YIGB_SHIFL
ID YIGB_SHIFL Reviewed; 238 AA.
AC P0ADP1; P23306; P76757;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Flavin mononucleotide phosphatase YigB;
DE EC=3.1.3.-;
DE AltName: Full=FMN phosphatase;
GN Name=yigB; OrderedLocusNames=SF3890, S3866;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the dephosphorylation of flavin mononucleotide
CC (FMN). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Magnesium. Can also use other divalent metal cations as manganese,
CC cobalt or zinc. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE005674; AAN45326.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18874.1; -; Genomic_DNA.
DR RefSeq; NP_709619.1; NC_004337.2.
DR RefSeq; WP_001213584.1; NZ_WPGW01000139.1.
DR AlphaFoldDB; P0ADP1; -.
DR SMR; P0ADP1; -.
DR STRING; 198214.SF3890; -.
DR PRIDE; P0ADP1; -.
DR EnsemblBacteria; AAN45326; AAN45326; SF3890.
DR EnsemblBacteria; AAP18874; AAP18874; S3866.
DR GeneID; 1025991; -.
DR GeneID; 67414402; -.
DR KEGG; sfl:SF3890; -.
DR KEGG; sfx:S3866; -.
DR PATRIC; fig|198214.7.peg.4587; -.
DR HOGENOM; CLU_045011_8_2_6; -.
DR OMA; PQETHDT; -.
DR OrthoDB; 1204073at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..238
FT /note="Flavin mononucleotide phosphatase YigB"
FT /id="PRO_0000169652"
FT ACT_SITE 16
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 16..18
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 238 AA; 27122 MW; 9C1BDE710641E0D6 CRC64;
MRFYRPLGRI SALTFDLDDT LYDNRPVILR TEREALTFVQ NYHPALRSFQ NEDLQRLRQA
VREAEPEIYH DVTRWRFRSI EQAMLDAGLS AEEASAGAHA AMINFAKWRS RIDVPQQTHD
TLKQLAKKWP LVAITNGNAQ PELFGLGDYF EFVLRAGPHG RSKPFSDMYF LAAEKLNVPI
GEILHVGDDL TTDVGGAIRS GMQACWIRPE NGDLMQTWDS RLLPHLEISR LASLTSLI
