YCLC_BACSU
ID YCLC_BACSU Reviewed; 473 AA.
AC P94405;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
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:18388975, ECO:0000305|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:0000305|PubMed:15979273};
GN Name=bsdC {ECO:0000303|PubMed:15979273};
GN Synonyms=ubiD {ECO:0000303|PubMed:26658822},
GN yclC {ECO:0000303|PubMed:8969502}; OrderedLocusNames=BSU03640;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=168;
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 [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=17295427; DOI=10.1002/pmic.200600706;
RA Duy N.V., Maeder U., Tran N.P., Cavin J.-F., Tam le T., Albrecht D.,
RA Hecker M., Antelmann H.;
RT "The proteome and transcriptome analysis of Bacillus subtilis in response
RT to salicylic acid.";
RL Proteomics 7:698-710(2007).
RN [5]
RP FUNCTION IN DETOXIFICATION OF PHENOLIC DERIVATIVES, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=18388975; DOI=10.1139/w07-113;
RA Lupa B., Lyon D., Shaw L.N., Sieprawska-Lupa M., Wiegel J.;
RT "Properties of the reversible nonoxidative vanillate/4-hydroxybenzoate
RT decarboxylase from Bacillus subtilis.";
RL Can. J. Microbiol. 54:75-81(2008).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / 3NA;
RX PubMed=26658822; DOI=10.1007/s00253-015-7197-6;
RA Graf N., Wenzel M., Altenbuchner J.;
RT "Identification and characterization of the vanillin dehydrogenase YfmT in
RT Bacillus subtilis 3NA.";
RL Appl. Microbiol. Biotechnol. 100:3511-3521(2016).
CC -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC detoxification of phenolic derivatives under both aerobic and anaerobic
CC conditions (PubMed:15979273, PubMed:18388975). Phenolic acid
CC decarboxylase that catalyzes the reversible decarboxylation of 4-
CC hydroxybenzoate and vanillate (PubMed:15979273, PubMed:18388975). Could
CC also catalyze the decarboxylation of salicylate (Probable). Is not
CC active on di- and tri-hydroxybenzoate derivatives (PubMed:18388975).
CC {ECO:0000269|PubMed:15979273, ECO:0000269|PubMed:18388975,
CC ECO:0000305|PubMed:17295427}.
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:18388975, ECO:0000305|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:0000305|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 -!- INDUCTION: Up-regulated by salicylate via the transcriptional regulator
CC BsdA. {ECO:0000269|PubMed:17295427}.
CC -!- DISRUPTION PHENOTYPE: A triple bsdB-bsdC-bsdD deletion mutant no longer
CC converts vanillin to guaiacol, the conversion stops at vanillic acid
CC (PubMed:26658822). {ECO:0000269|PubMed:26658822}.
CC -!- MISCELLANEOUS: It is not known, if phenolic acid decarboxylase forms a
CC complex composed of BsdB, BsdC and BsdD. 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; D50453; BAA08997.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12158.1; -; Genomic_DNA.
DR PIR; H69761; H69761.
DR RefSeq; NP_388246.1; NC_000964.3.
DR RefSeq; WP_003246683.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P94405; -.
DR SMR; P94405; -.
DR STRING; 224308.BSU03640; -.
DR PaxDb; P94405; -.
DR PRIDE; P94405; -.
DR EnsemblBacteria; CAB12158; CAB12158; BSU_03640.
DR GeneID; 938291; -.
DR KEGG; bsu:BSU03640; -.
DR PATRIC; fig|224308.179.peg.383; -.
DR eggNOG; COG0043; Bacteria.
DR InParanoid; P94405; -.
DR OMA; TEGGCCW; -.
DR PhylomeDB; P94405; -.
DR BioCyc; BSUB:BSU03640-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008694; F:3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0018799; F:4-hydroxybenzoate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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 GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
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..473
FT /note="Phenolic acid decarboxylase"
FT /id="PRO_0000157369"
FT ACT_SITE 273
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 160..165
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT BINDING 160
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 473 AA; 53027 MW; A97B23814FDE98BF CRC64;
MAYQDFREFL AALEKEGQLL TVNEEVKPEP DLGASARAAS NLGDKSPALL FNNIYGYHNA
RIAMNVIGSW PNHAMMLGMP KDTPVKEQFF EFAKRYDQFP MPVKREETAP FHENEITEDI
NLFDILPLFR INQGDGGYYL DKACVISRDL EDPDNFGKQN VGIYRMQVKG KDRLGIQPVP
QHDIAIHLRQ AEERGINLPV TIALGCEPVI TTAASTPLLY DQSEYEMAGA IQGEPYRIVK
SKLSDLDVPW GAEVVLEGEI IAGEREYEGP FGEFTGHYSG GRSMPIIKIK RVYHRNNPIF
EHLYLGMPWT ECDYMIGINT CVPLYQQLKE AYPNEIVAVN AMYTHGLIAI VSTKTRYGGF
AKAVGMRALT TPHGLGYCKM VIVVDEDVDP FNLPQVMWAL STKMHPKHDA VIIPDLSVLP
LDPGSNPSGI THKMILDATT PVAPETRGHY SQPLDSPLTT KEWEQKLMDL MNK
