ID   B7ISF5_BACC2            Unreviewed;       907 AA.
AC   B7ISF5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
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:ACK94745.1};
GN   OrderedLocusNames=BCG9842_B1593 {ECO:0000313|EMBL:ACK94745.1};
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK94745.1, ECO:0000313|Proteomes:UP000006744};
RN   [1] {ECO:0000313|EMBL:ACK94745.1, ECO:0000313|Proteomes:UP000006744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842 {ECO:0000313|EMBL:ACK94745.1,
RC   ECO:0000313|Proteomes:UP000006744};
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) 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   -!- 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}.
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DR   EMBL; CP001186; ACK94745.1; -; Genomic_DNA.
DR   RefSeq; WP_000238553.1; NC_011772.1.
DR   AlphaFoldDB; B7ISF5; -.
DR   KEGG; bcg:BCG9842_B1593; -.
DR   HOGENOM; CLU_013476_2_1_9; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000006744; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd01586; AcnA_IRP; 1.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   Gene3D; 6.10.190.10; -; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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   NCBIfam; TIGR01341; aconitase_1; 1.
DR   PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR   PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 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   SUPFAM; SSF52016; LeuD/IlvD-like; 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:ACK94745.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          76..571
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          701..828
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   907 AA;  99054 MW;  406D24884514C121 CRC64;
     MVKHNPFQSR ATFEVDGKTY HYYDLKALEN AGVGNVSQLP YSVKVLLESV LRQVDGRVIT
     EEHVTNLAKW GTKDVQDIDV PFKPSRVILQ DFTGVPAVVD LASLRKAMAD MGGDPDKINP
     EITVDLVIDH SVQVDRAGTA DALAFNMDLE FKRNEERYKF LSWAQKSFDN YRAVPPATGI
     VHQVNLEYLA PVVHAVKNAE GDLVAYPDSL VGTDSHTTMI NGIGVLGWGV GGIEAEAGML
     GQPSYFPVPE VIGVKLTGTL PSGTTATDVA LKVTQVLRQK GVVGKFVEFF GNGLKSMPLA
     DRATISNMAP EYGATCGFFP IDDISLEYLR LTGRDEEQIR IVEEYCKANG LFYTADSKDP
     IYTDLVEIDL NTIESNLSGP KRPQDLIPLS DMKDAFHKAV LAPVGTQGLG FNEQEFDKEV
     KVTLEDKEVT MKTGAIAIAA ITSCTNTSNP YVLIGAGLVA KKAIEKGLVV PEYVKTSLAP
     GSKVVTEYLD KSGLTTYLDQ LGFQTVGYGC TTCIGNSGPL APELEESIAA NDLLVTSVLS
     GNRNFEGRIH PLVKANYLAS PPLVVAYALA GTVDIDLKND EIGKDANGNA VYFNDIWPSA
     KEIEDVVQSV VTSELFKKEY AQVFNSNERW NEIQTSNEAL YTWDNDSTYI QNPPFFEGLS
     KEPGEVETLS GLRIVGKFGD SVTTDHISPA GSIGKHTPAG RYLLENGVQP VDFNSYGSRR
     GNHEVMMRGT FANIRIKNQI APGTEGGYTT YWPTGEVTSI YDAAMKYKED GTGLLVVAGK
     DYGMGSSRDW AAKGTNLLGI KAVIAESFER IHRSNLVLMG VLPLQFKEGE SAETLGLVGN
     ESFEIQIDKS VRPRDLVKVV ATDLDGNEKQ FEVVARFDSE VEIDYYRHGG ILQMVLREKI
     EESKVSN
//