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Database: UniProt
Entry: Q63UW9_BURPS
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Original site: Q63UW9_BURPS 
ID   Q63UW9_BURPS            Unreviewed;       442 AA.
AC   Q63UW9;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   08-MAY-2019, entry version 94.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   Name=hom {ECO:0000313|EMBL:CAH35478.1};
GN   OrderedLocusNames=BPSL1477 {ECO:0000313|EMBL:CAH35478.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH35478.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH35478.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH35478.1,
RC   ECO:0000313|Proteomes:UP000000605};
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.,
RA   Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA   Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA   Chillingworth T., Cronin A., Crosset B., Davis P., DeShazer D.,
RA   Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA   Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis,
RT   Burkholderia pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|RuleBase:RU000579};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; BX571965; CAH35478.1; -; Genomic_DNA.
DR   RefSeq; WP_004193856.1; NZ_CP009538.1.
DR   RefSeq; YP_108097.1; NC_006350.1.
DR   STRING; 272560.BPSL1477; -.
DR   PRIDE; Q63UW9; -.
DR   EnsemblBacteria; CAH35478; CAH35478; BPSL1477.
DR   GeneID; 3094454; -.
DR   KEGG; bps:BPSL1477; -.
DR   PATRIC; fig|272560.51.peg.3508; -.
DR   eggNOG; ENOG4105D6E; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   HOGENOM; HOG000076615; -.
DR   KO; K00003; -.
DR   OMA; FEASVCG; -.
DR   BioCyc; BPSE272560:G1G3Q-1538-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR016204; HDH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU000579};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000605};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000579,
KW   ECO:0000313|EMBL:CAH35478.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      358    438       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    208    208       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     108    108       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     193    193       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   442 AA;  47003 MW;  723D13F196A91498 CRC64;
     MEPIKVGLLG FGTVGGGTFK VLRRNQEEIK RRAGRGIEIA RVAVRNPAKA LAALDGDANG
     VSIGDDFNAV VDDPSIAIVA EMIGGTGLAR ELVLRAIANG KHVVTANKAL LAVHGTEIFE
     AARAKGVMVA FEAAVAGGIP IIKALREGLT ANRIQYIAGI INGTTNYILS EMRERGLDFA
     TALKAAQELG YAEADPTFDI EGVDAAHKAT IMSAIAFGVP VQFDRAYVEG ISRLAATDIK
     YAEELGYRIK LLGITRRTER GIELRVHPTL IPAKRLLANV EGAMNAVVVH GDAVGTTLYY
     GKGAGAEPTA SAVVADLVDV TRLHTADPEH RVPHLAFQPD SLSNTPILPI EEVTSGYYLR
     LRVADQTGVL ADITRILAES GISIDALLQK ESEQVDDANG ETDIILITHE TVEKNVNAAI
     ARIESLATVV SKVTKLRMEA LN
//
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