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Protein

L-lactate dehydrogenase

Gene

ldh

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. L-lactate dehydrogenase (ldh)
This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei91SubstrateBy similarity1
Binding sitei123NAD or substrateBy similarity1
Binding sitei154SubstrateBy similarity1
Active sitei178Proton acceptorBy similarity1
Binding sitei232SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 42NADBy similarityAdd BLAST29

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandNAD

Enzyme and pathway databases

BioCyciBSUB:BSU03050-MONOMER.
SABIO-RKP13714.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase (EC:1.1.1.27)
Short name:
L-LDH
Gene namesi
Name:ldh
Synonyms:lctE
Ordered Locus Names:BSU03050
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001683291 – 320L-lactate dehydrogenaseAdd BLAST320

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei223Phosphotyrosine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP13714.

PTM databases

iPTMnetiP13714.

Expressioni

Inductioni

Strongly induced under anaerobic conditions. Activated by ResDE, Fnr and ArfM.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001683.

Structurei

Secondary structure

1320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi15 – 27Combined sources13
Beta strandi31 – 36Combined sources6
Helixi40 – 52Combined sources13
Helixi54 – 56Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi62 – 66Combined sources5
Helixi68 – 71Combined sources4
Beta strandi75 – 79Combined sources5
Helixi91 – 111Combined sources21
Beta strandi116 – 120Combined sources5
Beta strandi122 – 124Combined sources3
Helixi125 – 136Combined sources12
Helixi140 – 142Combined sources3
Beta strandi143 – 145Combined sources3
Helixi149 – 160Combined sources12
Turni161 – 164Combined sources4
Helixi167 – 169Combined sources3
Beta strandi174 – 179Combined sources6
Helixi186 – 188Combined sources3
Helixi196 – 201Combined sources6
Beta strandi204 – 206Combined sources3
Helixi208 – 229Combined sources22
Helixi234 – 248Combined sources15
Beta strandi253 – 255Combined sources3
Beta strandi258 – 263Combined sources6
Helixi264 – 266Combined sources3
Beta strandi268 – 273Combined sources6
Beta strandi276 – 279Combined sources4
Beta strandi282 – 286Combined sources5
Helixi293 – 310Combined sources18
Turni311 – 313Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PQDX-ray2.38A/B/C/D/E/F/G/H1-320[»]
3PQEX-ray2.20A/B/C/D1-320[»]
3PQFX-ray2.49A/B/C/D1-320[»]
ProteinModelPortaliP13714.
SMRiP13714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. LDH family.Curated

Phylogenomic databases

eggNOGiENOG4105C80. Bacteria.
COG0039. LUCA.
HOGENOMiHOG000213793.
InParanoidiP13714.
KOiK00016.
OMAiNNEHRVL.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog. 1 hit.
InterProiView protein in InterPro
IPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
PfamiView protein in Pfam
PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiView protein in PROSITE
PS00064. L_LDH. 1 hit.

Sequencei

Sequence statusi: Complete.

P13714-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKHVNKVAL IGAGFVGSSY AFALINQGIT DELVVIDVNK EKAMGDVMDL
60 70 80 90 100
NHGKAFAPQP VKTSYGTYED CKDADIVCIC AGANQKPGET RLELVEKNLK
110 120 130 140 150
IFKGIVSEVM ASGFDGIFLV ATNPVDILTY ATWKFSGLPK ERVIGSGTTL
160 170 180 190 200
DSARFRFMLS EYFGAAPQNV HAHIIGEHGD TELPVWSHAN VGGVPVSELV
210 220 230 240 250
EKNDAYKQEE LDQIVDDVKN AAYHIIEKKG ATYYGVAMSL ARITKAILHN
260 270 280 290 300
ENSILTVSTY LDGQYGADDV YIGVPAVVNR GGIAGITELN LNEKEKEQFL
310 320
HSAGVLKNIL KPHFAEQKVN
Length:320
Mass (Da):34,802
Last modified:May 26, 2009 - v3
Checksum:iF0B71F5A760FCAE1
GO

Sequence cautioni

The sequence BAA08939 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAB12099 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38V → L AA sequence (PubMed:3098260).Curated1
Sequence conflicti51N → P in BAA08939 (PubMed:8969502).Curated1
Sequence conflicti57 – 58AP → GL in BAA08939 (PubMed:8969502).Curated2
Sequence conflicti120V → I AA sequence (PubMed:3098260).Curated1
Sequence conflicti224H → T AA sequence (PubMed:3098260).Curated1
Sequence conflicti315 – 318Missing AA sequence (PubMed:3098260).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50453 Genomic DNA. Translation: BAA08939.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12099.2. Different initiation.
PIRiE69649.
RefSeqiNP_388187.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12099; CAB12099; BSU03050.
GeneIDi938348.
KEGGibsu:BSU03050.
PATRICi18972169. VBIBacSub10457_0313.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50453 Genomic DNA. Translation: BAA08939.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12099.2. Different initiation.
PIRiE69649.
RefSeqiNP_388187.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PQDX-ray2.38A/B/C/D/E/F/G/H1-320[»]
3PQEX-ray2.20A/B/C/D1-320[»]
3PQFX-ray2.49A/B/C/D1-320[»]
ProteinModelPortaliP13714.
SMRiP13714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001683.

PTM databases

iPTMnetiP13714.

Proteomic databases

PaxDbiP13714.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12099; CAB12099; BSU03050.
GeneIDi938348.
KEGGibsu:BSU03050.
PATRICi18972169. VBIBacSub10457_0313.

Phylogenomic databases

eggNOGiENOG4105C80. Bacteria.
COG0039. LUCA.
HOGENOMiHOG000213793.
InParanoidiP13714.
KOiK00016.
OMAiNNEHRVL.

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
BioCyciBSUB:BSU03050-MONOMER.
SABIO-RKP13714.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog. 1 hit.
InterProiView protein in InterPro
IPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
PfamiView protein in Pfam
PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiView protein in PROSITE
PS00064. L_LDH. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLDH_BACSU
AccessioniPrimary (citable) accession number: P13714
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 26, 2009
Last modified: February 15, 2017
This is version 148 of the entry and version 3 of the sequence. See 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.