ID   BSDD_BACSU              Reviewed;          75 AA.
AC   C0H3U9; P94406; Q797P7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Protein BsdD {ECO:0000305|PubMed:18388975};
DE   AltName: Full=Phenolic acid decarboxylase subunit D {ECO:0000303|PubMed:18388975};
DE            Short=PAD {ECO:0000303|PubMed:18388975};
GN   Name=bsdD {ECO:0000303|PubMed:18388975}; OrderedLocusNames=BSU03651;
GN   ORFNames=BSU03650;
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   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   [4]
RP   FUNCTION IN DETOXIFICATION OF PHENOLIC DERIVATIVES, NOMENCLATURE, AND
RP   SEQUENCE REVISION TO 75.
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   [5]
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, however the precise biochemical function of BsdD in
CC       metabolism of phenolic acid is unknown. {ECO:0000269|PubMed:18388975}.
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       {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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA08998.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D50453; BAA08998.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAX52546.1; -; Genomic_DNA.
DR   PIR; A69762; A69762.
DR   RefSeq; WP_010886405.1; NZ_JNCM01000031.1.
DR   RefSeq; YP_003097675.1; NC_000964.3.
DR   AlphaFoldDB; C0H3U9; -.
DR   SMR; C0H3U9; -.
DR   STRING; 224308.BSU03651; -.
DR   EnsemblBacteria; CAX52546; CAX52546; BSU_03651.
DR   GeneID; 8302940; -.
DR   KEGG; bsu:BSU03651; -.
DR   PATRIC; fig|224308.179.peg.384; -.
DR   eggNOG; ENOG5032SBW; Bacteria.
DR   OMA; EGAWEVY; -.
DR   BioCyc; BSUB:BSU03651-MON; -.
DR   BRENDA; 4.1.1.61; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Detoxification; Reference proteome.
FT   CHAIN           1..75
FT                   /note="Protein BsdD"
FT                   /id="PRO_0000378108"
SQ   SEQUENCE   75 AA;  8569 MW;  7F106D92370FF997 CRC64;
     MHTCPRCDSK KGEVMSKSPV EGAWEVYQCQ TCFFTWRSCE PESITNPEKY NPAFKIDPKE
     TETAIEVPAV PERKA