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Database: UniProt
Entry: A0A1I7G9K3_9FIRM
LinkDB: A0A1I7G9K3_9FIRM
Original site: A0A1I7G9K3_9FIRM 
ID   A0A1I7G9K3_9FIRM        Unreviewed;       641 AA.
AC   A0A1I7G9K3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE   AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE   AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN   ORFNames=SAMN05216508_10588 {ECO:0000313|EMBL:SFU45108.1};
OS   Eubacterium pyruvativorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=155865 {ECO:0000313|EMBL:SFU45108.1, ECO:0000313|Proteomes:UP000198817};
RN   [1] {ECO:0000313|EMBL:SFU45108.1, ECO:0000313|Proteomes:UP000198817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KHGC13 {ECO:0000313|EMBL:SFU45108.1,
RC   ECO:0000313|Proteomes:UP000198817};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
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DR   EMBL; FPBT01000005; SFU45108.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7G9K3; -.
DR   STRING; 155865.SAMN05216515_10689; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000198817; 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   CDD; cd01579; AcnA_Bact_Swivel; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
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.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000198817}.
FT   DOMAIN          7..283
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          283..407
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          520..578
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   641 AA;  68527 MW;  0249F92AA0F056DA CRC64;
     MGLTIAQKII KAHLREGDMT PGTEVGLRID QTLTQDATGT MAYLEFEAMG VPRVKTDLSV
     AYIDHNTLQS GFMNADDHRF IQSMAKKHGL KFSRPGNGIC HQVHLERFGK PGKTLIGSDS
     HTPTGGGIGM LAMGAGGLDV AVAMGGGTYY ITMPKMIRVN LTGHLKPFVT AKDISLEILR
     ILSVKGGVGY IIEWGGPGIR DLSVPERATI TNMGTELGAT TSIFPSDEVT RAFLKAEGRE
     EDWTPLASDP DAVYDRVIDI DLDTLEPKIA CPHSPDAVVD VASLKGTKVD QVCIGSCTNS
     SLFDMLKVAA LLKGKTIRPE VSLSISPGSK QVLRMLADCG ALSDIIASGA RVLECACGPC
     IGMGFSPNSG GVSLRTFNRN FLGRSGTKDG KVYLVSPETA VAAALTGEIT DPQLLGEMPE
     ITMPEAFTID DTAVIEPAAE GPEADAVEIL KGPNIKECPL GEPLGDELYA EAILKVGDNI
     TTDHIMPAGS KILPYRSNIP HLSQFCFEVV DETFPERAKA AGRSFIIGGE NYGQGSSREH
     AALVPLYLGV RAVITKSFAR IHVANLINAG ILPLTFEDPA DYDRISQGDE LKLTGIREGL
     ESGVFLLTDG EQQIRLKGEF TERQKGMLLA GGLLRYVGQE K
//
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