ID   ACON_CORJK              Reviewed;         936 AA.
AC   Q4JVM4;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   01-MAY-2013, entry version 59.
DE   RecName: Full=Aconitate hydratase;
DE            EC=4.2.1.3;
GN   Name=acn; OrderedLocusNames=jk0969;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B.,
RA   Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T.,
RA   Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P.,
RA   Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant
RT   nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring
RT   bacterium of the human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via
CC       cis-aconitate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 2/2.
CC   -!- INDUCTION: Repressed by AcnR (By similarity).
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
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DR   EMBL; CR931997; CAI37133.1; -; Genomic_DNA.
DR   RefSeq; YP_250751.1; NC_007164.1.
DR   ProteinModelPortal; Q4JVM4; -.
DR   STRING; 306537.jk0969; -.
DR   EnsemblBacteria; CAI37133; CAI37133; jk0969.
DR   GeneID; 3432029; -.
DR   KEGG; cjk:jk0969; -.
DR   PATRIC; 21512848; VBICorJei31838_0980.
DR   eggNOG; COG1048; -.
DR   HOGENOM; HOG000025704; -.
DR   KO; K01681; -.
DR   OMA; YSKAQGM; -.
DR   ProtClustDB; PRK09277; -.
DR   BioCyc; CJEI306537:GJ8V-1004-MONOMER; -.
DR   UniPathway; UPA00223; UER00718.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
DR   GO; GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 3.
DR   Gene3D; 3.40.1060.10; -; 1.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR015937; Acoase/IPM_deHydtase.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
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   PANTHER; PTHR11670; PTHR11670; 1.
DR   PANTHER; PTHR11670:SF1; PTHR11670:SF1; 1.
DR   Pfam; PF00330; Aconitase; 2.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 1.
DR   SUPFAM; SSF53732; Aconitase_N; 1.
DR   TIGRFAMs; TIGR01341; aconitase_1; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    936       Aconitate hydratase.
FT                                /FTId=PRO_0000076660.
FT   METAL       472    472       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       538    538       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       541    541       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   936 AA;  101295 MW;  55B605AD2F117308 CRC64;
     MAESINSFDS KSTLQVGEKS YDYFALDAVP GMEKLPYSLK VLGENLLRNE DGKNITREHI
     EAIANWDPSA EPNFEIQFTP ARVIMQDFTG VACIVDLATI RDAVVALGGD ADDVNPLNPA
     EMVIDHSVII EAFGDSDALE KNVEIEYQRN DERYKFLRWG TGAFENFRVV PPGTGIVHQV
     NIEYLARSVF DNNGLAYPDT CVGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPISMLIP
     RVVGFKLTGE IPTGVTATDV VLTITDMLRQ HGVVGKFVEF YGKGVGELPL ANRATIGNMS
     PEFGSTAAMF PIDEETVKYL ELTGRDQETL ERVEAYAKAQ GMWLDPEKEV EYSEYLELDL
     STVVPSIAGP KRPQDRIELN DSKAQFRKDL HNYVEADASA VTPDFDAEGP ATENTSAQTA
     GTPASAADAK GNIPSAAAGA EGRPSNPVTV NYNGEDIELD HGMVAIASIT SCTNTSNPSV
     MVGAGLLARN AAAKGLKSAP WVKTSMAPGS QVVNGYYEKA GLWKDLEAMG FYLVGYGCTT
     CIGNSGPLPE EISAGINEGD LAATAVLSGN RNFEGRINPD VKMNYLASPI LVIAYAIAGT
     MDFDFETQPL GQDQDGNDVF LKDIWPSTED IEEVIASSIT KDLYAEDYAN VFEGDERWRS
     LDVPSGKTFD WDPKSTYIRK APYFDGMSKE PEAVNDVKGA RVLALLGDSV TTDHISPAST
     IKPGTPAAQY LDANGVERKD YNSLGARRGN HEVMVRGTFA NIRLQNQLLD GVSGGYTRDF
     TQEGGPQSFI YDAAMNYQKE NTPLVVLGGK EYGTGSSRDW AAKGTLLLGV KAVIAESFER
     IHRSNLIGMG VVPLQFPEGE SWKSLGIEGT ETFDIEGIEE LNNGSTPKTV KVTATKENGE
     KIEFDAVTRI DTPGEADYYR NGGILQFVLR NMMSGK
//