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B8ZMG1 (ALR_STRPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 40. 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:SPN23F16970
OrganismStreptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1) [Complete proteome] [HAMAP]
Taxonomic identifier561276 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length367 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 – 367367Alanine racemase HAMAP-Rule MF_01201
PRO_1000164629

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
B8ZMG1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: A79E2F1B439B18B7

FASTA36739,858
        10         20         30         40         50         60 
MKASPHRPTK ALIHLGAIRQ NIQQMGAHIP QGTLKLAVVK ANAYGHGAVA VAKAIQDDVD 

        70         80         90        100        110        120 
GFCVSNIDEA IELRQAGLSK PILILGVSEI EAVALAKEYD FTLTVAGLEW IQALLDKEVD 

       130        140        150        160        170        180 
LTGLTVHLKI DSGMGRIGFR EASEVEQAQD LLQQHGVCVE GIFTHFATAD EESDDYFNAQ 

       190        200        210        220        230        240 
LERFKTILAS MKEVPELVHA SNSATTLWHV ETIFNAVRMG DAMYGLNPSG AVLDLPYDLI 

       250        260        270        280        290        300 
PALTLESALV HVKTVPAGAC MGYGATYQAD SEQVIATVPI GYADGWTRDM QNFSVLVDGQ 

       310        320        330        340        350        360 
ACPIVGRVSM DQITIRLPKL YPLGTKVTLI GSNGDKEITA TQVATYRVTI NYEVVCLLSD 


RIPREYY 

« Hide

References

[1]"Role of conjugative elements in the evolution of the multidrug-resistant pandemic clone Streptococcus pneumoniae Spain23F ST81."
Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D., Mitchell T.J.
J. Bacteriol. 191:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700669 / Spain 23F-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM211187 Genomic DNA. Translation: CAR69468.1.
RefSeqYP_002511585.1. NC_011900.1.

3D structure databases

ProteinModelPortalB8ZMG1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561276.SPN23F_16970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR69468; CAR69468; SPN23F16970.
GeneID7327444.
KEGGsne:SPN23F_16970.
PATRIC19674766. VBIStrPne132160_1785.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
KOK01775.
OMAIYSHLAL.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycSPNE561276:GJFJ-1628-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_STRPJ
AccessionPrimary (citable) accession number: B8ZMG1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 40 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