PDUL_RHOPB
ID PDUL_RHOPB Reviewed; 226 AA.
AC Q21A54;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Phosphate propanoyltransferase;
DE EC=2.3.1.222 {ECO:0000269|PubMed:26959993};
DE AltName: Full=Phosphate acyltransferase PduL;
DE AltName: Full=Phosphotransacylase PduL {ECO:0000303|PubMed:26959993};
DE Short=PTAC {ECO:0000303|PubMed:26959993};
DE AltName: Full=Propanediol utilization protein PduL {ECO:0000305};
GN Name=pduL {ECO:0000303|PubMed:26959993}; OrderedLocusNames=RPC_1169;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5CUO, ECO:0007744|PDB:5CUP}
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 34-226 IN COMPLEX WITH ZINC WITH
RP AND WITHOUT COENZYME A OR PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF 1-MET--THR-33.
RC STRAIN=BisB18;
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).
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. CoA
CC is regenerated within the pdu BMC (for use by PduP) via this enzyme,
CC although there must also be cofactor transport across the BMC
CC (PubMed:26959993). Directly targeted to the BMC (By similarity).
CC Phosphate is probably the first substrate to bind in the forward
CC direction. CoA is probably the first substrate to bind in the reverse
CC direction, and might bind to the enzyme as the BMC assembles, ensuring
CC cofactor encapsulation (Probable). {ECO:0000250|UniProtKB:Q9XDN5,
CC ECO:0000269|PubMed:26959993, ECO:0000305|PubMed:26959993}.
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:26959993};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28048;
CC Evidence={ECO:0000269|PubMed:26959993};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:26959993, ECO:0007744|PDB:5CUO,
CC ECO:0007744|PDB:5CUP};
CC Note=There are 2 Zn(2+) ions per monomer; Zn(2+) and CoA bind inbetween
CC the 2 domains in each monomer. {ECO:0000269|PubMed:26959993};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC -!- SUBUNIT: Full-length protein forms large oligomers. Homodimer, when
CC purified in the absence of the encapsulation peptide (EP, residues 1-
CC 47). The EP may influence oligomerization.
CC {ECO:0000269|PubMed:26959993}.
CC -!- INTERACTION:
CC Q21A54; Q21A54: RPC_1169; NbExp=3; IntAct=EBI-16201701, EBI-16201701;
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:26959993}. Note=Probably located inside the BMC
CC shell. {ECO:0000305|PubMed:26959993}.
CC -!- DOMAIN: Formed by 2 beta-barrels, each is capped on both ends by short
CC alpha-helices. {ECO:0000269|PubMed:26959993}.
CC -!- SIMILARITY: Belongs to the PduL family. {ECO:0000305|PubMed:26959993}.
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DR EMBL; CP000301; ABD86732.1; -; Genomic_DNA.
DR RefSeq; WP_011471637.1; NC_007925.1.
DR PDB; 5CUO; X-ray; 1.54 A; A/B=34-226.
DR PDB; 5CUP; X-ray; 2.10 A; A/B=34-226.
DR PDBsum; 5CUO; -.
DR PDBsum; 5CUP; -.
DR SMR; Q21A54; -.
DR DIP; DIP-61925N; -.
DR STRING; 316056.RPC_1169; -.
DR EnsemblBacteria; ABD86732; ABD86732; RPC_1169.
DR KEGG; rpc:RPC_1169; -.
DR eggNOG; COG4869; Bacteria.
DR HOGENOM; CLU_080676_1_0_5; -.
DR OMA; EMRERPI; -.
DR OrthoDB; 1156172at2; -.
DR BRENDA; 2.3.1.222; 5412.
DR UniPathway; UPA00621; -.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR008300; PTAC.
DR PANTHER; PTHR39453; PTHR39453; 1.
DR Pfam; PF06130; PTAC; 2.
DR PIRSF; PIRSF010130; PduL; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Bacterial microcompartment; Metal-binding;
KW Transferase; Zinc.
FT CHAIN 1..226
FT /note="Phosphate propanoyltransferase"
FT /id="PRO_0000454245"
FT BINDING 44..46
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO, ECO:0007744|PDB:5CUP"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO, ECO:0007744|PDB:5CUP"
FT BINDING 72
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO"
FT BINDING 90
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO"
FT BINDING 97
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO"
FT BINDING 103
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUP"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO, ECO:0007744|PDB:5CUP"
FT BINDING 116
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO, ECO:0007744|PDB:5CUP"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO, ECO:0007744|PDB:5CUP"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO, ECO:0007744|PDB:5CUP"
FT BINDING 211
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:26959993,
FT ECO:0007744|PDB:5CUO"
FT MUTAGEN 1..33
FT /note="Missing: Enzyme active, produces crystals."
FT /evidence="ECO:0000269|PubMed:26959993"
SQ SEQUENCE 226 AA; 24099 MW; 2700579CA759150B CRC64;
MDMQQETIER IIRQVLGQVG PAGGSIATLS GDAGVDPFQV AVGVSNRHIH LSRTDMDTLF
GPGAELQRKK AMKQPGQFAA EETVTLKGPK GSLSKVRVLG PLRRETQVEV SVADGFALGI
TPPLRQSGQL DDTPGLTIIG PQGSVTKDHG VIVAQRHIHM HPSTAAKLGL RNGDEVDVEA
GGERGGVMHR VLIRVAEASA DEMHIDVEEA NALCLKNDDV VRICKK
