ID   CITE_KLEPN              Reviewed;         289 AA.
AC   P17725;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 117.
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   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 13882 / NBRC 13541 / NCTC 8172;
RX   PubMed=2205500; DOI=10.1111/j.1432-1033.1990.tb19209.x;
RA   Hupperich M., Henschen A., Eggerer H.;
RT   "Citrate lyase from Klebsiella pneumoniae. The complete primary structure
RT   of the acyl lyase subunit.";
RL   Eur. J. Biochem. 192:161-166(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13882 / NBRC 13541 / NCTC 8172;
RX   PubMed=7830578; DOI=10.1111/j.1365-2958.1994.tb01295.x;
RA   Bott M., Dimroth P.;
RT   "Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase:
RT   localization, sequencing, and expression.";
RL   Mol. Microbiol. 14:347-356(1994).
CC   -!- FUNCTION: Represents a citryl-ACP lyase.
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase
CC       beta subunit subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X79817; CAA56216.1; -; Genomic_DNA.
DR   PIR; S60775; S60775.
DR   RefSeq; WP_004151372.1; NZ_WYAL01000016.1.
DR   AlphaFoldDB; P17725; -.
DR   SMR; P17725; -.
DR   OrthoDB; 1107373at2; -.
DR   BioCyc; MetaCyc:MON-16999; -.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..289
FT                   /note="Citrate lyase subunit beta"
FT                   /id="PRO_0000089759"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        216
FT                   /note="N -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  31352 MW;  C70A92DCAC3EABC2 CRC64;
     MKPRRSMLFI PGANAAMLST SFVYGADAVM FDLEDAVSLR EKDTARLLVY QALQHPLYQD
     IETVVRINPL NTPFGLADLE AVVRAGVDMV RLPKTDSKED IHELEAHVER IERECGREVG
     STKLMAAIES ALGVVNAVEI ARASPRLAAI ALAAFDYVMD MGTSRGDGTE LFYARCAVLH
     AARVAGIAAY DVVWSDINNE EGFLAEANLA KNLGFNGKSL VNPRQIELLH QVYAPTRKEV
     DHALEVIAAA EEAETRGLGV VSLNGKMIDG PIIDHARKVV ALSASGIRD