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Database: UniProt
Entry: A0A344U507_9ACTN
LinkDB: A0A344U507_9ACTN
Original site: A0A344U507_9ACTN 
ID   A0A344U507_9ACTN        Unreviewed;       275 AA.
AC   A0A344U507;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:AXE25978.1};
GN   ORFNames=C0216_23210 {ECO:0000313|EMBL:AXE25978.1};
OS   Streptomyces globosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE25978.1, ECO:0000313|Proteomes:UP000252004};
RN   [1] {ECO:0000313|EMBL:AXE25978.1, ECO:0000313|Proteomes:UP000252004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LZH-48 {ECO:0000313|EMBL:AXE25978.1,
RC   ECO:0000313|Proteomes:UP000252004};
RA   Ran K., Li Z., Wei S., Dong R.;
RT   "Draft genome Sequence of streptomyces globosus LZH-48.";
RL   Submitted (JAN-2018) 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; CP030862; AXE25978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344U507; -.
DR   KEGG; sgz:C0216_23210; -.
DR   OrthoDB; 4322898at2; -.
DR   Proteomes; UP000252004; 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:AXE25978.1};
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:UP000252004}.
FT   DOMAIN          5..208
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   275 AA;  28748 MW;  A844C61EF7FD54E0 CRC64;
     MILTWLYAPG DHQDTVAKAL HCGADAVIVD LEDAVPASRK EYARAATAEL LAERPPVPVY
     VRVNAPDSPW AGADLAALAG LRGLAGVRLP KVTAPEQVVQ AAERTGGVAL YALLESALGV
     ERAYEIARAH PALRGLALGE ADLCADLGCG TEEGLDWPRS RVVVAARAAG LAPPAQSPFP
     DIRDLEALAA SCARGRTLGF LGRAAIHPRQ LPVIERAYLP GPEEVGAAQE VVTAARRNPG
     AAVLPDGRFV DAAVLAVAER VVALSRRETP VRLPS
//
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