PDUL_SALTY
ID PDUL_SALTY Reviewed; 210 AA.
AC Q9XDN5; Q7BV79;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Phosphate propanoyltransferase;
DE EC=2.3.1.222 {ECO:0000269|PubMed:17158662};
DE AltName: Full=Phosphate acyltransferase PduL;
DE AltName: Full=Phosphotransacylase PduL {ECO:0000303|PubMed:17158662};
DE Short=PTAC {ECO:0000303|PubMed:17158662};
DE AltName: Full=Propanediol utilization protein PduL;
GN Name=pduL {ECO:0000303|PubMed:10498708}; OrderedLocusNames=STM2047;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=10498708; DOI=10.1128/jb.181.19.5967-5975.1999;
RA Bobik T.A., Havemann G.D., Busch R.J., Williams D.S., Aldrich H.C.;
RT "The propanediol utilization (pdu) operon of Salmonella enterica serovar
RT typhimurium LT2 includes genes necessary for formation of polyhedral
RT organelles involved in coenzyme B(12)-dependent 1, 2-propanediol
RT degradation.";
RL J. Bacteriol. 181:5967-5975(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP BACTERIAL MICROCOMPARTMENT ABUNDANCE.
RC STRAIN=LT2;
RX PubMed=12923081; DOI=10.1128/jb.185.17.5086-5095.2003;
RA Havemann G.D., Bobik T.A.;
RT "Protein content of polyhedral organelles involved in coenzyme B12-
RT dependent degradation of 1,2-propanediol in Salmonella enterica serovar
RT Typhimurium LT2.";
RL J. Bacteriol. 185:5086-5095(2003).
RN [4]
RP FUNCTION IN PROPANEDIOL UTILIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=17158662; DOI=10.1128/jb.01151-06;
RA Liu Y., Leal N.A., Sampson E.M., Johnson C.L., Havemann G.D., Bobik T.A.;
RT "PduL is an evolutionarily distinct phosphotransacylase involved in B12-
RT dependent 1,2-propanediol degradation by Salmonella enterica serovar
RT typhimurium LT2.";
RL J. Bacteriol. 189:1589-1596(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 2-ASP--LEU-5 AND 2-ASP--VAL-10.
RC STRAIN=LT2;
RX PubMed=25962918; DOI=10.1128/jb.00056-15;
RA Liu Y., Jorda J., Yeates T.O., Bobik T.A.;
RT "The PduL Phosphotransacylase Is Used To Recycle Coenzyme A within the Pdu
RT Microcompartment.";
RL J. Bacteriol. 197:2392-2399(2015).
RN [6]
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=LT2;
RX PubMed=26959993; DOI=10.1371/journal.pbio.1002399;
RA Erbilgin O., Sutter M., Kerfeld C.A.;
RT "The Structural Basis of Coenzyme A Recycling in a Bacterial Organelle.";
RL PLoS Biol. 14:e1002399-e1002399(2016).
RN [7]
RP SYSTEM-MODELING, AND FUNCTION.
RC STRAIN=LT2;
RX PubMed=28475631; DOI=10.1371/journal.pcbi.1005525;
RA Jakobson C.M., Tullman-Ercek D., Slininger M.F., Mangan N.M.;
RT "A systems-level model reveals that 1,2-Propanediol utilization
RT microcompartments enhance pathway flux through intermediate
RT sequestration.";
RL PLoS Comput. Biol. 13:e1005525-e1005525(2017).
CC -!- FUNCTION: Involved in 1,2-propanediol (1,2-PD) utilization in the
CC bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by
CC catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. Also
CC able to catalyze the reverse reaction. Also has phosphate
CC acetyltransferase activity to a lesser extent (PubMed:17158662).
CC Required for optimal growth on 1,2-PD when the BMC is intact. CoA is
CC regenerated within the BMC (for use by PduP) via this enzyme, although
CC there must also be cofactor transport across the BMC. Directly targeted
CC to the BMC (PubMed:25962918). {ECO:0000269|PubMed:17158662,
CC ECO:0000269|PubMed:25962918}.
CC -!- FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC)
CC concentrates low levels of 1,2-PD catabolic enzymes, concentrates
CC volatile reaction intermediates thus enhancing pathway flux and keeps
CC the level of toxic, mutagenic propionaldehyde low.
CC {ECO:0000305|PubMed:28475631}.
