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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//