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Database: UniProt
Entry: A0A0A7FX77_9CLOT
LinkDB: A0A0A7FX77_9CLOT
Original site: A0A0A7FX77_9CLOT 
ID   A0A0A7FX77_9CLOT        Unreviewed;       219 AA.
AC   A0A0A7FX77;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=U729_807 {ECO:0000313|EMBL:AIY84207.1};
OS   Clostridium baratii str. Sullivan.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY84207.1, ECO:0000313|Proteomes:UP000030635};
RN   [1] {ECO:0000313|EMBL:AIY84207.1, ECO:0000313|Proteomes:UP000030635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sullivan {ECO:0000313|EMBL:AIY84207.1};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
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}.
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DR   EMBL; CP006905; AIY84207.1; -; Genomic_DNA.
DR   RefSeq; WP_039311883.1; NZ_CP006905.1.
DR   AlphaFoldDB; A0A0A7FX77; -.
DR   STRING; 1561.NPD11_2184; -.
DR   KEGG; cbv:U729_807; -.
DR   eggNOG; COG4869; Bacteria.
DR   HOGENOM; CLU_080676_1_0_9; -.
DR   OrthoDB; 9784365at2; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000030635; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030635};
KW   Transferase {ECO:0000256|PIRNR:PIRNR010130}.
FT   COILED          1..28
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   219 AA;  24087 MW;  46E6C49F995AA62A CRC64;
     MENLEEVLKL LLTAVKESEE KKKEIKESFE IPVGISNKHI HLSKKHVEAL FGQGYQLTKL
     KDLSQKGQYA CKETITICGP RGSIEKVRVL GPVRSKTQVE LSIGDCRKTG VSPIVRLSGD
     LKNTSGITLI GPKGSVQLEE GVIVAQRHIH MNNKHAEHFG VTDGEIVKIE VDGLRGGILN
     NVSIRTNDSF SLECHLDVEE ANSFGITPKS KIKIVRESA
//
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