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Q9P5N3 (ALR2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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:
Putative alanine racemase C359.02

EC=5.1.1.1
Gene names
ORF Names:SPBC359.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

L-alanine = D-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Sequence similarities

Belongs to the alanine racemase family.

Ontologies

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

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Molecular functionalanine racemase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Putative alanine racemase C359.02
PRO_0000114605

Sites

Active site381Proton acceptor; specific for D-alanine By similarity
Active site2661Proton acceptor; specific for L-alanine By similarity

Amino acid modifications

Modified residue381N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9P5N3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: FEE9674CE1A91831

FASTA37041,148
        10         20         30         40         50         60 
MRGARAVIDL RAIGYNYNLI RELLDEKNPD AHILCILKAN AYGHGAVEVA QFLAKYCSAE 

        70         80         90        100        110        120 
GFGVASIEEA LELRLSGIQN RILLLEGFFT DEDELSLIDK YNFSITIHCE EQLKSFMNYP 

       130        140        150        160        170        180 
FKKPVEVHLK LDSGMNRLGF TPAEYADKYR LLKNHKNVSG IVKATHFAFA DIPEKSEYTL 

       190        200        210        220        230        240 
KQWRIFEKAA GCLPDPLSAG GGVIVVGWLN TIHMDWLRTG SMLYGLDPYD LDAKAPELPK 

       250        260        270        280        290        300 
PLIPAMKLMS TIVCVKHVEK DQPIGYGGAY VTTRDSLIGV VAIGYGDGFP QVRNGCPVII 

       310        320        330        340        350        360 
NGKRVPTVGK VCMDMLAIDV TDVPDVKRGD DVVLWGNPEL TIEEVSTFSN ENPFEIITGL 

       370 
TRRVPLQYTF 

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB91571.1.
RefSeqNP_595052.1. NM_001020958.1.

3D structure databases

ProteinModelPortalQ9P5N3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9P5N3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC359.02.1; SPBC359.02.1:pep; SPBC359.02.
GeneID2540953.
KEGGspo:SPBC359.02.
NMPDRfig|4896.1.peg.918.

Organism-specific databases

GeneDB_SpombeSPBC359.02.

Phylogenomic databases

eggNOGCOG0787.
GeneTreeEFGT00050000008702.
HOGENOMHBG712172.
OMAANAHAGD.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-003157-MONOMER.

Gene expression databases

ArrayExpressQ9P5N3.

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 nameALR2_SCHPO
AccessionPrimary (citable) accession number: Q9P5N3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 76 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

SIMILARITY comments

Index of protein domains and families