(data stored in ACNUC7421 zone)

SWISSPROT: YCSE_BACSU

ID   YCSE_BACSU              Reviewed;         249 AA.
AC   P42962;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   11-DEC-2019, entry version 128.
DE   RecName: Full=5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YcsE {ECO:0000305|PubMed:26316208};
DE            EC=3.1.3.104 {ECO:0000269|PubMed:26316208};
GN   Name=ycsE; OrderedLocusNames=BSU04040;
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=8574415; DOI=10.1099/13500872-141-12-3241;
RA   Akagawa E., Kurita K., Sugawara T., Nakamura K., Kasahara Y., Ogasawara N.,
RA   Yamane K.;
RT   "Determination of a 17,484 bp nucleotide sequence around the 39 degrees
RT   region of the Bacillus subtilis chromosome and similarity analysis of the
RT   products of putative ORFs.";
RL   Microbiology 141:3241-3245(1995).
RN   [2]
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   [3]
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   [4]
RP   SEQUENCE REVISION TO 155-158 AND 181-186.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   PATHWAY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=26316208; DOI=10.1002/cbic.201500352;
RA   Sarge S., Haase I., Illarionov B., Laudert D., Hohmann H.P., Bacher A.,
RA   Fischer M.;
RT   "Catalysis of an essential step in Vitamin B2 biosynthesis by a consortium
RT   of broad spectrum hydrolases.";
RL   ChemBioChem 16:2466-2469(2015).
RN   [6]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA   Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA   Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA   Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA   Allen K.N., Farelli J.D.;
RT   "Panoramic view of a superfamily of phosphatases through substrate
RT   profiling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of the riboflavin precursor
CC       5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide
CC       (FMN) in vitro (PubMed:26316208). To a lesser extent, may also catalyze
CC       the dephosphorylation of a broad range of substrates such as
CC       phosphorylated sugars and triphosphate nucleotides in vitro
CC       (PubMed:26316208, PubMed:25848029). {ECO:0000269|PubMed:25848029,
CC       ECO:0000269|PubMed:26316208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-
CC         (D-ribitylamino)uracil + phosphate; Xref=Rhea:RHEA:25197,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58421; EC=3.1.3.104;
CC         Evidence={ECO:0000269|PubMed:26316208};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:25848029, ECO:0000269|PubMed:26316208};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=54 uM for 5-amino-6-(5-phospho-D-ribitylamino)uracil
CC         {ECO:0000269|PubMed:26316208};
CC         Vmax=12 umol/min/mg enzyme with 5-amino-6-(5-phospho-D-
CC         ribitylamino)uracil as substrate {ECO:0000269|PubMed:26316208};
CC         Vmax=25 umol/min/mg enzyme with flavin mononucleotide as substrate
CC         {ECO:0000269|PubMed:26316208};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 4/4. {ECO:0000269|PubMed:26316208}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC       {ECO:0000305}.
DR   EMBL; D38161; BAA07356.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA09035.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12212.2; -; Genomic_DNA.
DR   PIR; I39893; I39893.
DR   RefSeq; NP_388286.2; NC_000964.3.
DR   RefSeq; WP_003234424.1; NZ_JNCM01000031.1.
DR   SMR; P42962; -.
DR   STRING; 224308.BSU04040; -.
DR   PRIDE; P42962; -.
DR   EnsemblBacteria; CAB12212; CAB12212; BSU04040.
DR   GeneID; 938252; -.
DR   KEGG; bsu:BSU04040; -.
DR   PATRIC; fig|224308.179.peg.430; -.
DR   HOGENOM; HOG000184780; -.
DR   InParanoid; P42962; -.
DR   KO; K21064; -.
DR   OMA; SAYTHEV; -.
DR   PhylomeDB; P42962; -.
DR   BioCyc; BSUB:BSU04040-MONOMER; -.
DR   BioCyc; MetaCyc:BSU04040-MONOMER; -.
DR   SABIO-RK; P42962; -.
DR   UniPathway; UPA00275; UER00403.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   PROSITE; PS01228; COF_1; 1.
DR   PROSITE; PS01229; COF_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P42962.
DR   SWISS-2DPAGE; P42962.
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome;
KW   Riboflavin biosynthesis.
FT   CHAIN           1..249
FT                   /note="5-amino-6-(5-phospho-D-ribitylamino)uracil
FT                   phosphatase YcsE"
FT                   /id="PRO_0000054429"
FT   REGION          50..51
FT                   /note="Phosphate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        16
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   METAL           16
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           18
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           200
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           201
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /note="Phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        155..158
FT                   /note="NKEL -> TKSS (in Ref. 1; BAA07356 and 2; BAA09035)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181..186
FT                   /note="LAKVTE -> PCQGYG (in Ref. 1; BAA07356 and 2;
FT                   BAA09035)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  28186 MW;  A193E3CDACFF3EF2 CRC64;
     MSVQREDVDI KLIAIDMDGT LLNDEQLISD ENRKAIREAE DKGVYVVIST GRTLMTCREL
     AESLKLSSFL ITANGSEIWD SNFNLVERKL LHTDHIQMMW DLRNKHNTNF WASTVNKVWR
     GEFPENITDH EWLKFGFDIE DDDIRNEVLE ELRKNKELEI TNSSPTNIEV NALGINKAAA
     LAKVTEKLGF TMENVMAMGD SLNDIAMIKE AGLGVAMGNA QDIVKETADY ITDTNIEDGV
     AKAIRHWVL
//

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