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A1VF31 (ALR_DESVV) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 56. 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:Dvul_2031
OrganismDesulfovibrio vulgaris subsp. vulgaris (strain DP4) [Complete proteome] [HAMAP]
Taxonomic identifier391774 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length376 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 – 376376Alanine racemase HAMAP-Rule MF_01201
PRO_1000164594

Sites

Active site361Proton acceptor; specific for D-alanine By similarity
Active site2661Proton acceptor; specific for L-alanine By similarity
Binding site1341Substrate By similarity
Binding site3141Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue361N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1VF31 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F41CD28AB3346EA6

FASTA37639,410
        10         20         30         40         50         60 
MPISYNKASV VVSLQSIIAN YRRIRTVAQR PMPVIKSDAY GHGLEAVGMA LEAEGARECA 

        70         80         90        100        110        120 
VGTVGEGAKL RKAGFGADIV ALLGALDRED AQLAASSGII PTVLDIAGLE RLAAQGTTER 

       130        140        150        160        170        180 
PVRVALKFDT GMARLGFTEH DVSALCERLR TLPSVRPVMA VSHLAVADDP TQSAFTMAQG 

       190        200        210        220        230        240 
AAFARIMAGL RSNFPDIMGS LSNSAATLAH PQLHWDVQRP GIALYGSNPL RGTALARHGE 

       250        260        270        280        290        300 
GLLPAMSVSV PVLQVHPLPA GRSISYGRTY TATKDATVAI IAAGYADNYS RALSGRGVAV 

       310        320        330        340        350        360 
AGGRRVPVLG RVCMQTTAID VTDVPGIATG DRVWLLGGPG PATVSADELA DLWGTISYEV 

       370 
LCLLGMNPRR HDDSVE 

« Hide

References

[1]"Contribution of mobile genetic elements to Desulfovibrio vulgaris genome plasticity."
Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S., He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P., Stahl D.A.
Environ. Microbiol. 11:2244-2252(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000527 Genomic DNA. Translation: ABM29047.1.
RefSeqYP_967474.1. NC_008751.1.

3D structure databases

ProteinModelPortalA1VF31.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391774.Dvul_2031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM29047; ABM29047; Dvul_2031.
GeneID4662479.
KEGGdvl:Dvul_2031.
PATRIC21767952. VBIDesVul62463_2246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAISHFACA.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycDVUL391774:GHS0-2091-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_DESVV
AccessionPrimary (citable) accession number: A1VF31
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 56 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