ID   ACON1_ECOLI             Reviewed;         891 AA.
AC   P25516; P78060; P78148;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   25-NOV-2008, entry version 82.
DE   RecName: Full=Aconitate hydratase 1;
DE            Short=Aconitase 1;
DE            EC=4.2.1.3;
DE   AltName: Full=Citrate hydro-lyase 1;
GN   Name=acnA; Synonyms=acn; OrderedLocusNames=b1276, JW1268;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92174916; PubMed=1541275;
RX   DOI=10.1111/j.1432-1033.1992.tb16673.x;
RA   Prodromou C., Artymiuk P.J., Guest J.R.;
RT   "The aconitase of Escherichia coli. Nucleotide sequence of the
RT   aconitase gene and amino acid sequence similarity with mitochondrial
RT   aconitases, the iron-responsive-element-binding protein and
RT   isopropylmalate isomerases.";
RL   Eur. J. Biochem. 204:599-609(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97251357; PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-19.
RX   MEDLINE=92148368; PubMed=1838390;
RA   Prodromou C., Haynes M.J., Guest J.R.;
RT   "The aconitase of Escherichia coli: purification of the enzyme and
RT   molecular cloning and map location of the gene (acn).";
RL   J. Gen. Microbiol. 137:2505-2515(1991).
RN   [6]
RP   CHARACTERIZATION, MAGNETIC CIRCULAR DICHROISM, AND EPR SPECTROSCOPY.
RX   MEDLINE=20053887; PubMed=10585860; DOI=10.1042/0264-6021:3440739;
RA   Jordan P.A., Tang Y., Bradbury A.J., Thomson A.J., Guest J.R.;
RT   "Biochemical and spectroscopic characterization of Escherichia coli
RT   aconitases (AcnA and AcnB).";
RL   Biochem. J. 344:739-746(1999).
CC   -!- FUNCTION: May have an iron-responsive regulatory function.
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       P18843:nadE; NbExp=1; IntAct=EBI-549739, EBI-548960;
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
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DR   EMBL; X60293; CAA42834.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74358.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14828.1; -; Genomic_DNA.
DR   PIR; G64875; G64875.
DR   RefSeq; AP_001902.1; -.
DR   RefSeq; NP_415792.1; -.
DR   DIP; DIP:9043N; -.
DR   IntAct; P25516; -.
DR   GeneID; 946724; -.
DR   GenomeReviews; U00096_GR; b1276.
DR   GenomeReviews; AP009048_GR; JW1268.
DR   KEGG; ecj:JW1268; -.
DR   KEGG; eco:b1276; -.
DR   EchoBASE; EB1301; -.
DR   EcoGene; EG11325; acnA.
DR   HOGENOM; P25516; -.
DR   BioCyc; EcoCyc:ACONITASE-MON; -.
DR   BioCyc; MetaCyc:ACONITASE-MON; -.
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:0005515; F:protein binding; IPI:IntAct.
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; 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   4Fe-4S; Complete proteome; Direct protein sequencing; Iron;
KW   Iron-sulfur; Lyase; Metal-binding; Tricarboxylic acid cycle.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    891       Aconitate hydratase 1.
FT                                /FTId=PRO_0000076661.
FT   METAL       435    435       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       501    501       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       504    504       Iron-sulfur (4Fe-4S) (By similarity).
FT   CONFLICT    522    522       S -> G (in Ref. 1; CAA42834 and 4;
FT                                BAA14828).
SQ   SEQUENCE   891 AA;  97677 MW;  EB47E5B3C3F9C56C CRC64;
     MSSTLREASK DTLQAKDKTY HYYSLPLAAK SLGDITRLPK SLKVLLENLL RWQDGNSVTE
     EDIHALAGWL KNAHADREIA YRPARVLMQD FTGVPAVVDL AAMREAVKRL GGDTAKVNPL
     SPVDLVIDHS VTVDRFGDDE AFEENVRLEM ERNHERYVFL KWGKQAFSRF SVVPPGTGIC
     HQVNLEYLGK AVWSELQDGE WIAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
     PVSMLIPDVV GFKLTGKLRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR
     ATIANMSPEY GATCGFFPID AVTLDYMRLS GRSEDQVELV EKYAKAQGMW RNPGDEPIFT
     STLELDMNDV EASLAGPKRP QDRVALPDVP KAFAASNELE VNATHKDRQP VDYVMNGHQY
     QLPDGAVVIA AITSCTNTSN PSVLMAAGLL AKKAVTLGLK RQPWVKASLA PGSKVVSDYL
     AKAKLTPYLD ELGFNLVGYG CTTCIGNSGP LPDPIETAIK KSDLTVGAVL SGNRNFEGRI
     HPLVKTNWLA SPPLVVAYAL AGNMNINLAS EPIGHDRKGD PVYLKDIWPS AQEIARAVEQ
     VSTEMFRKEY AEVFEGTAEW KGINVTRSDT YGWQEDSTYI RLSPFFDEMQ ATPAPVEDIH
     GARILAMLGD SVTTDHISPA GSIKPDSPAG RYLQGRGVER KDFNSYGSRR GNHEVMMRGT
     FANIRIRNEM VPGVEGGMTR HLPDSDVVSI YDAAMRYKQE QTPLAVIAGK EYGSGSSRDW
     AAKGPRLLGI RVVIAESFER IHRSNLIGMG ILPLEFPQGV TRKTLGLTGE EKIDIGDLQN
     LQPGATVPVT LTRADGSQEV VPCRCRIDTA TELTYYQNDG ILHYVIRNML K
//