ID B0VND1_ACIBS Unreviewed; 576 AA.
AC B0VND1;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
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 ECO:0000313|EMBL:CAO99501.1};
GN OrderedLocusNames=ABSDF0088 {ECO:0000313|EMBL:CAO99501.1};
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAO99501.1, ECO:0000313|Proteomes:UP000001741};
RN [1] {ECO:0000313|EMBL:CAO99501.1, ECO:0000313|Proteomes:UP000001741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF {ECO:0000313|EMBL:CAO99501.1,
RC ECO:0000313|Proteomes:UP000001741};
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
CC -!- FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate.
CC {ECO:0000256|HAMAP-Rule:MF_02092, ECO:0000256|PIRNR:PIRNR000101}.
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 ECO:0000256|PIRNR:PIRNR000101};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_02092, ECO:0000256|PIRNR:PIRNR000101,
CC ECO:0000256|PIRSR:PIRSR000101-1};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02092}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02092}; 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}.
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DR EMBL; CU468230; CAO99501.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VND1; -.
DR KEGG; abm:ABSDF0088; -.
DR HOGENOM; CLU_034094_0_0_6; -.
DR Proteomes; UP000001741; Chromosome.
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 InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF3; QUINONE-DEPENDENT D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF01565; FAD_binding_4; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02092};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02092};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_02092};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02092,
KW ECO:0000256|PIRNR:PIRNR000101}; Membrane {ECO:0000256|HAMAP-Rule:MF_02092};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02092,
KW ECO:0000256|PIRNR:PIRNR000101};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_02092, ECO:0000256|PIRNR:PIRNR000101}.
FT DOMAIN 47..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT BINDING 81..85
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 89..90
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 148
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 155
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 165
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 263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 268
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 576 AA; 65070 MW; FAE032B9149BB6BF CRC64;
MDDQKETIMQ TFSPKAVIER LQNIVGRSYV LTDDQSTRQY RQGRRFGEGK VLAVVVPGTL
LEQWQVLQAA IEAGCIVIMQ AANTGLTGGS TPYGDDYDRP VLVMSTRRLK GIQVIHDGKQ
VICLPGATLD NLEQILKGYD REPHSVIGSS CIGASVLGGV CNNSGGALVR RGPAYTELAL
YAQVNAAGQL ELVNHLGVNL GSTPEEILTR LEKQQYQAVD ILDDNEKQAS DHRYGHDVTQ
VDEDTPARFN ADPSRLFEAS GSAGKVCVFA VRLDTYEKVE SSVFYIGSND ADDLTAIRRY
LLTSLPSLPI AGEYIHRDAY LIGEKYGKDT FLFIEKFGTA NVPKAFAMKD KVDGFLEKFK
IKGLTDQILQ AITFFLPSHL PKRMTEYRDR YEHHLVLRVE NNSKAQTEQF LKEYFTVHQS
GNYFVCSEEE GRKAFLHRFA IAGAAIRYRD THRSEVEDIV ALDIALRRND REWVEQLPAE
MEKKIIHKLY YGHFFCHVFH QDYILKKGHD PLEIEHQMWK LLDARRAEYP AEHNVGHLYI
AKPALANFYQ KLDPTNSFNV GIGHTSKLKY WGKAKS
//
