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Database: UniProt
Entry: A0A160JFD8_9PROT
LinkDB: A0A160JFD8_9PROT
Original site: A0A160JFD8_9PROT 
ID   A0A160JFD8_9PROT        Unreviewed;       434 AA.
AC   A0A160JFD8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=A6A40_06580 {ECO:0000313|EMBL:ANC91592.1};
OS   Azospirillum humicireducens.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC91592.1, ECO:0000313|Proteomes:UP000077405};
RN   [1] {ECO:0000313|EMBL:ANC91592.1, ECO:0000313|Proteomes:UP000077405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC91592.1,
RC   ECO:0000313|Proteomes:UP000077405};
RX   PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA   Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT   "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT   from a microbial fuel cell.";
RL   Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
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; CP015285; ANC91592.1; -; Genomic_DNA.
DR   RefSeq; WP_063634689.1; NZ_CP015285.1.
DR   AlphaFoldDB; A0A160JFD8; -.
DR   STRING; 1226968.A6A40_06580; -.
DR   KEGG; ahu:A6A40_06580; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000077405; 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   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   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:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000579};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN          355..430
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT   BINDING         14..21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         111
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ   SEQUENCE   434 AA;  45438 MW;  CEB5C59425737F1C CRC64;
     MPNAQQAPLK IAVAGLGTVG AGVLKLLDTQ ASLIEQRCGR RIEVVAVSAR SKGKDRGVDL
     SKVQWFDDPV AMAAQSGADL VVELIGGSEG PARDTVATAI ETGKHVVTAN KALLAVHGTE
     IAQKAEARGL TVAFEAAVAG GIPIIKGLRE GLAGNAVSEI HGILNGTCNY ILTEMRTTGR
     DFADVLADAQ ALGYAEADPS FDIDGVDAAH KLAILASVAF GTPVDFPSVY VEGIRQVSAI
     DFDYADQLGF RIKLLGIARR TDAGVEQRVH PCMVPKTAPI ASVDGVFNAV VAQADFADRV
     LFVGRGAGAG PTASAVVADL IDIARGRSTP TFGVPADRLG AAPPSPMETR RGSYYVRLMV
     VDRPGVIADI AAAMRDQNVS MEQFLQRGRS PGEGVPVVLT THDTDEAAMQ RALATIAASD
     NVLEPPRMIR IEQF
//
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