ID Q9S2U9_STRCO Unreviewed; 274 AA.
AC Q9S2U9;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=Citrate lyase beta chain {ECO:0000313|EMBL:CAB51425.1};
GN OrderedLocusNames=SCO2033 {ECO:0000313|EMBL:CAB51425.1};
GN ORFNames=SC4G6.02 {ECO:0000313|EMBL:CAB51425.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB51425.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB51425.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AL939111; CAB51425.1; -; Genomic_DNA.
DR PIR; T35062; T35062.
DR RefSeq; NP_626293.1; NC_003888.3.
DR RefSeq; WP_011028109.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9S2U9; -.
DR STRING; 100226.gene:17759631; -.
DR PaxDb; 100226-SCO2033; -.
DR PATRIC; fig|100226.15.peg.2064; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_2_11; -.
DR InParanoid; Q9S2U9; -.
DR OrthoDB; 4322898at2; -.
DR PhylomeDB; Q9S2U9; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
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:CAB51425.1};
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:UP000001973}.
FT DOMAIN 8..211
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 118
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"
SQ SEQUENCE 274 AA; 28469 MW; 514F1E7A7E6FB198 CRC64;
MTAPPLTWLY VPGDRPRVVA KALAAGADVV VVDLEDAVAA DRKEYARDAT AELLTEPQPV
PVHVRVNALD GPLAAGDLAA LAALPGLSGL RLPKVTAPEQ VTGVAALTGG PPLYALLETA
LGVERAYRIA AAHPALRGIA LGEADLRADL GVRGDAGLDW SRSRVVVAAR AAGLAPPSQT
VHPDTRDLEG LAASCAHGRA LGFLGRAAIH PRQLPIIERA YLPTERELEE AETIVKAATV
QPGAQALPDG RFIDAAVVAT ARRTLSLARR PTLS
//
