ACON_DICDI
ID ACON_DICDI Reviewed; 771 AA.
AC Q54XS2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable aconitate hydratase, mitochondrial;
DE Short=Aconitase;
DE EC=4.2.1.3;
DE AltName: Full=Citrate hydro-lyase;
DE Flags: Precursor;
GN Name=aco2; Synonyms=acnB; ORFNames=DDB_G0278779;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {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:0000250}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000024; EAL67991.1; -; Genomic_DNA.
DR RefSeq; XP_641958.1; XM_636866.1.
DR AlphaFoldDB; Q54XS2; -.
DR SMR; Q54XS2; -.
DR STRING; 44689.DDB0230168; -.
DR PaxDb; Q54XS2; -.
DR EnsemblProtists; EAL67991; EAL67991; DDB_G0278779.
DR GeneID; 8621690; -.
DR KEGG; ddi:DDB_G0278779; -.
DR dictyBase; DDB_G0278779; aco2.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; Q54XS2; -.
DR OMA; GCIGMGQ; -.
DR PhylomeDB; Q54XS2; -.
DR Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00718.
DR PRO; PR:Q54XS2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
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:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..771
FT /note="Probable aconitate hydratase, mitochondrial"
FT /id="PRO_0000328572"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179..181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 594
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 657..658
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 771 AA; 83542 MW; 152D8580014A1152 CRC64;
MNSLVKGISK VRSTRSFSTV SMSPLEPNKK LNYEGIDAKL KQFRLHHNKP LTLAEKIIYG
HLEDPSTKVE RGITYLKLHP DRVAMQDATA QMAVLQFMSA GLPETAVPTT IHCDHLIEAY
KGGEKDLEVA KDINKEVYDF LSTSAKKFGM GFWKPGSGII HQIVLENYAF PGGLMIGTDS
HTPNAGGLGM VAVGVGGADA VDVMAGIPWE LKAPKIIGVK LTGSLKGWSS PKDVILRVAD
ILTVKGGTGA IVEYFGSGVE SLSCTGMATI CNMGAEIGAT TSLFPFNKRM VDYLNSTGRS
NIANAANSFK HNLVADPNAH YDQLIELNLD TLEPYINGPF TPDLGHPLSK FAESVKTNNW
PAELKVGLIG SCTNSSYEDM SRSASVAQQA LDKGITAKAK FTITPGSEQI RATIERDGQM
KVLEKVGGVV LANACGPCIG QWKREDVPKG EKNSIITSYN RNFTGRNDSN VNTHAFVASP
EIVTALTIAG DITFNPMTDF LTDKDGNKFK LTPPTGDELP SRGFDAGENT YQPPSPNGQN
INVIVDSESS RLQLLQPFAP WDKKDLVDMQ VLIKVQGKCT TDHISMAGPW LKYRGHLDNI
SNNMLIGAIN SENGKANAVL NQFTGEIGPV PTVARDYKKR GVNWIVVGDE NYGEGSSREH
AALEPRHLGG KAILVKSFAR IHETNLKKQG ILPLTFANPS DYDKISGDDR ISIIGLKDLA
PGKQLTLIVK SAKQGSEFEI KANHTMNAGQ IEWFKAGSAL NYIKSEKAKK N
