ID   A0A317FAF4_9PROT        Unreviewed;       285 AA.
AC   A0A317FAF4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:PWS36121.1};
GN   ORFNames=DFH01_13015 {ECO:0000313|EMBL:PWS36121.1};
OS   Falsiroseomonas bella.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Falsiroseomonas.
OX   NCBI_TaxID=2184016 {ECO:0000313|EMBL:PWS36121.1, ECO:0000313|Proteomes:UP000245765};
RN   [1] {ECO:0000313|Proteomes:UP000245765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQN31 {ECO:0000313|Proteomes:UP000245765};
RA   Du Z., Wang X.;
RL   Submitted (MAY-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:PWS36121.1}.
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DR   EMBL; QGNA01000003; PWS36121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317FAF4; -.
DR   Proteomes; UP000245765; 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:PWS36121.1};
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:UP000245765}.
FT   DOMAIN          10..224
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   285 AA;  30021 MW;  08AC0ECBB637E080 CRC64;
     MSAMRAATWR SLLYVPANVP RFVAKAPGAG ADAIILDLED SVPVAQKDAA REGLADAMRI
     CREGPAAVLV RINRPLRLAV RDVEAAVACG ADGILVTKAM DAGHVRLVAE LLDELEGGTP
     RAAILPLIET AAAVARMEEI AAASSRVAAL LCGAEDLAAE MGCTADDEVI ALIKRRMVIA
     AAAAGVTPLG TLGSIADFRD HEKLRDVIAR SRRAGFGGAT CIHPGVVPLL NEGFAPTEKE
     LDLARRQIAA AEEAEREGRG SFEVDGRMVD EPILRRARRI LAAAR
//