ID A4JK60_BURVG Unreviewed; 864 AA.
AC A4JK60;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN OrderedLocusNames=Bcep1808_3678 {ECO:0000313|EMBL:ABO56663.1};
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO56663.1, ECO:0000313|Proteomes:UP000002287};
RN [1] {ECO:0000313|Proteomes:UP000002287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) 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; CP000615; ABO56663.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JK60; -.
DR KEGG; bvi:Bcep1808_3678; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_4; -.
DR Proteomes; UP000002287; Chromosome 2.
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:ABO56663.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002287}.
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 864 AA; 94035 MW; 93B5A360E67F0FB1 CRC64;
MNTAYRKPLP GTSLDYFDAR AAIDAIAPGA YDTLPYTSRV LAENLVRRCD PAILADSLKQ
IIERKRERDF PWFPARVVCH DILGQTALVD LAGLRDAIAE RGGDPAKVNP VVPVQLIVDH
SLAVECGGFD PDAFAKNRAI EDRRNEDRFH FIEWTKKSFE NVDVIPPGNG IMHQINLEKM
SPVIQVQDGI AYPDTCVGTD SHTPHVDALG VIAIGVGGLE AENVMLGRAS WMRLPDIVGV
ELTGKRQPGI TATDVVLALT EFLRKEKVVG AYLEFRGAGA ASLTLGDRAT ISNMAPEYGA
TAAMFFIDGQ TTDYLRLTGR SDEQVKLVET YAKAAGLWAD TLAHAQYERT LTFDLSSVVR
NMAGPSNPHK RLPTSDLAAR GIAGQWEEKP GEMPDGAVII AAITSCTNTS NPRNVIAAAL
LARNANARGL TRKPWVKSSL APGSKAVELY LKEANLLPEL EKLGFGIVAF ACTTCNGMSG
ALDPKIQQEI VDRDLYATAV LSGNRNFDGR IHPYAKQAFL ASPPLVVAYA IAGTIRFDIE
KDALGHDAHG KPVTLKDIWP TDEEIDAIVA SSVKPEQFRK VYEPMFARTA DAGERAAPLY
EWRPQSTYIR RPPYWEGALA GERTLKGMRP LAVLGDNITT DHLSPSNAIL ATSAAGEYLT
KMGLPEEDFN SYATHRGDHL TAQRATFANP TLVNEMAVVD GAVKKGSLAR VEPDGKVMRM
WEAIETYMNR KQPLIVIAGA DYGQGSSRDW AAKGVRLAGV EAIVAEGFER IHRTNLIGMG
VLPLEFKPGT NRKTLGIDGT ETFDVIGART PRADLTLVIH RRDGERVEVP VTCRLDTAEE
VSIYDAGGVL QRFAQDFLES SQAA
//
