ID   A0A221R3Z5_9MICC        Unreviewed;       280 AA.
AC   A0A221R3Z5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:ASN51594.1};
GN   ORFNames=CGQ25_05525 {ECO:0000313|EMBL:ASN51594.1};
OS   Sinomonas sp. R1AF57.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Sinomonas.
OX   NCBI_TaxID=2020377 {ECO:0000313|EMBL:ASN51594.1, ECO:0000313|Proteomes:UP000199767};
RN   [1] {ECO:0000313|EMBL:ASN51594.1, ECO:0000313|Proteomes:UP000199767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1AF57 {ECO:0000313|EMBL:ASN51594.1,
RC   ECO:0000313|Proteomes:UP000199767};
RA   Sastre D.E., Santos L., Kagohara E., Andrade L.H.;
RT   "Draft Genome Sequence of Sinomonas sp., Isolated from Brazilian Amazon
RT   Soils with Potential for Applications in Biocatalysis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP022463; ASN51594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221R3Z5; -.
DR   Proteomes; UP000199767; 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: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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:ASN51594.1};
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:UP000199767}.
FT   DOMAIN          15..220
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   280 AA;  28699 MW;  169191FCD5CCE828 CRC64;
     MTPISSPGFS MGPALLFCPA DRPERFAKAA ERADAVILDL EDAVSPDAKA EARLNLAEVP
     LDPERTIVRV NSAGPTLSSG DFEADLEALE ATPYRTVMLA KAESADQLAL LRQYRVIALC
     ETAAGVLAAP SIAAEPNAVA LMWGAEDLVA SLGGTSSRAG DGAYRAVALH ARSSVLLAAG
     ACGKAAIDAV YTDIPDLDGL AAESADAVAS GFAAKACIHP SQVGAVRAAY APTPEAVEAA
     RELLAAAQEA GAGVFQFHGK MIDGPILRHA EAVLRRAGLD
//