PADL_ECO57
ID PADL_ECO57 Reviewed; 197 AA.
AC P69772; Q9X728;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=ecdB {ECO:0000303|PubMed:15979273}; Synonyms=pad1;
GN OrderedLocusNames=Z4047, ECs3593;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / EHEC;
RA Carter P.E., Thomson-Carter F.M.;
RT "Comparison of the mutS-rpoS region from Escherichia coli O157:H7,
RT verocytotoxin-containing and non-verocytotoxin-containing E.coli.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [4]
RP FUNCTION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15459342; DOI=10.1110/ps.04953004;
RA Rangarajan E.S., Li Y., Iannuzzi P., Tocilj A., Hung L.-W., Matte A.,
RA Cygler M.;
RT "Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase
RT (Pad1) from Escherichia coli O157: H7.";
RL Protein Sci. 13:3006-3016(2004).
CC -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC detoxification of phenolic derivatives under both aerobic and anaerobic
CC conditions (PubMed:15979273). 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:15979273}.
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 ECO:0000269|PubMed:15459342}.
CC -!- MISCELLANEOUS: It is not known, if phenolic acid decarboxylase forms a
CC complex composed of EdcB, EdcC and EdcD. 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; AJ006210; CAB43500.1; -; Genomic_DNA.
DR EMBL; AE005174; AAG57846.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37016.1; -; Genomic_DNA.
DR PIR; A91078; A91078.
DR PIR; T44998; T44998.
DR RefSeq; NP_311620.1; NC_002695.1.
DR RefSeq; WP_000767724.1; NZ_SWKA01000005.1.
DR PDB; 1SBZ; X-ray; 2.00 A; A/B/C/D=1-197.
DR PDBsum; 1SBZ; -.
DR AlphaFoldDB; P69772; -.
DR SMR; P69772; -.
DR STRING; 155864.EDL933_3908; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR EnsemblBacteria; AAG57846; AAG57846; Z4047.
DR EnsemblBacteria; BAB37016; BAB37016; ECs_3593.
DR GeneID; 914685; -.
DR KEGG; ece:Z4047; -.
DR KEGG; ecs:ECs_3593; -.
DR PATRIC; fig|386585.9.peg.3756; -.
DR eggNOG; COG0163; Bacteria.
DR HOGENOM; CLU_074522_0_1_6; -.
DR OMA; FERWNGW; -.
DR BRENDA; 4.1.1.98; 2026.
DR EvolutionaryTrace; P69772; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Detoxification;
KW Flavoprotein; FMN; Prenyltransferase; Reference proteome; Transferase.
FT CHAIN 1..197
FT /note="Probable UbiX-like flavin prenyltransferase"
FT /id="PRO_0000134963"
FT BINDING 9..11
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01986,
FT ECO:0000269|PubMed:15459342, ECO:0007744|PDB:1SBZ"
FT BINDING 36
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01986,
FT ECO:0000269|PubMed:15459342, ECO:0007744|PDB:1SBZ"
FT BINDING 87..90
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01986,
FT ECO:0000269|PubMed:15459342, ECO:0007744|PDB:1SBZ"
FT BINDING 122
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01986,
FT ECO:0000269|PubMed:15459342, ECO:0007744|PDB:1SBZ"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1SBZ"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1SBZ"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1SBZ"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1SBZ"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:1SBZ"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1SBZ"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:1SBZ"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:1SBZ"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1SBZ"
SQ SEQUENCE 197 AA; 21470 MW; 447F942D2C03428F CRC64;
MKLIVGMTGA TGAPLGVALL QALREMPNVE THLVMSKWAK TTIELETPYS ARDVAALADF
SHNPADQAAT ISSGSFRTDG MIVIPCSMKT LAGIRAGYAD GLVGRAADVV LKEGRKLVLV
PREMPLSTIH LENMLALSRM GVAMVPPMPA FYNHPETVDD IVHHVVARVL DQFGLEHPYA
RRWQGLPQAR NFSQENE
