ID ACOC_CUCMC Reviewed; 764 AA. AC Q42669; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-JUN-2009, entry version 54. DE RecName: Full=Aconitate hydratase; DE Short=Aconitase; DE EC=4.2.1.3; DE AltName: Full=Citrate hydro-lyase; DE Flags: Fragment; GN Name=ACO; OS Cucumis melo var. conomon (Oriental pickling melon). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucumis. OX NCBI_TaxID=3657; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Cantaloupe; TISSUE=Fruit; RX MEDLINE=95229629; PubMed=7713917; DOI=10.1074/jbc.270.14.8131; RA Peyret P., Perez P., Alric M.; RT "Structure, genomic organization, and expression of the Arabidopsis RT thaliana aconitase gene. Plant aconitase show significant homology RT with mammalian iron-responsive element-binding protein."; RL J. Biol. Chem. 270:8131-8137(1995). CC -!- CATALYTIC ACTIVITY: Citrate = isocitrate. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate and dicarboxylate CC metabolism. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X82840; CAA58047.1; -; mRNA. DR PIR; S49849; S49849. DR HSSP; P20004; 1AMJ. DR BRENDA; 4.2.1.3; 289996. 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:0006097; P:glyoxylate 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; Glyoxylate bypass; Iron; Iron-sulfur; Lyase; KW Metal-binding. FT CHAIN <1 764 Aconitate hydratase. FT /FTId=PRO_0000076653. FT METAL 307 307 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 372 372 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 375 375 Iron-sulfur (4Fe-4S) (By similarity). FT NON_TER 1 1 SQ SEQUENCE 764 AA; 83274 MW; E4A9B011FC6922F0 CRC64; HEAKTENAVQ ANMELEFKRN RERFGFLKWG SSAFHNMLVV PPGSGIVHQV NLEYLGRVVF NTNGLLYPDS VVGTDSHTTM IDGLGVAGWG VGGIEAEAAM LGQPMSMVLP GVVGFKLVGK LRNGVTATDL VLTVTQMLRK HGVVGKFVEF YGEGMGELSL ADRATIANMS PEYGATMGFF PVDHVTLQYL KLTGRKDETI SMIESYLLAN KMFVDYSEPQ VERVYSSHIE LNLSDVEPCI SGPKRPHDRV PLKEMKADWH ACLDNRVGFK GFAIPKEAQV KVAEFNFHGS PAQLRHGDVV IAAITSCTNT SSSVMLGAAL VAKKACELGL EVKPWIKTVL LQALGVVTKY LAKSGLQKYL NQLGFNIVGY GCTTCIGNSG DIDESVASAI TGNDIVAAAV LSGNRNFEGR VHPLTRANYL ASPPLVVAYA LAGTVDIDFE SEPIGVGKDG KKVFFRDIWP TSEEVAVVVN SNVLPDMFRA TYQAITEGNA TWNLLSVPEG TLYSWDPTST YIHEPPYFKD MSMSPPGPHG VKNAYCLLNF GDSITTDHIS PAGSIHKDSP AAKYLLERGV DRRDFNSYGV AVVMMRLWHV HFANIRIVNK LLKGEVGPKT IHIPSREKLS VFDAAMRYKS EGQDTIILAG AEYGIGSSRD WAAKGPMLLG VKAVIAKSFE RIHRSNLVGM GIIPLCFKAG EDADSLGLTG HERFTIDLPS NVGEIRPGQD VAVVTDTGKS FSCILRFDTE VELAYFDHGG ILQYVIRNLI HSKH //