRC64;
     MLNTLIVGAS GYTGAELAAY LQRHSHVHLS GLMVSSQSSD AGKCFSELYP QYKGRLDLPL
     QPLTNVSEAA EGIDVVFLAT DHAISHDIAP IFLEAGCIVF DLSGAYRVQN TQFYKKYYGF
     EHKNAEWLQQ AVYGLAEWQA EKIKQARLIA VPGCYPTVSQ LSLKPLLEQG LLDIEHWPVI
     NAVSGVSGAG RKASITNSFC EVSLHPYGVF NHRHQPEIAT HLGTEVIFTP HLGNFSRGIL
     ATITCKLKSG VEEAQISAAY QQAYHDKPLI RLYNKGLPAL KAVVGLPFCD IGFAVQGQYL
     IIVGAEDNLL KGAAAQAVQC MNIRFGYEET QALL
//

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