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Database: UniProt
Entry: A0A1H1Q6K0_9FLAO
LinkDB: A0A1H1Q6K0_9FLAO
Original site: A0A1H1Q6K0_9FLAO 
ID   A0A1H1Q6K0_9FLAO        Unreviewed;       333 AA.
AC   A0A1H1Q6K0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:SDS19131.1};
GN   ORFNames=SAMN04515667_1614 {ECO:0000313|EMBL:SDS19131.1};
OS   Formosa sp. Hel1_31_208.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1798225 {ECO:0000313|EMBL:SDS19131.1, ECO:0000313|Proteomes:UP000199458};
RN   [1] {ECO:0000313|EMBL:SDS19131.1, ECO:0000313|Proteomes:UP000199458}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_31_208 {ECO:0000313|EMBL:SDS19131.1,
RC   ECO:0000313|Proteomes:UP000199458};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; LT629733; SDS19131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1Q6K0; -.
DR   STRING; 1798225.SAMN04515667_1614; -.
DR   OrthoDB; 9777288at2; -.
DR   Proteomes; UP000199458; 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; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199458}.
FT   DOMAIN          3..327
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   333 AA;  37443 MW;  3933313D290E94D8 CRC64;
     MKVLVYSAKA FEIPYLEKAN HQKHQLTFVE NALSSETAMQ AVGYEIISIF SADDACFLTL
     EKLKDFGVKY ISLRSVGHDN VNLRAATRLN IRVANVPAYS PYAIAEHGVS LLLTLNRKLI
     ESNHRVKQYN FNLDDLVGFD LNKKTVGIIG TGKIGSVMAK IMNGFGCKLL GYDISEDKNL
     VQNYNLKYTA LQELCEQSDI ISIHVPLNAE THYLIDEELI FHMKKDVIII NTARGAIINT
     EHLIDALKKD KIGAYGSDVF ENEKGIFFKN RSKHIPDDLL LIQLNAFPNV LLTGHHAFLT
     EEALTNIAET TIDNLNRWSL NEETENELTD IST
//
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