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Q87L78 (ALR1_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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 1

EC=5.1.1.1
Gene names
Name:alr1
Ordered Locus Names:VP2734
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length358 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 – 358358Alanine racemase 1 HAMAP-Rule MF_01201
PRO_0000114593

Sites

Active site341Proton acceptor; specific for D-alanine By similarity
Active site2541Proton acceptor; specific for L-alanine By similarity
Binding site1291Substrate By similarity
Binding site3021Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue341N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87L78 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 462AE69D3291E22D

FASTA35839,084
        10         20         30         40         50         60 
MKAAKACIDL SALQHNLQRV KAQAPESKVM AVVKANGYGH GLRHVAKHAN HADAFGVARI 

        70         80         90        100        110        120 
EEALQLRACG VVKPILLLEG FYSPGDLPVL VTNNIQTVVH CEEQLIALEQ ADLETPVVVW 

       130        140        150        160        170        180 
LKIDSGMHRL GVRPEQYDEF ISRLKTCPNV AKPLRYMSHF GCADELDSSI TPQQIELFMS 

       190        200        210        220        230        240 
LTSGCQGERS LAASAGLLAW PQSQLEWVRP GIIMYGVSPF SDKTAQDLGY QPVMTLKSHL 

       250        260        270        280        290        300 
IAVREVKQGE SVGYGGIWTS ERDTKVGVIA VGYGDGYPRS APNGTPVWVN GRTVPIAGRV 

       310        320        330        340        350 
SMDMLTVDLG PDATDKVSDE AILWGKELPV EEVANHIGTI AYELVTKLTP RVEMEYTK 

« 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
BA000031 Genomic DNA. Translation: BAC60997.1.
RefSeqNP_799113.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87L78.
SMRQ87L78. Positions 1-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP2734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60997; BAC60997; BAC60997.
GeneID1190284.
KEGGvpa:VP2734.
PATRIC20143678. VBIVibPar50997_2631.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMACIDEALT.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-2828-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 nameALR1_VIBPA
AccessionPrimary (citable) accession number: Q87L78
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 75 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