DLD_ECOLI
ID DLD_ECOLI Reviewed; 571 AA.
AC P06149; Q2MAU6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Quinone-dependent D-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000305};
DE EC=1.1.5.12 {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:3013300, ECO:0000269|PubMed:7578233};
DE AltName: Full=(R)-lactate:quinone 2-oxidoreductase {ECO:0000305};
DE AltName: Full=D-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000303|PubMed:4575624, ECO:0000303|PubMed:4582730};
DE Short=D-LDH {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000303|PubMed:3882663};
DE AltName: Full=Respiratory D-lactate dehydrogenase {ECO:0000305};
GN Name=dld {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000303|PubMed:6386470};
GN OrderedLocusNames=b2133, JW2121;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6386470; DOI=10.1111/j.1432-1033.1984.tb08473.x;
RA Campbell H.D., Rogers B.L., Young I.G.;
RT "Nucleotide sequence of the respiratory D-lactate dehydrogenase gene of
RT Escherichia coli.";
RL Eur. J. Biochem. 144:367-373(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-18.
RX PubMed=3882663; DOI=10.1128/jb.161.3.1059-1068.1985;
RA Rule G.S., Pratt E.A., Chin C.C.Q., Wold F., Ho C.;
RT "Overproduction and nucleotide sequence of the respiratory D-lactate
RT dehydrogenase of Escherichia coli.";
RL J. Bacteriol. 161:1059-1068(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [7]
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=4575624; DOI=10.1021/bi00737a016;
RA Futai M.;
RT "Membrane D-lactate dehydrogenase from Escherichia coli. Purification and
RT properties.";
RL Biochemistry 12:2468-2474(1973).
RN [8]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=ML 308-225;
RX PubMed=4582730; DOI=10.1016/s0021-9258(19)43353-x;
RA Kohn L.D., Kaback H.R.;
RT "Mechanisms of active transport in isolated bacterial membrane vesicles.
RT XV. Purification and properties of the membrane-bound D-lactate
RT dehydrogenase from Escherichia coli.";
RL J. Biol. Chem. 248:7012-7017(1973).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=ML 308-225;
RX PubMed=1092688; DOI=10.1016/s0021-9258(19)41416-6;
RA Short S.A., Kaback H.R., Kohn L.D.;
RT "Localization of D-lactate dehydrogenase in native and reconstituted
RT Escherichia coli membrane vesicles.";
RL J. Biol. Chem. 250:4291-4296(1975).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3013300; DOI=10.1021/bi00357a004;
RA Matsushita K., Kaback H.R.;
RT "D-lactate oxidation and generation of the proton electrochemical gradient
RT in membrane vesicles from Escherichia coli GR19N and in proteoliposomes
RT reconstituted with purified D-lactate dehydrogenase and cytochrome o
RT oxidase.";
RL Biochemistry 25:2321-2327(1986).
RN [11]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2185834; DOI=10.1021/bi00465a017;
RA Peersen O.B., Pratt E.A., Truong H.T., Ho C., Rule G.S.;
RT "Site-specific incorporation of 5-fluorotryptophan as a probe of the
RT structure and function of the membrane-bound D-lactate dehydrogenase of
RT Escherichia coli: a 19F nuclear magnetic resonance study.";
RL Biochemistry 29:3256-3262(1990).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=7578233; DOI=10.1016/0167-4838(95)00120-j;
RA Sun Z.Y., Dowd S.R., Felix C., Hyde J.S., Ho C.;
RT "Stopped-flow kinetic and biophysical studies of membrane-associated D-
RT lactate dehydrogenase of Escherichia coli.";
RL Biochim. Biophys. Acta 1252:269-277(1995).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT TRP-368 IN COMPLEX WITH
RP FAD, COFACTOR, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=10944213; DOI=10.1073/pnas.97.17.9413;
RA Dym O., Pratt E.A., Ho C., Eisenberg D.;
RT "The crystal structure of D-lactate dehydrogenase, a peripheral membrane
RT respiratory enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9413-9418(2000).
CC -!- FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate. Electrons
CC derived from D-lactate oxidation are transferred to the
CC ubiquinone/cytochrome electron transfer chain, where they may be used
CC to provide energy for the active transport of a variety of amino acids
CC and sugars across the membrane. {ECO:0000269|PubMed:2185834,
CC ECO:0000269|PubMed:3013300, ECO:0000269|PubMed:4575624,
CC ECO:0000269|PubMed:4582730, ECO:0000269|PubMed:7578233}.
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:0000255|HAMAP-Rule:MF_02092,
CC ECO:0000269|PubMed:3013300, ECO:0000269|PubMed:7578233};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02092,
CC ECO:0000269|PubMed:10944213, ECO:0000269|PubMed:4575624,
CC ECO:0000269|PubMed:4582730, ECO:0000269|PubMed:7578233};
CC -!- ACTIVITY REGULATION: Inhibited by 2-hydroxy-3-butynoic acid, but not by
CC p-chloromercuribenzoate, n-ethylmaleimide, or 5,5'-dithiobis(2-
CC nitrobenzoic acid). {ECO:0000269|PubMed:4582730}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for D-lactate {ECO:0000269|PubMed:2185834};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02092, ECO:0000269|PubMed:1092688, ECO:0000269|PubMed:4575624,
CC ECO:0000269|PubMed:4582730}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02092,
CC ECO:0000269|PubMed:1092688}. Note=May bind the membrane through
CC electrostatic rather than hydrophobic forces.
