ACOHC_CHICK
ID ACOHC_CHICK Reviewed; 889 AA.
AC Q90875;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
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; Synonyms=IREB1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8156162; DOI=10.1007/bf00710129;
RA Saitoh Y., Ogawa A., Hori T., Kunita R., Mizuno S.;
RT "Identification and localization of two genes on the chicken Z chromosome:
RT implication of evolutionary conservation of the Z chromosome among avian
RT species.";
RL Chromosome Res. 1:239-251(1993).
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:0000250|UniProtKB:P21399}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P21399}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; D16150; BAA03715.1; -; mRNA.
DR RefSeq; NP_001025707.1; NM_001030536.1.
DR AlphaFoldDB; Q90875; -.
DR SMR; Q90875; -.
DR STRING; 9031.ENSGALP00000003381; -.
DR PaxDb; Q90875; -.
DR PRIDE; Q90875; -.
DR GeneID; 373916; -.
DR KEGG; gga:373916; -.
DR CTD; 48; -.
DR VEuPathDB; HostDB:geneid_373916; -.
DR eggNOG; KOG0452; Eukaryota.
DR InParanoid; Q90875; -.
DR OrthoDB; 190960at2759; -.
DR PhylomeDB; Q90875; -.
DR PRO; PR:Q90875; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; 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:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR GO; GO:0010040; P:response to iron(II) ion; IEA:InterPro.
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_0000076679"
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; 98074 MW; 527314F6AE08C842 CRC64;
MSNPFVQIVE PLDAKEPVKK FFNLSKLEDV RYARLPFSIR VLLEAAIRNC DEFLVKKQDV
ENILNWKVMQ HKNVEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGD PEKINPICPA
DLVIDHSIQV DFNRRSDSLQ KNQDLEFERN KERFEFLKWG SQAFKNMRII PPGSGIIHQV
NLEYLARVVM DQDGYYYPDS VVGTDSHTTM VDGLGVLGWG VGGIEAEAVM LGQPISMVLP
EVVGYKLLGN PQPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC
PEYGATAAYF PVDDISIGYL VQTGRDKEKV LCTKKYLEAV GMLRDFKNSS QDPDFTQVVE
LDLHTVVPCC SGPKRPQDKV AVSDMKKDFE TCLGAKQGFK GFQIAPDRHN SVIKFNFEGC
DFELAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVEAG LTVKPYIKTS LSPGSGVVTY
YLRESGVMSY LSQLGFDVVG YGCMTCIGNS GPLPDSVVEA ITQGDLVAVG VLSGNRNFEG
RVHPNTRANY LASPPLVIAY AIAGTVRIDF EKEPLGISAS GKKIFLKDIW PTRNEIQAVE
RQYVIPGMFK EVYQKIETVN EAWNALDAPS DKLYTWNPKS TYIKSPPFFD GLTLALQTPK
TIEDAYVLLN FGDSVTTDHI SPAGNIARNS PAARYLTSRG LTPREFNSYG SRRGNDAVMA
RGTFANIRLV NKFIDKQGPQ TIHFPSGETL DVFDAAERYK QAGHPLIVLA GKEYGAGSSR
DWAAKGPFLL GVKAVLAESY ERIHRSNLVG MGVIPLQYLP GEDARTLGLT GRERYTIIIP
ENLKPQMNIQ IKLDTGKTFH AIMRFDTDVE LTYFHNGGIL NYMIRKMAS
