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Protein

D-lactate dehydrogenase

Gene

dld

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

First component of the membrane-bound D-lactate oxidase, which is believed to play an important role in the energization of the active transport of a variety of sugars and amino acids.

Catalytic activityi

(R)-lactate + NAD+ = pyruvate + NADH.

Cofactori

Enzyme regulationi

Requires phospholipid for maximal activity.

GO - Molecular functioni

  • D-lactate dehydrogenase activity Source: UniProtKB-EC
  • electron carrier activity Source: EcoCyc
  • flavin adenine dinucleotide binding Source: EcoCyc
  • NAD binding Source: InterPro
  • oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor Source: EcoCyc

GO - Biological processi

  • aerobic respiration Source: EcoCyc
  • anaerobic respiration Source: EcoCyc
  • lactate oxidation Source: EcoCyc
  • respiratory electron transport chain Source: EcoCyc
  • transmembrane transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciEcoCyc:DLACTDEHYDROGFAD-MONOMER.
ECOL316407:JW2121-MONOMER.
MetaCyc:DLACTDEHYDROGFAD-MONOMER.
BRENDAi1.1.1.28. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
D-lactate dehydrogenase (EC:1.1.1.28)
Alternative name(s):
Respiratory D-lactate dehydrogenase
Gene namesi
Name:dld
Ordered Locus Names:b2133, JW2121
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10231. dld.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of cytoplasmic side of plasma membrane Source: EcoCyc
  • integral component of plasma membrane Source: InterPro
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.
DB00756. Hexachlorophene.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 571570D-lactate dehydrogenasePRO_0000079928Add
BLAST

Proteomic databases

EPDiP06149.
PaxDbiP06149.
PRIDEiP06149.

Interactioni

Protein-protein interaction databases

BioGridi4260452. 15 interactions.
IntActiP06149. 17 interactions.
STRINGi511145.b2133.

Chemistry

BindingDBiP06149.

Structurei

Secondary structure

1
571
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2011Combined sources
Helixi22 – 243Combined sources
Helixi29 – 368Combined sources
Beta strandi39 – 413Combined sources
Beta strandi47 – 504Combined sources
Helixi55 – 6713Combined sources
Beta strandi71 – 777Combined sources
Beta strandi81 – 833Combined sources
Beta strandi96 – 1005Combined sources
Beta strandi107 – 1104Combined sources
Turni111 – 1144Combined sources
Beta strandi115 – 1184Combined sources
Helixi124 – 1318Combined sources
Helixi132 – 1343Combined sources
Helixi143 – 1475Combined sources
Helixi151 – 1566Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi191 – 1933Combined sources
Helixi199 – 2079Combined sources
Helixi213 – 2153Combined sources
Helixi228 – 2336Combined sources
Helixi247 – 2493Combined sources
Beta strandi259 – 26810Combined sources
Beta strandi277 – 2848Combined sources
Helixi286 – 29914Combined sources
Beta strandi305 – 3117Combined sources
Helixi312 – 3187Combined sources
Helixi379 – 3879Combined sources
Beta strandi389 – 3968Combined sources
Helixi400 – 41415Combined sources
Beta strandi418 – 4214Combined sources
Helixi424 – 43411Combined sources
Helixi437 – 44711Combined sources
Helixi449 – 4513Combined sources
Beta strandi452 – 46110Combined sources
Helixi475 – 4784Combined sources
Beta strandi481 – 4899Combined sources
Turni490 – 4934Combined sources
Beta strandi494 – 5029Combined sources
Helixi507 – 52014Combined sources
Beta strandi527 – 5293Combined sources
Turni532 – 5343Combined sources
Helixi539 – 54810Combined sources
Turni556 – 5605Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F0XX-ray1.90A/B1-571[»]
ProteinModelPortaliP06149.
SMRiP06149. Positions 9-567.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 213172FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CXG. Bacteria.
COG0277. LUCA.
HOGENOMiHOG000122232.
InParanoidiP06149.
KOiK03777.
OMAiRDRYEHH.
OrthoDBiEOG6Z3KJX.

