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Database: UniProt
Entry: I5D0C3_9BURK
LinkDB: I5D0C3_9BURK
Original site: I5D0C3_9BURK 
ID   I5D0C3_9BURK            Unreviewed;       335 AA.
AC   I5D0C3;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:EIN01592.1};
GN   ORFNames=WQE_08422 {ECO:0000313|EMBL:EIN01592.1};
OS   Paraburkholderia hospita BS001.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1171375 {ECO:0000313|EMBL:EIN01592.1};
RN   [1] {ECO:0000313|EMBL:EIN01592.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS001 {ECO:0000313|EMBL:EIN01592.1};
RX   PubMed=22843604; DOI=10.1128/JB.00725-12;
RA   Nazir R., Hansen M.A., Sorensen S., van Elsas J.D.;
RT   "Draft Genome Sequence of the Soil Bacterium Burkholderia terrae Strain
RT   BS001, Which Interacts with Fungal Surface Structures.";
RL   J. Bacteriol. 194:4480-4481(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EIN01592.1}.
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DR   EMBL; AKAU01000055; EIN01592.1; -; Genomic_DNA.
DR   AlphaFoldDB; I5D0C3; -.
DR   PATRIC; fig|1171375.3.peg.1710; -.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.960; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR040186; Citramalyl-CoA_lyase.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR11105:SF0; CITRAMALYL-COA LYASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11105; CITRATE LYASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          82..241
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   335 AA;  36764 MW;  295A7EF5FABFF828 CRC64;
     MRALTPAEVL FDGEAPPTVL PACDHYAGSE KLMLKSLALQ QELGPVFDIT LDCEDGAQVG
     REAEHAELVA SLLGGEHDRF GRVGVRIHDF NHAHWRDDVR LILRAAKRAP AFITLPKIRN
     VPDAAEMCAF IEATRRELGI AKPVPVELLI ETHGALTRVF DLAALPAVES LSFGLMDFVS
     AHDGAIPDTA MRSPGQFDHP LVRRAKLEIS AACHAHGKVP SHNVSTEVRD MDVVANDALR
     ARNEFGYTRM WSIHPAQIPA IVSAFAPRDE EIATATEILL AAQSAQWGPT RHRDTLHDRA
     SYRYYWSVLR RARSTGRSVP AEAAPLFGPN EESAS
//
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