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Database: UniProt
Entry: W1DPG2_KLEPN
LinkDB: W1DPG2_KLEPN
Original site: W1DPG2_KLEPN 
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
//
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