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Database: UniProt
Entry: A0A1C7H3R2_9BACE
LinkDB: A0A1C7H3R2_9BACE
Original site: A0A1C7H3R2_9BACE 
ID   A0A1C7H3R2_9BACE        Unreviewed;       747 AA.
AC   A0A1C7H3R2;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=A4V03_13490 {ECO:0000313|EMBL:ANU58460.1};
OS   Bacteroides caecimuris.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1796613 {ECO:0000313|EMBL:ANU58460.1, ECO:0000313|Proteomes:UP000092631};
RN   [1] {ECO:0000313|Proteomes:UP000092631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I48 {ECO:0000313|Proteomes:UP000092631};
RA   Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA   McCoy K.D., Macpherson A.J.;
RT   "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT   Diverse Mouse Microbiota 2 (sDMDMm2).";
RL   Submitted (APR-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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185}.
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DR   EMBL; CP015401; ANU58460.1; -; Genomic_DNA.
DR   RefSeq; WP_065539321.1; NZ_NHMU01000003.1.
DR   AlphaFoldDB; A0A1C7H3R2; -.
DR   GeneID; 82188156; -.
DR   KEGG; bcae:A4V03_13490; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000092631; Chromosome.
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   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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092631}.
FT   DOMAIN          34..477
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          554..682
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   747 AA;  81986 MW;  8CD1DD98CBBD08C0 CRC64;
     MVYDVTMLEA FYAAYKGKVE HVRAILKRPL TLTEKILYAH LYDVADLKDY KRGEDYVNFR
     PDRVAMQDAT AQMALLQFMN AGKDQVAVPS TVHCDHLIQA YKGAKADIAT ARLTNEEVYD
     FLRDVSSRYG IGFWKPGAGI IHQVVLENYA FPGGMMVGTD SHTPNAGGLG MVAIGVGGAD
     AVDVMTGMEW ELKMPKIIGV RLTGKLSGWT SPKDVILKLA GILTVKGGTN AIIEYFGPGT
     ESLSATGKAT ICNMGAEVGA TTSLFPFDGR MATYLRATGR DCVVDWAESV DADLRADDIV
     TDEPFNYYDC VIEIDLSELE PYINGPFTPD AATPISKFAE KVLLNGYPRK MEVGLIGSCT
     NSSYQDLSRA ASLAKQVTEK NLSVASPLIV NPGSEQIRAT AERDGMIEAF ERLGATIMAN
     ACGPCIGQWK RQTDDPTRKN SIVTSFNRNF AKRADGNPNT YAFVASPELT MALTIAGDLC
     FNPLKDRLVN HNGEKMKLSE PVGDELPLKG FEQGNEGYIA PHGAKTEIRV KSDSQRLQLL
     TPFPAWDGQD LLNMPLLIKA QGKCTTDHIS MAGPWLRFRG HLENISDNML MGAVNAFNGE
     TNRVWNRSTN TYGTVSGTAK MYKSEGIPSI VVAEENYGEG SSREHAAMEP RFLNVRVILA
     KSFARIHETN LKKQGMLALT FVDKADYDKI QEHDLLSVSG LVHFAPGRNL MIILHHEDGT
     KESFEVQHTY NVQQIAWFRA GSALNAR
//
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