ACON_SCHPO
ID ACON_SCHPO Reviewed; 789 AA.
AC O13966;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Aconitate hydratase, mitochondrial;
DE Short=Aconitase;
DE EC=4.2.1.3;
DE AltName: Full=Citrate hydro-lyase;
DE Flags: Precursor;
GN ORFNames=SPAC24C9.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate, a step in the citric acid cycle. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11263.2; -; Genomic_DNA.
DR PIR; T38347; T38347.
DR RefSeq; NP_594031.2; NM_001019456.2.
DR AlphaFoldDB; O13966; -.
DR SMR; O13966; -.
DR BioGRID; 277955; 2.
DR STRING; 4896.SPAC24C9.06c.1; -.
DR MaxQB; O13966; -.
DR PaxDb; O13966; -.
DR PRIDE; O13966; -.
DR EnsemblFungi; SPAC24C9.06c.1; SPAC24C9.06c.1:pep; SPAC24C9.06c.
DR GeneID; 2541450; -.
DR KEGG; spo:SPAC24C9.06c; -.
DR PomBase; SPAC24C9.06c; -.
DR VEuPathDB; FungiDB:SPAC24C9.06c; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; O13966; -.
DR OMA; GCIGMGQ; -.
DR Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00718.
DR PRO; PR:O13966; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; ISO:PomBase.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006536; P:glutamate metabolic process; NAS:PomBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISO:PomBase.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01340; aconitase_mito; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..789
FT /note="Aconitate hydratase, mitochondrial"
FT /id="PRO_0000000546"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199..201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 613
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 676..677
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 789 AA; 86113 MW; B80A9654690BA9FA CRC64;
MFCKISRAPA RMGSRIFTQS TLRSFSCAPV AANIDAKKVA MSNFEKNKFI NYQRIKDNLE
IVKKRLNRPL TYSEKILYGH LDDPVNQDIE RGVSYLKLRP DRVACQDATA QMAILQFMSA
GMPEVAVPVT VHCDHLIEAY EGGPIDLERA NVTNKEVYDF LQTACAKYNI GFWRPGSGII
HQIVLENYAF PGGLLIGTDS HTPNAGGLGM VAIGVGGADA VDVMANLPWE LKCPKVIGVK
LTGQLKGWTS PKDVILKVAG ILTVKGGTGA IVEYFGPGVE SLSCTGMGTI CNMGAEIGAT
TSIFPFNPRM SEYLRATNRS AIADYAEEFA PIIAADENAH YDQIIEIDLN TLEPHLNGPF
TPDLATPISK FKEAVKKNDW PQELKVGLIG SCTNSSYEDM SRAASICQQA IDKGIKTKSL
FTITPGSEQV RATLTRDGQL DTMRKAGGIV LANACGPCIG QWKRTDVKKG EKNSIVTSYN
RNFTGRNDAN PATHAFVTSP DIVTAMVFSG DMNFNPLTDT LKDKDGNDFK FEPPTGAGLP
SKGYDPGSNT YVAPSSVNVK DVAIDPHSKR LQRLTPFKKW DGKDMKGLKI LIKAKGKCTT
DHISAAGPWL KYRGHLQNIS NNYMIGAINA ENGEANKLKD QLTGEYKTVP NVAIDYRDHG
IRWVTLGEQN FGEGSSREHA ALEPRYLGGA AVITKSFARI HETNLKKQGL LPLTFADPAA
YDKISPFDTV DIDGLTTFAP GKPLTLVVHP ADGSAEWSTK LNHTFNKDQI EWFKAGSALN
HMANMHKQK
