ID   A0A437MNG5_9PROT        Unreviewed;       313 AA.
AC   A0A437MNG5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:RVT99195.1};
GN   ORFNames=EOD42_03595 {ECO:0000313|EMBL:RVT99195.1};
OS   Rhodovarius crocodyli.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Rhodovarius.
OX   NCBI_TaxID=1979269 {ECO:0000313|EMBL:RVT99195.1, ECO:0000313|Proteomes:UP000282957};
RN   [1] {ECO:0000313|EMBL:RVT99195.1, ECO:0000313|Proteomes:UP000282957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP-6 {ECO:0000313|EMBL:RVT99195.1,
RC   ECO:0000313|Proteomes:UP000282957};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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:RVT99195.1}.
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DR   EMBL; SACL01000001; RVT99195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437MNG5; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000282957; 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:SF10; CITRATE LYASE SUBUNIT BETA; 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:RVT99195.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282957}.
FT   DOMAIN          17..249
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         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   313 AA;  33821 MW;  26881FE507FCD9B8 CRC64;
     MSFRTVVEAT PRLHRSELAV PASRPAIFEK AAASAADLVF LDLEDAVAPD EKEAARRNAI
     DALRTIDWGS KIMAVRINGL DTHYMYRDVV DLIEQAGERL DLFIVPKVGD AKDVYALDML
     TSQVEAAMGR RKRMGFSLIV ETALGLANVE RIAEESPRIE ALQMGVADLA ASLRMRTTNI
     GGPVDDYASA AGVLDAWQFP MSRVIAAARA AGRRPIAGPF GNFKDAEGLE AAARRARALG
     AEGMMAIHPS QIGIINTVFT PSEAEIRQAR RILEAMEEAT RAGRGAVALD GRLLDIASIR
     QAEALLEKVK MLG
//