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Q9P7D4 (ACON2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Probable aconitate hydratase 2
Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase
Gene names
ORF Names:SPBP4H10.15
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 length918 AA.
Sequence statusComplete.
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.

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

Chain1 – 918918Probable aconitate hydratase 2
PRO_0000316198

Regions

Region198 – 2003Substrate binding By similarity
Region680 – 6812Substrate binding By similarity

Sites

Metal binding3941Iron-sulfur (4Fe-4S) By similarity
Metal binding4571Iron-sulfur (4Fe-4S) By similarity
Metal binding4601Iron-sulfur (4Fe-4S) By similarity
Binding site1051Substrate By similarity
Binding site4841Substrate By similarity
Binding site4891Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9P7D4 [UniParc].

Last modified July 11, 2012. Version 3.
Checksum: A17A3132B7B21D90

FASTA91899,901
        10         20         30         40         50         60 
MATFARMKLC LSGSSQAIPS KGISLVAARF QSTASRASYV TPPYEKLMGK LQQVRKFLPG 

        70         80         90        100        110        120 
QKLTLAEKVL YSHLVNPEES FSGVSPSDIR GSLYLKLNPD RVAMQDASAQ MALLQFMTCG 

       130        140        150        160        170        180 
LEKTMIPASI HCDHLIVGHR GANSDIPDSI ANNKEIFDFL QSAAKKYGIQ FWGPGSGIIH 

       190        200        210        220        230        240 
QIVLENYAAP GGMMLGTDSH TPNAGGLGMI AIGVGGADAV DAMTNTPWEL KAPKIIGVNL 

       250        260        270        280        290        300 
TGAMSGWTTP KDLILHLAGK LTVRGGTGHI IEYFGPGVAS LSCTGMATVC NMGAEVGATT 

       310        320        330        340        350        360 
SIFPYTDSMR RYLIATHRAE VADAASEVHS EYNYLAADTG AKYDQIIDIN LSELTPSLNG 

       370        380        390        400        410        420 
PFTPDLSTPV SKFGEAIEKN KWPKKLSAGL IGSCTNSSYQ DMTCVVDVVE QAISAGLKPK 

       430        440        450        460        470        480 
VPFLVTPGSE QIRATIERDG ITERLEEAGA TVLANACGPC IGMWKRTDDI ASGEPNAILT 

       490        500        510        520        530        540 
SFNRNFRSRN DGNPSTMNFL TSPVIVAAKI FSSDLAFDPT HDTLQTPDGK AFKFRPPQGV 

       550        560        570        580        590        600 
ELPSAGFIAG DSSYIPEPNP QPVPETEVTI DPKSDRLEAL EPFEPYQGGE MENLKVAVKV 

       610        620        630        640        650        660 
KGKCTTDHIS AAGKWLKYKG HLSNICNNTL IGAMNAATGE VNRAYDNGKG MTIPELMWKW 

       670        680        690        700        710        720 
KKDGQPWLVV AEHNYGEGSA REHAALQPRA MNGRIILTKS FARIHETNLK KQGVLPLTFV 

       730        740        750        760        770        780 
NEADYEKIDA EDKVSTRGIE QLLEGVLDQP ITLVVTKKDG SVVEIPCKHT MSKDQIEFFK 

       790        800        810        820        830        840 
AGSALNLIRE KAHSGVVNQK VIDSIKQQPD HYADAYIFNR HFVIAKGDQL GLPFHLKGVQ 

       850        860        870        880        890        900 
VGDTIRLDKI ASFGSRDFTL FGNPYVDPSL FTIEAVVLSF PKSALSVRVK HKRRHRHDRV 

       910 
MKHKQTYTIL RVTELKLN

« 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		CU329671 Genomic DNA. Translation: CAB83173.3.
RefSeqNP_596189.3. NM_001022108.3.

3D structure databases

HSSPHSSP built from PDB template 1AMJ based on UniProtKB P20004.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPBP4H10.15-1.

Proteomic databases

PaxDbQ9P7D4.
PRIDEQ9P7D4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBP4H10.15.1; SPBP4H10.15.1:pep; SPBP4H10.15.
GeneID2541348.
KEGGspo:SPBP4H10.15.

Organism-specific databases

PomBaseSPBP4H10.15.

Phylogenomic databases

eggNOGCOG1048.
HOGENOMHOG000224293.
KOK01681.
OrthoDBEOG47M561.

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.
IPR001787. Ribosomal_L21.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF5. PTHR11670:SF5. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
PF00829. Ribosomal_L21p. 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

NextBio20802457.

Entry information

Entry nameACON2_SCHPO
AccessionPrimary (citable) accession number: Q9P7D4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 11, 2012
Last modified: May 1, 2013
This is version 80 of the entry and version 3 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

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