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B0AYA6 (B0AYA6_BACAN) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase 3 HAMAP MF_00488
Short name=L-LDH 3 HAMAP MF_00488
EC=1.1.1.27 HAMAP MF_00488
Gene names
Name:ldh1 EMBL EDR16627.1
Synonyms:ldh3 HAMAP MF_00488
ORF Names:BAC_1943 EMBL EDR16627.1
OrganismBacillus anthracis str. A0488 EMBL EDR16627.1
Taxonomic identifier486624 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus 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. HAMAP MF_00488

Ontologies

Keywords
   Biological processGlycolysis HAMAP MF_00488
   Cellular componentCytoplasm HAMAP MF_00488
   LigandNAD HAMAP MF_00488
   Molecular functionOxidoreductase HAMAP MF_00488 EMBL EDR16627.1
   PTMPhosphoprotein HAMAP MF_00488
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-lactate dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding14 – 4229NAD By similarity HAMAP MF_00488

Sites

Active site1781Proton acceptor By similarity HAMAP MF_00488
Binding site911Substrate By similarity HAMAP MF_00488
Binding site1231NAD or substrate By similarity HAMAP MF_00488
Binding site1541Substrate By similarity HAMAP MF_00488
Binding site2321Substrate By similarity HAMAP MF_00488

Amino acid modifications

Modified residue2231Phosphotyrosine By similarity HAMAP MF_00488

Sequences

Sequence LengthMass (Da)Tools
B0AYA6 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: A99C911C2A2306E6

FASTA31434,788
        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 EYFNIGPHNI 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

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References

[1]"Genome sequence of Bacillus anthracis A0488."
Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., Sutton G., Brettin T.S.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A0488 EMBL EDR16627.1.
[2]Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A0488 EMBL EDR16627.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		ABJC01000048 Genomic DNA. Translation: EDR16627.1.

3D structure databases

ProteinModelPortalB0AYA6.
SMRB0AYA6. Positions 4-311.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC24649088. VBIBacAnt7575_5405.

Phylogenomic databases

OMAIHPLSCH.

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.
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 nameB0AYA6_BACAN
AccessionPrimary (citable) accession number: B0AYA6
Entry history
Integrated into UniProtKB/TrEMBL: February 26, 2008
Last sequence update: February 26, 2008
Last modified: December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info