ID Q0STS1_CLOPS Unreviewed; 296 AA.
AC Q0STS1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
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};
GN Name=citE {ECO:0000313|EMBL:ABG86551.1};
GN OrderedLocusNames=CPR_1164 {ECO:0000313|EMBL:ABG86551.1};
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380 {ECO:0000313|EMBL:ABG86551.1, ECO:0000313|Proteomes:UP000001824};
RN [1] {ECO:0000313|EMBL:ABG86551.1, ECO:0000313|Proteomes:UP000001824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A {ECO:0000313|Proteomes:UP000001824};
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., Deboy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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; CP000312; ABG86551.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0STS1; -.
DR KEGG; cpr:CPR_1164; -.
DR Proteomes; UP000001824; 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:ABG86551.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 6..225
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 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 296 AA; 32509 MW; 1E6F2B9825D372F9 CRC64;
MPRLRRSMMF VPGSKPAMIK DCTIYGADSV MFDLEDSVSI AEKDSARRLV YHALTSMDFG
DTETVVRVNA LDSDFGIEDL KAIVRAQPDV IRLPKTETAQ DVLDMEKVIA SIEEEIGLPI
GKTKMMAAIE SALGVLNAYE IATSSKRLMG IALGAEDFVT DMKTHRSPEG NELFAARSHI
ILASRAAKIS AFDTVYSDVN NEEGFIKEAT LIKQLGFDGK SLINPRQIDL LHKVFEPTEK
EIDKAIKIIE AAKEAEKRGS GVVSLNGKMI DKPVIARAER VLMLAKASGI SYEKEV
//
