ID G4R604_PELHB Unreviewed; 277 AA.
AC G4R604;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:AEQ51119.1};
GN OrderedLocusNames=KKY_1085 {ECO:0000313|EMBL:AEQ51119.1};
OS Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS B2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Devosiaceae; Pelagibacterium.
OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ51119.1, ECO:0000313|Proteomes:UP000008850};
RN [1] {ECO:0000313|EMBL:AEQ51119.1, ECO:0000313|Proteomes:UP000008850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC {ECO:0000313|Proteomes:UP000008850};
RX PubMed=22156395; DOI=10.1128/JB.06343-11;
RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL J. Bacteriol. 194:197-198(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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DR EMBL; CP003075; AEQ51119.1; -; Genomic_DNA.
DR RefSeq; WP_014130268.1; NC_016078.1.
DR AlphaFoldDB; G4R604; -.
DR STRING; 1082931.KKY_1085; -.
DR KEGG; phl:KKY_1085; -.
DR PATRIC; fig|1082931.4.peg.1074; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_2_5; -.
DR Proteomes; UP000008850; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AEQ51119.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008850}.
FT DOMAIN 4..219
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 277 AA; 29264 MW; F50A71A7E3468868 CRC64;
MRLRSLLFVP GDRPDRMEKA LKSGADAVIV DLEDSVLPER KPWARKDVAQ FLSSASREVT
VMVRVNPLGS SDLAADLEAI LPAKPEALVL PKSESGTSVA ELAAMLGLAH IPILPIATET
PKAVFGLGTY GAVASRLCGL TWGAEDLPAA IGATTARRPG GSYTPPYELV RSLTLFGAHA
AGVPAIETVY TDFIDTQGLR AYAARARRDG FSGMMAIHPT QIAVINAAFA PTEAEIAHAR
AVIAAFAENP GAGAIKLNDK MIDRPHLLAA QRLLARL
//
