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Database: UniProt
Entry: C0M6B3_STRE4
LinkDB: C0M6B3_STRE4
Original site: C0M6B3_STRE4 
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
//
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