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Database: UniProt
Entry: A0A1H8HD14_9BURK
LinkDB: A0A1H8HD14_9BURK
Original site: A0A1H8HD14_9BURK 
ID   A0A1H8HD14_9BURK        Unreviewed;       343 AA.
AC   A0A1H8HD14;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:SEN54162.1};
GN   ORFNames=SAMN05428959_102316 {ECO:0000313|EMBL:SEN54162.1};
OS   Duganella sp. CF517.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEN54162.1, ECO:0000313|Proteomes:UP000198691};
RN   [1] {ECO:0000313|Proteomes:UP000198691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA   Varghese N., Submissions S.;
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; FODC01000002; SEN54162.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8HD14; -.
DR   STRING; 1881038.SAMN05428959_102316; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000198691; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198691}.
FT   DOMAIN          4..335
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          117..305
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   343 AA;  36752 MW;  151ABBE563633373 CRC64;
     MKIAVYSAQP YDRRFLDEAR LDALAATPAS PIDAVYFDNR LTIDTVPLAH GCAVVCVFVN
     DILDAEVLDA LHALGVRAVL LRCAGFNNVD VQAGERLGMF MARVPTYAPE AVAEHALALV
     MTLNRRTHRA YARVREGNFA LDGLLGMTLH GKTVGIIGAG QIGTAAAQIF KGIGCTVLVS
     DPAPQLQLQL GAIAARVTLE QLLAQSDIVS LHCPLMEATR HLINADSLAL MKPGAMLVNT
     SRGALIDTMA VIAALKSKQL GALAIDVYEQ ESDLFFHDHS SDIIDDDVFQ RLMTFPNVLV
     TGHQGFFTIE AMREIAAVTF ANLAAYMRGE PTANALGTGA RPT
//
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