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Database: UniProt
Entry: L7VKY5_CLOSH
LinkDB: L7VKY5_CLOSH
Original site: L7VKY5_CLOSH 
ID   L7VKY5_CLOSH            Unreviewed;       423 AA.
AC   L7VKY5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   10-APR-2019, entry version 41.
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:AGC67329.1};
GN   OrderedLocusNames=Cst_c03050 {ECO:0000313|EMBL:AGC67329.1};
OS   Clostridium stercorarium subsp. stercorarium (strain ATCC 35414 / DSM
OS   8532 / NCIMB 11754).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Hungateiclostridiaceae; Thermoclostridium.
OX   NCBI_TaxID=1121335 {ECO:0000313|EMBL:AGC67329.1, ECO:0000313|Proteomes:UP000011220};
RN   [1] {ECO:0000313|EMBL:AGC67329.1, ECO:0000313|Proteomes:UP000011220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35414 / DSM 8532 / NCIMB 11754
RC   {ECO:0000313|Proteomes:UP000011220};
RX   PubMed=23516204; DOI=10.1128/genomeA.00073-13;
RA   Poehlein A., Zverlov V.V., Daniel R., Schwarz W.H., Liebl W.;
RT   "Complete genome sequence of Clostridium stercorarium subsp.
RT   stercorarium strain DSM 8532, a thermophilic degrader of plant cell
RT   wall fibers.";
RL   Genome Announc. 1:E0007313-E0007313(2013).
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; CP004044; AGC67329.1; -; Genomic_DNA.
DR   RefSeq; WP_015358026.1; NC_020887.2.
DR   STRING; 1121335.Clst_0288; -.
DR   EnsemblBacteria; AGC67329; AGC67329; Cst_c03050.
DR   KEGG; csd:Clst_0288; -.
DR   KEGG; css:Cst_c03050; -.
DR   PATRIC; fig|1121335.3.peg.294; -.
DR   KO; K00003; -.
DR   BioCyc; CSTE1121335:G1HGA-285-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000011220; Chromosome.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011220};
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:AGC67329.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011220};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      346    420       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   COILED      166    186       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    205    205       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     105    105       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     190    190       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   423 AA;  47153 MW;  5A4DEAEEDE1E4612 CRC64;
     MREVQIAFLG LGNVGSGVYK ILQMRKKEFE EKEDLRINIK RILVRNINKK RAVEVDRNIL
     TDNPDDILND PEISIVAEFI GGEKPALEYL LKALNSGKTV VTANKEVIAR HWEKLDEAAK
     ASGAGLYYEA SVCGGIPVIK AIQESLQANR IERIMGIING TTNYILTKMS ENNERFEEAL
     RKAQELGYAE PDPTADIEGY DAAFKLSILS TLCFHKRVHL DNILREGITN ITLEDISYGR
     ELGYALKLLA IAKDNDGKVE ARVHPTFIPL NHPLSSVRSS FNAVYLKGDC FGDMMFFGRG
     AGDLPTGSAV VSDILTACGR KEHRYMDFGK KTADAVYNDD WKTKYYVRLT VKDQPGVLAE
     IAGYFGKYQV SIASVIQKGY GDTTAPLIFV THEASEKSIQ KAIAEIRESK YVISVDNLIR
     VEE
//
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