ID A0A0A6YSJ2_9FLAO Unreviewed; 563 AA.
AC A0A0A6YSJ2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Quinone-dependent D-lactate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02092};
DE EC=1.1.5.12 {ECO:0000256|HAMAP-Rule:MF_02092};
DE AltName: Full=D-lactate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02092};
DE Short=D-LDH {ECO:0000256|HAMAP-Rule:MF_02092};
GN Name=dld {ECO:0000256|HAMAP-Rule:MF_02092};
GN ORFNames=HMPREF9074_09170 {ECO:0000313|EMBL:KHE68358.1};
OS Capnocytophaga sp. oral taxon 329 str. F0087.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE68358.1, ECO:0000313|Proteomes:UP000030579};
RN [1] {ECO:0000313|EMBL:KHE68358.1, ECO:0000313|Proteomes:UP000030579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0087 {ECO:0000313|EMBL:KHE68358.1,
RC ECO:0000313|Proteomes:UP000030579};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_02092};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_02092, ECO:0000256|PIRSR:PIRSR000101-1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02092};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_02092};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02092}.
CC -!- SIMILARITY: Belongs to the quinone-dependent D-lactate dehydrogenase
CC family. {ECO:0000256|HAMAP-Rule:MF_02092}.
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:KHE68358.1}.
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DR EMBL; AFHP02000185; KHE68358.1; -; Genomic_DNA.
DR RefSeq; WP_009391238.1; NZ_KN390041.1.
DR AlphaFoldDB; A0A0A6YSJ2; -.
DR STRING; 706436.HMPREF9074_09170; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_034094_0_0_10; -.
DR OrthoDB; 9772552at2; -.
DR Proteomes; UP000030579; Unassembled WGS sequence.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.610; D-lactate dehydrogenase, cap domain, subdomain 1; 2.
DR Gene3D; 3.30.1370.20; D-lactate dehydrogenase, cap domain, subdomain 2; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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 PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF3; QUINONE-DEPENDENT D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF09330; Lact-deh-memb; 1.
DR PIRSF; PIRSF000101; D-lactate_dh; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02092};
KW FAD {ECO:0000256|HAMAP-Rule:MF_02092, ECO:0000256|PIRSR:PIRSR000101-1};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02092};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02092};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02092};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_02092}.
FT DOMAIN 36..207
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT BINDING 70..74
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02092,
FT ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 78..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02092,
FT ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02092,
FT ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02092,
FT ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 154
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02092,
FT ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 251
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 256
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02092,
FT ECO:0000256|PIRSR:PIRSR000101-1"
SQ SEQUENCE 563 AA; 63358 MW; 489AEED443C18356 CRC64;
MNTQNLLATL RNIVGAKYVM TDPAQTERFR TGYRFGTGNA IAVVRPATLW EQWQVLEACV
AADVIVISQA ANTGITGGSN PFGNDYDRDV VIINTMRNDN VQLILNAEQA VCLPGSTLNH
LEAELKPYGR EPHSVIGSSC IGASVIGGVC NNSGGSLVQR GPAYTEMSLF AQLNAEGKLE
LINHLGIDLG ETPKEILTNL QEGKYQTKDI KNTGKKGHDH HYCDHVRQIN ADTPARFNAD
PARLYEASGS AGRLAIFAVR VDTFAAEKNT AVFYIGTNDT AVLTKLRRDM LGSFEQIPIS
GEYIHRTAFD IAAKYGKDTF WYIKNVGTEY LPRLFAMKAW GDRVAKKLPF MPNHFSEKFL
QATSKLMPKH LPQILWDYRN QYEHHLILKM GGKGVEEARE YLKKEFADSS KGAYIECDAK
LAQAAMLLRF AVASAAIRYR SVHEKEVEDI VALDIALRRN DEDWFEKLPP EIDNKILHKL
YYGHFMCHVF HQDYVIKKGY NCEEIEEEML KLLDKRGAQY PAEHNVGHLY HANDDLKNFY
NSLDPTNTFN PGIGKTSKKK DWK
//
