PDUL_CLONN
ID PDUL_CLONN Reviewed; 216 AA.
AC A0Q2W0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=NT01CX_0491;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
CC -!- FUNCTION: Involved in 1,2-propanediol (1,2-PD) utilization within the
CC bacterial microcompartment (BMC) dedicated to 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: Bacterial microcompartment
CC {ECO:0000250|UniProtKB:Q9XDN5}.
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; CP000382; ABK62483.1; -; Genomic_DNA.
DR RefSeq; WP_011722944.1; NC_008593.1.
DR AlphaFoldDB; A0Q2W0; -.
DR SMR; A0Q2W0; -.
DR STRING; 386415.NT01CX_0491; -.
DR EnsemblBacteria; ABK62483; ABK62483; NT01CX_0491.
DR KEGG; cno:NT01CX_0491; -.
DR PATRIC; fig|386415.7.peg.1999; -.
DR eggNOG; COG4869; Bacteria.
DR HOGENOM; CLU_080676_1_0_9; -.
DR OMA; EMRERPI; -.
DR OrthoDB; 1156172at2; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000008220; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; 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 PANTHER; PTHR39453; PTHR39453; 1.
DR Pfam; PF06130; PTAC; 2.
DR PIRSF; PIRSF010130; PduL; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Bacterial microcompartment; Metal-binding;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..216
FT /note="Phosphate propanoyltransferase"
FT /id="PRO_0000407716"
FT BINDING 32..34
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
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 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 78
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 85
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 91
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 199
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
SQ SEQUENCE 216 AA; 24022 MW; AC147C1DF8512F47 CRC64;
MNVEEQLVQD IAKEIFQKSQ VKDRSLSIPV GVSNRHIHLN KEDLRILFGE NYELKVKSKI
SQVGQFAAEE TVCIAGPKGC FTKVRVLGPI REYSQIELSK TDSYTLGIKA PVRVSGDIEG
SANLCVIGPK GMKVFNEKVI CAKRHVHMLP KDADKYGVKD GDLVDVETIG DRSVVFKDVL
VRVTNKSALE MHIDTDEANA SGVKSKDMVR IIRINR
