ID   A0A317KHR8_9ACTN        Unreviewed;       318 AA.
AC   A0A317KHR8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:PWU52867.1};
GN   ORFNames=DKL51_27400 {ECO:0000313|EMBL:RQW86574.1}, DLJ46_02205
GN   {ECO:0000313|EMBL:PWU52867.1};
OS   Micromonospora globispora.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1450148 {ECO:0000313|EMBL:PWU52867.1, ECO:0000313|Proteomes:UP000245683};
RN   [1] {ECO:0000313|EMBL:PWU52867.1, ECO:0000313|Proteomes:UP000280363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2901 {ECO:0000313|EMBL:RQW86574.1,
RC   ECO:0000313|Proteomes:UP000280363}, and S2904
RC   {ECO:0000313|EMBL:PWU52867.1};
RA   Carro L., Veyisoglu A., Cetin D., Klenk H.-P., Trujillo M.E., Sahin N.;
RT   "Micromonospora globispora sp. nov. and Micromonospora rugosa sp. nov.,
RT   isolated from marine sediment.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000245683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2904 {ECO:0000313|Proteomes:UP000245683};
RA   Carro L., Aysel V., Cetin D., Igual J.M., Klenk H.-P., Trujillo M.E.,
RA   Sahin N.;
RT   "Micromonospora globispora sp. nov. and Micromonospora rugosa sp. nov.,
RT   isolated from marine sediment.";
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   -!- 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:PWU52867.1}.
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DR   EMBL; QGSV01000057; PWU52867.1; -; Genomic_DNA.
DR   EMBL; QGGF01000504; RQW86574.1; -; Genomic_DNA.
DR   OrthoDB; 9768429at2; -.
DR   Proteomes; UP000245683; Unassembled WGS sequence.
DR   Proteomes; UP000280363; 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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:PWU52867.1};
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:UP000245683}.
FT   DOMAIN          11..240
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   318 AA;  33968 MW;  9971CC3A84C8340A CRC64;
     MNTLRPARPR RSCLAVPGSS EKMLKKAQGL PADQVFLDLE DSVAPIAKPP ARANIIQALN
     HGDWSGKTRV VRINDADTKW AHEDVLTVVR GAGANLDCIM LPKVERVAHI HWLDVLLTQV
     ERELALPDGG IGIEAQIEGP AGLSEIDAIA AATSRTETLI FGPGDFMAAM KMPALTIGVP
     GATGYDPFDT VLMTIAMTAR KYGLQAIDGP FALIKDTEGY RASAERAAAY GYDGKWVLHP
     GQIDTANTVF APSQDDYDKA ELIIEAYAHH TSASGGGVGA AMLGDEMIDE ASRKVALVTA
     ERGRVLGMSR TTYFDPTA
//