ID K5XQQ7_9PROT Unreviewed; 570 AA.
AC K5XQQ7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=MXAZACID_12812 {ECO:0000313|EMBL:EKM99009.1};
OS Acidocella sp. MX-AZ02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKM99009.1, ECO:0000313|Proteomes:UP000006217};
RN [1] {ECO:0000313|EMBL:EKM99009.1, ECO:0000313|Proteomes:UP000006217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKM99009.1,
RC ECO:0000313|Proteomes:UP000006217};
RX PubMed=23405365;
RA Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT AZ02.";
RL Genome Announc. 1:E00041-12(2013).
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}.
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:EKM99009.1}.
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DR EMBL; AMPS01000183; EKM99009.1; -; Genomic_DNA.
DR RefSeq; WP_008494817.1; NZ_JH976209.1.
DR AlphaFoldDB; K5XQQ7; -.
DR STRING; 1214225.MXAZACID_12812; -.
DR PATRIC; fig|1214225.3.peg.2479; -.
DR HOGENOM; CLU_034094_0_0_5; -.
DR Proteomes; UP000006217; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006217}.
FT DOMAIN 38..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT BINDING 72..76
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 80..81
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 139
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 146
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 156
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 254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 259
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 570 AA; 62131 MW; 7DC6799F1445CE98 CRC64;
MPDRNADLIT ALQGAVGAGH VLTAEAATRR FRTGYRFGTG KVLAVVRPGS LVEQWRVLQA
CHQAGVIIIM QASNTGLTGG STPDGDEYDR PIVLISTTRM AKIHLLEGGR QVVCLPGATL
FQLEKTLRPL GREPHSVIGS SCLGASVLGG ISNNSGGALI HRGPAFTQLA IYARVNEAGA
IELVNHIGLR LGNDPEAMLT RLERGDFTAD EIEHPAGRAA SDPDYARHVR EIDAATPARF
NADPRRLCEA SGSAGKLMIF AVRLDSFAAE KETAVFYIGS NDAAALTRIR RDILGGFANL
PVAGEYIHRT AFDIAALYGK DTVIAIEKLG TDRLPALFAA KAKFDAFASN FSFLPKDLSD
RLMQAASQLF PQHLPARMRD YRDRFEHHLL LKMSGPGIAE ARTYLASLFP SAGGDFFECT
PEEGAKAFLH RFAVAGAAIR YRAIHRDTVS DIVALDVALR RNDQEWVERL PAEMDGKLLH
KLYYGHFFCH VFHQDYVVKA GHDPIAIEHE MWGLLDGRGA EYPAEHNVGH LYPAKPALAA
HYQALDPCNC FNPGIGQTSK LYCWGEEEAA
//
