ID   A0A101JE50_9ACTN        Unreviewed;       324 AA.
AC   A0A101JE50;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:KUL25110.1};
GN   ORFNames=ADL12_35965 {ECO:0000313|EMBL:KUL25110.1};
OS   Streptomyces regalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL25110.1, ECO:0000313|Proteomes:UP000053923};
RN   [1] {ECO:0000313|Proteomes:UP000053923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (OCT-2015) 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:KUL25110.1}.
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DR   EMBL; LLZG01000373; KUL25110.1; -; Genomic_DNA.
DR   RefSeq; WP_062710442.1; NZ_LLZG01000373.1.
DR   AlphaFoldDB; A0A101JE50; -.
DR   OrthoDB; 9768429at2; -.
DR   Proteomes; UP000053923; 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:KUL25110.1};
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:UP000053923}.
FT   DOMAIN          15..245
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         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   324 AA;  35570 MW;  8E27F8E0781BABA4 CRC64;
     MTTPAPQVNR LRPRRSCLAV PGSNPRFLEK AQGLPADQVF LDLEDACAPL AKPEARHTIV
     KFLNEGDWTG KTRVVRVNDW TTEWTYRDVV TVVEGAGQNL DCIMLPKVQT AEQIVALDLL
     LTQIEKTMGF EVGKIGIEAQ IENAQGLNNV NEIATASQRV ETIIFGPADF MASINMKSLV
     VGEQPPGYPA DAYHYILMKI LMAARANNLQ AIDGPYLQIR NIDGYREVAQ RAAALGFDGK
     WVLHPGQVEA SNEIFSPSQE DYDHAELILD AYDYYTSEAG GKKGSAMLGD EMIDEASRKM
     ALVIAGKGRA AGMQRTGKFE IPEA
//