ACON_CAEEL
ID ACON_CAEEL Reviewed; 777 AA.
AC P34455; Q8IG17; Q8WQF0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
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=aco-2 {ECO:0000312|WormBase:F54H12.1a};
GN ORFNames=F54H12.1 {ECO:0000312|WormBase:F54H12.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F54H12.1a};
CC IsoId=P34455-1; Sequence=Displayed;
CC Name=c {ECO:0000312|WormBase:F54H12.1c};
CC IsoId=P34455-3; Sequence=VSP_016115;
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CCD63454.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD63456.1; -; Genomic_DNA.
DR PIR; S44831; S44831.
DR RefSeq; NP_498738.2; NM_066337.5. [P34455-3]
DR RefSeq; NP_741235.1; NM_171200.4. [P34455-1]
DR AlphaFoldDB; P34455; -.
DR SMR; P34455; -.
DR BioGRID; 41327; 55.
DR STRING; 6239.F54H12.1a; -.
DR World-2DPAGE; 0020:P34455; -.
DR EPD; P34455; -.
DR PaxDb; P34455; -.
DR PeptideAtlas; P34455; -.
DR EnsemblMetazoa; F54H12.1a.1; F54H12.1a.1; WBGene00000041. [P34455-1]
DR EnsemblMetazoa; F54H12.1c.1; F54H12.1c.1; WBGene00000041. [P34455-3]
DR EnsemblMetazoa; F54H12.1c.2; F54H12.1c.2; WBGene00000041. [P34455-3]
DR EnsemblMetazoa; F54H12.1c.3; F54H12.1c.3; WBGene00000041. [P34455-3]
DR GeneID; 176121; -.
DR KEGG; cel:CELE_F54H12.1; -.
DR UCSC; F54H12.1c.2; c. elegans. [P34455-1]
DR CTD; 176121; -.
DR WormBase; F54H12.1a; CE25005; WBGene00000041; aco-2. [P34455-1]
DR WormBase; F54H12.1c; CE32436; WBGene00000041; aco-2. [P34455-3]
DR eggNOG; KOG0453; Eukaryota.
DR GeneTree; ENSGT00940000154892; -.
DR InParanoid; P34455; -.
DR OMA; GCIGMGQ; -.
DR OrthoDB; 190960at2759; -.
DR PhylomeDB; P34455; -.
DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00718.
DR PRO; PR:P34455; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000041; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
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; Alternative splicing; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..777
FT /note="Probable aconitate hydratase, mitochondrial"
FT /id="PRO_0000000545"
FT REGION 534..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189..191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 601
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 664..665
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_016115"
SQ SEQUENCE 777 AA; 84047 MW; D482AAD48BAB0844 CRC64;
MNSLLRLSHL AGPAHYRALH SSSSIWSKVA ISKFEPKSYL PYEKLSQTVK IVKDRLKRPL
TLSEKILYGH LDQPKTQDIE RGVSYLRLRP DRVAMQDATA QMAMLQFISS GLPKTAVPST
IHCDHLIEAQ KGGAQDLARA KDLNKEVFNF LATAGSKYGV GFWKPGSGII HQIILENYAF
PGLLLIGTDS HTPNGGGLGG LCIGVGGADA VDVMADIPWE LKCPKVIGIK LTGKLNGWTS
AKDVILKVAD ILTVKGGTGA IVEYFGPGVD SISATGMGTI CNMGAEIGAT TSVFPYNESM
YKYLEATGRK EIAEEARKYK DLLTADDGAN YDQIIEINLD TLTPHVNGPF TPDLASSIDK
LGENAKKNGW PLDVKVSLIG SCTNSSYEDM TRAASIAKQA LDKGLKAKTI FTITPGSEQV
RATIERDGLS KIFADFGGMV LANACGPCIG QWDRQDVKKG EKNTIVTSYN RNFTGRNDAN
PATHGFVTSP DITTAMAISG RLDFNPLTDE LTAADGSKFK LQAPTGLDLP PKGYDPGEDT
FQAPSGSGQV DVSPSSDRLQ LLSPFDKWDG KDLEDMKILI KVTGKCTTDH ISAAGPWLKY
RGHLDNISNN LFLTAINADN GEMNKVKNQV TGEYGAVPAT ARKYKADGVR WVAIGDENYG
EGSSREHAAL EPRHLGGRAI IVKSFARIHE TNLKKQGMLP LTFANPADYD KIDPSDNVSI
VGLSSFAPGK PLTAIFKKTN GSKVEVTLNH TFNEQQIEWF KAGSALNRMK EVFAKSK
