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Database: UniProt
Entry: H0F981_9BURK
LinkDB: H0F981_9BURK
Original site: H0F981_9BURK 
ID   H0F981_9BURK            Unreviewed;       431 AA.
AC   H0F981;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=KYC_16667 {ECO:0000313|EMBL:EHK65146.1};
OS   Achromobacter arsenitoxydans SY8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK65146.1, ECO:0000313|Proteomes:UP000003113};
RN   [1] {ECO:0000313|EMBL:EHK65146.1, ECO:0000313|Proteomes:UP000003113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8 {ECO:0000313|EMBL:EHK65146.1,
RC   ECO:0000313|Proteomes:UP000003113};
RX   PubMed=22328747; DOI=10.1128/JB.06667-11;
RA   Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT   "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT   Achromobacter arsenitoxydans SY8.";
RL   J. Bacteriol. 194:1243-1244(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC         NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001406};
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006753, ECO:0000256|RuleBase:RU004171}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK65146.1}.
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DR   EMBL; AGUF01000055; EHK65146.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0F981; -.
DR   STRING; 477184.KYC_16667; -.
DR   PATRIC; fig|477184.5.peg.3288; -.
DR   eggNOG; COG0460; Bacteria.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000003113; Unassembled WGS sequence.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04881; ACT_HSDH-Hom; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
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   PANTHER; PTHR43331; HOMOSERINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43331:SF1; HOMOSERINE DEHYDROGENASE; 1.
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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EHK65146.1}.
FT   DOMAIN          352..427
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT   BINDING         6..13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         102
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ   SEQUENCE   431 AA;  46246 MW;  271AC555B07E79AA CRC64;
     MKVGLLGLGV VGGGTWTVLS RNAEEIARRA GRRIEVTRAA VRDVAKARAR VGDAILVDTD
     VHALVRDPEI DIVVELIGGD TLARELVLEA IANGKHVVTA NKALLAKHGN EIFAAASERG
     VMVNFEAAVA GGIPIIKAIR EGLTANRIQW VAGIINGTTN FILSEMRTRG LPFADVLAEA
     QRLGYAEADP TFDVEGVDAA HKLTLLASLA FGVPVQFDRA YIEGISQLAA EDIEHAERLG
     YRIKLLGITK RRPDGIELRV HPSLVPSERL LANVEGAMNA VLVKGDAVGP TLYYGQGAGE
     EPTASAVVAD LVDVTRLHTA DPGNRVPHLA FQPDAMSDTP ILPIEQVSTS YYLRLRVDDQ
     PGVLADIARI LADRSISIGS MIQQPSHIGG ADIIFLTHEA VEGNVNQAIE RIESLPFVRS
     KVTRLRVENL T
//
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