YWPJ_BACSU
ID YWPJ_BACSU Reviewed; 285 AA.
AC P94592; Q795B2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Phosphatase YwpJ {ECO:0000305|PubMed:26316208};
DE EC=3.1.3.- {ECO:0000269|PubMed:26316208};
GN Name=ywpJ; OrderedLocusNames=BSU36290;
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=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PHOSPHATE AND CALCIUM
RP IONS.
RG Midwest center for structural genomics (MCSG);
RT "The structure of a haloacid dehalogenase-like hydrolase from B.
RT subtilis.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the dephosphorylation of phosphorylated 5-6 carbon
CC sugars and monophosphate nucleotides (NMP) in vitro (By similarity). To
CC a lesser extent, dephosphorylates flavin mononucleotide (FMN) in vitro
CC (PubMed:26316208). {ECO:0000250|UniProtKB:P96741,
CC 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 Vmax=0.009 umol/min/mg enzyme with flavin mononucleotide
CC {ECO:0000269|PubMed:26316208};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC {ECO:0000305}.
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DR EMBL; Z83337; CAB05952.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15646.1; -; Genomic_DNA.
DR PIR; C70066; C70066.
DR RefSeq; NP_391510.1; NC_000964.3.
DR RefSeq; WP_003242946.1; NZ_JNCM01000034.1.
DR PDB; 1NRW; X-ray; 1.70 A; A=1-285.
DR PDBsum; 1NRW; -.
DR AlphaFoldDB; P94592; -.
DR SMR; P94592; -.
DR STRING; 224308.BSU36290; -.
DR PaxDb; P94592; -.
DR PRIDE; P94592; -.
DR EnsemblBacteria; CAB15646; CAB15646; BSU_36290.
DR GeneID; 936907; -.
DR KEGG; bsu:BSU36290; -.
DR PATRIC; fig|224308.179.peg.3928; -.
DR eggNOG; COG0561; Bacteria.
DR InParanoid; P94592; -.
DR OMA; YYYEVFT; -.
DR PhylomeDB; P94592; -.
DR BioCyc; BSUB:BSU36290-MON; -.
DR EvolutionaryTrace; P94592; -.
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 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.
DR PROSITE; PS01228; COF_1; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..285
FT /note="Phosphatase YwpJ"
FT /id="PRO_0000360521"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 8
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 41..42
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 214
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 240
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 282..283
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 8..12
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1NRW"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:1NRW"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1NRW"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:1NRW"
SQ SEQUENCE 285 AA; 31955 MW; 003BFFF619CBC439 CRC64;
MKLIAIDLDG TLLNSKHQVS LENENALRQA QRDGIEVVVS TGRAHFDVMS IFEPLGIKTW
VISANGAVIH DPEGRLYHHE TIDKKRAYDI LSWLESENYY YEVFTGSAIY TPQNGRELLD
VELDRFRSAN PEADLSVLKQ AAEVQYSQSG FAYINSFQEL FEADEPIDFY NILGFSFFKE
KLEAGWKRYE HAEDLTLVSS AEHNFELSSR KASKGQALKR LAKQLNIPLE ETAAVGDSLN
DKSMLEAAGK GVAMGNARED IKSIADAVTL TNDEHGVAHM MKHLL
