PDUL_PLAL2
ID PDUL_PLAL2 Reviewed; 244 AA.
AC D5SXM0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
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};
GN Synonyms=pvmB {ECO:0000303|PubMed:24487526}; OrderedLocusNames=Plim_1757;
OS Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS (Planctomyces limnophilus).
OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctopirus.
OX NCBI_TaxID=521674;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290;
RX PubMed=21304691; DOI=10.4056/sigs.1052813;
RA Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT 290).";
RL Stand. Genomic Sci. 3:47-56(2010).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=24487526; DOI=10.1128/aem.03887-13;
RA Erbilgin O., McDonald K.L., Kerfeld C.A.;
RT "Characterization of a planctomycetal organelle: a novel bacterial
RT microcompartment for the aerobic degradation of plant saccharides.";
RL Appl. Environ. Microbiol. 80:2193-2205(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290;
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: Part of a bacterial microcompartment (BMC) locus required for
CC growth on plant and algal sugars, including L-fucose and L-rhamnose
CC (PubMed:24487526). Thought to be active on lactyl-CoA in a
CC lactaldehyde-degradation pathway (Probable). CoA is regenerated within
CC the BMC via this enzyme, although there must also be cofactor transport
CC across the BMC. Directly targeted to the BMC (Probable).
CC {ECO:0000269|PubMed:24487526, 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 -!- 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 -!- SUBUNIT: Full-length protein forms large oligomers. Possible homotrimer
CC and monomer, when purified in the absence of the encapsulation peptide
CC (EP, residues 1-20). The EP may influence oligomerization.
CC {ECO:0000269|PubMed:26959993}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:26959993}.
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|PubMed:26959993}.
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DR EMBL; CP001744; ADG67587.1; -; Genomic_DNA.
DR RefSeq; WP_013110018.1; NC_014148.1.
DR DIP; DIP-61926N; -.
DR STRING; 521674.Plim_1757; -.
DR EnsemblBacteria; ADG67587; ADG67587; Plim_1757.
DR KEGG; plm:Plim_1757; -.
DR eggNOG; COG4869; Bacteria.
DR HOGENOM; CLU_080676_0_1_0; -.
DR OMA; EMRERPI; -.
DR OrthoDB; 1156172at2; -.
DR Proteomes; UP000002220; 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 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..244
FT /note="Phosphate propanoyltransferase"
FT /id="PRO_0000454244"
FT BINDING 52..54
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 106
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 112
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
FT BINDING 221
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q21A54"
SQ SEQUENCE 244 AA; 26163 MW; 384A684AF0D9766D CRC64;
MSSDSVVAGN ISRADVERVV RAVLTRQLAG ATTSSGSVSS AGGPPNPLVV NISARHVHLT
EEHVEVLFGK GVKLEPMKWL YQDGYYAAKQ TVTIFGPRRR MIPDVRVLGP CRNASQVELA
FTDGISLGID LPVRISGDHH DTVGCVLVGP AGVVELKSGV IRAMRHVHMS PADCAYYGVK
NGDEMDLKIH SGPCTTTLEH VTVREDKDVK LEVHIDTDEG NAVDLSHATK VELVKPVGCG
CHSK
