PADL_ECOLX
ID PADL_ECOLX Reviewed; 197 AA.
AC P69774; Q9X728;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=4-hydroxybenzoate decarboxylase subunit B {ECO:0000255|HAMAP-Rule:MF_01986};
DE AltName: Full=Phenolic acid decarboxylase subunit B {ECO:0000255|HAMAP-Rule:MF_01986};
GN Name=ecdB; Synonyms=pad1;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O26:NM / DEC 9f / EHEC, and O55:H6 / DEC 1a / EPEC;
RX PubMed=10986240; DOI=10.1128/jb.182.19.5381-5390.2000;
RA Herbelin C.J., Chirillo S.C., Melnick K.A., Whittam T.S.;
RT "Gene conservation and loss in the mutS-rpoS genomic region of pathogenic
RT Escherichia coli.";
RL J. Bacteriol. 182:5381-5390(2000).
CC -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of the
CC prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase C.
CC Involved in the decarboxylation and detoxification of phenolic
CC derivatives under both aerobic and anaerobic conditions.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01986};
CC -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_01986}.
CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. YclB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01986}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF242209; AAG14979.1; -; Genomic_DNA.
DR EMBL; AF242210; AAG14986.1; -; Genomic_DNA.
DR RefSeq; WP_000767718.1; NZ_WVWF01000002.1.
DR RefSeq; WP_000767729.1; NZ_UGGC01000001.1.
DR AlphaFoldDB; P69774; -.
DR SMR; P69774; -.
DR STRING; 585034.ECIAI1_2838; -.
DR GeneID; 58463093; -.
DR OMA; FERWNGW; -.
DR GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Flavoprotein; FMN; Prenyltransferase; Transferase.
FT CHAIN 1..197
FT /note="Probable UbiX-like flavin prenyltransferase"
FT /id="PRO_0000134965"
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"
FT VARIANT 37
FT /note="K -> T (in strain: DEC 1a)"
FT VARIANT 52
FT /note="R -> H (in strain: DEC 1a)"
FT VARIANT 70
FT /note="I -> T (in strain: DEC 1a)"
FT VARIANT 124
FT /note="M -> T (in strain: DEC 1a)"
SQ SEQUENCE 197 AA; 21456 MW; DD6E78415C12B283 CRC64;
MKLIVGMTGA TGAPLGVALL QALREMPNVE THLVMSKWAK TTIELETPYS ARDVAALADF
SHNPADQAAI ISSGSFRTDG MIVIPCSMKT LAGIRAGYAD GLVGRAADVV LKEGRKLVLV
PREMPLSTIH LENMLALSRM GVAMVPPMPA FYNHPETVDD IVHHVVARVL DQFGLEHPHA
RRWQGLPQAR NFSQENE