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

Q9RAE7 (ALR2_RHIL3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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, catabolic

EC=5.1.1.1
Gene names
Name:dadX
Ordered Locus Names:pRL120416
Encoded onPlasmid pRL12 Ref.2
OrganismRhizobium leguminosarum bv. viciae (strain 3841) [Complete proteome] [HAMAP]
Taxonomic identifier216596 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. HAMAP-Rule MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201

Sequence similarities

Belongs to the alanine racemase family.

Sequence caution

The sequence CAB53547.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological_processalanine metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   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 – 377377Alanine racemase, catabolic HAMAP-Rule MF_01201
PRO_0000114554

Sites

Active site511Proton acceptor; specific for D-alanine By similarity
Active site2721Proton acceptor; specific for L-alanine By similarity
Binding site1501Substrate By similarity
Binding site3201Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue511N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RAE7 [UniParc].

Last modified June 27, 2006. Version 3.
Checksum: BB38DAC35BD3DBF2

FASTA37740,548
        10         20         30         40         50         60 
MDSDILVSRT RTATIAQGAT GYLMIDLAAL GRNYRKLVSM LAPVRAGAVV KADAYGLGAE 

        70         80         90        100        110        120 
RVARTLYSEG CRHFFVAQFV EAVRLRPALA HDAQIFVLNG LQPGNEIACA EMGIVPVLNS 

       130        140        150        160        170        180 
LAQWRQWSAA ARILKRCLPA VLQFDTGMSR LGFPREERRE LAAALRDGSN VEILFIMSHL 

       190        200        210        220        230        240 
ASADDMGSEQ NGEQFAEMSR IADEFPGFDI SFANSGGVFL GEAYYGVLAR PGIALYGGAP 

       250        260        270        280        290        300 
NAGEKNPMEP VVSLNVAVVQ TRTVPAGAKV GYGGAHVTQR ETRLATIAAG YADGLPRCLS 

       310        320        330        340        350        360 
DRGAVYFKGV RLPIVGRVSM DSTTVDITAL PEGALTFGSL VEVLGRHQTL EDIARDAGTI 

       370 
SYEILTGLGD RYDRQYR 

« Hide

References

« Hide 'large scale' references
[1]"Identification of alanine dehydrogenase and its role in mixed secretion of ammonium and alanine by pea bacteroids."
Allaway D.A., Lodwig E.M., Crompton L.A., Wood M., Parsons R., Wheeler T.R., Poole P.S.
Mol. Microbiol. 36:508-515(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome of Rhizobium leguminosarum has recognizable core and accessory components."
Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I., Chillingworth T., Clarke K. expand/collapse author list , Cronin A., Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.
Genome Biol. 7:R34.1-R34.20(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 3841.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ249196 Genomic DNA. Translation: CAB53547.1. Different initiation.
AM236086 Genomic DNA. Translation: CAK12125.1.
RefSeqYP_764923.1. NC_008378.1.

3D structure databases

ProteinModelPortalQ9RAE7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216596.pRL120416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK12125; CAK12125; pRL120416.
GeneID4398234.
KEGGrle:pRL120416.
PATRIC23134919. VBIRhiLeg32091_0421.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031445.
KOK01775.
OMARHFFVAH.
OrthoDBEOG6PP9NJ.
ProtClustDBCLSK881831.

Enzyme and pathway databases

BioCycRLEG216596:GKE5-5230-MONOMER.

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...

Entry information

Entry nameALR2_RHIL3
AccessionPrimary (citable) accession number: Q9RAE7
Secondary accession number(s): Q1M447
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 86 of the entry and version 3 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