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Q1IYK9 (ALR_DEIGD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:Dgeo_1380
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length355 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 – 355355Alanine racemase HAMAP-Rule MF_01201
PRO_1000065986

Sites

Active site371Proton acceptor; specific for D-alanine By similarity
Active site2511Proton acceptor; specific for L-alanine By similarity
Binding site1291Substrate By similarity
Binding site2991Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue371N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IYK9 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: C5D67E1FA1372C70

FASTA35537,475
        10         20         30         40         50         60 
MQEMQARAQA LISESALRSN LTALARQAGT QLLLPVKADA YGHGMEIVAR LAARHPAVWG 

        70         80         90        100        110        120 
FAVAVPREAA TLAALGLGKP ILLLTPPTLE EMGPLADLGV RLPVASLAEA EALPAHARAH 

       130        140        150        160        170        180 
LKVDTGMNRL GARPEEAVRV GQRLAERGLL EGAYTHFATA DEPDLSFARQ QFARFQEVLA 

       190        200        210        220        230        240 
ALPPVLAHAA NGGGVLSFGP LPSLSLARPG LASYGFAPAH LRGVAPLTPV MTLQARVTHV 

       250        260        270        280        290        300 
HAVYPGESVS YGGLWRATRK TIVATVGIGY ADGYPRNATG KACVLVRGEC RPVLGRICMD 

       310        320        330        340        350 
QCMVDVTDLE VRVGDWVEVW GTDKITVTDV AAWGGTVEYE VLTGLGARVE RVAAG 

« Hide

References

[1]"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."
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., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000359 Genomic DNA. Translation: ABF45675.1.
RefSeqYP_604844.1. NC_008025.1.

3D structure databases

ProteinModelPortalQ1IYK9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319795.Dgeo_1380.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF45675; ABF45675; Dgeo_1380.
GeneID4057539.
KEGGdge:Dgeo_1380.
PATRIC21624663. VBIDeiGeo41128_1966.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAELMAVQH.
OrthoDBEOG6PP9NJ.
ProtClustDBCLSK444872.

Enzyme and pathway databases

BioCycDGEO319795:GHMU-1404-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.
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 nameALR_DEIGD
AccessionPrimary (citable) accession number: Q1IYK9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 62 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