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B3R2F9 (ALR_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:RALTA_A1734
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length373 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
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 – 373373Alanine racemase HAMAP-Rule MF_01201
PRO_1000138593

Sites

Active site351Proton acceptor; specific for D-alanine By similarity
Active site2531Proton acceptor; specific for L-alanine By similarity
Binding site1301Substrate By similarity
Binding site3051Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3R2F9 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 5D4ECB10307A1389

FASTA37339,900
        10         20         30         40         50         60 
MPRPIQAVIH QPALANNLDV IRRKAPDARV WAVVKANAYG HGIRRVFAAL RGADGFGLLD 

        70         80         90        100        110        120 
LNEAVLLRDL GWQGPILLLE GFFQPQDIAL IEQYRLTTAI HCDEQLRMLE SARPKGPLAI 

       130        140        150        160        170        180 
QLKLNTGMNR LGFHPAEYRA AWERARAMPC VGSIVHMTHF SDADGPRGIA HQVEAFDAAT 

       190        200        210        220        230        240 
ANLPGEASLS NSAAVLWHPQ AHRAWVRPGI ILYGASPTGR DADIAGTGLQ PAMSLHSELI 

       250        260        270        280        290        300 
AVQDLQPGDT VGYGSLFTAE RPMRIGVVAC GYADGYPRHA SGWGEQRAPV LVDGVRTELV 

       310        320        330        340        350        360 
GRVSMDMLCV DLTPCPKARV GSPVTLWGQG LPIDEVAQAS GTVGYELMCA LAPRVPTTVA 

       370 
TITASDSAAP AVA 

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU633749 Genomic DNA. Translation: CAQ69677.1.
RefSeqYP_002005742.1. NC_010528.1.

3D structure databases

ProteinModelPortalB3R2F9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164546.RALTA_A1734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ69677; CAQ69677; RALTA_A1734.
GeneID6454959.
KEGGcti:RALTA_A1734.
PATRIC21530076. VBICupTai42494_1699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMARDLELCS.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycCTAI164546:GJNE-1715-MONOMER.
CTAI977880:GLC7-1715-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 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.
[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.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR_CUPTR
AccessionPrimary (citable) accession number: B3R2F9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 45 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