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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911SubstrateBy similarity
Binding sitei123 – 1231NAD or substrateBy similarity
Binding sitei154 – 1541SubstrateBy similarity
Active sitei178 – 1781Proton acceptorBy similarity
Binding sitei232 – 2321SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 4229NADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320L-lactate dehydrogenasePRO_0000168329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei223 – 2231Phosphotyrosine1 Publication

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

1
320
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi15 – 2713Combined sources
Beta strandi31 – 366Combined sources
Helixi40 – 5213Combined sources
Helixi54 – 563Combined sources
Beta strandi57 – 593Combined sources
Beta strandi62 – 665Combined sources
Helixi68 – 714Combined sources
Beta strandi75 – 795Combined sources
Helixi91 – 11121Combined sources
Beta strandi116 – 1205Combined sources
Beta strandi122 – 1243Combined sources
Helixi125 – 13612Combined sources
Helixi140 – 1423Combined sources
Beta strandi143 – 1453Combined sources
Helixi149 – 16012Combined sources
Turni161 – 1644Combined sources
Helixi167 – 1693Combined sources
Beta strandi174 – 1796Combined sources
Helixi186 – 1883Combined sources
Helixi196 – 2016Combined sources
Beta strandi204 – 2063Combined sources
Helixi208 – 22922Combined sources
Helixi234 – 24815Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi258 – 2636Combined sources
Helixi264 – 2663Combined sources
Beta strandi268 – 2736Combined sources
Beta strandi276 – 2794Combined sources
Beta strandi282 – 2865Combined sources
Helixi293 – 31018Combined sources
Turni311 – 3133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 7-314.
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.
InterProiIPR001557. 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.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381V → L AA sequence (PubMed:3098260).Curated
Sequence conflicti51 – 511N → P in BAA08939 (PubMed:8969502).Curated
Sequence conflicti57 – 582AP → GL in BAA08939 (PubMed:8969502).Curated
Sequence conflicti120 – 1201V → I AA sequence (PubMed:3098260).Curated
Sequence conflicti224 – 2241H → T AA sequence (PubMed:3098260).Curated
Sequence conflicti315 – 3184Missing AA sequence (PubMed:3098260).Curated

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
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. Positions 7-314.
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.
InterProiIPR001557. 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.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLDH_BACSU
AccessioniPrimary (citable) accession number: P13714
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 26, 2009
Last modified: September 7, 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. 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.