CC {ECO:0000305|PubMed:10944213}.
CC -!- DOMAIN: Contains 3 domains: the flavin adenine dinucleotide (FAD)-
CC binding domain, the cap domain and the membrane-binding domain.
CC {ECO:0000269|PubMed:10944213}.
CC -!- SIMILARITY: Belongs to the quinone-dependent D-lactate dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60530.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M10038; AAA23688.1; -; Genomic_DNA.
DR EMBL; X01067; CAA25531.1; -; Genomic_DNA.
DR EMBL; U00007; AAA60530.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75194.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76610.1; -; Genomic_DNA.
DR PIR; A21893; DEECDL.
DR RefSeq; NP_416637.1; NC_000913.3.
DR RefSeq; WP_000097403.1; NZ_LN832404.1.
DR PDB; 1F0X; X-ray; 1.90 A; A/B=1-571.
DR PDBsum; 1F0X; -.
DR AlphaFoldDB; P06149; -.
DR SMR; P06149; -.
DR BioGRID; 4260452; 20.
DR IntAct; P06149; 17.
DR STRING; 511145.b2133; -.
DR BindingDB; P06149; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB00756; Hexachlorophene.
DR DrugCentral; P06149; -.
DR jPOST; P06149; -.
DR PaxDb; P06149; -.
DR PRIDE; P06149; -.
DR EnsemblBacteria; AAC75194; AAC75194; b2133.
DR EnsemblBacteria; BAE76610; BAE76610; BAE76610.
DR GeneID; 946653; -.
DR KEGG; ecj:JW2121; -.
DR KEGG; eco:b2133; -.
DR PATRIC; fig|1411691.4.peg.110; -.
DR EchoBASE; EB0227; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_034094_0_0_6; -.
DR InParanoid; P06149; -.
DR OMA; YEHHLML; -.
DR PhylomeDB; P06149; -.
DR BioCyc; EcoCyc:DLACTDEHYDROGFAD-MON; -.
DR BioCyc; MetaCyc:DLACTDEHYDROGFAD-MON; -.
DR BRENDA; 1.1.1.28; 2026.
DR EvolutionaryTrace; P06149; -.
DR PRO; PR:P06149; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0102029; F:D-lactate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0016901; F:oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor; IDA:EcoCyc.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IDA:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IDA:EcoCyc.
DR GO; GO:0019516; P:lactate oxidation; IDA:EcoCyc.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.30.1370.20; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.610; -; 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 Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF09330; Lact-deh-memb; 1.
DR PIRSF; PIRSF000101; D-lactate_dh; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW Quinone; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3882663"
FT CHAIN 2..571
FT /note="Quinone-dependent D-lactate dehydrogenase"
FT /id="PRO_0000079928"
FT DOMAIN 42..213
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092"
FT REGION 546..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092,
FT ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X"
FT BINDING 84..85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092,
FT ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X"
FT BINDING 143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092,
FT ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X"
FT BINDING 150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092,
FT ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092,
FT ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X"
FT BINDING 262
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02092,
FT ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1F0X"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 259..268
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 379..387
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 400..414
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 437..447
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 452..461
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:1F0X"
FT TURN 490..493
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 494..502
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 507..520
FT /evidence="ECO:0007829|PDB:1F0X"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:1F0X"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:1F0X"
FT HELIX 539..548
FT /evidence="ECO:0007829|PDB:1F0X"
FT TURN 556..560
FT /evidence="ECO:0007829|PDB:1F0X"
SQ SEQUENCE 571 AA; 64612 MW; 77FB2C467CB4389F CRC64;
MSSMTTTDNK AFLNELARLV GSSHLLTDPA KTARYRKGFR SGQGDALAVV FPGSLLELWR
VLKACVTADK IILMQAANTG LTEGSTPNGN DYDRDVVIIS TLRLDKLHVL GKGEQVLAYP
GTTLYSLEKA LKPLGREPHS VIGSSCIGAS VIGGICNNSG GSLVQRGPAY TEMSLFARIN
EDGKLTLVNH LGIDLGETPE QILSKLDDDR IKDDDVRHDG RHAHDYDYVH RVRDIEADTP
ARYNADPDRL FESSGCAGKL AVFAVRLDTF EAEKNQQVFY IGTNQPEVLT EIRRHILANF
ENLPVAGEYM HRDIYDIAEK YGKDTFLMID KLGTDKMPFF FNLKGRTDAM LEKVKFFRPH
FTDRAMQKFG HLFPSHLPPR MKNWRDKYEH HLLLKMAGDG VGEAKSWLVD YFKQAEGDFF
VCTPEEGSKA FLHRFAAAGA AIRYQAVHSD EVEDILALDI ALRRNDTEWY EHLPPEIDSQ
LVHKLYYGHF MCYVFHQDYI VKKGVDVHAL KEQMLELLQQ RGAQYPAEHN VGHLYKAPET
LQKFYRENDP TNSMNPGIGK TSKRKNWQEV E
