ID A0A1Q4WE73_9ACTN Unreviewed; 320 AA.
AC A0A1Q4WE73;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:OKI08403.1};
GN ORFNames=AMK13_07620 {ECO:0000313|EMBL:OKI08403.1};
OS Streptomyces sp. CB02056.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI08403.1, ECO:0000313|Proteomes:UP000186379};
RN [1] {ECO:0000313|EMBL:OKI08403.1, ECO:0000313|Proteomes:UP000186379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02056 {ECO:0000313|EMBL:OKI08403.1,
RC ECO:0000313|Proteomes:UP000186379};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI08403.1}.
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DR EMBL; LIPD01000003; OKI08403.1; -; Genomic_DNA.
DR RefSeq; WP_049655662.1; NZ_LIPD01000003.1.
DR AlphaFoldDB; A0A1Q4WE73; -.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000186379; 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:OKI08403.1};
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:UP000186379}.
FT DOMAIN 11..241
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 320 AA; 34987 MW; 22E43882580E7C10 CRC64;
MTAVNRLRPR RSCLAVPGSN PRFLEKAQGL PADQVFLDLE DACAPLVKES ARHNIVDALN
NGDWGGKTRV VRVNDWTTHW TYRDVITVVE GAGPNLDCIM LPKVQDAEQV KALDLLLTQI
EKTMGFEVGR IGIEAQIENA KGLINVDAIA EASPRLETII FGPADFMASI NMKSLVVGEQ
PPGYGADAYH YILMRILMAA RANDLQAIDG PYLQIRNQEG YREVARRSAA LGFDGKWVLH
PDQVAAANEI YSPSQEDYDH AELILDAYDY CTSEAGGAKG SAMLGDEMID EASRKMALVV
AGKGRAAGLQ RTTKFEIPEA
//
