ID L0DBV4_SINAD Unreviewed; 227 AA.
AC L0DBV4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Phosphate propanoyltransferase {ECO:0000256|ARBA:ARBA00020837, ECO:0000256|PIRNR:PIRNR010130};
DE EC=2.3.1.222 {ECO:0000256|ARBA:ARBA00012206, ECO:0000256|PIRNR:PIRNR010130};
GN OrderedLocusNames=Sinac_1775 {ECO:0000313|EMBL:AGA26146.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA26146.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA26146.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in 1,2-propanediol (1,2-PD) degradation by
CC catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate.
CC {ECO:0000256|PIRNR:PIRNR010130}.
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:0000256|PIRNR:PIRNR010130};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000256|PIRNR:PIRNR010130}.
CC -!- SIMILARITY: Belongs to the PduL family. {ECO:0000256|ARBA:ARBA00007342,
CC ECO:0000256|PIRNR:PIRNR010130}.
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DR EMBL; CP003364; AGA26146.1; -; Genomic_DNA.
DR RefSeq; WP_015245315.1; NZ_JH621477.1.
DR AlphaFoldDB; L0DBV4; -.
DR STRING; 886293.Sinac_1775; -.
DR KEGG; saci:Sinac_1775; -.
DR eggNOG; COG4869; Bacteria.
DR HOGENOM; CLU_080676_0_1_0; -.
DR OrthoDB; 9784365at2; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000010798; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR008300; PTAC.
DR PANTHER; PTHR39453; PHOSPHATE PROPANOYLTRANSFERASE; 1.
DR PANTHER; PTHR39453:SF1; PHOSPHATE PROPANOYLTRANSFERASE; 1.
DR Pfam; PF06130; PTAC; 2.
DR PIRSF; PIRSF010130; PduL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|PIRNR:PIRNR010130};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Transferase {ECO:0000256|PIRNR:PIRNR010130}.
SQ SEQUENCE 227 AA; 24698 MW; F48DD66714554E88 CRC64;
MSSLEASRDL VEQLVRSILT QQLGNGTAGN GQAGLAKPNV VANISARHCH LTQEDVNVLF
GDGYQLTEMK RLYQATDFAA NETVAVVGPR QRMIPGVRIL GPCRQFSQVE LSFTDSISLG
IDIPVRLSGD VEGTPGCLLV GPKGSLVMPK GVIRAERHVH MGTNDAAYYG VKHLDRLNMR
VDSPCPTTLE GLLVRVNPDW KLEVHIDTDE ANCCDLVHAT NVTLFRP
//