YITU_BACSU
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 03-AUG-2022, entry version 127.
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; Firmicutes; 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; P70947; -.
DR PRIDE; P70947; -.
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 OMA; CCAERGI; -.
DR PhylomeDB; P70947; -.
DR BioCyc; BSUB:BSU11140-MON; -.
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 Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR000150; Cof.
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; TIGR00099; Cof-subfamily; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 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
