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Database: UniProt
Entry: Q8X8E8_ECO57
LinkDB: Q8X8E8_ECO57
Original site: Q8X8E8_ECO57 
ID   Q8X8E8_ECO57            Unreviewed;       678 AA.
AC   Q8X8E8; A0A0H3JQZ1; A0A6M0JN11; Q7A9B9;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:BAB38223.1};
GN   Name=yihQ {ECO:0000313|EMBL:BAB38223.1};
GN   ORFNames=ECs_4800 {ECO:0000313|EMBL:BAB38223.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB38223.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB38223.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; BA000007; BAB38223.1; -; Genomic_DNA.
DR   RefSeq; NP_312827.1; NC_002695.1.
DR   RefSeq; WP_000380861.1; NZ_VOAI01000016.1.
DR   AlphaFoldDB; Q8X8E8; -.
DR   STRING; 155864.Z5414; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GeneID; 915098; -.
DR   KEGG; ecs:ECs_4800; -.
DR   PATRIC; fig|386585.9.peg.5015; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_017110_0_1_6; -.
DR   OMA; CLTYSSE; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06594; GH31_glucosidase_YihQ; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR044112; YihQ_TIM-like.
DR   PANTHER; PTHR46959; SULFOQUINOVOSIDASE; 1.
DR   PANTHER; PTHR46959:SF2; SULFOQUINOVOSIDASE; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
FT   DOMAIN          91..162
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          267..557
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          583..666
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
SQ   SEQUENCE   678 AA;  77377 MW;  8B9D2CE4BFCC9DDE CRC64;
     MDTPRPQLPD FEFHQNNDSF TLHFRQRLIL THSKDNPCLW IGSGIADIDM FRGNFSIKDK
     LQEKIALTDA IVSQSPDGWL IHFSRGSDIS ATLNISADDQ GRLLLELQND NLNHNRIWLR
     LAAQPEDHIY GCGEQFSYFD LRGKPFPLWT SEQGVGRNKQ TYVTWQADCK ENAGGDYYWT
     FFPQPTFVST QKYYCHVDNS CYMNFDFSAP EYHELALWED KATLRFECAD TYISLLEKLT
     ALLGRQPELP DWIYDGVTLG IQGGTEVCQK KLDTMRNAGV KVNGIWAQDW SGIRMTSFGK
     RVMWNWKWNS ENYPQLDSRI KQWNKEGVQF LAYINPYVAS DKDLCEEAAK RGYLAKDVAG
     GDYLVEFGEF YGGVVDLTNP EAYAWFKEVI KKNMIELGCG GWMADFGEYL PTDTYLHNGI
     SAEIMHNAWP ALWAKCNYEA LEETGKLGEI LFFMRAGSTG SQKYSTMMWA GDQNVDWSLD
     DGLASVVPAA LSLAMTGHGL HHSDIGGYTT LFEMKRSKEL LLRWCDFSAF TPMMRTHEGN
     RPGDNWQFDG DAETIAHFAR MTTVFTTLKP YLKEAVALNA KSGLPVMRPL FLHYEDDAQT
     YSLKYQYLLG RDILVAPVHE EGRSDWTLYL PEDNWVHAWT GETFHGGEIT VEAPIGKPPV
     FYRADSEWAA LFASLKNI
//
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