ID Q39UD3_GEOMG Unreviewed; 847 AA. AC Q39UD3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 125. 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:ABB32141.1}; GN OrderedLocusNames=Gmet_1912 {ECO:0000313|EMBL:ABB32141.1}; OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB32141.1, ECO:0000313|Proteomes:UP000007073}; RN [1] {ECO:0000313|EMBL:ABB32141.1, ECO:0000313|Proteomes:UP000007073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53774 / DSM 7210 / GS-15 RC {ECO:0000313|Proteomes:UP000007073}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Geobacter metallireducens GS-15."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABB32141.1, ECO:0000313|Proteomes:UP000007073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53774 / DSM 7210 / GS-15 RC {ECO:0000313|Proteomes:UP000007073}; RX PubMed=19473543; DOI=10.1186/1471-2180-9-109; RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.; RT "The genome sequence of Geobacter metallireducens: features of metabolism, RT physiology and regulation common and dissimilar to Geobacter RT sulfurreducens."; RL BMC Microbiol. 9:109-109(2009). 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; CP000148; ABB32141.1; -; Genomic_DNA. DR RefSeq; WP_011365887.1; NC_007517.1. DR AlphaFoldDB; Q39UD3; -. DR STRING; 269799.Gmet_1912; -. DR KEGG; gme:Gmet_1912; -. DR eggNOG; COG1049; Bacteria. DR HOGENOM; CLU_016536_0_0_7; -. DR UniPathway; UPA00223; UER00718. DR UniPathway; UPA00946; -. DR Proteomes; UP000007073; 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:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd01581; AcnB; 1. DR CDD; cd01576; AcnB_Swivel; 1. DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1. DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2. DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1. DR Gene3D; 1.25.40.310; Aconitate B, HEAT-like domain; 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 NCBIfam; TIGR00117; acnB; 1. DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1. DR PANTHER; PTHR43160:SF4; ACONITATE HYDRATASE B; 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; SSF74778; Aconitase B, N-terminal domain; 1. DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1. DR SUPFAM; SSF52016; LeuD/IlvD-like; 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|PIRNR:PIRNR036687}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR036687-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007073}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|PIRNR:PIRNR036687}. FT DOMAIN 4..155 FT /note="Aconitase B HEAT-like" FT /evidence="ECO:0000259|Pfam:PF11791" FT DOMAIN 167..371 FT /note="Aconitase B swivel" FT /evidence="ECO:0000259|Pfam:PF06434" FT DOMAIN 461..810 FT /note="Aconitase/3-isopropylmalate dehydratase large FT subunit alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF00330" FT BINDING 190 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 233..235 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 403..405 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 487 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 703 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT BINDING 762 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT BINDING 765 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1" FT BINDING 784 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" FT BINDING 789 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2" SQ SEQUENCE 847 AA; 91141 MW; 22B62FC749FA30B6 CRC64; MIEAYLAHEA ERKAQGIPAL PLNPEQTADL CNLLQNPPAG KEEFLLNLLK ERVSPGVDPA AKVKAAFLAE IVKGTKKSPL VSKVDAIRIL GTMIGGYNVG PLVEALKDAE LAEEAACALS RMTLVYDGFD QVVELSKSNA AAKKVLESWA NAEWFTNRPG VPETIKVKVF KVEGEINTDD FSPAGDAWSR PDIPLHALAM GKTRFPNRLK DIADWRAAGH QVAFVGDVVG TGSSRKSACN SVLWHMGQDI PAVPNKKTAG VIIGGVIAPI FFNTAQDSGA LPLKADVTKM NDGDVITINT AKGEISNDKG EVISTFKISP NTLADEFRAG GRIPLIIGRA ITEKARKALG LGDTDVFTKP VNPAPKAGQG YSLAQKMVGK ACGVAGILPG TACEPKMTTV GSQDTTGPMT ADELKELACL KFLSPMFMQS FCHTAAYPKP ADVKMHKNLP GFIIERGGVP LKPGDGVIHS WLNRLLLPDT VGTGGDSHTR FPIGISFPAG SGLVAFAGAM GFMPLDMPES VLVRFKGKLN PGITLRDAVN AIPYWAIKQG KLTVPKKNKI NIFNGRILEM EGLPDLTVEQ AFELTDAAAE RSAAAGCIQL SKESVATYLR SNVALMKKMI ADGYQDAQTL QNRIDAVNEW LKNPQLLEAD KNAVETGAYA DVIEIDLAEI TEPILACPND PDDVKLLSDV AGTPIQDVFL GSCMTNIGHF RAAAEIWRGL KFNPSVRTWI CPPTRMDQKQ LKDEAYFSVY SAFGARIEIA GCSLCMGNQA RVPDGVNMFS TSTRNFDDRI GDGAKVFLGS AELGAVTATL GKLPTVAEFM AAYKEKVEPK KDVVYKYLQF DEMPEYK //