YCLC_ECO57
ID YCLC_ECO57 Reviewed; 475 AA.
AC Q7DBA7; Q7ABA7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phenolic acid decarboxylase {ECO:0000255|HAMAP-Rule:MF_01985, ECO:0000303|PubMed:15979273};
DE Short=PAD {ECO:0000255|HAMAP-Rule:MF_01985, ECO:0000303|PubMed:15979273};
DE AltName: Full=4-hydroxybenzoate decarboxylase {ECO:0000303|PubMed:15979273};
DE Short=4-hydroxybenzoate DC {ECO:0000303|PubMed:15979273};
DE EC=4.1.1.61 {ECO:0000269|PubMed:15979273};
DE AltName: Full=Phenolic acid decarboxylase subunit C {ECO:0000303|PubMed:15979273};
DE AltName: Full=Vanillate decarboxylase {ECO:0000303|PubMed:15979273};
DE Short=Vanillate DC {ECO:0000303|PubMed:15979273};
DE EC=4.1.1.- {ECO:0000269|PubMed:15979273};
GN Name=edcC {ECO:0000303|PubMed:15979273}; Synonyms=yclC;
GN OrderedLocusNames=ECs3592, Z4046;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
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 [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 FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
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).
CC -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC detoxification of phenolic derivatives under both aerobic and anaerobic
CC conditions. Phenolic acid decarboxylase that catalyzes the reversible
CC decarboxylation of 4-hydroxybenzoate and vanillate.
CC {ECO:0000269|PubMed:15979273}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + H(+) = CO2 + phenol; Xref=Rhea:RHEA:10876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15882, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17879; EC=4.1.1.61;
CC Evidence={ECO:0000269|PubMed:15979273};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + vanillate = CO2 + guaiacol; Xref=Rhea:RHEA:51528,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16632,
CC ChEBI:CHEBI:28591; Evidence={ECO:0000269|PubMed:15979273};
CC -!- COFACTOR:
CC Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01985};
CC Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01985};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01985};
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 UbiD family. YclC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01985}.
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DR EMBL; AE005174; AAG57845.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37015.1; -; Genomic_DNA.
DR RefSeq; NP_311619.1; NC_002695.1.
DR RefSeq; WP_000863205.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q7DBA7; -.
DR SMR; Q7DBA7; -.
DR STRING; 155864.EDL933_3907; -.
DR EnsemblBacteria; AAG57845; AAG57845; Z4046.
DR EnsemblBacteria; BAB37015; BAB37015; ECs_3592.
DR GeneID; 914686; -.
DR KEGG; ece:Z4046; -.
DR KEGG; ecs:ECs_3592; -.
DR PATRIC; fig|386585.9.peg.3755; -.
DR eggNOG; COG0043; Bacteria.
DR HOGENOM; CLU_023348_3_2_6; -.
DR OMA; TEGGCCW; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0018799; F:4-hydroxybenzoate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 HAMAP; MF_01985; UbiD_YclC; 1.
DR InterPro; IPR032902; BsdC.
DR InterPro; IPR002830; UbiD.
DR PANTHER; PTHR30108; PTHR30108; 1.
DR Pfam; PF01977; UbiD; 1.
DR TIGRFAMs; TIGR00148; TIGR00148; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Decarboxylase; Detoxification;
KW Flavoprotein; FMN; Lyase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..475
FT /note="Phenolic acid decarboxylase"
FT /id="PRO_0000434527"
FT ACT_SITE 274
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 161..166
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 182..183
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
SQ SEQUENCE 475 AA; 52395 MW; 88869E1A0AA431C7 CRC64;
MAFDDLRSFL QALDDHGQLL KISEEVNAEP DLAAAANATG RIGDGAPALW FDNIRGFTDA
RVAMNTIGSW QNHAISLGLP PNTPVKKQID EFIRRWDNFP IAPERRANPA WAQNTVDGDE
INLFDILPLF RLNDGDGGFY LDKACVVSRD PLDPDNFGKQ NVGIYRMEVK GKRKLGLQPV
PMHDIALHLH KAEERGEDLP IAITLGNDPI ITLMGATPLK YDQSEYEMAG ALRESPYPIA
TAPLTGFDVP WGSEVILEGV IESRKREIEG PFGEFTGHYS GGRNMTVVRI DKVSYRTRPI
FESLYLGMPW TEIDYLMGPA TCVPLYQQLK AEFPEVQAVN AMYTHGLLAI ISTKKRYGGF
ARAVGLRAMT TPHGLGYVKM VIMVDEDVDP FNLPQVMWAL SSKVNPAGDL VQLPNMSVLE
LDPGSSPAGI TDKLIIDATT PVAPDNRGHY SQPVVDLPET KAWAEKLTAM LAARK
