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 03-AUG-2022, entry version 133.
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 / 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 (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}.
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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 AlphaFoldDB; P94404; -.
DR SMR; P94404; -.
DR IntAct; P94404; 1.
DR STRING; 224308.BSU03630; -.
DR PaxDb; P94404; -.
DR PRIDE; P94404; -.
DR EnsemblBacteria; CAB12157; CAB12157; BSU_03630.
DR GeneID; 938296; -.
DR KEGG; bsu:BSU03630; -.
DR PATRIC; fig|224308.43.peg.375; -.
DR eggNOG; COG0163; Bacteria.
DR InParanoid; P94404; -.
DR OMA; FERWNGW; -.
DR PhylomeDB; P94404; -.
DR BioCyc; BSUB:BSU03630-MON; -.
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: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; 2.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
DR TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE 1: Evidence at protein level;
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 BINDING 21..23
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT BINDING 47
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT BINDING 98..101
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01986"
FT BINDING 133
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
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
