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
//