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A5IW27 (LDH2_STAA9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:SaurJH9_2624
OrganismStaphylococcus aureus (strain JH9) [Complete proteome] [HAMAP]
Taxonomic identifier359786 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Contributes to S.aureus growth during nitrosative stress in both aerobically and anaerobically cultured cells, despite playing a secondary role in this resistance mechanism By similarity. HAMAP MF_00488

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
Stress response
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

response to stress

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 – 319319L-lactate dehydrogenase 2 HAMAP MF_00488
PRO_0000343837

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 site2311Substrate By similarity

Amino acid modifications

Modified residue2221Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IW27 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 7779343BCA801CED

FASTA31934,432
        10         20         30         40         50         60 
MKTFGKKVVL IGDGSVGSSY AFAMVTQGVA DEFVIIDIAK DKVKADVQDL NHGTVHSPSP 

        70         80         90        100        110        120 
VDVKAGEYED CKDADLVVIT AGAPQKPGET RLQLVEKNTK IMKSIVKSVM DSGFDGYFLI 

       130        140        150        160        170        180 
AANPVDILTR FVKEYTGLPA ERVIGSGTVL DSARLQYLIS QELGVAPSSV DASIIGEHGD 

       190        200        210        220        230        240 
TELAVWSQAN VAGISVYDTL KEQTGSEAKA EEIYVNTRDA AYEIIQAKGS TYYGIALALM 

       250        260        270        280        290        300 
RISKAILNNE NNVLNVSIQL DGQYGGHKGV YLGVPTLVNQ HGAVKIYEMP LSAEEQALFD 

       310 
KSVKILEDTF DSIKYLLED 

« Hide

References

[1]"Complete sequence of chromosome of Staphylococcus aureus subsp. aureus JH9."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Tomasz A., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JH9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000703 Genomic DNA. Translation: ABQ50400.1.
RefSeqYP_001247976.1. NC_009487.1.

3D structure databases

ProteinModelPortalA5IW27.
SMRA5IW27. Positions 5-313.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5IW27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000017581; EBSTAP00000017000; EBSTAG00000017580.
GeneID5167570.
GenomeReviewsGene locus SaurJH9_2624 in contig CP000703_GR.
KEGGsaj:SaurJH9_2624.
PATRIC19543263. VBIStaAur42398_2770.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
GeneTreeEBGT00050000024431.
HOGENOMHBG566126.
OMAIHPLSCH.
ProtClustDBCLSK886101.

Enzyme and pathway databases

BioCycSAUR359786:SAURJH9_2624-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_STAA9
AccessionPrimary (citable) accession number: A5IW27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: June 26, 2007
Last modified: January 25, 2012
This is version 39 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