ID A0A1X3L991_ECOLX Unreviewed; 865 AA. AC A0A1X3L991; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 28-MAR-2018, entry version 7. 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 ORFNames=EAXG_02443 {ECO:0000313|EMBL:OSL66639.1}; OS Escherichia coli TA054. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656433 {ECO:0000313|EMBL:OSL66639.1, ECO:0000313|Proteomes:UP000193131}; RN [1] {ECO:0000313|EMBL:OSL66639.1, ECO:0000313|Proteomes:UP000193131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TA054 {ECO:0000313|EMBL:OSL66639.1, RC ECO:0000313|Proteomes:UP000193131}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., RA Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I., RA Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T., Park D., RA Pearson M., Richards J., Roberts A., Saif S., Shea T.D., Shenoy N., RA Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C., RA Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli TA054."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = CC (Z)-but-2-ene-1,2,3-tricarboxylate + H(2)O. CC {ECO:0000256|PIRNR:PIRNR036687}. CC -!- CATALYTIC ACTIVITY: Citrate = isocitrate. CC {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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OSL66639.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ADKB01000025; OSL66639.1; -; Genomic_DNA. DR RefSeq; WP_001303793.1; NZ_ADKB01000025.1. DR UniPathway; UPA00223; UER00718. DR Proteomes; UP000193131; Unassembled WGS sequence. 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; -; 2. 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; KW 4Fe-4S {ECO:0000256|PIRSR:PIRSR036687-1, KW ECO:0000256|SAAS:SAAS00991595}; KW Complete proteome {ECO:0000313|Proteomes:UP000193131}; KW Iron {ECO:0000256|PIRSR:PIRSR036687-1}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR036687-1}; KW Lyase {ECO:0000256|PIRNR:PIRNR036687, ECO:0000256|SAAS:SAAS00432333}; 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; 93484 MW; 0BFEDFB96F8BF6DE CRC64; MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPGVDEA 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 ILCAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT YRYLNFNQLS QYTEKADGVI FQTAV //