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Database: UniProt
Entry: F3ZP74_9BACE
LinkDB: F3ZP74_9BACE
Original site: F3ZP74_9BACE 
ID   F3ZP74_9BACE            Unreviewed;       747 AA.
AC   F3ZP74;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=Bcop_0082 {ECO:0000313|EMBL:EGJ70301.1};
OS   Bacteroides coprosuis DSM 18011.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ70301.1, ECO:0000313|Proteomes:UP000018439};
RN   [1] {ECO:0000313|EMBL:EGJ70301.1, ECO:0000313|Proteomes:UP000018439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ70301.1,
RC   ECO:0000313|Proteomes:UP000018439};
RX   PubMed=21677860; DOI=10.4056/sigs.1784330;
RA   Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA   Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT   strain (PC139).";
RL   Stand. Genomic Sci. 4:233-243(2011).
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; CM001167; EGJ70301.1; -; Genomic_DNA.
DR   RefSeq; WP_006743459.1; NZ_CM001167.1.
DR   AlphaFoldDB; F3ZP74; -.
DR   STRING; 679937.Bcop_0082; -.
DR   eggNOG; COG1048; Bacteria.
DR   HOGENOM; CLU_006714_2_2_10; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000018439; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018439}.
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;  82241 MW;  3CDA82BF763975F5 CRC64;
     MVHDIEMIRN FYKAYPSKIA KVRSVLNRPL TLAEKIIYVH LFKDEDLKNY ERGVDYVNFR
     PDRVAMQDAT AQMALLQFMN AGKEKVAVPS TVHCDHLIQA YQGSKKDLQI ANKTNGEVYD
     FLRDVSSRYN IGFWEPGSGI IHQIVLENYA FPGGMMVGTD SHTPNAGGLG MVAIGVGGAD
     AVDVMTGMEW ELKMPKLIGV KLIGKLNGWA APKDVILKLA GILTVKGGTN AIIEYFGEGT
     KSLSGTGKGT ICNMGAEVGA TTSLFPYDDR MGVYLNATNR EEVAKLANTV EKDLRPDPEV
     EADPEKYYDR VIEIDLSQLE PYINGPFTPD AATPISEFAE KVKKNDYPRK MEVGLIGSCT
     NSSYEDITRA VSVAKQAVNK GIKVASPFIV NPGSEKIRAT IERDGMLDVF DKVGATIMAN
     ACGPCIGQWK RHTDDPTRKN SIVTSFNRNF AKRADGNPNT HAFVASPELV TALTIAGDLC
     FNPLTDKLKN DKGELVKLEE PSGYELPPKG FEDGSAGYTA PTGAKKEINV ASDSQRLQLL
     QPFPKWNGGD LVDMPLLIKA KGKCTTDHIS MAGPWLRFRG HLENISDNML MGAINAFNDE
     ANKVWNQLTS TYETVSGTAK QYKAKEISSI VVAEDNYGEG SSREHAAMEP RFLNVKAILA
     KSFARIHETN LKKQGMLAIT FINPADYNKI QEKDKLSIIG LKDFAPNKNL KVVVTHTDGS
     KDEFEVQHTY NQQQIEWFRA GSALNAR
//
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