Family and domain databases

Gene3Di3.30.1370.20. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.30.70.610. 2 hits.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016172. D-lactate_DH_C-sub1.
IPR016173. D-lactate_DH_C-sub2.
IPR012256. D_lactate_DH.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR015409. Lactate_DH_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]
PfamiPF01565. FAD_binding_4. 1 hit.
PF09330. Lact-deh-memb. 1 hit.
[Graphical view]
PIRSFiPIRSF000101. D-lactate_dh. 1 hit.
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06149-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSMTTTDNK AFLNELARLV GSSHLLTDPA KTARYRKGFR SGQGDALAVV
60 70 80 90 100
FPGSLLELWR VLKACVTADK IILMQAANTG LTEGSTPNGN DYDRDVVIIS
110 120 130 140 150
TLRLDKLHVL GKGEQVLAYP GTTLYSLEKA LKPLGREPHS VIGSSCIGAS
160 170 180 190 200
VIGGICNNSG GSLVQRGPAY TEMSLFARIN EDGKLTLVNH LGIDLGETPE
210 220 230 240 250
QILSKLDDDR IKDDDVRHDG RHAHDYDYVH RVRDIEADTP ARYNADPDRL
260 270 280 290 300
FESSGCAGKL AVFAVRLDTF EAEKNQQVFY IGTNQPEVLT EIRRHILANF
310 320 330 340 350
ENLPVAGEYM HRDIYDIAEK YGKDTFLMID KLGTDKMPFF FNLKGRTDAM
360 370 380 390 400
LEKVKFFRPH FTDRAMQKFG HLFPSHLPPR MKNWRDKYEH HLLLKMAGDG
410 420 430 440 450
VGEAKSWLVD YFKQAEGDFF VCTPEEGSKA FLHRFAAAGA AIRYQAVHSD
460 470 480 490 500
EVEDILALDI ALRRNDTEWY EHLPPEIDSQ LVHKLYYGHF MCYVFHQDYI
510 520 530 540 550
VKKGVDVHAL KEQMLELLQQ RGAQYPAEHN VGHLYKAPET LQKFYRENDP
560 570
TNSMNPGIGK TSKRKNWQEV E
Length:571
Mass (Da):64,612
Last modified:January 23, 2007 - v3
Checksum:i77FB2C467CB4389F
GO

Sequence cautioni

The sequence AAA60530.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10038 Genomic DNA. Translation: AAA23688.1.
X01067 Genomic DNA. Translation: CAA25531.1.
U00007 Genomic DNA. Translation: AAA60530.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75194.1.
AP009048 Genomic DNA. Translation: BAE76610.1.
PIRiA21893. DEECDL.
RefSeqiNP_416637.1. NC_000913.3.
WP_000097403.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75194; AAC75194; b2133.
BAE76610; BAE76610; BAE76610.
GeneIDi946653.
KEGGiecj:JW2121.
eco:b2133.
PATRICi32119607. VBIEscCol129921_2214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10038 Genomic DNA. Translation: AAA23688.1.
X01067 Genomic DNA. Translation: CAA25531.1.
U00007 Genomic DNA. Translation: AAA60530.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75194.1.
AP009048 Genomic DNA. Translation: BAE76610.1.
PIRiA21893. DEECDL.
RefSeqiNP_416637.1. NC_000913.3.
WP_000097403.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F0XX-ray1.90A/B1-571[»]
ProteinModelPortaliP06149.
SMRiP06149. Positions 9-567.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260452. 15 interactions.
IntActiP06149. 17 interactions.
STRINGi511145.b2133.

Chemistry

BindingDBiP06149.
DrugBankiDB03147. Flavin adenine dinucleotide.
DB00756. Hexachlorophene.

Proteomic databases

EPDiP06149.
PaxDbiP06149.
PRIDEiP06149.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75194; AAC75194; b2133.
BAE76610; BAE76610; BAE76610.
GeneIDi946653.
KEGGiecj:JW2121.
eco:b2133.
PATRICi32119607. VBIEscCol129921_2214.

Organism-specific databases

EchoBASEiEB0227.
EcoGeneiEG10231. dld.

Phylogenomic databases

eggNOGiENOG4105CXG. Bacteria.
COG0277. LUCA.
HOGENOMiHOG000122232.
InParanoidiP06149.
KOiK03777.
OMAiRDRYEHH.
OrthoDBiEOG6Z3KJX.

Enzyme and pathway databases

BioCyciEcoCyc:DLACTDEHYDROGFAD-MONOMER.
ECOL316407:JW2121-MONOMER.
MetaCyc:DLACTDEHYDROGFAD-MONOMER.
BRENDAi1.1.1.28. 2026.

Miscellaneous databases

EvolutionaryTraceiP06149.
PROiP06149.

Family and domain databases

Gene3Di3.30.1370.20. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.30.70.610. 2 hits.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016172. D-lactate_DH_C-sub1.
IPR016173. D-lactate_DH_C-sub2.
IPR012256. D_lactate_DH.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR015409. Lactate_DH_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]
PfamiPF01565. FAD_binding_4. 1 hit.
PF09330. Lact-deh-memb. 1 hit.
[Graphical view]
PIRSFiPIRSF000101. D-lactate_dh. 1 hit.
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the respiratory D-lactate dehydrogenase gene of Escherichia coli."
    Campbell H.D., Rogers B.L., Young I.G.
    Eur. J. Biochem. 144:367-373(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Overproduction and nucleotide sequence of the respiratory D-lactate dehydrogenase of Escherichia coli."
    Rule G.S., Pratt E.A., Chin C.C.Q., Wold F., Ho C.
    J. Bacteriol. 161:1059-1068(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18.
  3. "Automated multiplex sequencing of the E.coli genome."
    Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / BHB2600.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  7. "The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme."
    Dym O., Pratt E.A., Ho C., Eisenberg D.
    Proc. Natl. Acad. Sci. U.S.A. 97:9413-9418(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiDLD_ECOLI
AccessioniPrimary (citable) accession number: P06149
Secondary accession number(s): Q2MAU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.