ACOHC_HUMAN
ID ACOHC_HUMAN Reviewed; 889 AA.
AC P21399; D3DRK7; Q14652; Q5VZA7;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Cytoplasmic aconitate hydratase {ECO:0000305|PubMed:1946430};
DE Short=Aconitase;
DE EC=4.2.1.3 {ECO:0000269|PubMed:1281544, ECO:0000269|PubMed:1946430, ECO:0000269|PubMed:8041788};
DE AltName: Full=Citrate hydro-lyase;
DE AltName: Full=Ferritin repressor protein;
DE AltName: Full=Iron regulatory protein 1;
DE Short=IRP1;
DE AltName: Full=Iron-responsive element-binding protein 1;
DE Short=IRE-BP 1;
GN Name=ACO1; Synonyms=IREB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1738601; DOI=10.1093/nar/20.1.33;
RA Hirling H., Emery-Goodman A., Thompson N., Neupert B., Seiser C., Kuehn L.;
RT "Expression of active iron regulatory factor from a full-length human cDNA
RT by in vitro transcription/translation.";
RL Nucleic Acids Res. 20:33-39(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-889, RNA-BINDING, AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=2172968; DOI=10.1073/pnas.87.20.7958;
RA Rouault T.A., Tang C.K., Kaptain S., Burgess W.H., Haile D.J.,
RA Samaniego F., McBride O.W., Harford J.B., Klausner R.D.;
RT "Cloning of the cDNA encoding an RNA regulatory protein -- the human iron-
RT responsive element-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990).
RN [7]
RP SIMILARITY TO ACONITASES AND IPM ISOMERASES.
RX PubMed=1903202; DOI=10.1093/nar/19.8.1739;
RA Hentze M.W., Argos P.;
RT "Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and
RT isopropylmalate isomerase.";
RL Nucleic Acids Res. 19:1739-1740(1991).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1946430; DOI=10.1073/pnas.88.22.10109;
RA Kaptain S., Downey W.E., Tang C.K., Philpott C., Haile D.J., Orloff D.G.,
RA Harford J.B., Rouault T.A., Klausner R.D.;
RT "A regulated RNA binding protein also possesses aconitase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10109-10113(1991).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=1281544; DOI=10.1073/pnas.89.24.11735;
RA Haile D.J., Rouault T.A., Harford J.B., Kennedy M.C., Blondin G.A.,
RA Beinert H., Klausner R.D.;
RT "Cellular regulation of the iron-responsive element binding protein:
RT disassembly of the cubane iron-sulfur cluster results in high-affinity RNA
RT binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11735-11739(1992).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-300; CYS-437; CYS-503;
RP CYS-506; ARG-536; ARG-541; ARG-699; SER-778 AND ARG-780.
RX PubMed=8041788; DOI=10.1073/pnas.91.15.7321;
RA Philpott C.C., Klausner R.D., Rouault T.A.;
RT "The bifunctional iron-responsive element binding protein/cytosolic
RT aconitase: the role of active-site residues in ligand binding and
RT regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7321-7325(1994).
RN [11]
RP UBIQUITINATION, AND INTERACTION WITH FBXL5.
RX PubMed=19762596; DOI=10.1126/science.1176333;
RA Vashisht A.A., Zumbrennen K.B., Huang X., Powers D.N., Durazo A., Sun D.,
RA Bhaskaran N., Persson A., Uhlen M., Sangfelt O., Spruck C., Leibold E.A.,
RA Wohlschlegel J.A.;
RT "Control of iron homeostasis by an iron-regulated ubiquitin ligase.";
RL Science 326:718-721(2009).
RN [12]
RP UBIQUITINATION, AND INTERACTION WITH FBXL5.
RX PubMed=19762597; DOI=10.1126/science.1176326;
RA Salahudeen A.A., Thompson J.W., Ruiz J.C., Ma H.-W., Kinch L.N., Li Q.,
RA Grishin N.V., Bruick R.K.;
RT "An E3 ligase possessing an iron responsive hemerythrin domain is a
RT regulator of iron homeostasis.";
RL Science 326:722-726(2009).