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:0000269|PubMed:17158662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28047;
CC Evidence={ECO:0000269|PubMed:17158662};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28048;
CC Evidence={ECO:0000269|PubMed:17158662, ECO:0000269|PubMed:26959993};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.61 mM for propanoyl-phosphate {ECO:0000269|PubMed:17158662};
CC KM=0.97 mM for acetyl-phosphate {ECO:0000269|PubMed:17158662};
CC Vmax=51.7 uM/min/mg enzyme with propanoyl-phosphate as substrate
CC {ECO:0000269|PubMed:17158662};
CC Vmax=13.4 uM/min/mg enzyme with acetyl-phosphate as substrate
CC {ECO:0000269|PubMed:17158662};
CC Note=The above values were measured with a recombinant PduL fused to
CC eight C-terminal histidine residues (PduL-His8). The Vmax values may
CC be underestimated due to the instability of PduL-His8.
CC {ECO:0000269|PubMed:17158662};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000269|PubMed:17158662, ECO:0000305|PubMed:10498708}.
CC -!- SUBUNIT: Monomer, when purified in the absence of the encapsulation
CC peptide (EP, residues 1-27). The EP may influence oligomerization.
CC {ECO:0000269|PubMed:26959993}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:25962918}. Note=Probably located inside the BMC
CC shell. {ECO:0000305|PubMed:25962918}.
CC -!- INDUCTION: BMC production is induced by growth on 1,2-PD vitamin B12
CC medium. {ECO:0000269|PubMed:10498708}.
CC -!- DOMAIN: The N-terminal 20 residues target foreign proteins (tested with
CC eGFP) to the BMC (PubMed:25962918). Formed by 2 beta-barrels, each is
CC capped on both ends by short alpha-helices (By similarity).
CC {ECO:0000250|UniProtKB:Q21A54, ECO:0000269|PubMed:25962918}.
CC -!- DISRUPTION PHENOTYPE: Unable to ferment 1,2-PD, impaired for aerobic
CC growth on this compound. {ECO:0000269|PubMed:17158662}.
CC -!- MISCELLANEOUS: Evolutionarily distinct from Pta (phosphate
CC acetyltransferase). {ECO:0000305|PubMed:17158662}.
CC -!- MISCELLANEOUS: Bacterial microcompartments (BMC) 100-200 nm in cross
CC section are formed during aerobic growth on minimal 1,2-PD-B12 or
CC anaerobic growth on 1,2-PD-tetrathionate medium, but not during aerobic
CC growth on glucose, anerobic growth on glucose or pyruvate-tetrathionate
CC (PubMed:10498708). BMCs can constitute up to 10% of total cell protein
CC (PubMed:12923081). {ECO:0000269|PubMed:10498708,
CC ECO:0000269|PubMed:12923081}.
CC -!- SIMILARITY: Belongs to the PduL family. {ECO:0000305|PubMed:26959993}.
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DR EMBL; AF026270; AAD39011.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20951.1; -; Genomic_DNA.
DR RefSeq; NP_460992.1; NC_003197.2.
DR RefSeq; WP_000356709.1; NC_003197.2.
DR AlphaFoldDB; Q9XDN5; -.
DR SMR; Q9XDN5; -.
DR STRING; 99287.STM2047; -.
DR PaxDb; Q9XDN5; -.
DR EnsemblBacteria; AAL20951; AAL20951; STM2047.
DR GeneID; 1253568; -.
DR KEGG; stm:STM2047; -.
DR PATRIC; fig|99287.12.peg.2169; -.
DR HOGENOM; CLU_080676_1_0_6; -.
DR OMA; EMRERPI; -.
DR PhylomeDB; Q9XDN5; -.
DR BioCyc; MetaCyc:STM2047-MON; -.
DR BioCyc; SENT99287:STM2047-MON; -.
DR BRENDA; 2.3.1.222; 5542.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW Acyltransferase; Bacterial microcompartment; Metal-binding;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..210
FT /note="Phosphate propanoyltransferase"
FT /id="PRO_0000407698"
FT BINDING 26..28
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 71
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
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 84
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 193
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT MUTAGEN 2..10
FT /note="Missing: Considerably decreased amount of PduL in
FT BMCs, enzyme has greater than wild-type activity."
FT /evidence="ECO:0000269|PubMed:25962918"
FT MUTAGEN 2..5
FT /note="Missing: Decreased amount of PduL in BMCs, enzyme
FT has wild-type activity."
FT /evidence="ECO:0000269|PubMed:25962918"
SQ SEQUENCE 210 AA; 22972 MW; DF76055F88B9028C CRC64;
MDKELLQSTV RKVLDEMRQR PIPLGVSNRH IHLSAQDYER LFPGHPISEK KALLQPGQYA
AEQTVTLVGP KGQLKNVRLL GPLRSVSQVE ISRTDARTLG IAAPLRMSGN LKGTPGIRLV
SPFAELELPS GVIVAQRHIH MSPLDALILR VSHGDMVSVA IEGDDRGLIF NNVAIRVSPD
MRLEMHIDTD EANAAGADNP HAFARLVGPR
