ID   PADL_STRD7              Reviewed;         200 AA.
AC   Q9X696;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Probable UbiX-like flavin prenyltransferase {ECO:0000255|HAMAP-Rule:MF_01986};
DE            EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01986};
DE   AltName: Full=Phenolic acid decarboxylase subunit B {ECO:0000255|HAMAP-Rule:MF_01986};
DE            Short=PAD {ECO:0000255|HAMAP-Rule:MF_01986};
GN   Name=vdcB {ECO:0000303|PubMed:10517592};
OS   Streptomyces sp. (strain D7).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=92742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=D7 {ECO:0000312|EMBL:AAD28781.1};
RX   PubMed=10517592; DOI=10.1099/00221287-145-9-2393;
RA   Chow K.T., Pope M.K., Davies J.;
RT   "Characterization of a vanillic acid non-oxidative decarboxylation gene
RT   cluster from Streptomyces sp. D7.";
RL   Microbiology 145:2393-2403(1999).
CC   -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC       detoxification of phenolic derivatives under both aerobic and anaerobic
CC       conditions (PubMed:10517592). Flavin prenyltransferase that catalyzes
CC       the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic
CC       acid decarboxylase (By similarity). {ECO:0000255|HAMAP-Rule:MF_01986,
CC       ECO:0000269|PubMed:10517592}.
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:0000255|HAMAP-Rule:MF_01986};
CC   -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_01986}.
CC   -!- INDUCTION: By vanillate. {ECO:0000269|PubMed:10517592}.
CC   -!- MISCELLANEOUS: It is not known, if phenolic acid decarboxylase forms a
CC       complex composed of VdcB, VdcC and VdcD. The term subunit is often used
CC       in reference to the operon, however there is no experimental evidence
CC       to prove the existence of the complex. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. YclB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01986}.
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DR   EMBL; AF134589; AAD28781.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X696; -.
DR   SMR; Q9X696; -.
DR   GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
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; -; 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   PANTHER; PTHR43374; PTHR43374; 2.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; Detoxification; Flavoprotein; FMN;
KW   Prenyltransferase; Transferase.
FT   CHAIN           1..200
FT                   /note="Probable UbiX-like flavin prenyltransferase"
FT                   /id="PRO_0000444036"
FT   BINDING         9..11
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT   BINDING         36
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT   BINDING         87..90
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT   BINDING         122
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
SQ   SEQUENCE   200 AA;  21660 MW;  83D1B5C22C13CD3E CRC64;
     MRLVVGMTGA TGAPFGVRLL ENLRQLPGVE THLVLSRWAR TTIEMETGLS VAEVSALADV
     THHPEDQGAT ISSGSFRTDG MVIVPCSMKT LAGIRTGYAE GLVARAADVV LKERRRLVLV
     PRETPLSEIH LQNMLELARM GVQLVPPMPA FYNNPQTVDD IVDHVVARIL DQFDLPAPAA
     RRWAGMRAAR AAARSFGDAA