ID R9JWQ5_9FIRM Unreviewed; 215 AA.
AC R9JWQ5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=C808_02859 {ECO:0000313|EMBL:EOS38649.1};
OS Lachnospiraceae bacterium M18-1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235792 {ECO:0000313|EMBL:EOS38649.1, ECO:0000313|Proteomes:UP000014090};
RN [1] {ECO:0000313|EMBL:EOS38649.1, ECO:0000313|Proteomes:UP000014090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18-1 {ECO:0000313|EMBL:EOS38649.1,
RC ECO:0000313|Proteomes:UP000014090};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium M18-1.";
RL Submitted (APR-2013) 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|ARBA:ARBA00001434,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS38649.1}.
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DR EMBL; ASSV01000016; EOS38649.1; -; Genomic_DNA.
DR AlphaFoldDB; R9JWQ5; -.
DR STRING; 1235792.C808_02859; -.
DR PATRIC; fig|1235792.3.peg.3055; -.
DR eggNOG; COG4869; Bacteria.
DR HOGENOM; CLU_080676_1_0_9; -.
DR OrthoDB; 9784365at2; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000014090; Unassembled WGS sequence.
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:UP000014090};
KW Transferase {ECO:0000256|PIRNR:PIRNR010130}.
SQ SEQUENCE 215 AA; 23047 MW; 64D7436F5C7EED98 CRC64;
MDNSNVALIT KMVLEAIEKQ KASAENGYLV PVGVSARHIH LTQEHVEALF GEGYQLTKKK
ELMGGQYASN ETVTIVGLKL RAIENVRILG PVRSKSQVEV SATDAIRLGV KAPIRESGNI
AGSAAVAVVG PKGVIYLNEG CIIAKRHIHM APKDAMAAGV HDGDIVSVKA DNERGTVFNH
VQIRVDDSFT LEMHIDTDEA NASKIATGDT VRIIC
//
