CATD_BACSU
ID CATD_BACSU Reviewed; 134 AA.
AC P54720;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative oxidoreductase CatD;
DE EC=1.-.-.-;
GN Name=catD; Synonyms=yfiD; OrderedLocusNames=BSU08230;
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=8704981; DOI=10.1099/13500872-142-6-1417;
RA Yamamoto H., Uchiyama S., Fajar A.N., Ogasawara N., Sekiguchi J.;
RT "Determination of a 12 kb nucleotide sequence around the 76 degrees region
RT of the Bacillus subtilis chromosome.";
RL Microbiology 142:1417-1421(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, AND INDUCTION.
RC STRAIN=168;
RX PubMed=16872404; DOI=10.1111/j.1462-2920.2006.01034.x;
RA Tam le T., Eymann C., Albrecht D., Sietmann R., Schauer F., Hecker M.,
RA Antelmann H.;
RT "Differential gene expression in response to phenol and catechol reveals
RT different metabolic activities for the degradation of aromatic compounds in
RT Bacillus subtilis.";
RL Environ. Microbiol. 8:1408-1427(2006).
RN [4]
RP INDUCTION, AND NOMENCLATURE.
RC STRAIN=168;
RX PubMed=17407181; DOI=10.1002/pmic.200700008;
RA Nguyen V.D., Wolf C., Maeder U., Lalk M., Langer P., Lindequist U.,
RA Hecker M., Antelmann H.;
RT "Transcriptome and proteome analyses in response to 2-methylhydroquinone
RT and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems
RT involved in the catabolism of aromatic compounds in Bacillus subtilis.";
RL Proteomics 7:1391-1408(2007).
CC -!- FUNCTION: Essential for growth and viability in the presence of
CC catechol and probably involved in the detoxification of catechol.
CC {ECO:0000269|PubMed:16872404}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Strongly induced by catechol, less strongly by 2-
CC methylhydroquinone (2-MHQ) but only weakly by chromanon (6-brom-2-
CC vinyl-chroman-4-on). {ECO:0000269|PubMed:16872404,
CC ECO:0000269|PubMed:17407181}.
CC -!- SIMILARITY: Belongs to the DoxX family. {ECO:0000305}.
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DR EMBL; D50543; BAA09108.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12652.1; -; Genomic_DNA.
DR PIR; G69802; G69802.
DR RefSeq; NP_388704.1; NC_000964.3.
DR RefSeq; WP_003244204.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P54720; -.
DR SMR; P54720; -.
DR STRING; 224308.BSU08230; -.
DR PaxDb; P54720; -.
DR EnsemblBacteria; CAB12652; CAB12652; BSU_08230.
DR GeneID; 939204; -.
DR KEGG; bsu:BSU08230; -.
DR PATRIC; fig|224308.179.peg.889; -.
DR eggNOG; COG2259; Bacteria.
DR InParanoid; P54720; -.
DR OMA; YVIATIE; -.
DR PhylomeDB; P54720; -.
DR BioCyc; BSUB:BSU08230-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; 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 InterPro; IPR032808; DoxX.
DR Pfam; PF07681; DoxX; 1.
PE 2: Evidence at transcript level;
KW Aromatic hydrocarbons catabolism; Cell membrane; Detoxification; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..134
FT /note="Putative oxidoreductase CatD"
FT /id="PRO_0000049524"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 134 AA; 14419 MW; 6BCF8F7EDAB67117 CRC64;
MNKSFEIGTL LLRVITGIIF FVHGLSKFQG MEGTIQFFGS IGLPSFMAYV IAAIELIGGV
LVFFGLATRI VGVLFALTLI GAIITVKLKA PFMGNAEFDY LLLLTSIHLA LTGSRFLALD
PFVFKGKKNG NVSA