ID PDUL_ENTFA Reviewed; 211 AA.
AC Q834M4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Phosphate propanoyltransferase;
DE EC=2.3.1.222;
DE AltName: Full=Phosphate acyltransferase PduL;
DE AltName: Full=Phosphotransacylase PduL;
DE Short=PTAC;
DE AltName: Full=Propanediol utilization protein PduL;
GN Name=pduL; OrderedLocusNames=EF_1621;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- FUNCTION: Involved in 1,2-propanediol (1,2-PD) degradation by
CC catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate.
CC {ECO:0000250|UniProtKB:Q9XDN5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + propanoyl-CoA = CoA + propanoyl phosphate;
CC Xref=Rhea:RHEA:28046, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58933; EC=2.3.1.222;
CC Evidence={ECO:0000250|UniProtKB:Q9XDN5};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q21A54};
CC Note=There are 2 Zn(2+) ions per monomer; Zn(2+) and CoA bind inbetween
CC the 2 domains in each monomer. {ECO:0000250|UniProtKB:Q21A54};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: Formed by 2 beta-barrels, each is capped on both ends by short
CC alpha-helices. {ECO:0000250|UniProtKB:Q21A54}.
CC -!- SIMILARITY: Belongs to the PduL family. {ECO:0000305}.
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DR EMBL; AE016830; AAO81404.1; -; Genomic_DNA.
DR RefSeq; NP_815334.1; NC_004668.1.
DR RefSeq; WP_002357516.1; NZ_KE136528.1.
DR AlphaFoldDB; Q834M4; -.
DR SMR; Q834M4; -.
DR STRING; 226185.EF_1621; -.
DR EnsemblBacteria; AAO81404; AAO81404; EF_1621.
DR GeneID; 60893923; -.
DR KEGG; efa:EF1621; -.
DR PATRIC; fig|226185.9.peg.1524; -.
DR eggNOG; COG4869; Bacteria.
DR HOGENOM; CLU_080676_1_0_9; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR008300; PTAC.
DR NCBIfam; NF040837; BMC_EutD_Gpos; 1.
DR PANTHER; PTHR39453; PHOSPHATE PROPANOYLTRANSFERASE; 1.
DR PANTHER; PTHR39453:SF1; PHOSPHATE PROPANOYLTRANSFERASE; 1.
DR Pfam; PF06130; PTAC; 2.
DR PIRSF; PIRSF010130; PduL; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW Zinc.
FT CHAIN 1..211
FT /note="Phosphate propanoyltransferase"
FT /id="PRO_0000407706"
FT BINDING 30..32
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 76
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 89
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 197
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
SQ SEQUENCE 211 AA; 23309 MW; F48B9CD426610B39 CRC64;
MNKLDSMNEI VEEVVKRIQQ QQQNTFEVEA SGRHVHLSRQ EIDALFGPGY QLTKVKDLSQ
PGQFVCKERI TVAGPKGLFQ NVVILGPERS ESQVEVSMTD TRILGINAPV RESGKTEGTP
GVTLMNGSAV VTLSHGLIVA KRHIHMTPED ALKNKVSNSQ IVQVKVEGTR PLIFDDVVVR
ISPRFATYMH IDYDEANACG LTKGARGYIL K
//
