ID Q6D2B5_PECAS Unreviewed; 585 AA.
AC Q6D2B5;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
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:CAG76079.1};
GN OrderedLocusNames=ECA3181 {ECO:0000313|EMBL:CAG76079.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG76079.1, ECO:0000313|Proteomes:UP000007966};
RN [1] {ECO:0000313|EMBL:CAG76079.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG76079.1};
RA Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT "The genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica SCRI1043 and functional genomic
RT identification of novel virulence factors.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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; BX950851; CAG76079.1; -; Genomic_DNA.
DR RefSeq; WP_011094703.1; NC_004547.2.
DR AlphaFoldDB; Q6D2B5; -.
DR STRING; 218491.ECA3181; -.
DR GeneID; 57209866; -.
DR KEGG; eca:ECA3181; -.
DR PATRIC; fig|218491.5.peg.3221; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_034094_0_0_6; -.
DR OrthoDB; 9772552at2; -.
DR Proteomes; UP000007966; 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 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 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:UP000007966}.
FT DOMAIN 48..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT BINDING 82..86
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 90..91
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 149
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 166
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 585 AA; 66163 MW; 935460836C8B43CF CRC64;
MKDDVTSESR ISIDSHDLIR TLTRIVGKPH ILTDKNKTER YRKGFRSGSG EALAVVFPAS
LLEQWRVFKA SIEAGCIVLM QAANTGLTEG STPSGNDYDR EIVIINTLRL DSVQLLDEGR
QVVALPGSTL WHLERVLKPL GREPHSVIGS SCIGASVIGG ICNNSGGSLV HRGPAYTEMA
LYGRVNEQGQ VELINHLGIN LGDTPEAILT RLESQQYDVK DVIYDERQAS DHDYIERVRD
VDADTPSRFN ADERRLFEAA GCAGKLSIFA VRLDTFPAEK SQQVFYIGTN QPQVLTELRR
HMLADFKNLP VAGEYMHRDI FDIAETYGKD TFMMIDKLGT DKLPLFFNLK GQVDTIFSKV
PFLPSHLVDR TMQFLGRLLP SHLPARMKTY RDRFEHHLMV KMAGDGIDEA HRWLEEYFHD
ADGEFFVCTP EEGAKAFLHR FAAAGAAIRY HAVHSNDVEN ILALDIALRR NDREWFEHLP
ADISDMLVHR LYYGHFMCHV FHQDYIVKKG VDVHELKERM LALLDQRGAE YPAEHNVGHL
YQAKPQLKAF YQKSDPTNSL NPGIGKTTKL KNWGCTGCEE HHTNH
//
