(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 122.
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 / 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=4-hydroxy-3-methoxybenzoate + H(+) = CO2 + guaiacol;
CC         Xref=Rhea:RHEA:51528, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16632, ChEBI:CHEBI:28591;
CC         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}.
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   SMR; P94405; -.
DR   STRING; 224308.BSU03640; -.
DR   PaxDb; P94405; -.
DR   PRIDE; P94405; -.
DR   EnsemblBacteria; CAB12158; CAB12158; BSU03640.
DR   GeneID; 938291; -.
DR   KEGG; bsu:BSU03640; -.
DR   PATRIC; fig|224308.179.peg.383; -.
DR   eggNOG; ENOG4105D3H; Bacteria.
DR   eggNOG; COG0043; LUCA.
DR   HOGENOM; HOG000227665; -.
DR   InParanoid; P94405; -.
DR   KO; K01612; -.
DR   OMA; VLTEGGC; -.
DR   PhylomeDB; P94405; -.
DR   BioCyc; BSUB:BSU03640-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
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;
DR   PRODOM; P94405.
DR   SWISS-2DPAGE; P94405.
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   REGION          160..165
FT                   /note="Prenyl-FMN binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT   REGION          181..182
FT                   /note="Prenyl-FMN binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT   ACT_SITE        273
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT   METAL           160
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT   METAL           182
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01985"
FT   METAL           224
FT                   /note="Manganese"
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
//

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