ACOHC_BOVIN
ID ACOHC_BOVIN Reviewed; 889 AA.
AC Q0VCU1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytoplasmic aconitate hydratase {ECO:0000305};
DE Short=Aconitase;
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:P21399};
DE AltName: Full=Citrate hydro-lyase;
DE AltName: Full=Iron-responsive element-binding protein 1;
DE Short=IRE-BP 1;
GN Name=ACO1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, 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).
CC -!- FUNCTION: Bifunctional iron sensor that switches between 2 activities
CC depending on iron availability. Iron deprivation, promotes its mRNA
CC binding activity through which it regulates the expression of genes
CC involved in iron uptake, sequestration and utilization. Binds to iron-
CC responsive elements (IRES) in the untranslated region of target mRNAs
CC preventing for instance the translation of ferritin and aminolevulinic
CC acid synthase and stabilizing the transferrin receptor mRNA.
CC {ECO:0000269|PubMed:1281544}.
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:0000250|UniProtKB:P21399}.
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:0000250|UniProtKB:P21399};
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 (when associated with the 4Fe-4S) with FBXL5.
CC Interacts with frataxin(81-210). {ECO:0000250|UniProtKB:P21399}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1281544}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; BC120006; AAI20007.1; -; mRNA.
DR RefSeq; NP_001069059.1; NM_001075591.1.
DR AlphaFoldDB; Q0VCU1; -.
DR SMR; Q0VCU1; -.
DR STRING; 9913.ENSBTAP00000000731; -.
DR MoonProt; Q0VCU1; -.
DR PaxDb; Q0VCU1; -.
DR PeptideAtlas; Q0VCU1; -.
DR PRIDE; Q0VCU1; -.
DR GeneID; 512995; -.
DR KEGG; bta:512995; -.
DR CTD; 48; -.
DR eggNOG; KOG0452; Eukaryota.
DR InParanoid; Q0VCU1; -.
DR OrthoDB; 190960at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:CAFA.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:CAFA.
DR GO; GO:0003994; F:aconitate hydratase activity; IDA:CAFA.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008198; F:ferrous iron binding; IDA:CAFA.
DR GO; GO:0030350; F:iron-responsive element binding; IDA:CAFA.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0006101; P:citrate metabolic process; IDA:CAFA.
DR GO; GO:0010040; P:response to iron(II) ion; ISS: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 2: Evidence at transcript level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome; RNA-binding; Tricarboxylic acid cycle.
FT CHAIN 1..889
FT /note="Cytoplasmic aconitate hydratase"
FT /id="PRO_0000285207"
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"
SQ SEQUENCE 889 AA; 98204 MW; 2BDD83B6294E6342 CRC64;
MSNPFAHLVE PLDPAQPGKK FFNLNKLEDS RYGSLPFSIR VLLEAAIRNC DQFLVKKNDV
ENILNWKVMQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGN PEKINPICPA
DLVIDHSIQV DFNRRADSLK KNQDLEFERN KERFEFLKWG SQAFHNMRII PPGSGIIHQV
NLEYLARVVF DQDGYYYPDS LVGTDSHTTM IDGLGVLGWG VGGIEAEAVM LGQPISMVLP
QVIGYRLVGN PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC
PEYGATAAFF PVDEVSIKYL VQTGRDKEKV KHIKQYLQAV GMFRDFSDSS QDPDFAQVVE
LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQVAPDHHN DHKTFIYNNS
KFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LSVKPYIKTS LSPGSGVVTY
YLRESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEAVVEA IVQGDLVAVG VLSGNRNFEG
RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PTRDEIQAVE
RQYVIPGMFK EVYQKIETVN ESWNALAAPS DKLYCWNPKS TYIKSPPFFE DLTLDLQPPK
SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAIMA
RGTFANIRLL NKFLNKQAPQ TIHLPSGEIL DVFDAAERYQ QAGLPLIVLA GKEYGSGSSR
DWAAKGPFLL GIRAVLAESY ERIHRSNLVG MGVIPLEYLP GENADTLGLT GRERYTISIP
ETLKPRMKVQ IKLDTGKTFQ AVMRFDTDVE LTYFHNGGIL NYMIRKMTK
