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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}.
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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
 
 
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