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Database: UniProt
Entry: M5DRM0_9GAMM
LinkDB: M5DRM0_9GAMM
Original site: M5DRM0_9GAMM 
ID   M5DRM0_9GAMM            Unreviewed;       868 AA.
AC   M5DRM0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   ORFNames=TOL_1637 {ECO:0000313|EMBL:CCU72061.1};
OS   Thalassolituus oleivorans MIL-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Thalassolituus.
OX   NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU72061.1, ECO:0000313|Proteomes:UP000011866};
RN   [1] {ECO:0000313|EMBL:CCU72061.1, ECO:0000313|Proteomes:UP000011866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIL-1 {ECO:0000313|EMBL:CCU72061.1,
RC   ECO:0000313|Proteomes:UP000011866};
RX   PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA   Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA   Yakimov M.M., Teeling H., Golyshina O.V.;
RT   "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL   Genome Announc. 1:1-3(2013).
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   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185}.
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DR   EMBL; HF680312; CCU72061.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5DRM0; -.
DR   STRING; 187493.CN03_10005; -.
DR   KEGG; tol:TOL_1637; -.
DR   PATRIC; fig|1298593.3.peg.1568; -.
DR   eggNOG; COG1048; Bacteria.
DR   HOGENOM; CLU_013476_2_1_6; -.
DR   Proteomes; UP000011866; Chromosome.
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:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
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; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR02333; 2met_isocit_dHY; 1.
DR   PANTHER; PTHR11670:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 1.
DR   PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 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.
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:UP000011866}.
FT   DOMAIN          69..541
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          663..795
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   868 AA;  94804 MW;  A45F51AFA194A508 CRC64;
     MINMNTEFRK PLPNSVLEYY DTRAAVDAIK PGAYAKLPYT SRILAEQLVR RCDPAVLTES
     LVQLIDRKRD LDFPWYPARV VTHDILGQTA LVDLAGLRDA IAEQGGDPSK VNPVVQTQLI
     VDHSLAVECG GFDPDAFQKN RDIEERRNED RFHFIEWTKT AFDNVDVIPA GNGIMHQINL
     EKMSPVVQAR DGVAYPDTCV GTDSHTPHVD ALGVISVGVG GLEAETVMLG HPSMMRLPDI
     VGVELTGKRQ SGITATDIVL ALTEFLRKER VVGAYLEFYG EGASSLTIGD RATISNMTPE
     YGATAAMFSI DEQTIEYLTL TGREPEQVAL VEAFAKETGL WADDLKTAEY ERVLSFDLSS
     VGRNIAGPSN PHARVSTADL AAKGISGNLA SAQAEEAQGL MPDGAVIIAA ITSCTNTSNP
     RNVVAAGLLA KKANELGLVR KPWVKSSFAP GSKVAELYLK DSGLLPELEK LGFGIVAFAC
     TTCNGMSGAL DPVIQQEIID RDLYATAVLS GNRNFDGRIH PYAKQAFLAS PPLVVAYAIA
     GTIRFDIEQD VLAVVDGKEI RLKDIWPSDE EIDAIVKASV KPEQFREIYI PMFDLGEFKK
     ADSPLYDWRP MSTYIRRPPY WEGALAGERS LKGMRPLAVL PDNITTDHLS PSNAILMNSA
     AGEYLHKMGV PEEDFNSYAT HRGDHLTAQR ATFANPKLLN EMVLDDNGNV QQGSLARIEP
     EGKVTRMWEA IETYMERKQP LIIVAGADYG QGSSRDWAAK GVRLAGVEAI AAEGFERIHR
     TNLIGMGVLP LEFKPGTTRK TLGLDGTETY DVIGERSARC DLTLVITRKN GEVVEVPMTC
     RLDTADEVIT YDAGGVLQKF AQDFLKNA
//
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