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Q81EP4 (LDH1_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase 1

Short name=L-LDH 1
EC=1.1.1.27
Gene names
Name:ldh1
Ordered Locus Names:BC_1924
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-lactate + NAD+ = pyruvate + NADH. HAMAP MF_00488

Pathway

Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP MF_00488

Subunit structure

Homotetramer By similarity. HAMAP MF_00488

Subcellular location

Cytoplasm By similarity HAMAP MF_00488.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-lactate dehydrogenase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314L-lactate dehydrogenase 1 HAMAP MF_00488
PRO_0000168321

Regions

Nucleotide binding14 – 4229NAD By similarity

Sites

Active site1781Proton acceptor By similarity
Binding site911Substrate By similarity
Binding site1231NAD or substrate By similarity
Binding site1541Substrate By similarity
Binding site2321Substrate By similarity

Amino acid modifications

Modified residue2231Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81EP4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 19DC3B1C2083AB2B

FASTA31434,789
        10         20         30         40         50         60 
MKKGINRVVL VGTGAVGCSY AYCMINQAVA EEFVLVDVNE AKAEGEAMDL SHAVPFAPAP 

        70         80         90        100        110        120 
TRVWKGSYED CKDADLVVIT AGLPQKPGET RLDLVEKNAK IFKQIVRSIM DSGFDGIFLI 

       130        140        150        160        170        180 
ATNPVDILTY VTWKESGLPK ERVIGSGTTL DSARFRYMLG EYFDIGPHNI HAYIIGEHGD 

       190        200        210        220        230        240 
TELPVWSHVS VGIQKLQTLL EKDNTYNQED LDKIFINVRD AAYHIIERKG ATYYGIGMSL 

       250        260        270        280        290        300 
LRVTKAILND ENSVLTVSAY LEGQYGQKDV YIGVPAVLNR GGVREILEVE LSEDEELKFD 

       310 
HSVQVLKETM APVL 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP08895.1.
RefSeqNP_831694.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ81EP4.
SMRQ81EP4. Positions 4-311.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ81EP4.

Proteomic databases

PRIDEQ81EP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000033719; EBBACP00000032925; EBBACG00000033710.
GeneID1204273.
GenomeReviewsGene locus BC_1924 in contig AE016877_GR.
KEGGbce:BC1924.
PATRIC32599637. VBIBacCer54481_1927.

Phylogenomic databases

eggNOGCOG0039.
GeneTreeEBGT00050000001153.
HOGENOMHBG566126.
OMAIHPLSCH.
PhylomeDBQ81EP4.
ProtClustDBPRK00066.

Enzyme and pathway databases

BioCycBCER226900:BC_1924-MONOMER.

Family and domain databases

HAMAPMF_00488. Lactate_dehydrog.
[Tree]
InterProIPR001557. 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]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00016.
PANTHERPTHR11540:SF3. PTHR11540:SF3. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLDH1_BACCR
AccessionPrimary (citable) accession number: Q81EP4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families