YCLC_SEDHY
ID YCLC_SEDHY Reviewed; 480 AA.
AC Q9S4M7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Phenolic acid decarboxylase {ECO:0000255|HAMAP-Rule:MF_01985, ECO:0000303|PubMed:7744052};
DE Short=PAD {ECO:0000255|HAMAP-Rule:MF_01985, ECO:0000303|PubMed:7744052};
DE AltName: Full=3,4-dihydroxybenzoate decarboxylase {ECO:0000303|PubMed:7744052};
DE Short=3,4-dihydroxybenzoate DC {ECO:0000303|PubMed:7744052};
DE EC=4.1.1.63 {ECO:0000269|PubMed:7744052, ECO:0000305|PubMed:10438791};
DE AltName: Full=4-hydroxybenzoate decarboxylase {ECO:0000303|PubMed:10438791};
DE Short=4-HOB-DC {ECO:0000303|PubMed:10438791};
DE Short=4-hydroxybenzoate DC {ECO:0000303|PubMed:7744052};
DE EC=4.1.1.61 {ECO:0000269|PubMed:7744052, ECO:0000305|PubMed:10438791, ECO:0000305|PubMed:15979273};
DE AltName: Full=Phenolic acid decarboxylase subunit C {ECO:0000303|PubMed:7744052};
GN Name=shdC {ECO:0000303|PubMed:15979273};
GN Synonyms=ohb1 {ECO:0000303|PubMed:10438791};
OS Sedimentibacter hydroxybenzoicus (Clostridium hydroxybenzoicum).
OC Bacteria; Firmicutes; Tissierellia; Sedimentibacter.
OX NCBI_TaxID=29345;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 61-82; 245-268 AND
RP 384-407, FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1;
RX PubMed=10438791; DOI=10.1128/jb.181.16.5119-5122.1999;
RA Huang J., He Z., Wiegel J.;
RT "Cloning, characterization, and expression of a novel gene encoding a
RT reversible 4-hydroxybenzoate decarboxylase from Clostridium
RT hydroxybenzoicum.";
RL J. Bacteriol. 181:5119-5122(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-22, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1;
RX PubMed=7744052; DOI=10.1111/j.1432-1033.1995.tb20440.x;
RA He Z., Wiegel J.;
RT "Purification and characterization of an oxygen-sensitive reversible 4-
RT hydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum.";
RL Eur. J. Biochem. 229:77-82(1995).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1;
RX PubMed=24193968; DOI=10.1007/bf02543871;
RA Zhang X., Wiegel J.;
RT "Isolation and partial characterization of a Clostridium species
RT transforming para-hydroxybenzoate and 3,4-dihydroxybenzoate and producing
RT phenols as the final transformation products.";
RL Microb. Ecol. 20:103-121(1990).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1;
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 anaerobic conditions
CC (PubMed:10438791, PubMed:7744052, PubMed:24193968, PubMed:15979273).
CC Oxygen-sensitive phenolic acid decarboxylase that catalyzes the
CC reversible decarboxylation of 4-hydroxybenzoate and 3,4-
CC dihydroxybenzoate (PubMed:10438791, PubMed:7744052, PubMed:15979273).
CC {ECO:0000269|PubMed:10438791, ECO:0000269|PubMed:15979273,
CC ECO:0000269|PubMed:24193968, ECO:0000269|PubMed:7744052}.
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; Evidence={ECO:0000269|PubMed:7744052,
CC ECO:0000305|PubMed:10438791, ECO:0000305|PubMed:15979273};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoate + H(+) = catechol + CO2;
CC Xref=Rhea:RHEA:22416, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:36241; EC=4.1.1.63;
CC Evidence={ECO:0000269|PubMed:7744052, ECO:0000305|PubMed:10438791};
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 -!- ACTIVITY REGULATION: Inhibited by Zn(2+), (2,3,4)-trihydroxybenzoate
CC and (3,4,5)-trihydroxybenzoate (PubMed:7744052). Ammonium and rubidium
CC ions decrease the activity of the carboxylation of 3,4-
CC dihydroxybenzoate by about 20% (PubMed:7744052).
