ID   A0A367A4L8_9ACTN        Unreviewed;       311 AA.
AC   A0A367A4L8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:RBY83651.1};
GN   ORFNames=DQ238_00775 {ECO:0000313|EMBL:RBY83651.1};
OS   Geodermatophilus sp. TF02-6.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=2250575 {ECO:0000313|EMBL:RBY83651.1, ECO:0000313|Proteomes:UP000253027};
RN   [1] {ECO:0000313|EMBL:RBY83651.1, ECO:0000313|Proteomes:UP000253027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF02-6 {ECO:0000313|EMBL:RBY83651.1,
RC   ECO:0000313|Proteomes:UP000253027};
RA   Ennis N., Dharumadurai D., Sevigny J., Hall J., Simposon S., Morris K.,
RA   Thomas W.K., Tisa L.S.;
RT   "Genome Sequence of Geodermatophilus sp. TF02-6.";
RL   Submitted (JUL-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:RBY83651.1}.
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DR   EMBL; QOHF01000001; RBY83651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367A4L8; -.
DR   OrthoDB; 4322898at2; -.
DR   Proteomes; UP000253027; 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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:RBY83651.1};
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:UP000253027}.
FT   DOMAIN          5..227
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   REGION          291..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68
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         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   311 AA;  33019 MW;  CBC559C0CD9C063F CRC64;
     MVPYRTVLFV PGHKPAWVDK ALSAGADCVV LDLEDSVPAD LKEGARRTVA DSIRAVRRAE
     PRVGLFVRVN PLDTRTTGAD LEAVVVPGLT GVFAPKVGAA TDVLRYDALL DHFEDRNGVS
     GLEYIVPVET IGAIQDAREI AQASPRVGAM IGPTAEHADI ARAVGYRWTP EGEETLYLRS
     RVLLACREAG IHPLTGLWER LDDLAGLAAF AEHGRQLGFR GMVVIHPGHV PVVNDAFTPS
     AEDVAFHEGL VAAYERAAAE GSGAVRYRGV HIDKAHVDTA REWLAHARAL PGGGGPAPAD
     ALGIDAPEGG H
//