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B8E9P2 (ALR_SHEB2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:Sbal223_0738
OrganismShewanella baltica (strain OS223) [Complete proteome] [HAMAP]
Taxonomic identifier407976 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length358 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 – 358358Alanine racemase HAMAP-Rule MF_01201
PRO_1000164609

Sites

Active site351Proton acceptor; specific for D-alanine By similarity
Active site2551Proton acceptor; specific for L-alanine By similarity
Binding site1301Substrate By similarity
Binding site3031Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8E9P2 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: F22CA87C1D9EDE28

FASTA35838,433
        10         20         30         40         50         60 
MNPFPRAEIS SSALQTNLAA LRQQAPASRV MAVVKANGYG HGLLNVAHCL VSADGFGLAR 

        70         80         90        100        110        120 
LDEALELRAG GVTARLLLLE GFFRATDLPL LVGHDIDTVV HHSSQLEMLE QTVLSKPVTV 

       130        140        150        160        170        180 
WLKVDSGMHR LGFTPEQFST VYDRLMACPN VAKPIHLMTH FACADEPDNT YTSVQMAAFN 

       190        200        210        220        230        240 
SLTAGLPGFR TLANSAGALY WPQSQGDWIR PGIALYGVSP VTGDCGANHG LVPAMELVSQ 

       250        260        270        280        290        300 
LIAVRDHKAN QPVGYGCFWT AKQDTRLGVV AIGYGDGYPR NAPEGTPVWV NGRRVPIVGR 

       310        320        330        340        350 
VSMDMLTVDL GQDAQDKVGD SALLWGKALP VEEVAEHIGT IAYELVTKLT PRVAVCLA 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS223."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K., Tiedje J.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS223.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001252 Genomic DNA. Translation: ACK45257.1.
RefSeqYP_002356680.1. NC_011663.1.

3D structure databases

ProteinModelPortalB8E9P2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING407976.Sbal223_0738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK45257; ACK45257; Sbal223_0738.
GeneID7088130.
KEGGsbp:Sbal223_0738.
PATRIC23477494. VBISheBal125792_0767.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMAINNQLAP.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycSBAL407976:GJ6Y-756-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_SHEB2
AccessionPrimary (citable) accession number: B8E9P2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 37 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