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Database: UniProt
Entry: Q67KS3_SYMTH
LinkDB: Q67KS3_SYMTH
Original site: Q67KS3_SYMTH 
ID   Q67KS3_SYMTH            Unreviewed;       436 AA.
AC   Q67KS3;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   OrderedLocusNames=STH2739 {ECO:0000313|EMBL:BAD41724.1};
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD41724.1, ECO:0000313|Proteomes:UP000000417};
RN   [1] {ECO:0000313|EMBL:BAD41724.1, ECO:0000313|Proteomes:UP000000417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T.,
RA   Morimura K., Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable
RT   bacterium that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(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; AP006840; BAD41724.1; -; Genomic_DNA.
DR   STRING; 292459.STH2739; -.
DR   EnsemblBacteria; BAD41724; BAD41724; STH2739.
DR   KEGG; sth:STH2739; -.
DR   eggNOG; ENOG4105D6E; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   HOGENOM; HOG000076615; -.
DR   KO; K00003; -.
DR   OMA; FEASVCG; -.
DR   BioCyc; STHE292459:G1G28-2725-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000000417; 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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000417};
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   Reference proteome {ECO:0000313|Proteomes:UP000000417};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      352    433       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      11     18       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    206    206       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     106    106       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     191    191       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   436 AA;  47354 MW;  E0FC030CF1C3B763 CRC64;
     MEKQTMRFAI LGLGTVGKGV VKLLQESREM LHLKTGLNLE LAKVLVRDAS KPRPGFEGLP
     LTEDVSEILD DPSIRIVVEL MGGIEPARTY LVEALRRGKT IVTANKDVMA DYDKDLYDAG
     EIGDAEIYFE ASVGGGIPII RPLKEALAAN TMRQVMGIVN GTTNYILTQM SQYGRSYEEA
     LQEAQALGYA EPDPTNDVQG FDAARKLAIL CTICFLSRVK PGMVYTEGIT RVTPRDIEYG
     RRFGWVLKLL AIGKEVDGEI EARVHPAFIP HTHPLASVAG SFNAIYTVGD PVGETMFYGR
     GAGAGPTASA VVSDLIAAAL SKRTPGRRAG DAHTVYFEKR VLPIEETRSR YYLRLHAVDA
     PGSLARIAER FGEHGVSLAE VVQASGGPDH PDDGGAAELV LVTHTVQDAN LQAVVRDLKE
     MRDTVLRVDN VIRVEG
//
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