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C0M6I5 (ALR_STRE4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alanine racemase

EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:SEQ_0437
OrganismStreptococcus equi subsp. equi (strain 4047) [Complete proteome] [HAMAP]
Taxonomic identifier553482 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length366 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.

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity.

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

peptidoglycan biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionalanine racemase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366Alanine racemase HAMAP-Rule MF_01201
PRO_1000164627

Sites

Active site401Proton acceptor; specific for D-alanine By similarity
Active site2631Proton acceptor; specific for L-alanine By similarity
Binding site1361Substrate By similarity
Binding site3101Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue401N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C0M6I5 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 93BF7447BF1BA825

FASTA36640,169
        10         20         30         40         50         60 
MISSLHRPTV ARVDLEAIRA NIDHIHQHIP KKVRTYAVVK ANAYGHGAVA VSKAVEDQVD 

        70         80         90        100        110        120 
GYCVSNLDEA LELRQAGIDK EILILGVILA SELQLAIKHQ LTITVASLEW LELAKKESVD 

       130        140        150        160        170        180 
FSQLHVHVKV DSGMGRIGVR SLAEANQLIS ILSDMGVQLD GIFTHFATAD DSDHAMFDKQ 

       190        200        210        220        230        240 
LTFFKQLVEQ LDKRPALVHA SNSATSLWHS ETIFNAIRLG IVIYGLNPSG NSLSLPCPLK 

       250        260        270        280        290        300 
EALSLESRLV HVKQIQAGDS VGYGASYVAA EPEYVGTLPI GYADGWTRNM QGFKVLVEGE 

       310        320        330        340        350        360 
FCDIIGRVSM DQLTIRLPKA YPIGTKVTLI GQQGKQVITA TDVADYRGTI NYEVLCLLSD 


RIPREY 

« Hide

References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 4047.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM204883 Genomic DNA. Translation: CAW92611.1.
RefSeqYP_002745820.1. NC_012471.1.

3D structure databases

ProteinModelPortalC0M6I5.
ModBaseSearch...

Protein-protein interaction databases

STRING553482.SEQ_0437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW92611; CAW92611; SEQ_0437.
GeneID7696299.
KEGGseu:SEQ_0437.
PATRIC19645626. VBIStrEqu13040_0438.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAIRLPKAY.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycSEQU553482:GJOY-453-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. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR_STRE4
AccessionPrimary (citable) accession number: C0M6I5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: May 1, 2013
This is version 36 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