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Database: UniProt
Entry: A0A1G0WBR1_9BACT
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ID   A0A1G0WBR1_9BACT        Unreviewed;       754 AA.
AC   A0A1G0WBR1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE   AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE   AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE   AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN   ORFNames=A2475_11205 {ECO:0000313|EMBL:OGV18857.1};
OS   Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV18857.1, ECO:0000313|Proteomes:UP000177327};
RN   [1] {ECO:0000313|EMBL:OGV18857.1, ECO:0000313|Proteomes:UP000177327}
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   -!- 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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185}.
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:OGV18857.1}.
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DR   EMBL; MHAY01000100; OGV18857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0WBR1; -.
DR   STRING; 1798452.A2475_11205; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000177327; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; cd01584; AcnA_Mitochondrial; 1.
DR   Gene3D; 3.40.1060.10; Aconitase, Domain 2; 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; IPR015932; Aconitase_dom2.
DR   InterPro; IPR006248; Aconitase_mito-like.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR01340; aconitase_mito; 1.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          34..477
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          558..685
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   754 AA;  82270 MW;  61A61A3A0AA70300 CRC64;
     MIFDIEMIKA RYSSFATKVD EAKKVTGKPM TLAEKILYAH LHPDSPLKEF KRGVDYVYFA
     PDRVAMQDAT AQMALLQFMQ AGRPNVAVPS TVHCDHLIPA KINAAKDLEA AKDMNKEVYD
     FLSSVSNKYG IGFWKPGAGI IHQVILENYA FPGGMMIGTD SHTVNAGGLG MVAIGVGGAD
     AVDVMAGFPW ELKFPKLIGV RLTGKMSGWT SAKDVILKVA GILTVKGGTG AIVEYFGDGA
     NSISCTGKGT ICNMGAEIGA TTSIFGFDDK MYNYLVATNR KEVADMAKNI ALHLAGDKEV
     YVHPDKYFDQ VIEINLSELE PHINGPFTPD LAWPISQFAK AVKENNYPEK LDVGLIGSCT
     NSSYEDISRS ASLAMQAVEK KLKVKSQFTV TPGSEMVRYT IERDGYIDLF EKIGGVVLAN
     ACGPCIGQWM RPGADKQERN SIITSFNRNF AKRNDGNPNT HSFVASPEMV TAMAIAGSLL
     FNPLKDKLVN EEGKEVMLAE PSGEELPSKG FAVEDAGYQA PAADGSGVEV IVNPKSDRLQ
     ILSPFNSWNG EDLKGLKLLI KVKGKCTTDH ISMAGPWLKY RGHLDNISNN MLTGAVNSYN
     EKTNEVKNQL TGQYAGVPDV QRDYKAKGIG TVVVGDENYG EGSSREHAAM EPRHLGVRVV
     LAKSFARIHE TNLKKQGMLA LTFANKEDYE KIKEDDTIDL LGLKTFAPSV PLTMVFNHKD
     GSKDEIILNH TYNEAQIEWF KAGGALNIIK KQFS
//
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