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Q87HG4 (ALR2_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. 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 2

EC=5.1.1.1
Gene names
Name:alr2
Ordered Locus Names:VPA1001
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length409 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 – 409409Alanine racemase 2 HAMAP-Rule MF_01201
PRO_0000114594

Sites

Active site761Proton acceptor; specific for D-alanine By similarity
Active site3011Proton acceptor; specific for L-alanine By similarity
Binding site1751Substrate By similarity
Binding site3491Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue761N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87HG4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8BF46C9023224E8B

FASTA40944,326
        10         20         30         40         50         60 
MRLKKTLLSI AIAAATFTPA MHSIAAPLQL QATLDQESQI QSSNTWLEID LGQFKQNIEQ 

        70         80         90        100        110        120 
FKSHMNDQTK ICAVMKADAY GNGIAGLMPT IIEQQIPCVA IASNAEAQVV RDSGFKGQLM 

       130        140        150        160        170        180 
RVRSAEIGEI EGALDLNVEE LIGTLDQAKA IAALSKKANK TVKVHLALND GGMGRNGIDM 

       190        200        210        220        230        240 
TTENGKKEAL AIAKQSGVEI VGIMTHFPNY NAEEVRAKLG SFKESSAWLI KEANLKREDI 

       250        260        270        280        290        300 
LLHVANSYTA LNVPEAQLDM VRPGGVLYGD LPTNLEYPSI VSFKTRVASL HHLPKNSTVG 

       310        320        330        340        350        360 
YDSSFTTTKE SVMANLPVGY SDGYPRKMGN TADVLINGQR AKVVGVTSMN TTMIDVSDIK 

       370        380        390        400 
GVKPGSEVVL FGNQKSQTIN AAEIEKNADV IFPELYTIWG TSNPRVYVK 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000032 Genomic DNA. Translation: BAC62344.1.
RefSeqNP_800511.1. NC_004605.1.

3D structure databases

ProteinModelPortalQ87HG4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VPA1001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC62344; BAC62344; BAC62344.
GeneID1191694.
KEGGvpa:VPA1001.
PATRIC20146405. VBIVibPar50997_3932.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000279190.
KOK01775.
OMAQQIPCVA.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-4238-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 nameALR2_VIBPA
AccessionPrimary (citable) accession number: Q87HG4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 76 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