(data stored in SCRATCH zone)

SWISSPROT: PADL_BACSU

ID   PADL_BACSU              Reviewed;         204 AA.
AC   P94404;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 124.
DE   RecName: Full=Probable UbiX-like flavin prenyltransferase {ECO:0000255|HAMAP-Rule:MF_01986};
DE            EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01986};
DE   AltName: Full=Phenolic acid decarboxylase subunit B {ECO:0000255|HAMAP-Rule:MF_01986};
DE            Short=PAD {ECO:0000255|HAMAP-Rule:MF_01986};
GN   Name=bsdB {ECO:0000303|PubMed:18388975};
GN   Synonyms=ubiX {ECO:0000303|PubMed:26658822},
GN   yclB {ECO:0000303|PubMed:8969502}; OrderedLocusNames=BSU03630;
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, AND NOMENCLATURE.
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   [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 (PubMed:18388975). Flavin prenyltransferase that catalyzes
CC       the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic
CC       acid decarboxylase (By similarity). {ECO:0000255|HAMAP-Rule:MF_01986,
CC       ECO:0000269|PubMed:18388975}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2;
CC         Xref=Rhea:RHEA:37743, ChEBI:CHEBI:43474, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:87467, ChEBI:CHEBI:88052; EC=2.5.1.129;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01986};
CC   -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_01986}.
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 UbiX/PAD1 family. YclB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01986}.
DR   EMBL; D50453; BAA08996.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12157.1; -; Genomic_DNA.
DR   PIR; G69761; G69761.
DR   RefSeq; NP_388245.1; NC_000964.3.
DR   RefSeq; WP_009966530.1; NZ_JNCM01000031.1.
DR   SMR; P94404; -.
DR   IntAct; P94404; 1.
DR   STRING; 224308.BSU03630; -.
DR   PaxDb; P94404; -.
DR   PRIDE; P94404; -.
DR   EnsemblBacteria; CAB12157; CAB12157; BSU03630.
DR   GeneID; 938296; -.
DR   KEGG; bsu:BSU03630; -.
DR   PATRIC; fig|224308.43.peg.375; -.
DR   eggNOG; ENOG4108UMA; Bacteria.
DR   eggNOG; COG0163; LUCA.
DR   HOGENOM; HOG000225437; -.
DR   InParanoid; P94404; -.
DR   KO; K03186; -.
DR   OMA; DHIVFRT; -.
DR   PhylomeDB; P94404; -.
DR   BioCyc; BSUB:BSU03630-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009108; P:coenzyme biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   HAMAP; MF_01984; ubiX_pad; 1.
DR   HAMAP; MF_01986; ubiX_pad_yclB; 1.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR004507; UbiX-like.
DR   InterPro; IPR032901; UbiX_pad_YclB.
DR   PANTHER; PTHR43374; PTHR43374; 1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P94404.
DR   SWISS-2DPAGE; P94404.
KW   Aromatic hydrocarbons catabolism; Detoxification; Flavoprotein; FMN;
KW   Prenyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..204
FT                   /note="Probable UbiX-like flavin prenyltransferase"
FT                   /id="PRO_0000134957"
FT   NP_BIND         21..23
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT   NP_BIND         98..101
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT   BINDING         47
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT   BINDING         133
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
SQ   SEQUENCE   204 AA;  22539 MW;  F6C1A5219365D728 CRC64;
     MKAEFKRKGG GKVKLVVGMT GATGAIFGVR LLQWLKAAGV ETHLVVSPWA NVTIKHETGY
     TLQEVEQLAT YTYSHKDQAA AISSGSFDTD GMIVAPCSMK SLASIRTGMA DNLLTRAADV
     MLKERKKLVL LTRETPLNQI HLENMLALTK MGTIILPPMP AFYNRPRSLE EMVDHIVFRT
     LDQFGIRLPE AKRWNGIEKQ KGGA
//

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