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Database: UniProt
Entry: V2YHF8_9FIRM
LinkDB: V2YHF8_9FIRM
Original site: V2YHF8_9FIRM 
ID   V2YHF8_9FIRM            Unreviewed;       403 AA.
AC   V2YHF8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
GN   ORFNames=N510_00051 {ECO:0000313|EMBL:ESL15763.1}, N510_003153
GN   {ECO:0000313|EMBL:USF28194.1};
OS   Firmicutes bacterium ASF500.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL15763.1};
RN   [1] {ECO:0000313|EMBL:ESL15763.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF500 {ECO:0000313|EMBL:ESL15763.1};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
RN   [2] {ECO:0000313|EMBL:USF28194.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ASF500 {ECO:0000313|EMBL:USF28194.1};
RA   Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA   Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT   "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT   Model to Study Microbiome Function.";
RL   Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC         NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|RuleBase:RU000579};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 3/5. {ECO:0000256|RuleBase:RU000579}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006753, ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; AYJP01000002; ESL15763.1; -; Genomic_DNA.
DR   EMBL; CP097573; USF28194.1; -; Genomic_DNA.
DR   AlphaFoldDB; V2YHF8; -.
DR   STRING; 1378168.N510_00051; -.
DR   PATRIC; fig|1378168.3.peg.52; -.
DR   eggNOG; COG0460; Bacteria.
DR   HOGENOM; CLU_009116_1_0_9; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000017395; 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   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
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; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 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; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000579};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017395};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN          8..124
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          132..311
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
SQ   SEQUENCE   403 AA;  42577 MW;  C6CFE58225129E42 CRC64;
     MVHVAILGFG TVGSGVAEVL TTNGGLIDHR VDDLVRLKYI LDVRDFPDSP YAGLFVKDFA
     AIESDPEVDI VVETIGGATI ALDFTTRALR AGKSVVTSNK ELVATHGYEL LQLAKANGCS
     YLFEASVGGG IPILRPLTSC LAANELEQVT GILNGTTNYI LTRMIRAGLT FEQALAEAQA
     NGYAEKDPTA DVDGHDACRK ICILAALSFG RHVYPDQVPT QGIRGVTLED VAYADSVGCK
     IKLLGRALRQ PEGKVCAFVA PHLVAGENPL SGVEDVFNAI AVTGNAIGDV MFYGRGAGKL
     PTASAVVADV IDIAKDLKKD RHNGWEEGAP DLVVSTDGLA SPWYVRARLS ADEARKRCGD
     IQLLARSGAP AGEAAFLTAP MTEPELREKL SGADVGSLFR VLA
//
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