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Q4UQB5 (ALR_XANC8) 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:XC_3718
OrganismXanthomonas campestris pv. campestris (strain 8004) [Complete proteome] [HAMAP]
Taxonomic identifier314565 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length360 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 – 360360Alanine racemase HAMAP-Rule MF_01201
PRO_1000066063

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
Q4UQB5 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 254C37D9392DD6C5

FASTA36039,247
        10         20         30         40         50         60 
MRPAQALIDL DALRHNYRLA RQLGGGKALA VVKADAYGHG AVRCAQALEP EADGFAVACI 

        70         80         90        100        110        120 
EEALELRQAG VRAPILLLEG FFEHDELALI AEHDLWTVVA TPWQVRALAE FRSPRPLRVW 

       130        140        150        160        170        180 
LKLDSGMHRL GLSPEDFRAA WLHLRGLPQI DSLVLMTHLA QADELECSRT DEQAVAFALT 

       190        200        210        220        230        240 
CGGMRAETSL RNSPGLLGWP ALRNDWSRPG LMLYGANPFP QPSELTAQLR PVMTVRSRII 

       250        260        270        280        290        300 
SVRDLPAGEP VGYGARFVAE RPTRVGVVAM GYADGYPQFA PNGTPVLVDG KVCPLIGRVS 

       310        320        330        340        350        360 
MDMLTVDLTE HPHADVGTPV QLWGDAPQVS TLAAQCNVSA YQLLCGLKRV PRHYSTPAHA 

« Hide

References

[1]"Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris."
Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., Gu W.-Y., Lu G., Rong L. expand/collapse author list , Tian Y., Yao Z., Fu G., Chen B., Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.
Genome Res. 15:757-767(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 8004.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000050 Genomic DNA. Translation: AAY50758.1.
RefSeqYP_244778.1. NC_007086.1.

3D structure databases

ProteinModelPortalQ4UQB5.
SMRQ4UQB5. Positions 1-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314565.XC_3718.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY50758; AAY50758; XC_3718.
GeneID3379337.
KEGGxcb:XC_3718.
PATRIC24069153. VBIXanCam24967_3938.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMALWQLEAI.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycXCAM314565:GCQG-3742-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_XANC8
AccessionPrimary (citable) accession number: Q4UQB5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 5, 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