ID A0A397P3S7_9SPHN Unreviewed; 275 AA.
AC A0A397P3S7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Citrate lyase subunit beta/citryl-CoA lyase {ECO:0000313|EMBL:RIA43902.1};
GN ORFNames=DFR49_2134 {ECO:0000313|EMBL:RIA43902.1};
OS Hephaestia caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Hephaestia.
OX NCBI_TaxID=645617 {ECO:0000313|EMBL:RIA43902.1, ECO:0000313|Proteomes:UP000266568};
RN [1] {ECO:0000313|EMBL:RIA43902.1, ECO:0000313|Proteomes:UP000266568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25527 {ECO:0000313|EMBL:RIA43902.1,
RC ECO:0000313|Proteomes:UP000266568};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RIA43902.1}.
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DR EMBL; QXDC01000003; RIA43902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397P3S7; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000266568; Unassembled WGS sequence.
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:RIA43902.1};
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:UP000266568}.
FT DOMAIN 5..218
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 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 275 AA; 28750 MW; D829A32E84933A19 CRC64;
MPRLRSLLFV PGDRPDRMEK ALGLGADALI LDLEDAVAPD AKPAAREAVA AFLGTPRAMP
LFVRINPLDS DFIADDLAAM LPAAPDGIVL PKAEGASSLK ALDSWLPENM LILPIATETP
AAIFSAGTYG GITDRLAGLT WGAEDLPAAI GAATAREADG RFTPPYELAR ALTLFGAHAA
GVPAIETVYP DFRDLDGLAA YAARGRRDGF TGMMAIHPTQ VPVINAAFTP GDDEIAHARR
IVDLFATNPG AGALSLDGKM VDAPHLKAAQ RLLGL
//
