ID C0M6B3_STRE4 Unreviewed; 295 AA.
AC C0M6B3;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Citrate lyase subunit beta {ECO:0000256|ARBA:ARBA00015712};
DE EC=4.1.3.34 {ECO:0000256|ARBA:ARBA00012258};
DE EC=4.1.3.6 {ECO:0000256|ARBA:ARBA00012914};
DE AltName: Full=Citrate (pro-3S)-lyase subunit beta {ECO:0000256|ARBA:ARBA00030255};
DE AltName: Full=Citryl-CoA lyase subunit {ECO:0000256|ARBA:ARBA00032495};
DE Flags: Precursor;
GN OrderedLocusNames=SEQ_1200 {ECO:0000313|EMBL:CAW93913.1};
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482 {ECO:0000313|EMBL:CAW93913.1, ECO:0000313|Proteomes:UP000001365};
RN [1] {ECO:0000313|EMBL:CAW93913.1, ECO:0000313|Proteomes:UP000001365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047 {ECO:0000313|EMBL:CAW93913.1,
RC ECO:0000313|Proteomes:UP000001365};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
CC -!- FUNCTION: Represents a citryl-ACP lyase.
CC {ECO:0000256|ARBA:ARBA00003671}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-citryl-CoA = acetyl-CoA + oxaloacetate;
CC Xref=Rhea:RHEA:20812, ChEBI:CHEBI:16452, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57321; EC=4.1.3.34;
CC Evidence={ECO:0000256|ARBA:ARBA00001238};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = acetate + oxaloacetate; Xref=Rhea:RHEA:10760,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089; EC=4.1.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000263};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta,gamma)6.
CC {ECO:0000256|ARBA:ARBA00011382}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase
CC beta subunit subfamily. {ECO:0000256|ARBA:ARBA00005549}.
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DR EMBL; FM204883; CAW93913.1; -; Genomic_DNA.
DR RefSeq; WP_012679580.1; NC_012471.1.
DR AlphaFoldDB; C0M6B3; -.
DR KEGG; seu:SEQ_1200; -.
DR HOGENOM; CLU_044864_0_0_9; -.
DR OMA; AWLFCPA; -.
DR OrthoDB; 9786940at2; -.
DR Proteomes; UP000001365; Chromosome.
DR GO; GO:0009346; C:ATP-independent citrate lyase complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
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; IPR006475; Citrate_lyase_beta_bac.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01588; citE; 1.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lyase {ECO:0000313|EMBL:CAW93913.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 6..224
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 295 AA; 32301 MW; 1C487DD9CC052176 CRC64;
MERLRRTMMF VPGANAAMLR DAPLFGADSI MFDLEDSVSL KEKDTSRALV HFALKTFDYS
NVETVVRVNS LDSCGALDIE AVVLAGVDVI RLPKTETAQD IIDVEAVIER VERDNGIAVG
RTRMMAAIES AEGVLKAREI AKASNRLIGI ALGAEDYVTN MKTRRYPDGQ ELFFARSMIL
HAARAAGIAA IDTVYSDVNN TEGFQAEVRH IKQLGFDGKS VINPRQIPLV NEIYTPTEKE
ISHAKQVIWA IREAESKGSG VISLNGKMVD KPIVERAQRV IALATAAGVL TEEDI
//