CC {ECO:0000269|PubMed:7744052}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for 4-hydroxybenzoate {ECO:0000269|PubMed:7744052};
CC KM=1.2 mM for 3,4-dihydroxybenzoate {ECO:0000269|PubMed:7744052};
CC Note=kcat is 3300 min(-1) with 4-hydroxybenzoate as substrate. kcat
CC is 1100 min(-1) with 3,4-dihydroxybenzoate as substrate.
CC {ECO:0000269|PubMed:7744052};
CC pH dependence:
CC Optimum pH is between 5.6-6.2. {ECO:0000269|PubMed:7744052};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:7744052};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:7744052}.
CC -!- INDUCTION: By 4-hydroxybenzoate and 3,4-dihydroxybenzoate.
CC {ECO:0000305|PubMed:24193968}.
CC -!- MISCELLANEOUS: It is not known, if phenolic acid decarboxylase forms a
CC complex composed of ShdB, ShdC and ShdD. 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; AF128880; AAD50377.1; -; Genomic_DNA.
DR PDB; 7AE4; X-ray; 3.31 A; A/B/C/D/E/F=1-480.
DR PDB; 7AE5; X-ray; 2.19 A; A/B/C/D/E/F=1-480.
DR PDB; 7AE7; X-ray; 2.66 A; A/B/C/D/E/F=1-480.
DR PDBsum; 7AE4; -.
DR PDBsum; 7AE5; -.
DR PDBsum; 7AE7; -.
DR AlphaFoldDB; Q9S4M7; -.
DR SMR; Q9S4M7; -.
DR BRENDA; 4.1.1.61; 5658.
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:0050223; F:protocatechuate decarboxylase 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 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 3D-structure; Aromatic hydrocarbons catabolism; Decarboxylase;
KW Detoxification; Direct protein sequencing; Flavoprotein; FMN; Lyase;
KW Manganese; Metal-binding.
FT CHAIN 1..480
FT /note="Phenolic acid decarboxylase"
FT /id="PRO_0000434526"
FT REGION 443..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 163..168
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 184..185
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT CONFLICT 6
FT /note="K -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:7AE5"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:7AE7"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:7AE5"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:7AE7"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 287..299
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:7AE5"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 364..372
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 397..407
FT /evidence="ECO:0007829|PDB:7AE5"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:7AE5"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:7AE5"
FT HELIX 464..475
FT /evidence="ECO:0007829|PDB:7AE5"
SQ SEQUENCE 480 AA; 53961 MW; BA30D2E2C503D443 CRC64;
MAKVYKDLRE FLEVLEQEGQ LIRVKEEVNP EPDIAAAGRA AANLGKNQPA VFFEKIKGYK
YSVVTNVHGS WQNHALMLGL DKNTSTKDQF YELNRRWDKF PVPPNVVKRE AAPCKENVID
KDINLFEILP LYRINEQDGG FYISKASVVT ADPEYPDDFN KLNVGTYRIQ VKDRDRVGIQ
ALAMHDIAVQ LEKAEAENKP LPIAITIGNN PLVTFMASTP VGYNQNEYEF VGALQDGVPM
DIVKSDLYDH LYVPAGSEVV LEGHIIPRVR TVEGPFGEFP GSYSGARLQC EVKIDRITHR
TNPIFENLYL GIPWTEIDYL MALNTSVPLY KQLKETMPEV VAVNAMYTHG IGVIISTKVR
YGGYAKGVAF RLLSTPHGMP YSKIVIVVDE FVDPFNLEQV MWALTTRVHP GKDVSIIENC
PGMPLDPSTN PPGMHTKMII DATTPVPPEP NPRETQLLDP PDGTEEWEEK LKELLKNQNR
