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A4J8G6 (ALR_DESRM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. 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:Dred_2865
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum

Protein attributes

Sequence length370 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 – 370370Alanine racemase HAMAP-Rule MF_01201
PRO_1000138595

Sites

Active site361Proton acceptor; specific for D-alanine By similarity
Active site2651Proton acceptor; specific for L-alanine By similarity
Binding site1341Substrate By similarity
Binding site3131Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue361N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4J8G6 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 3D3D552D57529C0E

FASTA37040,808
        10         20         30         40         50         60 
MKEPIWAEIN LEAIRHNIKE IRKMVGPNRE IMAVVKANGY GHGAVPVARV ALEAGATRLA 

        70         80         90        100        110        120 
VARLSEAQEL RRAGLKVPIL LLGYISPDQI GDALEYNVTL TVFRFDLAKK IAAIAQGRGQ 

       130        140        150        160        170        180 
RATVHLKVDT GMGRIGFTPD EEGLAEITAV CALNGLDVEG IYTHFATADE QDKSYTRWQF 

       190        200        210        220        230        240 
KRFMLVLNRL EEQGITFSLR HCANSAAIME FPETYLDLVR PGIILYGLYP SEEVDKGKLL 

       250        260        270        280        290        300 
LQPAMTLKAR ITHVKKVNSG TKISYGCTYT VPQETDIASL PLGYADGYPR LLSSKGQVLV 

       310        320        330        340        350        360 
KGKRARVVGR VCMDQCMVDV GHIAEVKVHD EVIIFGGAEL PVEEVATWLG TINYEVVCWV 

       370 
GSRVPRVYIG 

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000612 Genomic DNA. Translation: ABO51369.1.
RefSeqYP_001114194.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J8G6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349161.Dred_2865.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO51369; ABO51369; Dred_2865.
GeneID4958620.
KEGGdrm:Dred_2865.
PATRIC21732185. VBIDesRed82656_3137.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAWRDMARR.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycDRED349161:GHP6-2945-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_DESRM
AccessionPrimary (citable) accession number: A4J8G6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 1, 2007
Last modified: June 11, 2014
This is version 57 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