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Q7V9Z2 (ALR_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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

EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:Pro_1681
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length386 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
Reference 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 – 386386Alanine racemase HAMAP-Rule MF_01201
PRO_1000066025

Sites

Active site481Proton acceptor; specific for D-alanine By similarity
Active site2791Proton acceptor; specific for L-alanine By similarity
Binding site1471Substrate By similarity
Binding site3271Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue481N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V9Z2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 8C7CF47477A917E5

FASTA38641,899
        10         20         30         40         50         60 
MATTSMPLNK IDPRQRAWVE VSPDAIKANT LAIRSLLDEQ CLLMAVVKAD GYGHGSETVA 

        70         80         90        100        110        120 
EAALAGGATN LGVATLQEAL ELRKAGIVCP ILVLGNLINP EDLDACIHWD LMPTLSSARE 

       130        140        150        160        170        180 
ALLCNQIAES HDKEFCVHIK VDTGMTRLGC DLRLASELIQ LVDNLKNLSL RGIYSHLALA 

       190        200        210        220        230        240 
DVEANGQANS FTSKQKEKFE TLLSSVMPRG KPLYRHLANS AGTLRDKGLH FDMVRVGLAL 

       250        260        270        280        290        300 
YGYSPLKDLR NNFSLQPALA VRAKVTLLRD VPSDTGVSYG HTFITQRPSR LAVVGIGYAD 

       310        320        330        340        350        360 
GISRALSGKM SVLIDGKFYP QVGSITMDQL VIDITESPQI QIGSVVTLLG VDGDSAITPY 

       370        380 
DWSEISGSIP WEILCSFKYR LPRVVI 

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAQ00725.1.
RefSeqNP_876072.1. NC_005042.1.

3D structure databases

ProteinModelPortalQ7V9Z2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro1681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ00725; AAQ00725; Pro_1681.
GeneID1463063.
KEGGpma:Pro_1681.
PATRIC23030191. VBIProMar8617_1775.

Phylogenomic databases

eggNOGCOG0787.
KOK01775.
OMAIYSHLAL.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-1719-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_PROMA
AccessionPrimary (citable) accession number: Q7V9Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 1, 2003
Last modified: June 11, 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