ACOHC_CAEEL
ID ACOHC_CAEEL Reviewed; 887 AA.
AC Q23500;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cytoplasmic aconitate hydratase {ECO:0000305|PubMed:12438312};
DE Short=Aconitase;
DE EC=4.2.1.3 {ECO:0000269|PubMed:12438312};
DE AltName: Full=Citrate hydro-lyase;
DE AltName: Full=Gex-3-interacting protein 22;
GN Name=aco-1; Synonyms=gei-22; ORFNames=ZK455.1;
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=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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12438312; DOI=10.1074/jbc.m210333200;
RA Gourley B.L., Parker S.B., Jones B.J., Zumbrennen K.B., Leibold E.A.;
RT "Cytosolic aconitase and ferritin are regulated by iron in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 278:3227-3234(2003).
RN [3]
RP INTERACTION WITH GEX-3.
RX PubMed=11922622; DOI=10.1006/bbrc.2002.6717;
RA Tsuboi D., Qadota H., Kasuya K., Amano M., Kaibuchi K.;
RT "Isolation of the interacting molecules with GEX-3 by a novel functional
RT screening.";
RL Biochem. Biophys. Res. Commun. 292:697-701(2002).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate (PubMed:12438312). Has probably no RNA-binding activity
CC (PubMed:12438312). {ECO:0000269|PubMed:12438312}.
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 Evidence={ECO:0000269|PubMed:12438312};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P21399};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P21399};
CC -!- SUBUNIT: Interacts with gex-3. {ECO:0000269|PubMed:11922622}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12438312}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; Z66567; CAA91491.1; -; Genomic_DNA.
DR PIR; T27868; T27868.
DR RefSeq; NP_509898.1; NM_077497.3.
DR AlphaFoldDB; Q23500; -.
DR SMR; Q23500; -.
DR BioGRID; 46233; 26.
DR DIP; DIP-26479N; -.
DR IntAct; Q23500; 1.
DR STRING; 6239.ZK455.1; -.
DR EPD; Q23500; -.
DR PaxDb; Q23500; -.
DR PeptideAtlas; Q23500; -.
DR PRIDE; Q23500; -.
DR EnsemblMetazoa; ZK455.1.1; ZK455.1.1; WBGene00000040.
DR GeneID; 181324; -.
DR KEGG; cel:CELE_ZK455.1; -.
DR UCSC; ZK455.1.1; c. elegans.
DR CTD; 181324; -.
DR WormBase; ZK455.1; CE03812; WBGene00000040; aco-1.
DR eggNOG; KOG0452; Eukaryota.
DR GeneTree; ENSGT00940000167487; -.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; Q23500; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 190960at2759; -.
DR PhylomeDB; Q23500; -.
DR BRENDA; 4.2.1.3; 1045.
DR Reactome; R-CEL-917937; Iron uptake and transport.
DR PRO; PR:Q23500; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000040; Expressed in larva and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
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; IDA:WormBase.
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:0006879; P:cellular iron ion homeostasis; ISS:WormBase.
DR GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR GO; GO:0072350; P:tricarboxylic acid metabolic process; IDA:WormBase.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01341; aconitase_1; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..887
FT /note="Cytoplasmic aconitate hydratase"
FT /id="PRO_0000076650"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204..206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 697
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 777..778
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 887 AA; 96660 MW; AB53EF890EBC88C4 CRC64;
MAFNNLIRNL AIGDNVYKYF DLNGLNDARY NELPISIKYL LEAAVRHCDE FHVLKKDVET
ILDWKNSQRN QAEIPFKPAR VILQDFTGVP AVVDLAAMRD AVQNMGADPA KINPVCPVDL
VIDHSVQVDH YGNLEALAKN QSIEFERNRE RFNFLKWGSK AFDNLLIVPP GSGIVHQVNL
EYLARTVFVG KDGVLYPDSV VGTDSHTTMI DGSGVLGWGV GGIEAEAVML GQPISMVIPE
VIGYELVGTL SDTVTSTDLV LTITKNLRDL GVVGKFVEFF GTGVASLSIA DRATIANMCP
EYGATIGFFP VDSRTIDYLT QTGRDTDYTQ RVEQYLKSVG MFVNFTDDSY RPTYTTTLKL
DLGSVVPSVS GPKRPHDRVE LASLAQDFSK GLTDKISFKA FGLKPEDATK SVTITNHGRT
AELTHGSVVI AAITSCTNTS NPSVMLAAGL VAKKAVELGL NVQPYVKTSL SPGSGVVTKY
LEASGLLPYL EKIGFNIAGY GCMTCIGNSG PLDEPVTKAI EENNLVVAGV LSGNRNFEGR
IHPHVRANYL ASPPLAVLYS IIGNVNVDIN GVLAVTPDGK EIRLADIWPT RKEVAKFEEE
FVKPQFFREV YANIELGSTE WQQLECPAVK LYPWDDASTY IKKVPFFDGM TSELPSQSDI
VNAHVLLNLG DSVTTDHISP AGSISKTSPA ARFLAGRGVT PRDFNTYGAR RGNDEIMARG
TFANIRLVNK LASKVGPITL HVPSGEELDI FDAAQKYKDA GIPAIILAGK EYGCGSSRDW
AAKGPFLQGV KAVIAESFER IHRSNLIGMG IIPFQYQAGQ NADSLGLTGK EQFSIGVPDD
LKPGQLIDVN VSNGSVFQVI CRFDTEVELT YYRNGGILQY MIRKLIQ
