ID D6YR41_PANVC Unreviewed; 201 AA.
AC D6YR41;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Probable UbiX-like flavin prenyltransferase {ECO:0000256|HAMAP-Rule:MF_01986};
DE EC=2.5.1.129 {ECO:0000256|HAMAP-Rule:MF_01986};
DE AltName: Full=Phenolic acid decarboxylase subunit B {ECO:0000256|HAMAP-Rule:MF_01986};
DE Short=PAD {ECO:0000256|HAMAP-Rule:MF_01986};
GN Name=pad {ECO:0000313|EMBL:ADI78474.1};
GN OrderedLocusNames=Pvag_pPag30405 {ECO:0000313|EMBL:ADI78474.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OG Plasmid pPag3 {ECO:0000313|EMBL:ADI78474.1,
OG ECO:0000313|Proteomes:UP000006631}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADI78474.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADI78474.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADI78474.1,
RC ECO:0000313|Proteomes:UP000006631};
RC PLASMID=pPag3 {ECO:0000313|EMBL:ADI78474.1};
RX PubMed=20487014; DOI=10.1111/j.1574-6968.2010.01994.x;
RA Smits T.H., Rezzonico F., Pelludat C., Goesmann A., Frey J.E., Duffy B.;
RT "Genomic and phenotypic characterization of a nonpigmented variant of
RT Pantoea vagans biocontrol strain C9-1 lacking the 530-kb megaplasmid
RT pPag3.";
RL FEMS Microbiol. Lett. 308:48-54(2010).
RN [2] {ECO:0000313|EMBL:ADI78474.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADI78474.1,
RC ECO:0000313|Proteomes:UP000006631};
RC PLASMID=pPag3 {ECO:0000313|EMBL:ADI78474.1};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
CC -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC detoxification of phenolic derivatives. Flavin prenyltransferase that
CC catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for
CC phenolic acid decarboxylase. {ECO:0000256|HAMAP-Rule:MF_01986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2;
CC Xref=Rhea:RHEA:37743, ChEBI:CHEBI:43474, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:87467, ChEBI:CHEBI:88052; EC=2.5.1.129;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01986};
CC -!- SUBUNIT: Homododecamer. {ECO:0000256|HAMAP-Rule:MF_01986}.
CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. YclB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01986}.
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DR EMBL; CP001895; ADI78474.1; -; Genomic_DNA.
DR RefSeq; WP_013196374.1; NC_014258.1.
DR AlphaFoldDB; D6YR41; -.
DR KEGG; pva:Pvag_pPag30405; -.
DR HOGENOM; CLU_074522_0_1_6; -.
DR OrthoDB; 9781577at2; -.
DR Proteomes; UP000006631; Plasmid pPag3.
DR GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 1.
DR HAMAP; MF_01984; ubiX_pad; 1.
DR HAMAP; MF_01986; ubiX_pad_yclB; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR InterPro; IPR004507; UbiX-like.
DR InterPro; IPR032901; UbiX_pad_YclB.
DR NCBIfam; TIGR00421; ubiX_pad; 1.
DR NCBIfam; NF041206; VdcB; 1.
DR PANTHER; PTHR43374; FLAVIN PRENYLTRANSFERASE; 1.
DR PANTHER; PTHR43374:SF1; FLAVIN PRENYLTRANSFERASE PAD1, MITOCHONDRIAL; 1.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01986};
KW Detoxification {ECO:0000256|HAMAP-Rule:MF_01986};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01986};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01986};
KW Lyase {ECO:0000313|EMBL:ADI78474.1}; Plasmid {ECO:0000313|EMBL:ADI78474.1};
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW Rule:MF_01986};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01986}.
FT DOMAIN 1..173
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT BINDING 9..11
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01986"
FT BINDING 36
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01986"
FT BINDING 87..90
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01986"
FT BINDING 122
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01986"
SQ SEQUENCE 201 AA; 21841 MW; 6927ACBB460C71A2 CRC64;
MRLIIGMTGA TGAPLGVALL KILQEIEDVE THLILSKWAK TTVELETPYS AREVMDMADF
VHGPADQAAT LSSGSFHTDG MIIIPCSMKS LAGIRSGYAE GLVGRAADVT IKEGRKLVLV
PRETPLSTIH LENMLALSRL GVSMIPPMPA FYNHPAVIDD VIDHVVARVL DQFGLASPRA
RRWEGIKQSS HIHHQGEKNG F
//
