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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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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 databases

DrugBankiDB03147. Flavin adenine dinucleotide.
DB00756. Hexachlorophene.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000799282 – 571D-lactate dehydrogenaseAdd BLAST570

Proteomic databases

EPDiP06149.
PaxDbiP06149.
PRIDEiP06149.

Interactioni

Protein-protein interaction databases

BioGridi4260452. 15 interactors.
IntActiP06149. 17 interactors.
STRINGi511145.b2133.

Chemistry databases

BindingDBiP06149.

Structurei

Secondary structure

1571
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 20Combined sources11
Helixi22 – 24Combined sources3
Helixi29 – 36Combined sources8
Beta strandi39 – 41Combined sources3
Beta strandi47 – 50Combined sources4
Helixi55 – 67Combined sources13
Beta strandi71 – 77Combined sources7
Beta strandi81 – 83Combined sources3
Beta strandi96 – 100Combined sources5
Beta strandi107 – 110Combined sources4
Turni111 – 114Combined sources4
Beta strandi115 – 118Combined sources4
Helixi124 – 131Combined sources8
Helixi132 – 134Combined sources3
Helixi143 – 147Combined sources5
Helixi151 – 156Combined sources6
Beta strandi174 – 179Combined sources6
Beta strandi185 – 189Combined sources5
Beta strandi191 – 193Combined sources3
Helixi199 – 207Combined sources9
Helixi213 – 215Combined sources3
Helixi228 – 233Combined sources6
Helixi247 – 249Combined sources3
Beta strandi259 – 268Combined sources10
Beta strandi277 – 284Combined sources8
Helixi286 – 299Combined sources14
Beta strandi305 – 311Combined sources7
Helixi312 – 318Combined sources7
Helixi379 – 387Combined sources9
Beta strandi389 – 396Combined sources8
Helixi400 – 414Combined sources15
Beta strandi418 – 421Combined sources4
Helixi424 – 434Combined sources11
Helixi437 – 447Combined sources11
Helixi449 – 451Combined sources3
Beta strandi452 – 461Combined sources10
Helixi475 – 478Combined sources4
Beta strandi481 – 489Combined sources9
Turni490 – 493Combined sources4
Beta strandi494 – 502Combined sources9
Helixi507 – 520Combined sources14
Beta strandi527 – 529Combined sources3
Turni532 – 534Combined sources3
Helixi539 – 548Combined sources10
Turni556 – 560Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP06149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 213FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST172

Sequence similaritiesi

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

Phylogenomic databases

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

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 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F0XX-ray1.90A/B1-571[»]
ProteinModelPortaliP06149.
SMRiP06149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260452. 15 interactors.
IntActiP06149. 17 interactors.
STRINGi511145.b2133.

Chemistry databases

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.

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...

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: November 30, 2016
This is version 149 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.