DLD_HAEIN
ID DLD_HAEIN Reviewed; 564 AA.
AC P45295;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Quinone-dependent D-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02092};
DE EC=1.1.5.12 {ECO:0000255|HAMAP-Rule:MF_02092};
DE AltName: Full=D-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02092};
DE Short=D-LDH {ECO:0000255|HAMAP-Rule:MF_02092};
GN Name=dld {ECO:0000255|HAMAP-Rule:MF_02092}; OrderedLocusNames=HI_1649;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate.
CC {ECO:0000255|HAMAP-Rule:MF_02092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + a quinone = a quinol + pyruvate;
CC Xref=Rhea:RHEA:51468, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02092};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02092};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02092}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02092}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02092}.
CC -!- SIMILARITY: Belongs to the quinone-dependent D-lactate dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_02092}.
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DR EMBL; L42023; AAC23296.1; -; Genomic_DNA.
DR PIR; I64134; I64134.
DR RefSeq; NP_439791.1; NC_000907.1.
DR RefSeq; WP_005694374.1; NC_000907.1.
DR AlphaFoldDB; P45295; -.
DR SMR; P45295; -.
DR STRING; 71421.HI_1649; -.
DR EnsemblBacteria; AAC23296; AAC23296; HI_1649.
DR KEGG; hin:HI_1649; -.
DR PATRIC; fig|71421.8.peg.1725; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_034094_0_0_6; -.
DR OMA; YEHHLML; -.
DR PhylomeDB; P45295; -.
DR BioCyc; HINF71421:G1GJ1-1666-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0102029; F:D-lactate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0019516; P:lactate oxidation; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.30.1370.20; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.610; -; 2.
DR HAMAP; MF_02092; DLDH_Dld; 1.
DR InterPro; IPR016172; D-lactate_DH_C-sub1.
DR InterPro; IPR016173; D-lactate_DH_C-sub2.
DR InterPro; IPR012256; D_lactate_DH.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR015409; Lactate_DH_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF09330; Lact-deh-memb; 1.
DR PIRSF; PIRSF000101; D-lactate_dh; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Quinone; Reference proteome.
FT CHAIN 1..564
FT /note="Quinone-dependent D-lactate dehydrogenase"
FT /id="PRO_0000084389"
FT DOMAIN 36..207
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 70..74
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 78..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 154
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT BINDING 256
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
SQ SEQUENCE 564 AA; 64126 MW; D1211B2D3D5C6418 CRC64;
MSVQQLISRL TDIVGSRYII TDPTKTEAYR SGYRFGTGNA LAVVRPATLL EFWNIVKVCV
EHDVIVINQA ANTGLTGGST PDGNDYDRDI VVINTMRIDG IQLINNASQV ICLPGSTLNE
LENQLKPFGR EPHSVIGSSC IGASVIGGIC NNSGGALVQR GPAYTEMALY AQLNEKGELE
LKNHLGIDLG ETPEEILTNL QEKRYQVKDI RQDCGHGHDH YYCNYVRQVD EGSPARFNAD
PARHYEASGC AGKLAVFAVR LDTFPLEKET AVFYIGTNQT SVLSDIRRHM LVNFEVLPIS
GEYIHRDAFD IAAKYGKDTF WVIKKFGTHW LPKLFSLKSN VDRIGKKFFF LPQHLSDKFM
QTVSKFIPEH LPQSLWDYRN KYEHHLIIKM GGKGIQEARE YLESYIADGS KGGYFECNAI
ETQAAMLHRF AVASAAIRYR AIHEKEVEEI VALDVALRRN DQDWFEVLPP EIDNRIISKL
YYGHFMCHVF HQDYIVKKGY DYEELEYEML KLLDKRGAQY PAEHNVGHLY EAKPTLRKFY
KELDPTNSFN PGIGKTTRKK YWAE
