(data stored in ACNUC7421 zone)

SWISSPROT: B7UIG6_ECO27

ID   B7UIG6_ECO27            Unreviewed;       865 AA.
AC   B7UIG6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Aconitate hydratase B {ECO:0000256|PIRNR:PIRNR036687};
DE            EC=4.2.1.3 {ECO:0000256|PIRNR:PIRNR036687};
DE            EC=4.2.1.99 {ECO:0000256|PIRNR:PIRNR036687};
DE   AltName: Full=2-methylisocitrate dehydratase {ECO:0000256|PIRNR:PIRNR036687};
GN   Name=acnB {ECO:0000313|EMBL:CAS07669.1};
GN   OrderedLocusNames=E2348C_0121 {ECO:0000313|EMBL:CAS07669.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07669.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07669.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-
CC         cis-aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036687};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = isocitrate; Xref=Rhea:RHEA:10336,
CC         ChEBI:CHEBI:16087, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036687};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036687-1};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR036687-1};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 2/2.
CC       {ECO:0000256|PIRNR:PIRNR036687}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|PIRNR:PIRNR036687}.
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DR   EMBL; FM180568; CAS07669.1; -; Genomic_DNA.
DR   RefSeq; WP_012578834.1; NC_011601.1.
DR   EnsemblBacteria; CAS07669; CAS07669; E2348C_0121.
DR   KEGG; ecg:E2348C_0121; -.
DR   HOGENOM; HOG000205991; -.
DR   KO; K01682; -.
DR   OMA; QDTTGAM; -.
DR   BioCyc; ECOL574521:E2348C_RS00625-MONOMER; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd01576; AcnB_Swivel; 1.
DR   Gene3D; 1.25.40.310; -; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 2.
DR   Gene3D; 3.40.1060.10; -; 1.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR004406; Aconitase_B.
DR   InterPro; IPR015933; Aconitase_B_HEAT-like_dom.
DR   InterPro; IPR036288; Aconitase_B_HEAT-like_dom_sf.
DR   InterPro; IPR015929; Aconitase_B_swivel.
DR   InterPro; IPR015932; Aconitase_dom2.
DR   PANTHER; PTHR43160:SF1; PTHR43160:SF1; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF06434; Aconitase_2_N; 1.
DR   Pfam; PF11791; Aconitase_B_N; 1.
DR   PIRSF; PIRSF036687; AcnB; 1.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   SUPFAM; SSF74778; SSF74778; 1.
DR   TIGRFAMs; TIGR00117; acnB; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UIG6.
DR   SWISS-2DPAGE; B7UIG6.
KW   4Fe-4S {ECO:0000256|PIRSR:PIRSR036687-1,
KW   ECO:0000256|SAAS:SAAS00319404};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Iron {ECO:0000256|PIRSR:PIRSR036687-1};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR036687-1};
KW   Lyase {ECO:0000256|PIRNR:PIRNR036687};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036687-1};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR036687}.
FT   DOMAIN        4    156       Aconitase_B_N. {ECO:0000259|Pfam:
FT                                PF11791}.
FT   DOMAIN      168    382       Aconitase_2_N. {ECO:0000259|Pfam:
FT                                PF06434}.
FT   DOMAIN      472    818       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   REGION      244    246       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   REGION      414    416       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   METAL       710    710       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   METAL       769    769       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   METAL       772    772       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   BINDING     191    191       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     498    498       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     791    791       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     796    796       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
SQ   SEQUENCE   865 AA;  93515 MW;  05E1C627969DE0D6 CRC64;
     MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPSVDEA
     AYVKAGFLAA VAKGEAKSPL LTPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS
     HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLNRP ALAEKLTVTV FKVTGETNTD
     DLSPAPDAWS RPDIPLHALA MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV
     GTGSSRKSAT NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN
     LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA
     LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM
     TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH
     SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM
     QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA
     ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLANPELLEA
     DADAEYAAVI DIDLADIKEP IICAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA
     GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA
     DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT
     YRYLNFDQLS QYTEKADGVI FQTAV
//

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