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Database: UniProt
Entry: W1N710_9GAMM
LinkDB: W1N710_9GAMM
Original site: W1N710_9GAMM 
ID   W1N710_9GAMM            Unreviewed;       325 AA.
AC   W1N710;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=D-lactate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BJB45_21595 {ECO:0000313|EMBL:ERL51303.1};
OS   Halomonas huangheensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL51303.1, ECO:0000313|Proteomes:UP000019113};
RN   [1] {ECO:0000313|EMBL:ERL51303.1, ECO:0000313|Proteomes:UP000019113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL51303.1,
RC   ECO:0000313|Proteomes:UP000019113};
RA   Miao C., Wan Y., Jin W.;
RT   "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL   Submitted (AUG-2013) 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}.
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:ERL51303.1}.
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DR   EMBL; AVBC01000030; ERL51303.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1N710; -.
DR   STRING; 1178482.AR456_19110; -.
DR   PATRIC; fig|1178482.3.peg.2072; -.
DR   eggNOG; COG1052; Bacteria.
DR   Proteomes; UP000019113; Unassembled WGS sequence.
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; 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; 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; 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:UP000019113}.
FT   DOMAIN          9..322
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..293
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   325 AA;  35953 MW;  287620D5BA508D4E CRC64;
     MIKVGFFSSQ KYERAFFPQQ ARADVNITHF EQTLTPRTVT LCQGLDAVCV FVNDELNRTV
     LERLAVVGVR LVALRCAGFN NVDLETARRL GIQVCRVPAY SPEAVAEHCV ALILTLSRRT
     HKAYNRVRED NFDLNGLLGF NLYGKTAGII GGGQIGRALA KILVGFGCRV LVSDTQPQQG
     DFEQVELAQL LAESDIISLH CPLNDATFHL IGEAQFAQMK DGVMLINTSR GALIDTHACI
     EALKSRKLGY LGLDVYEQES ELFFRDLSDS IQLDDVFARL ISFPNVLVTG HQGFFTREAL
     QEIANTTLDS LEAFAEGRPL DNKAL
//
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