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Database: UniProt
Entry: A0A1F9VGA7_9BACT
LinkDB: A0A1F9VGA7_9BACT
Original site: A0A1F9VGA7_9BACT 
ID   A0A1F9VGA7_9BACT        Unreviewed;       894 AA.
AC   A0A1F9VGA7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=A3G41_08910 {ECO:0000313|EMBL:OGS01940.1};
OS   Elusimicrobia bacterium RIFCSPLOWO2_12_FULL_59_9.
OC   Bacteria; Elusimicrobiota.
OX   NCBI_TaxID=1797952 {ECO:0000313|EMBL:OGS01940.1, ECO:0000313|Proteomes:UP000176685};
RN   [1] {ECO:0000313|EMBL:OGS01940.1, ECO:0000313|Proteomes:UP000176685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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   -!- 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:OGS01940.1}.
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DR   EMBL; MGUX01000131; OGS01940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F9VGA7; -.
DR   STRING; 1797952.A3G41_08910; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000176685; 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}.
FT   DOMAIN          73..564
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          694..820
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   894 AA;  97677 MW;  4540768CFD6CF260 CRC64;
     MDSFSTLKTL KAGGSSYRIF SIRALAQAGL GDIGRLPYSI RVLLENLLRH EDGLSVARDD
     IQALARWRPD QKPDKEIQFM PSRVLLQDFT GVPAVADLAA MRDAIAALGG DPQKINPLQQ
     SDLVIDHSVQ VDSYGLRDAF RLNAEKEFKR NQERYKFLCW GQKAFNNFRV VPPDTGIVHQ
     VNLEYLASVV YSRRTPEGLT AYPDTLVGTD SHTTMISGLG VLGWGVGGIE AEAAMLGQPI
     AMLAPPVVGF KLTGALAEGA TATDLVLTVT QMLREKGVVG KIVEFYGAGL SALALTDRAT
     LANMAPEYGA TTGFFPVDDE TLNYLRQTGR DPKQIRLVKA YLKEQGLFRT DDAPVPLYSD
     SLELDLSRVE PSLAGPRRPQ DRVPLRNSKP EFEKALGAFW PKQTAATPAA AKVPVQMNGQ
     RFELGHGSVV IASITSCTNT SNPQVMLQAG LLAQKAARAG LKSKPWVKTS LAPGSKVVMD
     YLQKSKLLPA LESLGFYLVG YGCTTCIGNS GPLPDAVEKA IQAANLVAAC VLSGNRNFEG
     RIHPSVRASY LASPPLVVAY ALAGRMDIDL YREPLGHDAS GKPVFLKDIW PSQKEVRLAV
     QKFIKKEMFH KQYGKIFQGD KRWKTLRVPG GSRFAWSKDS TYIKKPPFFA GMTREPEKPR
     PIAAARVLAL LGDSVTTDHI SPAGNIPADG PAGRYLIKQG VEKKDFNSFG ARRGNHEVML
     RGAFSNIRLR NLLAPGTEGG WTRRLPDGEV MTIYDAAMSY AKEKTDLLIL AGKEYGSGSS
     RDWAAKGAAL LGVRAVIAES YERIHRSNLV GMGILPLQFK LGENCRSLGL TGEETFDIEN
     VAEDFKPGRE MEIACLAPGG GKNRFKVLCR IDTPKELEYY RHGGILKYAL RQLL
//
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