ID A0A248KJE8_9ENTR Unreviewed; 329 AA.
AC A0A248KJE8; A0A6G9RL02;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:ASG63492.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:ASG63492.1};
GN ORFNames=CEW81_13365 {ECO:0000313|EMBL:ASG63492.1}, GY169_12845
GN {ECO:0000313|EMBL:QIR27634.1};
OS Kluyvera genomosp. 3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kluyvera.
OX NCBI_TaxID=2774055 {ECO:0000313|EMBL:ASG63492.1, ECO:0000313|Proteomes:UP000197098};
RN [1] {ECO:0000313|EMBL:ASG63492.1, ECO:0000313|Proteomes:UP000197098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YDC799 {ECO:0000313|EMBL:ASG63492.1,
RC ECO:0000313|Proteomes:UP000197098};
RA Ito R., Pacey M.P., Doi Y.;
RT "Origin of plasmid-mediated fosfomycin resistance gene fosA3.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QIR27634.1, ECO:0000313|Proteomes:UP000503580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PO2S7 {ECO:0000313|EMBL:QIR27634.1,
RC ECO:0000313|Proteomes:UP000503580};
RA Singha K.M.;
RT "Whole genome PO2S7.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP022114; ASG63492.1; -; Genomic_DNA.
DR EMBL; CP050321; QIR27634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248KJE8; -.
DR KEGG; kgo:CEW81_13365; -.
DR Proteomes; UP000197098; Chromosome.
DR Proteomes; UP000503580; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12183; LDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000197098}.
FT DOMAIN 3..328
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..297
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 329 AA; 36282 MW; 6897EFA29C37F1AA CRC64;
MKIAVYSTKQ YDKKYLQNVN QAYGFELEFF DFLLTEKTAK TAHGCEAVCI FVNDDGSRPV
LEELKKNGVK YIALRCAGFN NVDLDAAKEL GLRVVRVPAY DPEAVAEHAI GLMMTLNRRI
HRAYQRTRDA NFSLEGLTGF TMFGKTAGVI GTGKIGVAAL RILKGFGMRL LAFDPYPSAA
ALELGVEYVD LPTLFAESDV ISLHCPLTPE NYHLLNASAF EKMKDGVMIV NTSRGALIDS
QAAIEALKTQ KIGALGMDVY ENERDLFFED KSNDVIQDDV FRRLSACHNV LFTGHQAFLT
AEALTSISET TLQNLQQIDT GTDCPNAIA
//
