PDUL_LACP7
ID PDUL_LACP7 Reviewed; 213 AA.
AC A9KN62;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=Cphy_1183;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000885; ABX41561.1; -; Genomic_DNA.
DR RefSeq; WP_012199209.1; NC_010001.1.
DR AlphaFoldDB; A9KN62; -.
DR SMR; A9KN62; -.
DR STRING; 357809.Cphy_1183; -.
DR EnsemblBacteria; ABX41561; ABX41561; Cphy_1183.
DR KEGG; cpy:Cphy_1183; -.
DR eggNOG; COG4869; Bacteria.
DR HOGENOM; CLU_080676_1_0_9; -.
DR OMA; EMRERPI; -.
DR OrthoDB; 1156172at2; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000000370; 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..213
FT /note="Phosphate propanoyltransferase"
FT /id="PRO_0000407715"
FT BINDING 33..35
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 39
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 86
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 92
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 148
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="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 200
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
SQ SEQUENCE 213 AA; 23061 MW; BCE93FA81E0FE1D4 CRC64;
MEDNQIELIT RMVLNVLQEK QSGKTGFAVP VGVSARHLHL TQDHVEQLFG KGYELTKKKD
LMGGQFAANE TVTIVGLKLR AIENVRILGP VRKASQVEVS ATDAIKLGVK IPIRESGNIK
GSAPIAVVGP KGAIYLDEGC IIAKRHIHMS PTDASTAGVK DGDIVSVKVD DERETVFHQV
QIRVDSSFTL EMHIDTDEAN AAKITCGQIV TIL
