YIHX_SHIFL
ID YIHX_SHIFL Reviewed; 199 AA.
AC P0A8Y4; P32145;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alpha-D-glucose-1-phosphate phosphatase YihX;
DE Short=Alpha-D-glucose-1-P phosphatase;
DE EC=3.1.3.10;
DE AltName: Full=Alpha-D-glucose-1-phosphatase;
GN Name=yihX; OrderedLocusNames=SF3957, S3789;
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 alpha-D-glucose 1-
CC phosphate (Glc1P) and, to a lesser extent, of other sugar phosphates.
CC {ECO:0000250|UniProtKB:P0A8Y3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate;
CC Xref=Rhea:RHEA:19933, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=3.1.3.10;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y3};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y3};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0A8Y3};
CC Note=Magnesium. Can also use other divalent metal cations such as
CC manganese, cobalt or zinc. {ECO:0000250|UniProtKB:P0A8Y3};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. YihX family.
CC {ECO:0000305}.
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DR EMBL; AE005674; AAN45392.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18808.1; -; Genomic_DNA.
DR RefSeq; NP_709685.2; NC_004337.2.
DR RefSeq; WP_001295269.1; NZ_WPGW01000092.1.
DR AlphaFoldDB; P0A8Y4; -.
DR SMR; P0A8Y4; -.
DR STRING; 198214.SF3957; -.
DR PRIDE; P0A8Y4; -.
DR EnsemblBacteria; AAN45392; AAN45392; SF3957.
DR EnsemblBacteria; AAP18808; AAP18808; S3789.
DR GeneID; 1025513; -.
DR GeneID; 66672209; -.
DR KEGG; sfl:SF3957; -.
DR KEGG; sfx:S3789; -.
DR PATRIC; fig|198214.7.peg.4662; -.
DR HOGENOM; CLU_045011_9_5_6; -.
DR OMA; IDIDFNR; -.
DR OrthoDB; 1669868at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0008877; F:glucose-1-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR Gene3D; 1.10.150.240; -; 1.
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 InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..199
FT /note="Alpha-D-glucose-1-phosphate phosphatase YihX"
FT /id="PRO_0000066266"
FT ACT_SITE 6
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 6..8
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 6
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 107..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 199 AA; 22732 MW; 9451EA8917DFC0D2 CRC64;
MLYIFDLGNV IVDIDFNRVL GAWSDLTRIP LASLKKSFHM GEAFHQHERG EISDEAFAEA
LCHEMALPLS YEQFSHGWQA VFVALRPEVI AIMHKLREQG HRVVVLSNTN RLHTTFWPEE
YPEIRDAADH IYLSQDLGMR KPEARIYQHV LQAEGFSPSD TVFFDDNADN IEGANQLGIT
SILVKDKTTI PDYFAKVLC
