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Q3BNX4 (ALR_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. 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:XCV3808
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length365 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 – 365365Alanine racemase HAMAP-Rule MF_01201
PRO_1000066062

Sites

Active site331Proton acceptor; specific for D-alanine By similarity
Active site2531Proton acceptor; specific for L-alanine By similarity
Binding site1291Substrate By similarity
Binding site3011Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue331N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3BNX4 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 6C4CF755C2A0FB79

FASTA36539,737
        10         20         30         40         50         60 
MRPAQASIDL EALRHNYRLA RRLGGSKALA VVKADAYGHG AVRCAQALEP EADGFAVACI 

        70         80         90        100        110        120 
EEALELRQAG IRAPILLLEG FFEHDELRLI AEHDLWTVAA TQQQVRALAE FQSPRPLRVW 

       130        140        150        160        170        180 
LKMDSGMHRL GLSPEDFRAA WLRLRGLPQI ASLVLMTHLA RADELDCSRT DEQAVAFALT 

       190        200        210        220        230        240 
AGGMRAETSL RNSPGLLGWP ALRNDWSRPG LMLYGANPFP QHTENTAQLR PVMTLRSRII 

       250        260        270        280        290        300 
SVRELPAGEP VGYGARFVAE RPTRVGVVAM GYADGYPQFA PNGTPVLVDG QICPLIGRVS 

       310        320        330        340        350        360 
MDMLTVDLTD HPQADIGTPV QLWGDAPQVS ALAAQCNVSA YQLLCGLKRV PRIYVGEAAV 


GKLSA 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ25539.1.
RefSeqYP_365539.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BNX4.
SMRQ3BNX4. Positions 1-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV3808.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ25539; CAJ25539; XCV3808.
GeneID3732561.
KEGGxcv:XCV3808.
PATRIC24097252. VBIXanCam71633_4095.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMALWQLEAI.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycXCAM316273:GJF8-3911-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_XANC5
AccessionPrimary (citable) accession number: Q3BNX4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: June 11, 2014
This is version 61 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