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O13966 (ACON_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. 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:
Aconitate hydratase, mitochondrial
Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase
Gene names
ORF Names:SPAC24C9.06c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length789 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity.

Catalytic activity

Citrate = isocitrate.

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion Ref.3.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion Potential
Chain33 – 789757Aconitate hydratase, mitochondrial
PRO_0000000546

Regions

Region199 – 2013Substrate binding By similarity
Region676 – 6772Substrate binding By similarity

Sites

Metal binding3921Iron-sulfur (4Fe-4S) By similarity
Metal binding4551Iron-sulfur (4Fe-4S) By similarity
Metal binding4581Iron-sulfur (4Fe-4S) By similarity
Binding site1061Substrate By similarity
Binding site4811Substrate By similarity
Binding site4861Substrate By similarity
Binding site6131Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O13966 [UniParc].

Last modified April 18, 2012. Version 2.
Checksum: B80A9654690BA9FA

FASTA78986,113
        10         20         30         40         50         60 
MFCKISRAPA RMGSRIFTQS TLRSFSCAPV AANIDAKKVA MSNFEKNKFI NYQRIKDNLE 

        70         80         90        100        110        120 
IVKKRLNRPL TYSEKILYGH LDDPVNQDIE RGVSYLKLRP DRVACQDATA QMAILQFMSA 

       130        140        150        160        170        180 
GMPEVAVPVT VHCDHLIEAY EGGPIDLERA NVTNKEVYDF LQTACAKYNI GFWRPGSGII 

       190        200        210        220        230        240 
HQIVLENYAF PGGLLIGTDS HTPNAGGLGM VAIGVGGADA VDVMANLPWE LKCPKVIGVK 

       250        260        270        280        290        300 
LTGQLKGWTS PKDVILKVAG ILTVKGGTGA IVEYFGPGVE SLSCTGMGTI CNMGAEIGAT 

       310        320        330        340        350        360 
TSIFPFNPRM SEYLRATNRS AIADYAEEFA PIIAADENAH YDQIIEIDLN TLEPHLNGPF 

       370        380        390        400        410        420 
TPDLATPISK FKEAVKKNDW PQELKVGLIG SCTNSSYEDM SRAASICQQA IDKGIKTKSL 

       430        440        450        460        470        480 
FTITPGSEQV RATLTRDGQL DTMRKAGGIV LANACGPCIG QWKRTDVKKG EKNSIVTSYN 

       490        500        510        520        530        540 
RNFTGRNDAN PATHAFVTSP DIVTAMVFSG DMNFNPLTDT LKDKDGNDFK FEPPTGAGLP 

       550        560        570        580        590        600 
SKGYDPGSNT YVAPSSVNVK DVAIDPHSKR LQRLTPFKKW DGKDMKGLKI LIKAKGKCTT 

       610        620        630        640        650        660 
DHISAAGPWL KYRGHLQNIS NNYMIGAINA ENGEANKLKD QLTGEYKTVP NVAIDYRDHG 

       670        680        690        700        710        720 
IRWVTLGEQN FGEGSSREHA ALEPRYLGGA AVITKSFARI HETNLKKQGL LPLTFADPAA 

       730        740        750        760        770        780 
YDKISPFDTV DIDGLTTFAP GKPLTLVVHP ADGSAEWSTK LNHTFNKDQI EWFKAGSALN 


HMANMHKQK

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Comparative functional genomics of the fission yeasts."
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. expand/collapse author list , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.
[3]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB11263.2.
PIRT38347.
RefSeqNP_594031.2. NM_001019456.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC24C9.06c-1.

Proteomic databases

PaxDbO13966.
PRIDEO13966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC24C9.06c.1; SPAC24C9.06c.1:pep; SPAC24C9.06c.
GeneID2541450.
KEGGspo:SPAC24C9.06c.

Organism-specific databases

PomBaseSPAC24C9.06c.

Phylogenomic databases

eggNOGCOG1048.
HOGENOMHOG000224293.
KOK01681.
OrthoDBEOG4HX885.

Enzyme and pathway databases

UniPathwayUPA00223; UER00718.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF5. PTHR11670:SF5. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01340. aconitase_mito. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802552.

Entry information

Entry nameACON_SCHPO
AccessionPrimary (citable) accession number: O13966
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 18, 2012
Last modified: May 1, 2013
This is version 99 of the entry and version 2 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