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O08445 (ALR_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. 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:
Alanine racemase

EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:lp_0523
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity. HAMAP-Rule MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201

Sequence similarities

Belongs to the alanine racemase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processD-alanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionalanine racemase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Alanine racemase HAMAP-Rule MF_01201
PRO_0000114528

Sites

Active site411Proton acceptor; specific for D-alanine By similarity
Active site2701Proton acceptor; specific for L-alanine By similarity
Binding site1411Substrate By similarity
Binding site3171Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue411N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O08445 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 844E9BAC5FF3463B

FASTA37540,710
        10         20         30         40         50         60 
MVVIGEHRHT QVTVDLQAIK TNISNEMAQK DELTELWAVV KANGYGHGII QVAQAAKEAG 

        70         80         90        100        110        120 
ATGFCVAILD EALALRAAGF AEPILVLGIT EPEYAPLVAE KDISLAVGTQ DWLTTAAAIL 

       130        140        150        160        170        180 
AANQVTTPLH VHLALDTGMG RIGFQTPEEL ATAVTTLRQP QSPFDFEGIF THFATADQAD 

       190        200        210        220        230        240 
DTYFTHQLNN WKHLIAVVDE LPRYVHVSNS ATSLWHQACN GNMVRFGVAL YGLNPSGREL 

       250        260        270        280        290        300 
SAPYPLQPAL SLTARLTFVK RLARGKSVSY GATYTAAQDE WIGTVPIGYA DGYERRLQGF 

       310        320        330        340        350        360 
HVLVDGEFCE IVGRVCMDQL MVRLPHEVPV GAKVTLVGTD GARTISLQDI ADYCGTIHYE 

       370 
IACGLAPRVP RVYID 

« Hide

References

« Hide 'large scale' references
[1]"The alanine racemase gene is essential for growth of Lactobacillus plantarum."
Hols P., Defrenne C., Ferain T., Derzelle S., Delplace B., Delcour J.
J. Bacteriol. 179:3804-3807(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.
[2]"Complete genome sequence of Lactobacillus plantarum WCFS1."
Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J.
Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08941 Genomic DNA. Translation: CAA70140.1.
AL935263 Genomic DNA. Translation: CCC78013.1.
RefSeqYP_004888527.1. NC_004567.2.

3D structure databases

ProteinModelPortalO08445.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220668.lp_0523.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC78013; CCC78013; lp_0523.
GeneID1061815.
KEGGlpl:lp_0523.
PATRIC22247489. VBILacPla27411_0431.

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAYGHGLER.

Enzyme and pathway databases

BioCycLPLA220668-WGS:GSPK-434-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
SMARTSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR_LACPL
AccessionPrimary (citable) accession number: O08445
Secondary accession number(s): F9UKZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways