ID   ACOC_BOVIN              Reviewed;         889 AA.
AC   Q0VCU1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Cytoplasmic aconitate hydratase;
DE            Short=Aconitase;
DE            EC=4.2.1.3;
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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.
CC   -!- FUNCTION: Binds to iron-responsive elements (IRES), which are
CC       stem-loop structures found in the 5'-UTR of ferritin, and delta
CC       aminolevulinic acid synthase mRNAs, and in the 3'-UTR of
CC       transferrin receptor mRNA. Binding to the IRE element in ferritin
CC       results in the repression of its mRNA translation. Binding of the
CC       protein to the transferrin receptor mRNA inhibits the degradation
CC       of this otherwise rapidly degraded mRNA (By similarity). This
CC       protein also expresses aconitase activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
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DR   EMBL; BC120006; AAI20007.1; -; mRNA.
DR   IPI; IPI00685374; -.
DR   RefSeq; NP_001069059.1; -.
DR   UniGene; Bt.53789; -.
DR   SMR; Q0VCU1; 2-889.
DR   Ensembl; ENSBTAG00000000555; Bos taurus.
DR   GeneID; 512995; -.
DR   KEGG; bta:512995; -.
DR   HOVERGEN; Q0VCU1; -.
DR   BRENDA; 4.2.1.3; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015937; Aconitase-like_core.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR006249; Aconitase/Fe_reg_prot_2.
DR   InterPro; IPR015934; Aconitase/Fe_reg_prot_2/AcnD.
DR   InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   Gene3D; G3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 2.
DR   Gene3D; G3DSA:3.20.19.10; Aconitase/3IPM_dehydase_swvl; 1.
DR   Gene3D; G3DSA:3.40.1060.10; Aconitase/IPMdHydase_lsu_aba_2; 1.
DR   PANTHER; PTHR11670; Aconitase-like_core; 1.
DR   PANTHER; PTHR11670:SF1; Aconitase/Fe_reg_prot_2/AcnD; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   ProDom; PD000511; Aconitase_N; 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   RNA-binding; Tricarboxylic acid cycle.
FT   CHAIN         1    889       Cytoplasmic aconitate hydratase.
FT                                /FTId=PRO_0000285207.
FT   METAL       437    437       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       503    503       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       506    506       Iron-sulfur (4Fe-4S) (By similarity).
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
//