YCLC_STRD7
ID YCLC_STRD7 Reviewed; 474 AA.
AC Q9X697;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Phenolic acid decarboxylase {ECO:0000255|HAMAP-Rule:MF_01985, ECO:0000303|PubMed:10517592};
DE Short=PAD {ECO:0000255|HAMAP-Rule:MF_01985};
DE AltName: Full=Phenolic acid decarboxylase subunit C {ECO:0000303|PubMed:10517592};
DE AltName: Full=Vanillate decarboxylase {ECO:0000303|PubMed:10517592};
DE Short=Vanillate DC {ECO:0000303|PubMed:15979273};
DE EC=4.1.1.- {ECO:0000269|PubMed:15979273, ECO:0000305|PubMed:10517592};
GN Name=vdcC {ECO:0000303|PubMed:10517592};
OS Streptomyces sp. (strain D7).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=92742;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-23, FUNCTION,
RP CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=D7;
RX PubMed=10517592; DOI=10.1099/00221287-145-9-2393;
RA Chow K.T., Pope M.K., Davies J.;
RT "Characterization of a vanillic acid non-oxidative decarboxylation gene
RT cluster from Streptomyces sp. D7.";
RL Microbiology 145:2393-2403(1999).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=D7;
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 (PubMed:10517592, PubMed:15979273). Phenolic acid
CC decarboxylase that catalyzes the reversible decarboxylation of
CC vanillate (PubMed:10517592, PubMed:15979273).
CC {ECO:0000269|PubMed:10517592, 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 ECO:0000305|PubMed:10517592};
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 -!- INDUCTION: By vanillate. {ECO:0000269|PubMed:10517592}.
CC -!- MISCELLANEOUS: It is not known, if phenolic acid decarboxylase forms a
CC complex composed of VdcB, VdcC and VdcD. 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; AF134589; AAD28782.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X697; -.
DR SMR; Q9X697; -.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-UniRule.
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 Direct protein sequencing; Flavoprotein; FMN; Lyase; Manganese;
KW Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10517592"
FT CHAIN 2..474
FT /note="Phenolic acid decarboxylase"
FT /id="PRO_0000157367"
FT ACT_SITE 273
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 181..182
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 182
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 224
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
SQ SEQUENCE 474 AA; 52120 MW; 1D4E84542E75C75C CRC64;
MAYDDLRSFL DTLEKEGQLL RITDEVLPEP DLAAAANATG RIGENAPALH FDNVKGFTDA
RIAMNVHGSW ANHALALGLP KNTPVKEQVE EFARRWDAFP VAPERREEAP WRENTQEGED
VDLFSVLPLF RLNDGDGGFY LDKAAVVSRD PEDRDDFGKQ NVGTYRIQVI GTNRLAFHPA
MHDVAQHLRK AEEKGEDLPI AITLGNDPVM AIVAGMPMAY DQSEYEMAGA LRGAPAPIAT
APLTGFDVPW GSEVVIEGVI ESRKRRIEGP FGEFTGHYSG GRRMPVIRVE RVSYRHEPVF
ESLYLGMPWN ECDYLVGPNT CVPLLKQLRA EFPEVQAVNA MYTHGLMVII STAKRYGGFA
KAVGMRAMTT PHGLGYVAQV ILVDEDVDPF NLPQVMWAMS AKVNPKDDVV VIPNLSVLEL
APAAQPAGIS SKMIIDATTP VAPDVRGNFS TPAKDLPETA EWAARLQRLI AARV