RN [13]
RP INTERACTION WITH FRATAXIN(81-210).
RX PubMed=20053667; DOI=10.1093/hmg/ddp592;
RA Condo I., Malisan F., Guccini I., Serio D., Rufini A., Testi R.;
RT "Molecular control of the cytosolic aconitase/IRP1 switch by
RT extramitochondrial frataxin.";
RL Hum. Mol. Genet. 19:1221-1229(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=23891004; DOI=10.1016/j.cmet.2013.06.015;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and
RT maturation of different subsets of cytosolic-nuclear iron-sulfur
RT proteins.";
RL Cell Metab. 18:187-198(2013).
RN [16]
RP ERRATUM OF PUBMED:23891004.
RX PubMed=29320706; DOI=10.1016/j.cmet.2017.12.009;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B Integrate Iron Homeostasis and
RT Maturation of Different Subsets of Cytosolic-Nuclear Iron-Sulfur
RT Proteins.";
RL Cell Metab. 27:263-263(2018).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER,
RP AND COFACTOR.
RX PubMed=16407072; DOI=10.1016/j.str.2005.09.009;
RA Dupuy J., Volbeda A., Carpentier P., Darnault C., Moulis J.-M.,
RA Fontecilla-Camps J.C.;
RT "Crystal structure of human iron regulatory protein 1 as cytosolic
RT aconitase.";
RL Structure 14:129-139(2006).
RN [19]
RP VARIANT MET-318.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Bifunctional iron sensor that switches between 2 activities
CC depending on iron availability (PubMed:1946430, PubMed:1281544,
CC PubMed:8041788). Iron deprivation, promotes its mRNA binding activity
CC through which it regulates the expression of genes involved in iron
CC uptake, sequestration and utilization (PubMed:1946430, PubMed:1281544,
CC PubMed:8041788, PubMed:23891004). Binds to iron-responsive elements
CC (IRES) in the untranslated region of target mRNAs preventing for
CC instance the translation of ferritin and aminolevulinic acid synthase
CC and stabilizing the transferrin receptor mRNA (PubMed:1946430,
CC PubMed:1281544, PubMed:8041788, PubMed:23891004).
CC {ECO:0000269|PubMed:1281544, ECO:0000269|PubMed:1946430,
CC ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:8041788}.
CC -!- FUNCTION: Conversely, when cellular iron levels are high, binds a 4Fe-
CC 4S cluster which precludes RNA binding activity and promotes the
CC aconitase activity, the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000269|PubMed:1281544, ECO:0000269|PubMed:1946430,
CC ECO:0000269|PubMed:8041788}.
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:1281544, ECO:0000269|PubMed:1946430,
CC ECO:0000269|PubMed:8041788};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:16407072};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:16407072};
CC -!- SUBUNIT: Interacts (when associated with the 4Fe-4S) with FBXL5.
CC Interacts with frataxin(81-210). {ECO:0000269|PubMed:16407072,
CC ECO:0000269|PubMed:19762596, ECO:0000269|PubMed:19762597,
CC ECO:0000269|PubMed:20053667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1281544}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Aconitase entry;
CC URL="https://en.wikipedia.org/wiki/Aconitase";
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DR EMBL; Z11559; CAA77651.1; -; mRNA.
DR EMBL; DQ496106; ABF47095.1; -; Genomic_DNA.
DR EMBL; AL161783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58549.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58550.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58552.1; -; Genomic_DNA.
DR EMBL; BC018103; AAH18103.1; -; mRNA.
DR EMBL; M58510; AAA69900.1; -; mRNA.
DR CCDS; CCDS6525.1; -.
DR PIR; S26403; S26403.
DR RefSeq; NP_001265281.1; NM_001278352.1.
DR RefSeq; NP_002188.1; NM_002197.2.
DR RefSeq; XP_005251533.1; XM_005251476.1.
DR RefSeq; XP_011516190.1; XM_011517888.1.
DR PDB; 2B3X; X-ray; 2.54 A; A=2-889.
DR PDB; 2B3Y; X-ray; 1.85 A; A/B=2-889.
DR PDBsum; 2B3X; -.
