ID A0A1I6ZQQ1_9BACT Unreviewed; 333 AA.
AC A0A1I6ZQQ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:SFT64970.1};
GN ORFNames=SAMN04489724_1408 {ECO:0000313|EMBL:SFT64970.1};
OS Algoriphagus locisalis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=305507 {ECO:0000313|EMBL:SFT64970.1, ECO:0000313|Proteomes:UP000199673};
RN [1] {ECO:0000313|EMBL:SFT64970.1, ECO:0000313|Proteomes:UP000199673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23445 {ECO:0000313|EMBL:SFT64970.1,
RC ECO:0000313|Proteomes:UP000199673};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPBF01000002; SFT64970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6ZQQ1; -.
DR STRING; 305507.SAMN04489724_1408; -.
DR OrthoDB; 1522997at2; -.
DR Proteomes; UP000199673; 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; 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}.
FT DOMAIN 4..328
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; 37027 MW; CBD45A8DC13D901B CRC64;
MKVAFFSTKS YDRQSFDHYL PESSHDFTYF EPKLDHNTVA LAKGFDAICT FVNDHLDEKT
LKKLSKLGVN TIVLRCAGYN QVDLKTAAEL GFKICRVPAY SPEAVAEHAL ALLMTLSRKT
HKAYNRVREN NYSLEGLSGF NINGKTAGVI GTGAIGRAFC KIMLGMGCKV LAYDPYENEE
LTSLGVEYLA LEELLASSDI ISLHCPLTPD TFHLISQKTL AQMKDGVIII NTSRGALIET
KAVIKALKSK KVGNLGIDVY EQEEDLFFQN RSEEILQDET IARLMTFTNV LITGHQAFLT
NEALAQIATT TLENLDELEA GKKLTNEVVW KEE
//
