ID   PADL_SEDHY              Reviewed;         189 AA.
AC   Q4R101;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
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=shdB {ECO:0000303|PubMed:15979273};
OS   Sedimentibacter hydroxybenzoicus (Clostridium hydroxybenzoicum).
OC   Bacteria; Firmicutes; Tissierellia; Sedimentibacter.
OX   NCBI_TaxID=29345;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1;
RX   PubMed=10438791; DOI=10.1128/jb.181.16.5119-5122.1999;
RA   Huang J., He Z., Wiegel J.;
RT   "Cloning, characterization, and expression of a novel gene encoding a
RT   reversible 4-hydroxybenzoate decarboxylase from Clostridium
RT   hydroxybenzoicum.";
RL   J. Bacteriol. 181:5119-5122(1999).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RC   STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1;
RX   PubMed=24193968; DOI=10.1007/bf02543871;
RA   Zhang X., Wiegel J.;
RT   "Isolation and partial characterization of a Clostridium species
RT   transforming para-hydroxybenzoate and 3,4-dihydroxybenzoate and producing
RT   phenols as the final transformation products.";
RL   Microb. Ecol. 20:103-121(1990).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1;
RX   PubMed=15979273; DOI=10.1016/j.ygeno.2005.05.002;
RA   Lupa B., Lyon D., Gibbs M.D., Reeves R.A., Wiegel J.;
RT   "Distribution of genes encoding the microbial non-oxidative reversible
RT   hydroxyarylic acid decarboxylases/phenol carboxylases.";
RL   Genomics 86:342-351(2005).
CC   -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC       detoxification of phenolic derivatives under anaerobic conditions
CC       (PubMed:24193968, PubMed:15979273). Flavin prenyltransferase that
CC       catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for
CC       phenolic acid decarboxylase (By similarity). {ECO:0000255|HAMAP-
CC       Rule:MF_01986, ECO:0000269|PubMed:15979273,
CC       ECO:0000269|PubMed:24193968}.
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 4-hydroxybenzoate and 3,4-dihydroxybenzoate.
CC       {ECO:0000305|PubMed:24193968}.
CC   -!- MISCELLANEOUS: It is not known, if phenolic acid decarboxylase forms a
CC       complex composed of ShdB, ShdC and ShdD. 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; AF128880; AAY67850.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4R101; -.
DR   SMR; Q4R101; -.
DR   BRENDA; 4.1.1.61; 5658.
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..189
FT                   /note="Probable UbiX-like flavin prenyltransferase"
FT                   /id="PRO_0000434528"
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   189 AA;  20960 MW;  F3BEF9C418E09534 CRC64;
     MRLVIGISGA SGVVLGYHML KVLRFFPECE THLVISEGAK LTFGLETDLK IEDVEKLADF
     VYSNTNLAAS ISSGSFKTDG MIVIPCSMKT LSGIATGYAE NLLIRAADVC LKENRKVVLV
     PREMPFGKLH IRNMKEASDL GCVIIPPLLT FYNNPQTIEE QINHIIGKIL MQFGLEHEKF
     KAWEGTKDD