ID B2UHC2_RALPJ Unreviewed; 865 AA.
AC B2UHC2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN OrderedLocusNames=Rpic_3859 {ECO:0000313|EMBL:ACD28973.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD28973.1};
RN [1] {ECO:0000313|EMBL:ACD28973.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD28973.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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}.
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DR EMBL; CP001069; ACD28973.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UHC2; -.
DR STRING; 402626.Rpic_3859; -.
DR KEGG; rpi:Rpic_3859; -.
DR PATRIC; fig|402626.5.peg.101; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_4; -.
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 Lyase {ECO:0000313|EMBL:ACD28973.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 64..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 865 AA; 94659 MW; F77B9E251AEC1E77 CRC64;
MNTTHRKPLP GTKLDYFDAR EAVEAIKQGA YDKLPYTSRV LAENLVRRCD PATLTDSLKQ
LIERKRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAD QGGDPAKVNP VVPVQLIVDH
SLAVECGGFD PDAFAKNRAI EDRRNEDRFH FIDWTKLAFK NVDVIPAGNG IMHQINLEKM
SPVIQAHDGV AYPDTCVGTD SHTPHVDALG VIAIGVGGLE AENVMLGRAS WMRLPDIVGV
ELTGQRQPGI TATDIVLALT EFLRKQKVVG AYLEFYGEGA SKLTLGDRAT ISNMAPEYGA
TAAMFSIDDN TLDYLRLTGR TDEQVKLVET YAKTAGLWSD TLKHAEYERV LRFDLSSVVR
NMAGPSNPHA RVATTDLAAK GIAGKWEETP GQMPDGAVII AAITSCTNTS NPRNVIAAAL
LARNANRLGL TRKPWVKSSL APGSKAVELY LEEAGLKHEL EKLGFGIVAF ACTTCNGMSG
ALDPKIQQEI IDRDLYATAV LSGNRNFDGR IHPYAKQAFL ASPPLVVAYA IAGTVRFDIE
RDSFGTDANG KPILLKDLWP TDEEIDAIVR ASVKPEQFRT VYIPMFEQRS ESTAKVSPLY
NWRPQSTYIR RPPYWEGALA GERTLKGLRP LAVLGDNITT DHLSPSNAIL ASSAAGEYLA
KMGLPEEDFN SYATHRGDHL TAQRATFANP TLINEMAVVD GAVKKGSLAR IEPEGKVTRM
WEAIETYMDR KQPLIVIAGA DYGQGSSRDW AAKGVRLAGV EAIVAEGFER IHRTNLIGMG
VLPLEFKPGT TRLTLSIDGT ETYDVIGERK PRADLTLVIH RKNGERVEVP VTCRLDSDEE
VSIYEAGGVL QRFAQDFLES SKEAA
//
