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O13966 (ACON_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. 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:
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)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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 Potential.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 778Aconitate hydratase, mitochondrialPRO_0000000546

Regions

Region188 – 1903Substrate binding By similarity
Region665 – 6662Substrate binding By similarity

Sites

Metal binding3811Iron-sulfur (4Fe-4S) By similarity
Metal binding4441Iron-sulfur (4Fe-4S) By similarity
Metal binding4471Iron-sulfur (4Fe-4S) By similarity
Binding site951Substrate By similarity
Binding site4701Substrate By similarity
Binding site4751Substrate By similarity
Binding site6021Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O13966 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: FBAECB34392C7967

FASTA77884,852
        10         20         30         40         50         60 
MGSRIFTQST LRSFSCAPVA ANIDAKKVAM SNFEKNKFIN YQRIKDNLEI VKKRLNRPLT 

        70         80         90        100        110        120 
YSEKILYGHL DDPVNQDIER GVSYLKLRPD RVACQDATAQ MAILQFMSAG MPEVAVPVTV 

       130        140        150        160        170        180 
HCDHLIEAYE GGPIDLERAN VTNKEVYDFL QTACAKYNIG FWRPGSGIIH QIVLENYAFP 

       190        200        210        220        230        240 
GGLLIGTDSH TPNAGGLGMV AIGVGGADAV DVMANLPWEL KCPKVIGVKL TGQLKGWTSP 

       250        260        270        280        290        300 
KDVILKVAGI LTVKGGTGAI VEYFGPGVES LSCTGMGTIC NMGAEIGATT SIFPFNPRMS 

       310        320        330        340        350        360 
EYLRATNRSA IADYAEEFAP IIAADENAHY DQIIEIDLNT LEPHLNGPFT PDLATPISKF 

       370        380        390        400        410        420 
KEAVKKNDWP QELKVGLIGS CTNSSYEDMS RAASICQQAI DKGIKTKSLF TITPGSEQVR 

       430        440        450        460        470        480 
ATLTRDGQLD TMRKAGGIVL ANACGPCIGQ WKRTDVKKGE KNSIVTSYNR NFTGRNDANP 

       490        500        510        520        530        540 
ATHAFVTSPD IVTAMVFSGD MNFNPLTDTL KDKDGNDFKF EPPTGAGLPS KGYDPGSNTY 

       550        560        570        580        590        600 
VAPSSVNVKD VAIDPHSKRL QRLTPFKKWD GKDMKGLKIL IKAKGKCTTD HISAAGPWLK 

       610        620        630        640        650        660 
YRGHLQNISN NYMIGAINAE NGEANKLKDQ LTGEYKTVPN VAIDYRDHGI RWVTLGEQNF 

       670        680        690        700        710        720 
GEGSSREHAA LEPRYLGGAA VITKSFARIH ETNLKKQGLL PLTFADPAAY DKISPFDTVD 

       730        740        750        760        770 
IDGLTTFAPG KPLTLVVHPA DGSAEWSTKL NHTFNKDQIE WFKAGSALNH MANMHKQK 

« 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
CU329670 Genomic DNA. Translation: CAB11263.1.
PIRT38347.
RefSeqNP_594031.1. NM_001019456.1.

3D structure databases

ProteinModelPortalO13966.
SMRO13966. Positions 27-777.
ModBaseSearch...

Protein-protein interaction databases

STRINGO13966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2541450.
KEGGspo:SPAC24C9.06c.
NMPDRfig|4896.1.peg.4001.

Organism-specific databases

GeneDB_SpombeSPAC24C9.06c.

Phylogenomic databases

eggNOGfuNOG07263.
GeneTreeEFGT00050000001032.
HOGENOMHBG295973.
OMAAINAENK.
OrthoDBEOG4HX885.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001659-MONOMER.

Gene expression databases

ArrayExpressO13966.

Family and domain databases

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]
Gene3DG3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits.
G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit.
G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
KOK01681.
PANTHERPTHR11670. Aconitase-like_core. 1 hit.
PTHR11670:SF5. Aconitase_mito. 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...

Entry information

Entry nameACON_SCHPO
AccessionPrimary (citable) accession number: O13966
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: December 14, 2011
This is version 88 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