ID G7EP88_9GAMM Unreviewed; 326 AA.
AC G7EP88;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:GAA62711.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:GAA62711.1};
GN Name=ldhA {ECO:0000313|EMBL:GAA62711.1};
GN ORFNames=P20311_0484 {ECO:0000313|EMBL:GAA62711.1};
OS Pseudoalteromonas sp. BSi20311.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=383911 {ECO:0000313|EMBL:GAA62711.1, ECO:0000313|Proteomes:UP000005146};
RN [1] {ECO:0000313|Proteomes:UP000005146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSi20311 {ECO:0000313|Proteomes:UP000005146};
RX PubMed=22275105; DOI=10.1128/JB.06427-11;
RA Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT ice.";
RL J. Bacteriol. 194:908-909(2012).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA62711.1}.
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DR EMBL; BADU01000022; GAA62711.1; -; Genomic_DNA.
DR RefSeq; WP_008109263.1; NZ_BADU01000022.1.
DR AlphaFoldDB; G7EP88; -.
DR Proteomes; UP000005146; Unassembled WGS sequence.
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}.
FT DOMAIN 4..325
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 35939 MW; E1B919416F8C8374 CRC64;
MKIAFFSAQK YERPFFEQSL TGFSNIAITY FEQSLSTHTA VLAKEFDAVC VFVNDSVDKA
VIDQLAIFGV NTILLRCAGF NNVDLAAAKQ HGMRVLRVPA YSPEAVAEHC IALMLTLSRK
THKAYNRVRE DNFDLNGLLG FNLHNKTVGI IGCGKIGQAL CNILTGFGAH ILVCDPNAQA
GNYTITDLNT LLTQSDIISL HCPLNEHTHH LIDDDAFAAM KTGVMLINTS RGALVNSKAC
IKALKSQKLG YLGLDVYEQE SELFFKNHSD DINQDDIFSR LVSFKNVLIT GHQGFFTQEA
LTEIANITLQ NAFEVTQGKS LTNEVL
//