DR PDBsum; 2B3Y; -.
DR AlphaFoldDB; P21399; -.
DR SMR; P21399; -.
DR BioGRID; 106564; 34.
DR IntAct; P21399; 17.
DR MINT; P21399; -.
DR STRING; 9606.ENSP00000309477; -.
DR DrugBank; DB06757; Manganese.
DR MoonDB; P21399; Curated.
DR MoonProt; P21399; -.
DR GlyGen; P21399; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P21399; -.
DR MetOSite; P21399; -.
DR PhosphoSitePlus; P21399; -.
DR SwissPalm; P21399; -.
DR BioMuta; ACO1; -.
DR DMDM; 3123225; -.
DR REPRODUCTION-2DPAGE; IPI00008485; -.
DR UCD-2DPAGE; P21399; -.
DR EPD; P21399; -.
DR jPOST; P21399; -.
DR MassIVE; P21399; -.
DR PaxDb; P21399; -.
DR PeptideAtlas; P21399; -.
DR PRIDE; P21399; -.
DR ProteomicsDB; 53867; -.
DR Antibodypedia; 10637; 600 antibodies from 39 providers.
DR DNASU; 48; -.
DR Ensembl; ENST00000309951.8; ENSP00000309477.5; ENSG00000122729.19.
DR Ensembl; ENST00000379923.5; ENSP00000369255.1; ENSG00000122729.19.
DR Ensembl; ENST00000541043.5; ENSP00000438733.2; ENSG00000122729.19.
DR GeneID; 48; -.
DR KEGG; hsa:48; -.
DR MANE-Select; ENST00000309951.8; ENSP00000309477.5; NM_002197.3; NP_002188.1.
DR CTD; 48; -.
DR DisGeNET; 48; -.
DR GeneCards; ACO1; -.
DR HGNC; HGNC:117; ACO1.
DR HPA; ENSG00000122729; Tissue enhanced (liver).
DR MIM; 100880; gene.
DR neXtProt; NX_P21399; -.
DR OpenTargets; ENSG00000122729; -.
DR PharmGKB; PA24442; -.
DR VEuPathDB; HostDB:ENSG00000122729; -.
DR eggNOG; KOG0452; Eukaryota.
DR GeneTree; ENSGT00940000157772; -.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; P21399; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 190960at2759; -.
DR PhylomeDB; P21399; -.
DR TreeFam; TF313476; -.
DR BioCyc; MetaCyc:HS04597-MON; -.
DR BRENDA; 4.2.1.3; 2681.
DR PathwayCommons; P21399; -.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR SignaLink; P21399; -.
DR SIGNOR; P21399; -.
DR BioGRID-ORCS; 48; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; ACO1; human.
DR EvolutionaryTrace; P21399; -.
DR GenomeRNAi; 48; -.
DR Pharos; P21399; Tbio.
DR PRO; PR:P21399; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P21399; protein.
DR Bgee; ENSG00000122729; Expressed in right lobe of liver and 190 other tissues.
DR ExpressionAtlas; P21399; baseline and differential.
DR Genevisible; P21399; HS.
DR GO; GO:0005737; C:cytoplasm; IMP:CAFA.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IMP:CAFA.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0003994; F:aconitate hydratase activity; IDA:UniProtKB.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0030350; F:iron-responsive element binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0006101; P:citrate metabolic process; IDA:UniProtKB.
DR GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
DR GO; GO:0010040; P:response to iron(II) ion; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 InterPro; IPR029784; IRE-BP1.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR PANTHER; PTHR11670:SF32; PTHR11670:SF32; 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 3D-structure; 4Fe-4S; Cytoplasm; Direct protein sequencing; Iron;
KW Iron-sulfur; Lyase; Metal-binding; Phosphoprotein; Reference proteome;
KW RNA-binding; Tricarboxylic acid cycle.
FT CHAIN 1..889
FT /note="Cytoplasmic aconitate hydratase"
FT /id="PRO_0000076680"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 699
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 779..780
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 628
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 318
FT /note="T -> M (in dbSNP:rs150373174)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069413"
FT VARIANT 395
FT /note="A -> D (in dbSNP:rs3814519)"
FT /id="VAR_048180"
FT VARIANT 486
FT /note="G -> R (in dbSNP:rs34630459)"
FT /id="VAR_048181"
FT MUTAGEN 300
FT /note="C->S: No effect on aconitase activity or on RNA
FT binding."
