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Database: UniProt
Entry: A0A1I0GT33_9BACI
LinkDB: A0A1I0GT33_9BACI
Original site: A0A1I0GT33_9BACI 
ID   A0A1I0GT33_9BACI        Unreviewed;       651 AA.
AC   A0A1I0GT33;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:SET73616.1};
GN   ORFNames=SAMN05421676_107128 {ECO:0000313|EMBL:SET73616.1};
OS   Salinibacillus kushneri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX   NCBI_TaxID=237682 {ECO:0000313|EMBL:SET73616.1, ECO:0000313|Proteomes:UP000199095};
RN   [1] {ECO:0000313|EMBL:SET73616.1, ECO:0000313|Proteomes:UP000199095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SET73616.1,
RC   ECO:0000313|Proteomes:UP000199095};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR   EMBL; FOHJ01000007; SET73616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0GT33; -.
DR   STRING; 237682.SAMN05421676_107128; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000199095; Unassembled WGS sequence.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 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; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR006250; Aconitase_put.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR01342; acon_putative; 1.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00330; Aconitase; 2.
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.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          8..284
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          285..407
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          512..580
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   REGION          370..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  71444 MW;  503DCD8390FF7657 CRC64;
     MKLNVTQKLI KDHLVSGDMT PGEEIGLKID QTLTQDATGT MVMLELEAMG LDYAKTEASA
     QYVDHNLIQV DNKNPDDHLF LQSATRRFGL YYSRPGNGVS HPVHMQRLAK PGKTLLGSDS
     HTCANGCMGM LAMGAGGIDV AMAIAGEPFY VKMPKVWGIK LTGELPDWVG AKDVILELLR
     RHDVKGGVGR VIEYYGPGLK SLDAMDRHVI ANMGAELGAT GTVFPSDEEV KRFLKEQDRE
     EDWIKLHADK GAAYDIEEEI NLSEIEPLIA KPSSPGNVVP VKDIAGESIY QSYIGSSAQP
     GFNDFAMTAE IVKDKKIAEG VSLDINPTSR QMLTDLVQEG HIASLLQAGA RLHQAGCNGC
     IGMGQAPATG RNSLRTTPRN FPGRSGTKED SVFLCGPETA AASALKGEIT DPRTLEMKYP
     KIKDPKKPTV DDQLLDKPLS KEEARNVELY KGPNIASIPE MDKLPDELEV PILLKMDDNI
     STDEILAGGA RVLPFRSNLP EISKFTFEII DESYYDRAMD VRDQSGHAIV GGHNYGQGSS
     REHAALAPRY LGLRVAVVKD FARIHWQNLV NFGVLPLTFK VEEDFNKLEQ GDVLQFKNLQ
     QNVKEGNDIM ATVKGKGVEL ELTHALSSRQ KDMMIKGGLI NWVRERQNTN A
//
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