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Q9RLU5 (ALR_LACLM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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:llmg_1704
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]
Taxonomic identifier416870 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Biotechnological use

Homoalanine fermentation combined with the disruption of the alr gene allowed the industrial and stereospecific production (>99%) of L-alanine, which is used as a food sweetener and for pharmaceutical applications. 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 – 367367Alanine racemase HAMAP-Rule MF_01201
PRO_0000114527

Sites

Active site401Proton acceptor; specific for D-alanine By similarity
Active site2631Proton acceptor; specific for L-alanine By similarity
Binding site1361Substrate By similarity
Binding site3101Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue401N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RLU5 [UniParc].

Last modified March 5, 2002. Version 2.
Checksum: B6DE1496315FA814

FASTA36740,677
        10         20         30         40         50         60 
MKTSPHRNTS AIVDLKAIRN NIEKFKKHIN PNAEIWPAVK ADAYGHGSIE VSKAVSDLVG 

        70         80         90        100        110        120 
GFCVSNLDEA IELRNHLVTK PILVLSGIVP EDVDIAAALN ISLTAPSLEW LKLVVQEEAE 

       130        140        150        160        170        180 
LSDLKIHIGV DSGMGRIGIR DVEEANQMIE LADKYAINFE GIFTHFATAD MADETKFKNQ 

       190        200        210        220        230        240 
QARFNKIMAG LSRQPKFIHS TNTAAALWHK EQVQAIERLG ISMYGLNPSG KTLELPFEIE 

       250        260        270        280        290        300 
PALSLVSELT HIKKIAAGET VGYGATYETS EETWIGTVPI GYADGWTRQM QGFKVLVDGK 

       310        320        330        340        350        360 
FCEIVGRVCM DQMMIKLDKS YPLGTKVTLI GRDKANEITT TDVADWRGTI NYEVLCLLSD 


RIKRIYK 

« Hide

References

« Hide 'large scale' references
[1]"Conversion of Lactococcus lactis from homolactic to homoalanine fermentation through metabolic engineering."
Hols P., Kleerebezem M., Schank A.N., Ferain T., Hugenholtz J., Delcour J., De Vos W.M.
Nat. Biotechnol. 17:588-592(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MG1363.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y18148 Genomic DNA. Translation: CAB56755.2.
AM406671 Genomic DNA. Translation: CAL98277.1.
RefSeqYP_001032982.1. NC_009004.1.

3D structure databases

ProteinModelPortalQ9RLU5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416870.llmg_1704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL98277; CAL98277; llmg_1704.
GeneID4796695.
KEGGllm:llmg_1704.
PATRIC22284585. VBILacLac4574_1747.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAITMDQLM.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycLLAC416870:GCDT-1711-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_LACLM
AccessionPrimary (citable) accession number: Q9RLU5
Secondary accession number(s): A2RLV4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: February 19, 2014
This is version 84 of the entry and version 2 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