ID   YITU_BACSU              Reviewed;         270 AA.
AC   P70947; O08140; Q796P8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YitU {ECO:0000305|PubMed:26316208};
DE            EC=3.1.3.104 {ECO:0000269|PubMed:26316208};
GN   Name=yitU; OrderedLocusNames=BSU11140;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA   Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT   "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT   degrees) in Bacillus subtilis.";
RL   Microbiology 143:3305-3308(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9025291; DOI=10.1099/00221287-143-1-175;
RA   Levine A., Vannier F., Roche B., Autret S., Mavel D., Seror S.J.;
RT   "A 10.3 kbp segment from nprB to argJ at the 102 degrees region of the
RT   Bacillus subtilis chromosome.";
RL   Microbiology 143:175-177(1997).
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   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).
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). {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:26316208};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=81 uM for 5-amino-6-(5-phospho-D-ribitylamino)uracil
CC         {ECO:0000269|PubMed:26316208};
CC         Vmax=1.7 umol/min/mg enzyme with 5-amino-6-(5-phospho-D-
CC         ribitylamino)uracil as substrate {ECO:0000269|PubMed:26316208};
CC         Vmax=17 umol/min/mg enzyme with flavin mononucleotide
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}.
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DR   EMBL; Y09476; CAA70632.1; -; Genomic_DNA.
DR   EMBL; Z79580; CAB01836.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12954.1; -; Genomic_DNA.
DR   PIR; F69841; F69841.
DR   RefSeq; NP_388995.1; NC_000964.3.
DR   RefSeq; WP_003233007.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P70947; -.
DR   SMR; P70947; -.
DR   STRING; 224308.BSU11140; -.
DR   PaxDb; 224308-BSU11140; -.
DR   EnsemblBacteria; CAB12954; CAB12954; BSU_11140.
DR   GeneID; 939795; -.
DR   KEGG; bsu:BSU11140; -.
DR   PATRIC; fig|224308.179.peg.1198; -.
DR   eggNOG; COG0561; Bacteria.
DR   InParanoid; P70947; -.
DR   OrthoDB; 9781413at2; -.
DR   PhylomeDB; P70947; -.
DR   BioCyc; BSUB:BSU11140-MONOMER; -.
DR   BRENDA; 3.1.3.104; 658.
DR   SABIO-RK; P70947; -.
DR   UniPathway; UPA00275; UER00403.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043726; F:5-amino-6-(5-phosphoribitylamino)uracil phosphatase activity; IEA:RHEA.
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   CDD; cd07516; HAD_Pase; 1.
DR   Gene3D; 3.30.1240.10; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR000150; Cof.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR00099; Cof-subfamily; 1.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR10000:SF23; 5-AMINO-6-(5-PHOSPHO-D-RIBITYLAMINO)URACIL PHOSPHATASE YITU; 1.
DR   PANTHER; PTHR10000; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome;
KW   Riboflavin biosynthesis.
FT   CHAIN           1..270
FT                   /note="5-amino-6-(5-phospho-D-ribitylamino)uracil
FT                   phosphatase YitU"
FT                   /id="PRO_0000359903"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..46
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  30633 MW;  F8A909972758E25A CRC64;
     METKPYLIAL DLDGTLLKDD KTISENTLHT IQRLKDDGHY VCISTGRPYR SSSMYYQQME
     LTTPIVNFNG AFVHHPQDDS WGRYHTSLPL DVVKQLVDIS ESYNVHNVLA EVIDDVYFHY
     HDEHLIDAFN MNTTNVTVGD LRENLGEDVT SVLIHAKEED VPAIRSYLSD VHAEVIDHRR
     WAAPWHVIEI IKSGMNKAVG LQKISDYYGV PRERIIAFGD EDNDLEMLEF AGCGVAMGNG
     IDAVKQIANR TTATNEEDGV ARFLKEYFSL
//