ID A0A0Q5H5Y3_9BURK Unreviewed; 866 AA.
AC A0A0Q5H5Y3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=ASF77_09315 {ECO:0000313|EMBL:KQQ88905.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ88905.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ88905.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ88905.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ88905.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ88905.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQQ88905.1}.
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DR EMBL; LMOJ01000022; KQQ88905.1; -; Genomic_DNA.
DR RefSeq; WP_056339271.1; NZ_LMOJ01000022.1.
DR AlphaFoldDB; A0A0Q5H5Y3; -.
DR STRING; 1736272.ASF77_09315; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000051760; 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:UP000051760}.
FT DOMAIN 66..533
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 658..788
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 866 AA; 94623 MW; 73F16F6FCA558619 CRC64;
MNNAYRKPLH GTNLHYFDAR QAVEDIQAGA WDGLPYTSRV LAENLVRRCE PMALVPSLKQ
LIERKRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAQ EGGNPALVNP VVPTQLVVDH
SLAVECGGFD PDAFAKNRAI EDRRNEDRFH FIEWTKKAFQ NVDVIPPGNG ILHQINLERM
SPVVQVKDGV AFPDTLVGTD SHTPMVNALG VIAIGVGGLE AESVMLGRAS YMRLPDIVGV
ELTGKPQPGI TATDVVLALT EFLRASKVVS TYLEFFGAGA SNLTLGDRAT ISNMAPEFGA
TAAMFYIDEQ TIKYLRLTGR EDEQVKLVED YAKETGLWAD TLTNVDYERV LRFDLSTVVR
NIAGPSNPHK RVPTSELAAR GISGVVENEP GKMPDGAVII AAITSCTNTN NPRNMIAAGL
IARNANKLGL QRKPWVKSSL APGSKAVSLY LEEAGLLPEM EKLGFGVVAF ACTTCNGMSG
ALDPVIQQEI IARDLYATAV LSGNRNFDGR IHPYAKQAFL ASPPLVIAYA IAGTIRFDIE
KDVLGTDAQG NPVKLADIWP SDEEIDAVIE QSVKPEQFRK VYTPMFARVA DDGEQVSPLY
DWREMSTYIR RPPYWEGALA GERSLSGMRA LAVLGDNITT DHLSPSNAIM MDSAAGEYLF
KMGLPEEDFN SYATHRGDHL TAQRATFANP TLKNEMVRNP DGSVRAGSLA RIEPEGQVTR
MWEAIETYME RKQPLIVIAG ADYGQGSSRD WAAKGVRLAG VEAIVAEGFE RIHRTNLVGM
GVLPLEFMPG VNRLTLGLDG TETYDVLGER TPRATLRLVI NRRSGERIEV PVTCRLDTAE
EVSIYEAGGV LQRFAQDFLA SSKVAA
//
