ID D8MM49_ERWBE Unreviewed; 564 AA.
AC D8MM49;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=EbC_04020 {ECO:0000313|EMBL:CAX57933.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|EMBL:CAX57933.1, ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX57933.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX57933.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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; FP236843; CAX57933.1; -; Genomic_DNA.
DR RefSeq; WP_013200440.1; NC_014306.1.
DR AlphaFoldDB; D8MM49; -.
DR STRING; 634500.EbC_04020; -.
DR KEGG; ebi:EbC_04020; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_034094_0_0_6; -.
DR Proteomes; UP000008793; 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; 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 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:UP000008793}.
FT DOMAIN 37..265
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT BINDING 71..75
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 79..80
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 138
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 145
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 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 257
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 564 AA; 62900 MW; 93607A6802BEF877 CRC64;
MVKDSGVITR LEQVLGKEQV LTSEDSKAYY TKGFRVGGGN ALAVAIPQTL MQLWQVLQAC
VACDTIILMQ AANTGVTGGS TPDGADYDRE VVIVSTRRLK GVQVIDQARQ VLAFPGSTLT
ELEKALLPHG KEPHSVIGSS CIGASVIGGV CNNSGGSLIR RGPAFTEKSL FARINADGSL
QLVNHLGIEL GSTPEEMIAN LESQQFTTGT APDWEGKIWA DDYAAILRNV DADTPTRYNG
NVQYLHDSSG SAGKIAVFAV RLSTFDASDR TRTFYIGTND ETELVALRRY LLEGLSELPL
QAEYIHRDAF DLTVRYAKHM YWAINRFGPE ALPQLMANKA KWDIRVKNLK VLPANFVDKV
LQFANNVTPK GVAPRILDYR ERFEHHLMIK AEARHADELQ RLLDTFFSDR SGQYFACDAR
EERDAFLVRF GVGGCTISYC DYKGINTDQR LIAFDVALRR NDTEWRIKLP QALQDQVLED
SCCGHFFCFV NHQDYILKPG VDALAFKHDV LEYLDRRGAK YPAEHNVGHL YHASCEHESH
MRQLDPTNSC NPGIGKTSKK KFWQ
//
