Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B6J0J1 (ALR_COXB2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:CbuG_1133
OrganismCoxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)) [Complete proteome] [HAMAP]
Taxonomic identifier434923 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length364 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 – 364364Alanine racemase HAMAP-Rule MF_01201
PRO_1000138592

Sites

Active site341Proton acceptor; specific for D-alanine By similarity
Active site2591Proton acceptor; specific for L-alanine By similarity
Binding site1291Substrate By similarity
Binding site3071Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue341N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J0J1 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: FF70A1F28247F4A4

FASTA36439,962
        10         20         30         40         50         60 
MNRATATINV TALKHNLSQI KALAPKSLAW AMIKSNGYGH GLVRVAKALS DANAFGVACI 

        70         80         90        100        110        120 
DEALTLREVG IKSPIIVMKG FYNEAELSQF ARHRLGAVIH CSDQVSLLKK TNLTSSLSVW 

       130        140        150        160        170        180 
LKIDTGMNRL GFSVEQSPAV YNQLKTSSSI QKPIGLMTHL ADADNENKTF TELQIKRFFS 

       190        200        210        220        230        240 
VTEKMIGPKS IVNSAGFFAY PNALVDWIRP GIILYGISPF GINYNSFKEK IEKKFRPVMT 

       250        260        270        280        290        300 
LSAKIIAIKN RRKNDSVGYG CTWSCPEDMP IAIVSIGYGD GYPRHAPSGT PVLLNGKICP 

       310        320        330        340        350        360 
LIGRVSMDMI AIDLRSQPNA QVGDDVILWG EGLPVEIIAE KAGTIAYELL CKITQRVQFI 


EIEK 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CbuG_Q212.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001019 Genomic DNA. Translation: ACJ18469.1.
RefSeqYP_002303614.1. NC_011527.1.

3D structure databases

ProteinModelPortalB6J0J1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434923.CbuG_1133.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ18469; ACJ18469; CbuG_1133.
GeneID7013549.
KEGGcbg:CbuG_1133.
PATRIC17913330. VBICoxBur10955_1134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMACIDEALT.
OrthoDBEOG6PP9NJ.
ProtClustDBCLSK914375.

Enzyme and pathway databases

BioCycCBUR434923:GC8S-1131-MONOMER.
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.
[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.
ProtoNetSearch...

Entry information

Entry nameALR_COXB2
AccessionPrimary (citable) accession number: B6J0J1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: February 19, 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