ID A0A1I1RB71_9FLAO Unreviewed; 362 AA.
AC A0A1I1RB71;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN ORFNames=SAMN05216297_106178 {ECO:0000313|EMBL:SFD27640.1};
OS Flavobacterium phragmitis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=739143 {ECO:0000313|EMBL:SFD27640.1, ECO:0000313|Proteomes:UP000199672};
RN [1] {ECO:0000313|EMBL:SFD27640.1, ECO:0000313|Proteomes:UP000199672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10370 {ECO:0000313|EMBL:SFD27640.1,
RC ECO:0000313|Proteomes:UP000199672};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005062}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056}.
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DR EMBL; FOMH01000006; SFD27640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1RB71; -.
DR STRING; 739143.SAMN05216297_106178; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000199672; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43070; -; 1.
DR PANTHER; PTHR43070:SF3; 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.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 12..146
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 154..348
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
SQ SEQUENCE 362 AA; 40953 MW; 41C8872E5A0752A4 CRC64;
MSKLKINIIL FGIGNIGSTL INQIIESQEF FLESKNVDFH FPIITNSTVA FFEKEGLGYA
WETNFRQLAV PFKVEDIVEF AKENEFENLI AVDATASDEL VKHYNTLIQN GFNIVAVNKK
ANTLPIDLYK ELRSNLKKYD KEFLYETSVD TGIPVLQTLR DLYYSGEKIT KIRGVFSDNL
SYVFNRFSAE DVSFSSVLKD ASLLGLMKSN FKEDLSGNDT ARKLLILARE IGKDFEFSDI
QIKPFITDEH LEKNGVLNKD AIDKSFKATK ITQADNHVLR YIGEFDVEKN KLEVKLISEP
ADSPIGKLKG SDTIFEIFTQ SYADVPIVIQ SAPACKQAIS RGIIADILKV TEKIRNKEAV
WL
//