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Database: UniProt
Entry: Q4KDC5_PSEF5
LinkDB: Q4KDC5_PSEF5
Original site: Q4KDC5_PSEF5 
ID   Q4KDC5_PSEF5            Unreviewed;       270 AA.
AC   Q4KDC5;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=HpcH/HpaI aldolase/citrate lyase family protein {ECO:0000313|EMBL:AAY91924.1};
GN   OrderedLocusNames=PFL_2651 {ECO:0000313|EMBL:AAY91924.1};
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY91924.1, ECO:0000313|Proteomes:UP000008540};
RN   [1] {ECO:0000313|EMBL:AAY91924.1, ECO:0000313|Proteomes:UP000008540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC   {ECO:0000313|Proteomes:UP000008540};
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP000076; AAY91924.1; -; Genomic_DNA.
DR   RefSeq; WP_011060947.1; NC_004129.6.
DR   AlphaFoldDB; Q4KDC5; -.
DR   STRING; 220664.PFL_2651; -.
DR   KEGG; pfl:PFL_2651; -.
DR   PATRIC; fig|220664.5.peg.2702; -.
DR   eggNOG; COG2301; Bacteria.
DR   HOGENOM; CLU_044864_2_0_6; -.
DR   Proteomes; UP000008540; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:AAY91924.1};
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          7..214
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         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   270 AA;  28231 MW;  B263A835E65EECB0 CRC64;
     MSNPIVRSAL FVPGSRPERF AKALACGADA VIVDFEDAVE EPLKVQAREH LGRFLLAQPQ
     VRAWVRINAP EHPQHLADLA FCQAHAGVVG ILLPKVESAA QVARVAASGR LVWPIIESAR
     GLLALGEIAS APGVQRLSFG GLDLALDLNL SSGSAAAQFA LDQARLALIL HSRAAGLQAP
     LDGVFPGIAD SQGLAASVRH AYAMGFAGAL CIHPAQVPVI HQALAPSAEE LAWAQRVVEG
     GREGAGAYQV DGQMVDAPVL LRAQRLLAMA
//
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