FT /evidence="ECO:0000269|PubMed:8041788"
FT MUTAGEN 437
FT /note="C->S: Loss of aconitase activity. Leads to
FT constitutive RNA binding, irrespective of iron levels."
FT /evidence="ECO:0000269|PubMed:8041788"
FT MUTAGEN 503
FT /note="C->S: Loss of aconitase activity. Leads to
FT constitutive RNA binding, irrespective of iron levels."
FT /evidence="ECO:0000269|PubMed:8041788"
FT MUTAGEN 506
FT /note="C->S: Loss of aconitase activity. Leads to
FT constitutive RNA binding, irrespective of iron levels."
FT /evidence="ECO:0000269|PubMed:8041788"
FT MUTAGEN 536
FT /note="R->Q: Strongly reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:8041788"
FT MUTAGEN 541
FT /note="R->Q: Strongly reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:8041788"
FT MUTAGEN 699
FT /note="R->K: No effect on RNA binding."
FT /evidence="ECO:0000269|PubMed:8041788"
FT MUTAGEN 778
FT /note="S->A: No effect on iron-regulated RNA binding. Loss
FT of aconitase activity."
FT /evidence="ECO:0000269|PubMed:8041788"
FT MUTAGEN 780
FT /note="R->Q: Nearly abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:8041788"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:2B3Y"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 87..106
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 138..163
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 290..298
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 428..434
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 443..458
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 476..484
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 488..493
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:2B3X"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 515..524
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 529..535
FT /evidence="ECO:0007829|PDB:2B3Y"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:2B3X"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 554..563
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:2B3X"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:2B3Y"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 606..613
FT /evidence="ECO:0007829|PDB:2B3Y"
FT TURN 614..618
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 621..625
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 662..671
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 691..698
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 716..721
FT /evidence="ECO:0007829|PDB:2B3Y"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:2B3Y"
FT TURN 732..734
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 739..742
FT /evidence="ECO:0007829|PDB:2B3Y"
FT TURN 744..746
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 752..761
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 766..769
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 782..789
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 792..798
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 802..810
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 814..818
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 824..827
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 835..837
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 848..853
FT /evidence="ECO:0007829|PDB:2B3Y"
FT STRAND 858..863
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 868..876
FT /evidence="ECO:0007829|PDB:2B3Y"
FT HELIX 879..888
FT /evidence="ECO:0007829|PDB:2B3Y"
SQ SEQUENCE 889 AA; 98399 MW; E1A05AF701D46DCB CRC64;
MSNPFAHLAE PLDPVQPGKK FFNLNKLEDS RYGRLPFSIR VLLEAAIRNC DEFLVKKQDI
ENILHWNVTQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGD PEKINPVCPA
DLVIDHSIQV DFNRRADSLQ KNQDLEFERN RERFEFLKWG SQAFHNMRII PPGSGIIHQV
NLEYLARVVF DQDGYYYPDS LVGTDSHTTM IDGLGILGWG VGGIEAEAVM LGQPISMVLP
QVIGYRLMGK PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC
PEYGATAAFF PVDEVSITYL VQTGRDEEKL KYIKKYLQAV GMFRDFNDPS QDPDFTQVVE
LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQVAPEHHN DHKTFIYDNT
EFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LNVMPYIKTS LSPGSGVVTY
YLQESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG
RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PTRDEIQAVE
RQYVIPGMFK EVYQKIETVN ESWNALATPS DKLFFWNSKS TYIKSPPFFE NLTLDLQPPK
SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAVMA
RGTFANIRLL NRFLNKQAPQ TIHLPSGEIL DVFDAAERYQ QAGLPLIVLA GKEYGAGSSR
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GENADALGLT GQERYTIIIP
ENLKPQMKVQ VKLDTGKTFQ AVMRFDTDVE LTYFLNGGIL NYMIRKMAK
