CITE_LEUMC
ID CITE_LEUMC Reviewed; 302 AA.
AC O53078;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Citrate lyase subunit beta;
DE Short=Citrase beta chain;
DE EC=4.1.3.6;
DE AltName: Full=Citrate (pro-3S)-lyase subunit beta;
DE AltName: Full=Citryl-CoA lyase subunit;
DE EC=4.1.3.34;
GN Name=citE;
OS Leuconostoc mesenteroides subsp. cremoris.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=33965;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=195;
RX PubMed=9457870; DOI=10.1128/jb.180.3.647-654.1998;
RA Bekal S., van Beeumen J., Samyn B., Garmyn D., Henini S., Divies C.,
RA Prevost H.;
RT "Purification of Leuconostoc mesenteroides citrate lyase and cloning and
RT characterization of the citCDEFG gene cluster.";
RL J. Bacteriol. 180:647-654(1998).
CC -!- FUNCTION: Represents a citryl-ACP lyase. {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta,gamma)6.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase
CC beta subunit subfamily. {ECO:0000305}.
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DR EMBL; Y10621; CAA71632.1; -; Genomic_DNA.
DR RefSeq; WP_050892381.1; NZ_LAYV01000030.1.
DR AlphaFoldDB; O53078; -.
DR SMR; O53078; -.
DR PATRIC; fig|33965.3.peg.1361; -.
DR GO; GO:0009346; C:ATP-independent citrate lyase complex; IEA:InterPro.
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; -; 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 Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR01588; citE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..302
FT /note="Citrate lyase subunit beta"
FT /id="PRO_0000089760"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 302 AA; 33376 MW; E79C6D73DEDA1F7E CRC64;
MNNERLRRTM MFVPGNNPAM VKDAGIFGAD SIMFDLEDAV SLAEKDSARY LVYEALQTVD
YGSSELVVRI NGLDTPFYKN DIKAMVKAGI DVIRLPKVET AAMMHELESL ITDAEKEFGR
PVGTTHMMAA IESALGVVNA VEIANASDRM IGIALSAEDY TTDMKTHRYP DGQELLYARN
VILHAARAAG IAAFDTVFTN LNDEEGFYRE TQLIHQLGFD GKSLINPRQI EMVNKVYAPT
EKEINNAQNV IAAIEEAKQK GSGVISMNGQ MVDRPVVLRA QRVMKLANAN HLVDSEGNYI
EK
