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Database: UniProt
Entry: A0A1C6PML7_9ACTN
LinkDB: A0A1C6PML7_9ACTN
Original site: A0A1C6PML7_9ACTN 
ID   A0A1C6PML7_9ACTN        Unreviewed;       327 AA.
AC   A0A1C6PML7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SCK44612.1};
GN   ORFNames=H181DRAFT_03946 {ECO:0000313|EMBL:SCK44612.1};
OS   Streptomyces sp. WMMB 714.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1286822 {ECO:0000313|EMBL:SCK44612.1, ECO:0000313|Proteomes:UP000182206};
RN   [1] {ECO:0000313|Proteomes:UP000182206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMMB 714 {ECO:0000313|Proteomes:UP000182206};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) 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; FMHJ01000010; SCK44612.1; -; Genomic_DNA.
DR   RefSeq; WP_045865828.1; NZ_FMHJ01000010.1.
DR   AlphaFoldDB; A0A1C6PML7; -.
DR   STRING; 1286822.GCA_000964305_03924; -.
DR   OrthoDB; 9768429at2; -.
DR   Proteomes; UP000182206; 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:SCK44612.1};
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:UP000182206}.
FT   DOMAIN          18..248
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   327 AA;  35723 MW;  130FAFF1E7C7174F CRC64;
     MTAPSPDATP ASRLRPRRSC LAVPGSNPRF LEKAQGLPAD QVFLDLEDAC APLAKEGARH
     TIVKFLNEGD WSGKTRVVRV NDWTTHWTYR DVITVVEGAG HNLDCIMLPK VQDAQQVHAL
     DMLLTQIETT MGFEVGRIGI EAQIENAKGL VNVDEIAAAS PRMETIVFGP ADFMASINMK
     SLVVGEQPPG YPADAYHYIL MRILMAARTH DLQAIDGPYL MIKNLDGFRE VAGRAAAIGF
     DGKWVLHPSQ VEASNEIFSP SQDDYDHAEM ILDAYEYFTS EKGGKKGSAM LGDEMIDEAS
     RKMALVIAGK GRAAGMARTK SFEAPEA
//
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