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P0A2W8 (ALR_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:alaR
Ordered Locus Names:SP_1698
OrganismStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]
Taxonomic identifier170187 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.4

Pathway

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

Subunit structure

Homodimer. Ref.4

Sequence similarities

Belongs to the alanine racemase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical term3D-structure
Complete 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_0000114581

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 HAMAP-Rule MF_01201

Experimental info

Sequence conflict3541V → E in CAA90279. Ref.3

Secondary structure

......................................................................... 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A2W8 [UniParc].

Last modified March 15, 2005. 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

« Hide 'large scale' references
[1]Guynn L.J., Strych U., Benedik M.J.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.
[3]"The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination."
Martin B., Sharples G.J., Humbert O., Lloyd R.G., Claverys J.-P.
Mol. Microbiol. 19:1035-1045(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-367.
[4]"The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design."
Im H., Sharpe M.L., Strych U., Davlieva M., Krause K.L.
BMC Microbiol. 11:116-116(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-40, CARBOXYLATION AT LYS-129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF171873 Genomic DNA. Translation: AAD51027.1.
AE005672 Genomic DNA. Translation: AAK75776.1.
Z49988 Genomic DNA. Translation: CAA90279.1.
PIRG95197.
S71015.
RefSeqNP_346136.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S46X-ray2.00A/B1-367[»]
ProteinModelPortalP0A2W8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING170187.SP_1698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK75776; AAK75776; SP_1698.
GeneID931137.
KEGGspn:SP_1698.
PATRIC19707839. VBIStrPne105772_1762.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAITMDQLM.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycSPNE170187:GHGN-1705-MONOMER.
BRENDA5.1.1.1. 5946.
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...

Other

EvolutionaryTraceP0A2W8.

Entry information

Entry nameALR_STRPN
AccessionPrimary (citable) accession number: P0A2W8
Secondary accession number(s): Q54899, Q9S3V7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 68 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways