ID A0A0X8GZF5_9FIRM Unreviewed; 364 AA.
AC A0A0X8GZF5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|PIRNR:PIRNR036497};
DE Short=HDH {ECO:0000256|PIRNR:PIRNR036497};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|PIRNR:PIRNR036497};
GN ORFNames=AOC36_04475 {ECO:0000313|EMBL:AMC93252.1};
OS Erysipelothrix larvae.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Erysipelothrix.
OX NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC93252.1, ECO:0000313|Proteomes:UP000063781};
RN [1] {ECO:0000313|EMBL:AMC93252.1, ECO:0000313|Proteomes:UP000063781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LV19 {ECO:0000313|EMBL:AMC93252.1,
RC ECO:0000313|Proteomes:UP000063781};
RA Lim S., Kim B.-C.;
RT "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the
RT rhinoceros beetle, Trypoxylus dichotomus.";
RL Submitted (OCT-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|PIRNR:PIRNR036497,
CC 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|PIRNR:PIRNR036497,
CC ECO:0000256|RuleBase:RU004171}.
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DR EMBL; CP013213; AMC93252.1; -; Genomic_DNA.
DR RefSeq; WP_067631834.1; NZ_CP013213.1.
DR AlphaFoldDB; A0A0X8GZF5; -.
DR STRING; 1514105.AOC36_04475; -.
DR KEGG; erl:AOC36_04475; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000063781; 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; 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 Pfam; PF03447; NAD_binding_3; 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|PIRNR:PIRNR036497,
KW ECO:0000256|RuleBase:RU000579};
KW Branched-chain amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW ECO:0000256|RuleBase:RU000579};
KW Isoleucine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW ECO:0000256|RuleBase:RU000579};
KW Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW ECO:0000256|RuleBase:RU000579};
KW NADP {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|PIRSR:PIRSR036497-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036497};
KW Reference proteome {ECO:0000313|Proteomes:UP000063781};
KW Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 7..110
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 118..296
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT BINDING 7..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ SEQUENCE 364 AA; 39973 MW; 874D5280684343B6 CRC64;
MKIAVCGYGV VGKGVVDIID RRDDCEVLYI FTRETLDDKR YTTDYQDILN DKQVDLVVEA
MGGIEPAYSM LKAALEQGKH VVTSNKALVA KHGATLHLCA QKHGVHFLFE GSVGGGIPIL
SALRNGLAHE PIYKIEAILN GTSNYILTQV IETDASFETV LKRAQRLGYA ERDPSDDVDG
FDTARKIAIL GSILTKHFVD YESIYTVGIR HVHPAIYEFA KKMDFKLKLV ACLETTEAGV
TASVEPILLP KKHPLYQVDD VDNAVAVYGK DVGTIVFKGQ GAGREPTASA VVADVLACKN
PYLVNTTWDF EPVDVKRDKG MYAVWLPVEA EIKPFCNTEI SVVIMDYNEA QASGGVFVRI
EGEL
//
