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Database: UniProt
Entry: A0A1B1Z1B0_9BACI
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ID   A0A1B1Z1B0_9BACI        Unreviewed;       426 AA.
AC   A0A1B1Z1B0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=ABE41_004585 {ECO:0000313|EMBL:ANX11272.1};
OS   Fictibacillus arsenicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX11272.1, ECO:0000313|Proteomes:UP000077412};
RN   [1] {ECO:0000313|EMBL:ANX11272.1, ECO:0000313|Proteomes:UP000077412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-54 {ECO:0000313|EMBL:ANX11272.1,
RC   ECO:0000313|Proteomes:UP000077412};
RA   Zheng Z.;
RT   "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT   toxicity to nematodes and a potential arsenic-resistance activity.";
RL   Submitted (AUG-2016) 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; CP016761; ANX11272.1; -; Genomic_DNA.
DR   RefSeq; WP_066286944.1; NZ_CP016761.1.
DR   AlphaFoldDB; A0A1B1Z1B0; -.
DR   STRING; 255247.ABE41_004585; -.
DR   KEGG; far:ABE41_004585; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000077412; 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; 3.40.50.720; 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:UP000077412};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN          10..127
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          136..313
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
SQ   SEQUENCE   426 AA;  46097 MW;  8C856FA38A7979D6 CRC64;
     MAPIKAALLG FGTVGQGVYE ALKTHREQLK SVLGEEVIIE AILVKDGAKK RDVDEHILVT
     TDFDEVLNIP DLQIVFEAIV GEEPGFTYLS KAIEKGCRVI TANKVMFARH GKTLLEKAEA
     AGVSVGYEAT TAGGTPIIRS ISQLLQVNDI LSVEAILNGT SNYILTNMRE KGSAFEDVLK
     TAQDLGYAEA DPVNDVEGFD AFYKLMILSE LSFGSSPNWD EVERKGITEV SSEQIEVFTR
     WGYKVKHLAR IRSDSGLFTA SVKPVLVDSE HPLYGVEDVQ NAIMVETSLA GKVTVQGAGA
     GKLPTASAMV EDLTYVLQSH SGAAVRKKQS VLKVDSSSSE SGSSSLVGEY VVIGSSVGFN
     GSDDIQLLKQ DVRGDLVYLL IRCHEETAKS LKANSELVVY EVAGKLKPAE VKVEDRDLVL
     QRVINL
//
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