ID B1Z1L0_BURA4 Unreviewed; 334 AA.
AC B1Z1L0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:ACB66291.1};
GN OrderedLocusNames=BamMC406_3824 {ECO:0000313|EMBL:ACB66291.1};
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB66291.1, ECO:0000313|Proteomes:UP000001680};
RN [1] {ECO:0000313|Proteomes:UP000001680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP001026; ACB66291.1; -; Genomic_DNA.
DR RefSeq; WP_012365676.1; NC_010552.1.
DR AlphaFoldDB; B1Z1L0; -.
DR KEGG; bac:BamMC406_3824; -.
DR HOGENOM; CLU_073837_0_0_4; -.
DR OrthoDB; 8481499at2; -.
DR Proteomes; UP000001680; Chromosome 2.
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 49..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 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 334 AA; 35659 MW; 4C505C1435F87F0E CRC64;
MSALTPAQVL YDGASPPAIL PCCDHYAGSE KLMRKSLALQ AELGPVFDIT LDCEDGAAVG
QEAAHAQLVA ELLGSAENRF GRVGVRIHDF SHPHWRDDVR IVLRAARAPA YVTLPKIASA
ADAAEMVAFI EGTRRELGLA QPIPVDVLVE THGALAQAAA LAALPLVGTL SFGLMDFVSA
HHGAIPDAAM RSPGQFDHPL VRRAKLEIAA ACHAHGKTPS HNVTTEVRDM AVVAGDARRA
RDEFAFTRMW SIHPAQIRPI VAAFAPRTDE VALAAEILLA AQAADWGPTR HGDTLHDRAS
YRYYWSVLRR ARATGQPVPA EAAPLFGPAA GDAR
//
