ID W1DPG2_KLEPN Unreviewed; 289 AA.
AC W1DPG2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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};
OS Klebsiella pneumoniae IS43.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL10682.1, ECO:0000313|Proteomes:UP000019183};
RN [1] {ECO:0000313|EMBL:CDL10682.1, ECO:0000313|Proteomes:UP000019183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS43 {ECO:0000313|EMBL:CDL10682.1,
RC ECO:0000313|Proteomes:UP000019183};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL10682.1}.
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DR EMBL; CBWK010000535; CDL10682.1; -; Genomic_DNA.
DR AlphaFoldDB; W1DPG2; -.
DR SMR; W1DPG2; -.
DR Proteomes; UP000019183; Unassembled WGS sequence.
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:CDL10682.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..289
FT /note="Citrate lyase subunit beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004800442"
FT DOMAIN 5..223
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 66
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 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
//