ID C3LR45_VIBCM Unreviewed; 325 AA.
AC C3LR45;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=2-hydroxyacid dehydrogenase family protein {ECO:0000313|EMBL:ACP06723.1};
GN OrderedLocusNames=VCM66_2426 {ECO:0000313|EMBL:ACP06723.1};
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112 {ECO:0000313|EMBL:ACP06723.1, ECO:0000313|Proteomes:UP000001217};
RN [1] {ECO:0000313|EMBL:ACP06723.1, ECO:0000313|Proteomes:UP000001217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2 {ECO:0000313|EMBL:ACP06723.1,
RC ECO:0000313|Proteomes:UP000001217};
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001233; ACP06723.1; -; Genomic_DNA.
DR RefSeq; WP_000056892.1; NC_012578.1.
DR AlphaFoldDB; C3LR45; -.
DR KEGG; vcm:VCM66_2426; -.
DR HOGENOM; CLU_019796_1_3_6; -.
DR Proteomes; UP000001217; Chromosome I.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12162; 2-Hacid_dh_4; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; 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}.
FT DOMAIN 38..325
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 325 AA; 35451 MW; 1AAB12A2022EB5F1 CRC64;
MSLPTTSLPT VVFLDRATIP RHISLPALPF EHHWLEYDAC EPQQVVERLL AADIVITNKV
VLTREMLIQL PKLKLIAISA TGTNNVDLPA CRDLNIAVCN VQGYATRSVP EHVVAMMFAL
RRNLIGYHND IAAGEWQRHK QFCFFTHPIG DIAGSTMGII GSGALGQATA NLARALGMHV
LLAERKGQVE CRDGYTSFEQ VLAQSDVLSL HCPLTDETRN IISEAELAQM NPNALLINTG
RGGLVDEQAL VDALKRRQIA GAGVDVFSAE PADMDNPLIA NRDLPNLLLT PHVAWGSDSS
IQQLATILID NISAFMRGEA KNRVV
//
