ID A0A8A3SB61_ECO57 Unreviewed; 865 AA. AC A0A8A3SB61; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE RecName: Full=Aconitate hydratase B {ECO:0000256|ARBA:ARBA00019379, ECO:0000256|PIRNR:PIRNR036687}; DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|PIRNR:PIRNR036687}; DE EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250, ECO:0000256|PIRNR:PIRNR036687}; DE AltName: Full=2-methylisocitrate dehydratase {ECO:0000256|PIRNR:PIRNR036687}; GN Name=acnB {ECO:0000313|EMBL:QSZ69183.1}; GN ORFNames=E5F08_03975 {ECO:0000313|EMBL:QSZ69183.1}; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334 {ECO:0000313|EMBL:QSZ69183.1}; RN [1] {ECO:0000313|EMBL:QSZ69183.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TT12A {ECO:0000313|EMBL:QSZ69183.1}; RA Allue-Guardia A., Koenig S.K., Feng P., Bono J.L., Eppinger M.; RT "Impact of Shiga toxin phage carriage in the native EHEC O157:H7 genome RT background."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis- CC 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|ARBA:ARBA00000118, CC ECO:0000256|PIRNR:PIRNR036687}; CC -!- CATALYTIC ACTIVITY: CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00023501, 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; isocitrate CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717, CC ECO:0000256|PIRNR:PIRNR036687}. CC -!- PATHWAY: Organic acid metabolism; propanoate degradation. CC {ECO:0000256|ARBA:ARBA00005026}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|PIRNR:PIRNR036687}. 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; CP038496; QSZ69183.1; -; Genomic_DNA. DR RefSeq; WP_032212843.1; NZ_CP038496.1. DR UniPathway; UPA00223; UER00718. DR UniPathway; UPA00946; -. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0003994; F:aconitate hydratase activity; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. 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 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|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR036687-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR036687-1}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR036687- KW 1}; Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR036687}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR036687-1}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|PIRNR:PIRNR036687}. FT DOMAIN 4..156 FT /note="Aconitase_B_N" FT /evidence="ECO:0000259|Pfam:PF11791" FT DOMAIN 168..382 FT /note="Aconitase_2_N" FT /evidence="ECO:0000259|Pfam:PF06434" FT DOMAIN 472..818 FT /note="Aconitase" FT /evidence="ECO:0000259|Pfam:PF00330" FT REGION 244..246 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT REGION 414..416 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT METAL 710 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT METAL 769 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT METAL 772 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT BINDING 191 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 498 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 791 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 796 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" SQ SEQUENCE 865 AA; 93483 MW; 08D03870416C3CDE 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 ALPIEVNVSN 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 //