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A4VXD9 (ALR_STRSY) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. 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:SSU05_1812
OrganismStreptococcus suis (strain 05ZYH33) [Complete proteome] [HAMAP]
Taxonomic identifier391295 [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_1000066053

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
A4VXD9 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 5701743FE1F9D672

FASTA36740,211
        10         20         30         40         50         60 
MIESEHRPTQ IRVNLDAIAE NFEQVMTNLP PKTEAFAVVK ANAYGHGAVA VAKKLSSQAA 

        70         80         90        100        110        120 
GFCVSNLDEA LELRKAGIEH PILILGVVPV RFLPVAHQLN ISVTVASLDW LQDAKDLEAD 

       130        140        150        160        170        180 
LSGLTVHLKL DTGMGRIGFR KIADLLQAIA ILEELEYDIE GVYTHFATAD EVEQAHFESQ 

       190        200        210        220        230        240 
LSVFKEFLDV LPITPRWIHA SNSATSIWHA DTVFNLVRLG NILYGLNPSG RVLELPFGVQ 

       250        260        270        280        290        300 
PALSLVSEIV HVKQVEAGTT IGYGATYHST DSEWIATVPI GYADGLVRSL QGLSVLVDGQ 

       310        320        330        340        350        360 
ACEIVGRISM DQITIRLPRA YPLGQKVTLI GQDGDKTISV QEWADRIGTI NYEVVCLLTD 


RLPRIFE 

« Hide

References

[1]"A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates."
Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., Dong Y. expand/collapse author list , Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., Yang R., Wang J., Yu J.
PLoS ONE 2:E315-E315(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 05ZYH33.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000407 Genomic DNA. Translation: ABP90778.1.
RefSeqYP_001199178.1. NC_009442.1.

3D structure databases

ProteinModelPortalA4VXD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391295.SSU05_1812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP90778; ABP90778; SSU05_1812.
GeneID5099971.
KEGGssu:SSU05_1812.
PATRIC19775373. VBIStrSui128929_1781.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAIYSHLAL.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycSSUI391295:GHI8-1872-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_STRSY
AccessionPrimary (citable) accession number: A4VXD9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: June 11, 2014
This is version 52 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