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Database: UniProt
Entry: A0A1Q8Q2P4_9BACI
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ID   A0A1Q8Q2P4_9BACI        Unreviewed;       908 AA.
AC   A0A1Q8Q2P4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=BTO30_13880 {ECO:0000313|EMBL:OLN21572.1};
OS   Domibacillus antri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX   NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN21572.1, ECO:0000313|Proteomes:UP000185568};
RN   [1] {ECO:0000313|EMBL:OLN21572.1, ECO:0000313|Proteomes:UP000185568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XD80 {ECO:0000313|EMBL:OLN21572.1,
RC   ECO:0000313|Proteomes:UP000185568};
RA   Verma A., Krishnamurthi S.;
RT   "Domibacillus antri genome sequencing.";
RL   Submitted (DEC-2016) 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:OLN21572.1}.
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DR   EMBL; MSDU01000038; OLN21572.1; -; Genomic_DNA.
DR   RefSeq; WP_075399318.1; NZ_MSDU01000038.1.
DR   AlphaFoldDB; A0A1Q8Q2P4; -.
DR   STRING; 1714264.BTO30_13880; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000185568; 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..572
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          702..828
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   908 AA;  99218 MW;  C7C49433EA45EFD4 CRC64;
     MAKNDVFNAR ASFDLNGKRY NYYRLAALEE AGTAKISRLP YSIKVLLESV LRQYDGYVIK
     KDHVENLAKW GVDADKEAEV PFKPSRVILQ DFTGVPVVVD LASLRKAMAD IGGDPQVINP
     EIPVDLVIDH SVQVDAYGTP EALERNMELE FDRNAERYEF LSWAQKAFDN YRAVPPATGI
     VHQVNLEYLA SVVHAVETTE GEFETYPDTL VGTDSHTTMI NGIGVLGWGV GGIEAEAGML
     GQPSYFPIPE VVGVKLTGEL PDGATATDLA LKVTQILRQQ GVVGKFVEFF GAGVSTLPLA
     DRATIANMAP EYGATCGFFP VDAEALDYMR LTGRDEDHIQ VVEQYLKENG MFFTSANEDP
     IYTEVVELNL AEIEPNLSGP KRPQDLIPLS QMKKSFQEAV SAPQGNHGFG LTADELDRTT
     TVTFNDGTTA EMKTGAIGIA AITSCTNTSN PYVLLAAGLV AKKAVELGLQ VPKYVKTSLA
     PGSKVVTGYL RDSGLLPYME QIGFNVVGYG CTTCIGNSGP MKEEIEKAII DSDLLVTSVL
     SGNRNFEGRI HPLVKGNYLA SPPLVVAYAL AGNVNVDLKN EPIGKGKDGQ DVFFKDIWPG
     TEEVKEVVKR TVTPELFRKE YEQVFNSNAK WNQIQTSNEA LYSWDEDSTY IANPTFFQNL
     SPNPEPIQAL TGLRVMGKFG DSVTTDHISP AGAIGKDTPA GLYLRSKGVE PRDFNSYGSR
     RGNHEVMMRG TFANIRIRNQ IAPGTEGGFT TFWPTGEVMP IYDACMKYQE QGTGLVVLAG
     KDYGMGSSRD WAAKGTNLLG VKTVIAESYE RIHRSNLVMM GVLPLQFKLG ENATTLGLTG
     EETIEVAIND NVKPREVVKV TATDKDGKKT EFEALVRFDS EVDVDYYRHG GILQMVLRGK
     LQSVNAGK
//
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