ID   A0A1N7SUD3_9BURK        Unreviewed;       287 AA.
AC   A0A1N7SUD3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:SIT50952.1};
GN   ORFNames=BN2476_960103 {ECO:0000313|EMBL:SIT50952.1};
OS   Paraburkholderia piptadeniae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT50952.1, ECO:0000313|Proteomes:UP000195569};
RN   [1] {ECO:0000313|EMBL:SIT50952.1, ECO:0000313|Proteomes:UP000195569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM 7183 {ECO:0000313|EMBL:SIT50952.1,
RC   ECO:0000313|Proteomes:UP000195569};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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; CYGY02000096; SIT50952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7SUD3; -.
DR   Proteomes; UP000195569; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
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; PTHR32308:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-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|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          13..221
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   287 AA;  30669 MW;  09F00F58B67D2385 CRC64;
     MADMKSFDSA VTYLFVPGTR SERFEKAVRS GADVVILDLE DAVAPADKPI ARSAVLESWA
     SLNEVANEIG VALCIRVNSP REKTGRDDLA LCHLLKPSLI MVPKVESEAE LVSVSSEVPS
     ARVLALIETA NGVMEARKIA SAPNVARLVL GSVDLMVNLG VTDDREPLDW TRSMLVLASA
     GAGIAGPVDG VCTSINDLER VRLDTERART FGFTSKLCIH PKQIPAVSDA FKVTDEEVAW
     AKRVIDASES SAGAATAVDG AMVDVPVLLR AQRIVSRHDA IRRTAPD
//