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P62048 (LDH2_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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 2

Short name=L-LDH 2
EC=1.1.1.27
Gene names
Name:ldh2
Ordered Locus Names:BCE_5032
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [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
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 2 HAMAP MF_00488
PRO_0000168319

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
P62048 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: 82075E6DCC076A76

FASTA31434,606
        10         20         30         40         50         60 
MKKGINRVVL VGTGAVGCSY AYSMINQGVA EEFVLVDVNE AKAEGEAMDL SHAVPFSPSP 

        70         80         90        100        110        120 
TKVWSGSYAD CKDADLVVIT AGLPQKPGET RLDLVEKNTK IFKQIVRGIM DSGFDGIFLI 

       130        140        150        160        170        180 
ATNPVDILTY VTWKESGLPK ERVIGSGTTL DSARFRYMLG DYLDVDPRNV HAYIVGEHGD 

       190        200        210        220        230        240 
TELPVWSHAT IGVQKLETIL ANNEQYKQED LDKIFENVRD AAYHIIERKG ATYYGIGMSL 

       250        260        270        280        290        300 
LRVTKAILNN ENSVLTVSAY LEGQYGEKDA YVGVPAVINR EGVREIVELE LNEDEKAKFA 

       310 
HSVKVLKETM APVL 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS43933.1.
RefSeqNP_981325.1. NC_003909.8.

3D structure databases

ProteinModelPortalP62048.
SMRP62048. Positions 4-311.
ModBaseSearch...

Protein-protein interaction databases

STRINGP62048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000026347; EBBACP00000025697; EBBACG00000026338.
GeneID2752186.
GenomeReviewsGene locus BCE_5032 in contig AE017194_GR.
KEGGbca:BCE_5032.
NMPDRfig|222523.1.peg.4997.
PATRIC18858646. VBIBacCer118379_4818.
TIGRBCE_5032.

Phylogenomic databases

eggNOGCOG0039.
GeneTreeEBGT00050000001153.
HOGENOMHBG566126.
OMAMDLNHGV.
ProtClustDBPRK00066.

Enzyme and pathway databases

BioCycBCER405917:BCE_5032-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 nameLDH2_BACC1
AccessionPrimary (citable) accession number: P62048
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: January 25, 2012
This is version 63 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