ID A0A7U6DTY6_9ENTE Unreviewed; 899 AA. AC A0A7U6DTY6; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 4. DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275}; DE Short=Aconitase {ECO:0000256|RuleBase:RU361275}; DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275}; GN Name=acnA {ECO:0000313|EMBL:AYY09029.1}; GN ORFNames=EGX73_03725 {ECO:0000313|EMBL:AYY09029.1}; OS Enterococcus sp. FDAARGOS_553. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=2420313 {ECO:0000313|EMBL:AYY09029.1, ECO:0000313|Proteomes:UP000271079}; RN [1] {ECO:0000313|Proteomes:UP000271079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_553 {ECO:0000313|Proteomes:UP000271079}; RA Plongla R., Gilligan P., Tallon L., Sadzewicz L., Zhao X., Vavikolanu K., RA Mehta A., Aluvathingal J., Nadendla S., Geyer C., Nandy P., Yan Y., RA Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis- CC aconitate. {ECO:0000256|RuleBase:RU361275}. 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|RuleBase:RU361275}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966}; CC -!- COFACTOR: CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000256|RuleBase:RU361275}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}. CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}. 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; CP033740; AYY09029.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7U6DTY6; -. DR UniPathway; UPA00223; UER00718. DR Proteomes; UP000271079; Chromosome. 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd01580; AcnA_IRP_Swivel; 1. DR Gene3D; 3.20.19.10; -; 1. DR Gene3D; 3.30.499.10; -; 2. DR InterPro; IPR044137; AcnA_IRP_Swivel. 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; IPR006249; Aconitase/IRP2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR036008; Aconitase_4Fe-4S_dom. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1. DR Pfam; PF00330; Aconitase; 1. DR Pfam; PF00694; Aconitase_C; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1. DR TIGRFAMs; TIGR01341; aconitase_1; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|RuleBase:RU361275}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275}; KW Lyase {ECO:0000256|RuleBase:RU361275, ECO:0000313|EMBL:AYY09029.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 64..562 FT /note="Aconitase" FT /evidence="ECO:0000259|Pfam:PF00330" FT DOMAIN 691..817 FT /note="Aconitase_C" FT /evidence="ECO:0000259|Pfam:PF00694" SQ SEQUENCE 899 AA; 98413 MW; CE05DA5F0268E883 CRC64; MNWHTNLIVN DQRYTFIDLA KVAADFNAEL KRLPYSIRVL LESVARHQDE EITAVYLDYL VNWNAEQPTG VVPFKPERVV LQDFTGVPAV VDLAAMRDAI VALGGNADTI NPEIPVTLVV DHSVQVDCAG TPEAVAFNTA REFERNQERY QFLKWAQGSF DNFEVVPPET GIIHQVNIES LSDVILEKKI AGESFLFPDT LQGTDSHTTM INGLGVLGWG VGGIEAEAAI LGEPSFFPTP EVIGVCFVNE MPAGTTATDL ALTVTEVLRK EQVVGKFVEY FGTGYQRLSL ADRATLANMA PEYGATCGFC PIDEETLNYL ATTGRTPELI HKVAAYTKAN HLFYDATEIP DYTKTVTIDL AKIQPALAGP KRPQDRILLP EVGTDFDRSL TADIGPKGFG LSEKEWQKSS QVNWPNEPSE TLQTGDIVLA AITSCTNTSN PFVMLSAGLL AKKAVEKGLT VPKSVKTSLA PGSQIVTTYL TASGLLPYLE QLGFYLVGYG CTTCIGNSGP LEAPVAEAIE NENLLVASVL SGNRNFEGRI HPQIKANYLA SPPLVVAYAI AGTIRKDLTK EPLGVVAGQE IYLTDIWPSN EEVNEYIQAF VGPEAFRAAY AHLFDANERW NRIDTTASDC YAWEDTSTYI AHPPYFDSLT KELPIQTSLS DLKVLAKLGD SVTTDHISPA GSIGLDSPAG RFLQTKAVPY REFNSFGSRR GNHHIMMRGT FGNIRLQNQL VPGSTGGITH YFPTGETMSI YDAAMNYQKN EQSCIILAGK DYGMGSSRDW AAKGTQLLGV KVVLAESFER IHRSNLVMMG VIPLEYLAGQ TAASLGLDGS ESFFIQLPEE PQVNQQIDVT AKRTDETMIT FPTRLRFDAP ADIRYWKHQG ILPMVIRKKI EAGGTSNAF //