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Database: UniProt
Entry: A0A0M8K9A0_9CHLR
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ID   A0A0M8K9A0_9CHLR        Unreviewed;       345 AA.
AC   A0A0M8K9A0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=ARMA_1329 {ECO:0000313|EMBL:GAP62906.1}, SE16_01575
GN   {ECO:0000313|EMBL:KPL89218.1};
OS   Ardenticatena maritima.
OC   Bacteria; Chloroflexota; Ardenticatenia; Ardenticatenales;
OC   Ardenticatenaceae; Ardenticatena.
OX   NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP62906.1, ECO:0000313|Proteomes:UP000037784};
RN   [1] {ECO:0000313|EMBL:GAP62906.1, ECO:0000313|Proteomes:UP000037784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=110S {ECO:0000313|EMBL:GAP62906.1,
RC   ECO:0000313|Proteomes:UP000037784};
RA   Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT   "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic
RT   Thermophilic Bacterium, Ardenticatena maritima Strain 110ST.";
RL   Genome Announc. 3:e01145-15(2015).
RN   [2] {ECO:0000313|EMBL:KPL89218.1, ECO:0000313|Proteomes:UP000050502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=110S {ECO:0000313|EMBL:KPL89218.1,
RC   ECO:0000313|Proteomes:UP000050502};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Whole genome sequence of Ardenticatena maritima DSM 23922.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000037784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=110S {ECO:0000313|Proteomes:UP000037784};
RA   Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT   "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic Bacterium
RT   Ardenticatena maritima Strain 110S.";
RL   Submitted (AUG-2015) 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}.
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:GAP62906.1}.
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DR   EMBL; BBZA01000089; GAP62906.1; -; Genomic_DNA.
DR   EMBL; LGKN01000003; KPL89218.1; -; Genomic_DNA.
DR   RefSeq; WP_054492789.1; NZ_LGKN01000003.1.
DR   AlphaFoldDB; A0A0M8K9A0; -.
DR   STRING; 872965.SE16_01575; -.
DR   PATRIC; fig|872965.6.peg.261; -.
DR   InParanoid; A0A0M8K9A0; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000037784; Unassembled WGS sequence.
DR   Proteomes; UP000050502; Unassembled WGS sequence.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR022697; HDH_short.
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   PIRSF; PIRSF036497; HDH_short; 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|PIRSR:PIRSR036497-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000579};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037784};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN          160..338
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT   BINDING         10..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         128
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ   SEQUENCE   345 AA;  37450 MW;  73A8B09A96B44F72 CRC64;
     MQTIDVVLHG VGHVGRHLLR LFQTQADLLR ERHNLTVRVI AAVDSRGAAL NLNGLDIAAL
     LDAKQRSGSV AEAPHGQRGM TLQGVMANVR THAVLLEATP VNLETGEPGL SAMRTALERG
     WDVVSANKAP LVLAYRDLVQ IAHQRHARLA FSATVCGGLP VINVGRYDLA HATITRIEGI
     VNSTTNYILS EMRKGRSFDE ALREAQHAGI AEADPTLDVS GWDAANKLII MANAILHIHA
     TRHDVDVEGI EHLTREQLLD AETNGQTIRL VASAERQANG TYRLRVAPRA LPKTHPLAIL
     EGHQMGVVFE TDINGRIFLA IEEEDPTPTA AAMLRDIVLL ANPRG
//
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