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Database: UniProt
Entry: A0A0J1DFM7_9BURK
LinkDB: A0A0J1DFM7_9BURK
Original site: A0A0J1DFM7_9BURK 
ID   A0A0J1DFM7_9BURK        Unreviewed;       866 AA.
AC   A0A0J1DFM7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   ORFNames=AB595_05380 {ECO:0000313|EMBL:KLU37855.1};
OS   Massilia sp. WF1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU37855.1, ECO:0000313|Proteomes:UP000036336};
RN   [1] {ECO:0000313|Proteomes:UP000036336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA   Lou J., Gu H., Wang H., Xu J.;
RT   "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT   strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT   contaminated soil.";
RL   Submitted (JUN-2015) 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   -!- 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:KLU37855.1}.
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DR   EMBL; LELH02000006; KLU37855.1; -; Genomic_DNA.
DR   RefSeq; WP_047823129.1; NZ_LELH02000006.1.
DR   AlphaFoldDB; A0A0J1DFM7; -.
DR   PATRIC; fig|1406431.3.peg.4470; -.
DR   Proteomes; UP000036336; Unassembled WGS sequence.
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:UP000036336}.
FT   DOMAIN          66..533
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          657..788
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   866 AA;  94476 MW;  4EF222F998DC7FA8 CRC64;
     MNSQYRKPLH GTNLHYFDAK SAVEEIQPGA WDGLPYTSRV LAENLVRRCE PQALVPSLKQ
     LIERKRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAL QGGNPALVNP VVPTQLVVDH
     SLAVECGGFD PDAFDKNRAI EDRRNEDRFD FINWTKKAFQ NVDVIPPGNG ILHQINLERM
     SPVVQVKDGV AFPDTLVGTD SHTPMVDALG VIAIGVGGLE AESVMLGRAS YMRLPDIVGV
     ELTGAPQPGI TATDIVLALT EFLRKSKVVS AYLEFFGEGS ARLTLGDRAT ISNMAPEYGA
     TAAMFAIDEQ TIKYLKLTGR DDELVKLVEI YARETGLWAD TLARAEYERT LQFDLSTVVR
     NIAGPSNPHK RVPTSELAAQ GIAGKVENEP GLMPDGAVII AAITSCTNTN NPRNMIAAGL
     IARNANKLGL LRKPWVKSSL APGSKAVALY LEEAGLLPEL EKLGFGIVAF ACTTCNGMSG
     ALDPVIQKEV VERDLYATAV LSGNRNFDGR IHPYAKQAFL ASPALVVAYA IAGTIRFDIE
     KDVLGVDAAG REIRLADIWP SDAEIDAVVE QSVKPQQFRN VYDVMFARQE TSEEAVSPLY
     DWRPMSTYIR RPPYWEGALA GERTMKGMRA LAVLGDNITT DHLSPSNAIM MNSAAGEYLH
     KMGLPEEDFN SYATHRGDHL TAQRATFANP TLKNEMVRNP DGSVRAGSLA RIEPEGQVTR
     MWEAIETYME RKQPLIVIAG ADYGQGSSRD WAAKGVRLAG VEAIVAEGFE RIHRTNLVGM
     GVLPLEFMPG TTRLTLGLDG TETYDVVGER TPRAVLTLVI HRRNGETVEV PVTCRLDTAE
     EVSIYEAGGV LQRFAQDFLA TSKVAA
//
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