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Database: UniProt
Entry: J3A6F5_9PSED
LinkDB: J3A6F5_9PSED
Original site: J3A6F5_9PSED 
ID   J3A6F5_9PSED            Unreviewed;       865 AA.
AC   J3A6F5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   ORFNames=PMI30_05422 {ECO:0000313|EMBL:EJM60833.1};
OS   Pseudomonas sp. GM50.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1144332 {ECO:0000313|EMBL:EJM60833.1, ECO:0000313|Proteomes:UP000007513};
RN   [1] {ECO:0000313|EMBL:EJM60833.1, ECO:0000313|Proteomes:UP000007513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GM50 {ECO:0000313|EMBL:EJM60833.1,
RC   ECO:0000313|Proteomes:UP000007513};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJM60833.1}.
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DR   EMBL; AKJK01000117; EJM60833.1; -; Genomic_DNA.
DR   RefSeq; WP_008014110.1; NZ_AKJK01000117.1.
DR   AlphaFoldDB; J3A6F5; -.
DR   PATRIC; fig|1144332.3.peg.5228; -.
DR   Proteomes; UP000007513; 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}.
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..787
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   865 AA;  94671 MW;  123EFFBE97B59059 CRC64;
     MNTEFRKPLP GSHLDYFDVR AAVEAIQPGA YDALPYTSRV LAENLVRRCD PATLTESLKQ
     FIERKRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAL QGGDPAQVNP VVPTQLIVDH
     SLAVERGGFD PEAFEKNRAI EDRRNEDRFH FINWTKKAFK NVDVIPPGNG IMHQINLEKM
     SPVIQVRDGV AFPDTCVGTD SHTPHVDALG VIAIGVGGLE AESVMLGRAS WMRLPESVGV
     ELTGKLQPGI TATDMVLALT EYLRKQKVVG AWLEFFGEGA SALTLGDRAT ISNMAPEYGA
     TAAMFYIDQQ TIDYLKLTGR EDEQVQLVEN YAKQTGLWAD SLKGAQYERG LSFDLSSVVR
     NMAGPSNPHA RVATSDLAAQ GISGQWDDVP GQMPDGAVII AAITSCTNTS NPRNVIAAGL
     LARNANKLGL TRKPWVKSSL APGSKTVALY LDEAGLTKEL EQLGFGVVAF ACTTCNGMSG
     ALDPVIQQEI IDRDLYATAV LSGNRNFDGR IHPYAKNAFL ASPPLVVAYA IAGTIRFDIE
     KDVLGLDANG KEIRLKDIWP SDEEIDAVVK ASVKPEQFRQ VYIPMFAIHE DTGPKVTPLY
     DWREMSTYIR RPPYWEGALA GARPLKGMRP LAVLPDNITT DHLSPSNAIM LDSAAGEYLA
     KMGLPEEDFN SYATHRGDHL TAQRATFANP KLFNEMVREN GKVKQGSLAR VEPEGKVMRM
     WEAIETYMER KQPLIIIAGA DYGQGSSRDW AAKGVRLAGV EAIAAEGFER IHRTNLVGMG
     VLPLEFQPGT DRHTLAIDGS ETYDVIGDRT PRATLTLVIN RKNGERVEVP VTCRLDTAEE
     VSIYEAGGVL QRFAQDFLEE SAVAV
//
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