ID D4GMS7_PANAM Unreviewed; 575 AA.
AC D4GMS7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:ADD76412.1};
GN OrderedLocusNames=PANA_1245 {ECO:0000313|EMBL:ADD76412.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD76412.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD76412.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD76412.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(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; CP001875; ADD76412.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GMS7; -.
DR STRING; 706191.PANA_1245; -.
DR KEGG; pam:PANA_1245; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_034094_0_0_6; -.
DR Proteomes; UP000001702; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001702}.
FT DOMAIN 45..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT BINDING 79..83
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 87..88
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 153
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 163
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 260
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000101-1"
FT BINDING 265
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 575 AA; 64299 MW; 054D923423FE782B CRC64;
MHKTRELPMM TPSALIADLR RQVGSGNVLT EAAHTARYRK GFRSGEGDAL AVVFPATLLE
LWRVLQTLVT ADAIILMQAA NTGLTEGSTP QGNDYDRPLV IVSTLRLDKL QLIDNGKQVL
AFPGSTLYQL EKILAPLGRE PHSVIGSSCI GASVLGGICN NSGGSLIKRG PAYSEMALFA
QIDAQGRLKL VNHLGIELGT TPEEILGRLD DDRWQPGDVL HDGRHASDHD YAERVRDVDA
DTPARFNADA RRLFEASGCA GKLAVFAVRL DTFAREPQQQ VFYIGTNDAS VLGDLRCHML
ANFNNLPVAA EYMHRDIYDI AEVYGKDTFL MIDKLGTDKM PLFFSLKGRV DGWLNKLSFI
KPHLSDRLLQ RVSRLFPAHL PKRMKQYRDK YQHHLMLKMS GDGIAEARDY LREFFREGGG
EFFECEGKEG AHAFLHRFAA AGAAVRYHAV HADEVEDILA LDIALRRNDK AWFESLPDEI
TQSISHRLYY GHFFCHVFHQ DYIVKKGVDV HALKEKMLAI LHSRGAEYPA EHNVGHLYQA
QPQLTAFYRK LDPTNSFNPG IGKTSKLKGW AVKQP
//
