ID F2IYP9_POLGS Unreviewed; 285 AA.
AC F2IYP9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Citrate lyase, beta subunit protein {ECO:0000313|EMBL:ADZ69496.1};
GN OrderedLocusNames=SL003B_1067 {ECO:0000313|EMBL:ADZ69496.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ69496.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ69496.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
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; CP002568; ADZ69496.1; -; Genomic_DNA.
DR RefSeq; WP_013651813.1; NC_015259.1.
DR AlphaFoldDB; F2IYP9; -.
DR STRING; 991905.SL003B_1067; -.
DR KEGG; pgv:SL003B_1067; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_2_5; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000008130; 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:ADZ69496.1};
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:UP000008130}.
FT DOMAIN 2..227
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 127
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 285 AA; 29905 MW; F0A3C86FC70EFEEA CRC64;
MRSLLFVPGV SAKMMAKAAD CAADVVILDL EDAVQPQAKA EARALVAGHL AARPADRRPD
GPRIAVRVNG LDTPWCAADV AAVVPHAPDL LMLPKATGPQ DVARLAGLLA PFESDPGRTG
ILVVATETAE ATVSLLTRSW AHPRLRGLLW GGEDLSVDLG ATANRDEAGA YTEPFRMARN
FCLYGARLAG VPAIDAVYTD FRDTGGLRRE TEAARRDGFA AKAAIHPAQI GAINAVFTPA
EADLAWARAV VDALAVSSTG VAVVDGQMVD APHLARARRL LDAAR
//
