ID   B9YA92_9FIRM            Unreviewed;       201 AA.
AC   B9YA92;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=HOLDEFILI_02749 {ECO:0000313|EMBL:EEF67107.1};
OS   Holdemania filiformis DSM 12042.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Holdemania.
OX   NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF67107.1, ECO:0000313|Proteomes:UP000005950};
RN   [1] {ECO:0000313|EMBL:EEF67107.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF67107.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEF67107.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF67107.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL   Submitted (FEB-2009) 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:EEF67107.1}.
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DR   EMBL; ACCF01000174; EEF67107.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9YA92; -.
DR   STRING; 545696.HOLDEFILI_02749; -.
DR   eggNOG; COG4869; Bacteria.
DR   HOGENOM; CLU_080676_1_0_9; -.
DR   OrthoDB; 9784365at2; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000005950; 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   Transferase {ECO:0000256|PIRNR:PIRNR010130}.
SQ   SEQUENCE   201 AA;  21516 MW;  939A37700F7715DF CRC64;
     MNMKERGSKI MSEEKVLVEV SARHIHLTDA DVEALFGPGY KLTVKKELSQ PGQFASNEKV
     TIKGERGEMK LSVLGPTRPE TQVELSLTEA RTVGVKAMIR ESGDIEGTQG ITIIGPAGSI
     EITKGVIAAK RHIHMTPADA EKYGVTNGQI VSVKIDTDGR SLTFGDTVVR VSEKYALAMH
     IDTDEANAAA ISGSALGEII K
//