ID A0A1X3L991_ECOLX Unreviewed; 865 AA. AC A0A1X3L991; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 14-DEC-2022, entry version 25. 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 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., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., Saif S., RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., 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: 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A1X3L991; -. DR EnsemblBacteria; OSL66639; OSL66639; EAXG_02443. DR UniPathway; UPA00223; UER00718. DR UniPathway; UPA00946; -. 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:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA 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 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; SSF74778; Aconitase B, N-terminal domain; 1. DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 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 BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 244..246 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 414..416 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 498 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 710 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT BINDING 769 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT BINDING 772 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT BINDING 791 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 796 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR: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 //