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
//