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Database: UniProt
Entry: Q0B634_BURCM
LinkDB: Q0B634_BURCM
Original site: Q0B634_BURCM 
ID   Q0B634_BURCM            Unreviewed;       865 AA.
AC   Q0B634;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   OrderedLocusNames=Bamb_4840 {ECO:0000313|EMBL:ABI90389.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI90389.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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; CP000441; ABI90389.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0B634; -.
DR   KEGG; bam:Bamb_4840; -.
DR   eggNOG; COG1048; Bacteria.
DR   Proteomes; UP000000662; 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:ABI90389.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          66..534
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          658..789
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   865 AA;  94086 MW;  A5BB8AD9789176A5 CRC64;
     MMNTAYRKPL PGTSLDYFDA RAAVEAIAPG AYDTLPYTSR VLAENLVRRC DPAILADSLK
     QIIERKRDRD FPWFPARVVC HDILGQTALV DLAGLRDAIA DGGGDPAKVN PVVPVQLIVD
     HSLAVECGGF DPDAFAKNRA IEDRRNEDRF HFIEWTKKAF ENVDVIPPGN GIMHQINLEK
     MSPVIQAQDG VAFPDTCVGT DSHTPHVDAL GVIAIGVGGL EAENVMLGRA SWMRLPDIVG
     VELTGKRQPG ITATDVVLAL TEFLRKEKVV GAYLEFRGEG AASLTLGDRA TISNMAPEYG
     ATAAMFFIDG QTTDYLRLTG RSDEQVKLVE TYAKTAGLWA DTLGNVQYER TLTFDLSSVV
     RNMAGPSNPH KRLPTSDLAA RGIAGQWEEK PGEMPDGAVI IAAITSCTNT SNPRNVIAAA
     LLARNANAKG LTRKPWVKSS LAPGSKAVEL YLEEANLLPE LEKLGFGIVA FACTTCNGMS
     GALDPKIQQE IVDRDLYATA VLSGNRNFDG RIHPYAKQAF LASPPLVVAY AIAGTIRFDI
     EKDVLGHDQD GKPVTLKDIW PTDEEIDAIV ASSVKPEQFR KVYEPMFART ADAGERAAPL
     YDWRAQSTYI RRPPYWEGAL AGERTLKGMR PLAVLGDNIT TDHLSPSNAI LLDSAAGEYL
     AKMGLPEEDF NSYATHRGDH LTAQRATFAN PTLINEMAVV DGAVKKGSLA RVEPEGKVMR
     MWEAIETYMN RKQPLIVIAG ADYGQGSSRD WAAKGVRLAG VEAIVAEGFE RIHRTNLIGM
     GVLPLEFKPG TNRTTLGIDG TETFDVIGKR TPRADLTLVI QRKNGERVEV PVTCRLDTAE
     EVSIYDAGGV LQRFAQDFLE SSQAA
//
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