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
//