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Protein

D-lactate dehydrogenase

Gene

ldhA

Organism
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei176NADCombined sources1 Publication1
Binding sitei213NADCombined sources1 Publication1
Active sitei2361 Publication1
Binding sitei260NADCombined sources1 Publication1
Active sitei2651 Publication1
Active sitei297Proton donor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi156 – 157NADCombined sources1 Publication2
Nucleotide bindingi207 – 208NAD1 Publication2
Nucleotide bindingi234 – 236NAD1 Publication3

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.1.1.28. 2853.
SABIO-RKP26297.

Names & Taxonomyi

Protein namesi
Recommended name:
D-lactate dehydrogenase (EC:1.1.1.28)
Short name:
D-LDH
Alternative name(s):
D-specific 2-hydroxyacid dehydrogenase
Gene namesi
Name:ldhA
Ordered Locus Names:Ldb0101
OrganismiLactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778)
Taxonomic identifieri390333 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000001259 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi206H → Q: Increase of activity. 1 Publication1
Mutagenesisi236R → K: Decrease of activity. 1 Publication1
Mutagenesisi260D → N: Decrease of activity. 1 Publication1
Mutagenesisi265E → Q: Decrease of activity. 1 Publication1
Mutagenesisi297H → Q: 90% loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000759532 – 333D-lactate dehydrogenaseAdd BLAST332

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi390333.Ldb0101.

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Helixi11 – 13Combined sources3
Helixi14 – 22Combined sources9
Beta strandi27 – 31Combined sources5
Turni38 – 40Combined sources3
Helixi41 – 44Combined sources4
Beta strandi48 – 52Combined sources5
Helixi60 – 68Combined sources9
Beta strandi73 – 79Combined sources7
Helixi86 – 91Combined sources6
Beta strandi95 – 97Combined sources3
Helixi104 – 120Combined sources17
Helixi122 – 130Combined sources9
Helixi144 – 146Combined sources3
Beta strandi147 – 152Combined sources6
Helixi156 – 167Combined sources12
Beta strandi171 – 175Combined sources5
Helixi181 – 185Combined sources5
Helixi193 – 199Combined sources7
Beta strandi201 – 205Combined sources5
Helixi211 – 213Combined sources3
Helixi219 – 224Combined sources6
Beta strandi229 – 233Combined sources5
Helixi237 – 239Combined sources3
Helixi242 – 250Combined sources9
Beta strandi253 – 260Combined sources8
Turni266 – 270Combined sources5
Helixi281 – 288Combined sources8
Beta strandi292 – 294Combined sources3
Helixi303 – 321Combined sources19
Beta strandi327 – 329Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DLDmodel-A1-333[»]
1J49X-ray2.20A/B1-333[»]
1J4AX-ray1.90A/B/C/D1-333[»]
ProteinModelPortaliP26297.
SMRiP26297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26297.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C5I. Bacteria.
COG1052. LUCA.
HOGENOMiHOG000136695.
KOiK03778.
OMAiSAVVYQQ.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P26297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKIFAYAIR EDEKPFLKEW EDAHKDVEVE YTDKLLTPET VALAKGADGV
60 70 80 90 100
VVYQQLDYTA ETLQALADNG ITKMSLRNVG VDNIDMAKAK ELGFQITNVP
110 120 130 140 150
VYSPNAIAEH AAIQAARILR QDKAMDEKVA RHDLRWAPTI GREVRDQVVG
160 170 180 190 200
VIGTGHIGQV FMQIMEGFGA KVIAYDIFRN PELEKKGYYV DSLDDLYKQA
210 220 230 240 250
DVISLHVPDV PANVHMINDE SIAKMKQDVV IVNVSRGPLV DTDAVIRGLD
260 270 280 290 300
SGKIFGYAMD VYEGEVGIFN EDWEGKEFPD ARLADLIARP NVLVTPHTAF
310 320 330
YTTHAVRNMV VKAFDNNLEL VEGKEAETPV KVG
Length:333
Mass (Da):37,049
Last modified:January 23, 2007 - v3
Checksum:i16E8B68D54B9D9D4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41V → A in AAA25246 (PubMed:1569100).Curated1
Sequence conflicti117R → A in CAA42781 (PubMed:1915894).Curated1
Sequence conflicti122D → A in AAA25246 (PubMed:1569100).Curated1
Sequence conflicti152I → V in AAA25246 (PubMed:1569100).Curated1
Sequence conflicti174A → T in CAA42781 (PubMed:1915894).Curated1
Sequence conflicti220E → K in AAA25246 (PubMed:1569100).Curated1
Sequence conflicti254I → V in AAA25246 (PubMed:1569100).Curated1
Sequence conflicti268I → V in AAA25246 (PubMed:1569100).Curated1
Sequence conflicti273W → R in AAA25246 (PubMed:1569100).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60220 Genomic DNA. Translation: CAA42781.1.
M85224 Genomic DNA. Translation: AAA25246.1.
CR954253 Genomic DNA. Translation: CAI96942.1.
PIRiA38094.
RefSeqiWP_011543503.1. NZ_JQAV01000045.1.

Genome annotation databases

EnsemblBacteriaiCAI96942; CAI96942; Ldb0101.
GeneIDi4085369.
KEGGildb:Ldb0101.
PATRICi22215856. VBILacDel123523_0087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60220 Genomic DNA. Translation: CAA42781.1.
M85224 Genomic DNA. Translation: AAA25246.1.
CR954253 Genomic DNA. Translation: CAI96942.1.
PIRiA38094.
RefSeqiWP_011543503.1. NZ_JQAV01000045.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DLDmodel-A1-333[»]
1J49X-ray2.20A/B1-333[»]
1J4AX-ray1.90A/B/C/D1-333[»]
ProteinModelPortaliP26297.
SMRiP26297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi390333.Ldb0101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI96942; CAI96942; Ldb0101.
GeneIDi4085369.
KEGGildb:Ldb0101.
PATRICi22215856. VBILacDel123523_0087.

Phylogenomic databases

eggNOGiENOG4105C5I. Bacteria.
COG1052. LUCA.
HOGENOMiHOG000136695.
KOiK03778.
OMAiSAVVYQQ.

Enzyme and pathway databases

BRENDAi1.1.1.28. 2853.
SABIO-RKP26297.

Miscellaneous databases

EvolutionaryTraceiP26297.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLDHD_LACDA
AccessioniPrimary (citable) accession number: P26297
Secondary accession number(s): Q1G7V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 127 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.