ID J7WU35_BACCE Unreviewed; 907 AA.
AC J7WU35;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ORFNames=IC3_02664 {ECO:0000313|EMBL:EJP92363.1};
OS Bacillus cereus VD142.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=718224 {ECO:0000313|EMBL:EJP92363.1, ECO:0000313|Proteomes:UP000006969};
RN [1] {ECO:0000313|EMBL:EJP92363.1, ECO:0000313|Proteomes:UP000006969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD142 {ECO:0000313|EMBL:EJP92363.1,
RC ECO:0000313|Proteomes:UP000006969};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD142.";
RL Submitted (JAN-2013) 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}.
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:EJP92363.1}.
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DR EMBL; AHCL02000014; EJP92363.1; -; Genomic_DNA.
DR RefSeq; WP_002087788.1; NZ_KE150045.1.
DR AlphaFoldDB; J7WU35; -.
DR PATRIC; fig|718224.3.peg.2739; -.
DR HOGENOM; CLU_013476_2_1_9; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000006969; Unassembled WGS sequence.
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};
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; 99140 MW; 67C08CD42F13BC01 CRC64;
MVKHNPFQSR ATFELDGKTY HYYQLKALEN AGVGNVSQLP YSVKVLLESV LRQVDGRVIT
EEHVTNLAKW GTKDVQDIDV PFKPSRVILQ DFTGVPAVVD LASLRKAMAD MGGDPDKINP
EITVDLVIDH SVQVDRAGTA DSLAFNMDLE FKRNEERYKF LSWAQKSFDN YRAVPPATGI
VHQVNLEYLA PVVHAVKNAE GDLVAYPDSL VGTDSHTTMI NGIGVLGWGV GGIEAEAGML
GQPSYFPVPE VIGVKLTGTL PSGTTATDVA LKVTQVLRQK GVVGKFVEFF GSGLKSMPLA
DRATISNMAP EYGATCGFFP IDDISLEYLR LTGRDEEQIR VVEEYCKANG LFYTADSKDP
IYTDLVEIDL NTIESNLSGP KRPQDLIPLS DMKEEFHKAV VAPVGTQGLG FNEQEFDKEV
KVTLKDQEVT MKTGGIAIAA ITSCTNTSNP YVLIGAGLVA KKAIEKGLKV PGYVKTSLAP
GSKVVTEYLD KSGLTTYLDQ LGFQTVGYGC TTCIGNSGPL AEELEEAIAA NDLLVTSVLS
GNRNFEGRIH PLVKANYLAS PPLVVAYALA GTVDIDLKND EIGKDVNGNA VYFNDIWPSA
KEIEDVVQRV VTSELFKKEY AQVFNSNERW NEIQTSNEAL YTWDNDSTYI QNPPFFEGLS
KEPGEVETLS GLRIVGKFGD SVTTDHISPA GSIGKHTPAG RYLLENGVQP VDFNSYGSRR
GNHEVMMRGT FANIRIKNQI APGTEGGYTT YWPTGEVTSI YDAAMKYKED GTGLLVVAGK
DYGMGSSRDW AAKGTNLLGI KAVIAESFER IHRSNLVLMG VLPLQFKDGD SAETLGLVGD
ESFEIQIDKT VRPRDLVKVV AIDVEGKEKQ FEVVARFDSE VEIDYYRHGG ILQMVLRSKI
EESKVSN
//
