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O59828 (ALR1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alanine racemase, catabolic

EC=5.1.1.1
Gene names
Name:alr1
ORF Names:SPCC965.08c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-alanine = D-alanine.

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.

Sequence similarities

Belongs to the alanine racemase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 9.0-9.5.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processalanine metabolic process

Inferred from direct assay. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionalanine racemase activity

Inferred from direct assay. Source: GeneDB_Spombe

serine racemase activity

Inferred from direct assay. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Alanine racemase, catabolic
PRO_0000114604

Sites

Active site381Proton acceptor; specific for D-alanine By similarity
Active site2691Proton acceptor; specific for L-alanine By similarity

Amino acid modifications

Modified residue381N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O59828 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 76CEBD17E159E13F

FASTA37541,585
        10         20         30         40         50         60 
MRGAKSVIDL HAIAHNYNVA KQMMLQKNPS GHVLAIVKAN AYGHGAVQVA RFLLKHCSSI 

        70         80         90        100        110        120 
DGFGVSSIEE ALELRHGGIY NKIVLLEGFF TEEDELKLID DYNFSIIIHS EDQVNSFIKY 

       130        140        150        160        170        180 
PFNRPVEIWL KLDSGMNRLG FTPSQFMKFY NLLSNNKNVS NIGKITHFAF ADMLENPEHT 

       190        200        210        220        230        240 
LKQWDIFEKS VAHLPGPLSA GGSAIILGWL NTVCTDWLRA GIMLYGISPF LSKNKDSKTP 

       250        260        270        280        290        300 
ESVNIKPAMK LVSTIISVKH VDKGQPIGYG GRYVATRDMK LGVVAMGYGD GFPRQVKDGC 

       310        320        330        340        350        360 
PVLVNGVKAP IVGRVSMDML TVDLSDIPDV KPGDEVIFWG TPELTVADIA KYCSDTSPYE 

       370 
LVTKLTRRVP LQYTY 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Functional characterization of alanine racemase from Schizosaccharomyces pombe: a eucaryotic counterpart to bacterial alanine racemase."
Uo T., Yoshimura T., Tanaka N., Takegawa K., Esaki N.
J. Bacteriol. 183:2226-2233(2001) [PubMed: 11244061] [Abstract]
Cited for: CHARACTERIZATION.
Strain: SP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAA19068.1.
PIRT41661.
RefSeqNP_588518.1. NM_001023507.1.

3D structure databases

ProteinModelPortalO59828.
ModBaseSearch...

Protein-protein interaction databases

STRINGO59828.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC965.08c.1; SPCC965.08c.1:pep; SPCC965.08c.
GeneID2538742.
GenomeReviewsGene locus alr1 in contig CU329672_GR.
KEGGspo:SPCC965.08c.
NMPDRfig|4896.1.peg.856.

Organism-specific databases

GeneDB_SpombeSPCC965.08c.

Phylogenomic databases

eggNOGCOG0787.
GeneTreeEFGT00050000008702.
HOGENOMHBG712172.
OMAATAYINT.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-000419-MONOMER.
BRENDA5.1.1.1. 5615.

Gene expression databases

ArrayExpressO59828.

Family and domain databases

InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
[Graphical view]
Gene3DG3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit.
KOK01775.
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. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR00492. Alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR1_SCHPO
AccessionPrimary (citable) accession number: O59828
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families