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O94286 (MTND_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
EC=1.13.11.54
Alternative name(s):
Acireductone dioxygenase (Fe(2+)-requiring)
Short name=ARD
Short name=Fe-ARD
Gene names
Name:adi1
ORF Names:SPBC887.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) By similarity.

Catalytic activity

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate.

Cofactor

Binds 1 iron ion per monomer. Can also use other divalent metal cations By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6.

Subcellular location

Cytoplasm By similarity. Nucleus Ref.2.

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Methionine biosynthesis
   Cellular componentCytoplasm
Nucleus
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmethionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacireductone dioxygenase [iron(II)-requiring] activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1781781,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
PRO_0000315971

Sites

Metal binding821Iron or nickel By similarity
Metal binding841Iron or nickel By similarity
Metal binding881Iron or nickel By similarity
Metal binding1271Iron or nickel By similarity

Amino acid modifications

Modified residue1571Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
O94286 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 73DDAA2874371D90

FASTA17820,936
        10         20         30         40         50         60 
MRAYIFQDEG DQRKPNDSKI EVSAEDLEAA KVSYRHHDGD LHTFADGLMK EYGFKNRDEV 

        70         80         90        100        110        120 
VVSRKGLGDR YDNMVKKFFE EHLHEDEEIR LILDGNGYFD VRSVDDRWVR IFVEKGDLII 

       130        140        150        160        170 
LPPGIYHRFT TTTDDYIHAM RLFHENPKWI ALSRTDSTSE ELDARKSYLN SIKKSVYV

« 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.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAA21886.1.
PIRT40726.
RefSeqNP_596475.1. NM_001022395.1.

3D structure databases

ProteinModelPortalO94286.
ModBaseSearch...

Protein-protein interaction databases

STRINGO94286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC887.01.1; SPBC887.01.1:pep; SPBC887.01.
GeneID2541231.
GenomeReviewsGene locus adi1 in contig CU329671_GR.
KEGGspo:SPBC887.01.
NMPDRfig|4896.1.peg.2341.

Organism-specific databases

GeneDB_SpombeSPBC887.01.

Phylogenomic databases

eggNOGfuNOG09242.
GeneTreeEFGT00050000005318.
HOGENOMHBG660685.
OMAVDSANTI.
OrthoDBEOG498Z95.

Gene expression databases

ArrayExpressO94286.

Family and domain databases

InterProIPR004313. Acireductn_dOase_family.
IPR011051. Cupin_RmlC_type.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
KOK08967.
PANTHERPTHR23418. Acireductn_dOase. 1 hit.
PfamPF03079. ARD. 1 hit.
[Graphical view]
SUPFAMSSF51182. RmlC_like_cupin. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTND_SCHPO
AccessionPrimary (citable) accession number: O94286
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 70 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents