ID ACON_CORGL Reviewed; 939 AA. AC Q8NQ98; Q6M550; Q9WXJ0; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 2. DT 16-JUN-2009, entry version 50. DE RecName: Full=Aconitate hydratase; DE EC=4.2.1.3; GN Name=acn; OrderedLocusNames=Cgl1540, cg1737; OS Corynebacterium glutamicum (Brevibacterium flavum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1718; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567; RA Nakamura J., Kimura E., Oosumi T., Matsui K., Nakamatsu T.; RT "Brevibacterium lactofermentum ATCC 13869 acn gene for aconitase."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RA Nakagawa S.; RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- CATALYTIC ACTIVITY: Citrate = isocitrate. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. CC -!- INDUCTION: Repressed by acnR. 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; AB025424; BAA76717.1; -; Genomic_DNA. DR EMBL; BA000036; BAB98933.1; ALT_INIT; Genomic_DNA. DR EMBL; BX927152; CAF21548.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_600755.1; -. DR RefSeq; YP_225824.1; -. DR World-2DPAGE; 0001:Q8NQ98; -. DR GeneID; 1019512; -. DR GeneID; 3344469; -. DR GenomeReviews; BA000036_GR; Cgl1540. DR GenomeReviews; BX927147_GR; cg1737. DR KEGG; cgb:cg1737; -. DR KEGG; cgl:NCgl1482; -. DR HOGENOM; Q8NQ98; -. DR OMA; Q8NQ98; RIKNEML. DR BioCyc; CGLU196627-1:CG1737-MON; -. DR BRENDA; 4.2.1.3; 812. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0003994; F:aconitate hydratase activity; IEA:EC. DR GO; GO:0005506; F:iron ion 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 1: Evidence at protein level; KW Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW Tricarboxylic acid cycle. FT CHAIN 1 939 Aconitate hydratase. FT /FTId=PRO_0000076657. FT METAL 475 475 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 541 541 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 544 544 Iron-sulfur (4Fe-4S) (By similarity). FT CONFLICT 71 71 D -> N (in Ref. 1; BAA76717). FT CONFLICT 122 122 M -> V (in Ref. 1; BAA76717). FT CONFLICT 555 555 I -> Y (in Ref. 1; BAA76717). FT CONFLICT 745 745 N -> Y (in Ref. 1; BAA76717). FT CONFLICT 888 888 T -> I (in Ref. 1; BAA76717). SQ SEQUENCE 939 AA; 101726 MW; 3488BCA190A07F13 CRC64; MTESKNSFNA KSTLEVGDKS YDYFALSAVP GMEKLPYSLK VLGENLLRTE DGANITNEHI EAIANWDASS DPSIEIQFTP ARVLMQDFTG VPCVVDLATM REAVAALGGD PNDVNPLNPA EMVIDHSVIV EAFGRPDALA KNVEIEYERN EERYQFLRWG SESFSNFRVV PPGTGIVHQV NIEYLARVVF DNEGLAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP RVVGFKLTGE IPVGVTATDV VLTITEMLRD HGVVQKFVEF YGSGVKAVPL ANRATIGNMS PEFGSTCAMF PIDEETTKYL RLTGRPEEQV ALVEAYAKAQ GMWLDEDTVE AEYSEYLELD LSTVVPSIAG PKRPQDRILL SEAKEQFRKD LPTYTDDAVS VDTSIPATRM VNEGGGQPEG GVEADNYNAS WAGSGESLAT GAEGRPSKPV TVASPQGGEY TIDHGMVAIA SITSCTNTSN PSVMIGAGLI ARKAAEKGLK SKPWVKTICA PGSQVVDGYY QRADLWKDLE AMGFYLSGFG CTTCIGNSGP LPEEISAAIN EHDLTATAVL SGNRNFEGRI SPDVKMNYLA SPIMVIAYAI AGTMDFDFEN EALGQDQDGN DVFLKDIWPS TEEIEDTIQQ AISRELYEAD YADVFKGDKQ WQELDVPTGD TFEWDENSTY IRKAPYFDGM PVEPVAVTDI QGARVLAKLG DSVTTDHISP ASSIKPGTPA AQYLDEHGVE RHDYNSLGSR RGNHEVMMRG TFANIRLQNQ LVDIAGGYTR DFTQEGAPQA FIYDASVNYK AAGIPLVVLG GKEYGTGSSR DWAAKGTNLL GIRAVITESF ERIHRSNLIG MGVVPLQFPA GESHESLGLD GTETFDITGL TALNEGETPK TVKVTATKEN GDVVEFDAVV RIDTPGEADY YRHGGILQYV LRQMAASSK //