ID YIHQ_ECOLI Reviewed; 678 AA. AC P32138; P76775; Q2M8H5; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 31-OCT-2012, entry version 97. DE RecName: Full=Alpha-glucosidase yihQ; DE EC=3.2.1.20; GN Name=yihQ; OrderedLocusNames=b3878, JW3849; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=93347969; PubMed=8346018; DOI=10.1093/nar/21.15.3391; RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome. III. DNA sequence of the RT region from 87.2 to 89.2 minutes."; RL Nucleic Acids Res. 21:3391-3398(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION RP TO 358 AND 517. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP FUNCTION. RX PubMed=15294295; DOI=10.1016/j.pep.2004.05.008; RA Okuyama M., Mori H., Chiba S., Kimura A.; RT "Overexpression and characterization of two unknown proteins, YicI and RT YihQ, originated from Escherichia coli."; RL Protein Expr. Purif. 37:170-179(2004). CC -!- FUNCTION: Exhibits hydrolysis activity against alpha-glucosyl CC fluoride, although natural substrates, such as alpha-glucobioses CC are scarcely hydrolyzed. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing (1->4)- CC linked alpha-D-glucose residues with release of alpha-D-glucose. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L19201; AAB03011.1; -; Genomic_DNA. DR EMBL; U00096; AAC76875.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77431.1; -; Genomic_DNA. DR PIR; A65193; A65193. DR RefSeq; NP_418314.1; NC_000913.2. DR RefSeq; YP_491572.1; NC_007779.1. DR ProteinModelPortal; P32138; -. DR DIP; DIP-12498N; -. DR IntAct; P32138; 1. DR MINT; MINT-1249337; -. DR CAZy; GH31; Glycoside Hydrolase Family 31. DR EnsemblBacteria; EBESCT00000004457; EBESCP00000004457; EBESCG00000003636. DR EnsemblBacteria; EBESCT00000016724; EBESCP00000016015; EBESCG00000015783. DR GeneID; 12931872; -. DR GeneID; 948376; -. DR GenomeReviews; AP009048_GR; JW3849. DR GenomeReviews; U00096_GR; b3878. DR KEGG; ecj:Y75_p3308; -. DR KEGG; eco:b3878; -. DR PATRIC; 32123259; VBIEscCol129921_3990. DR EchoBASE; EB1789; -. DR EcoGene; EG11843; yihQ. DR eggNOG; COG1501; -. DR HOGENOM; HOG000064244; -. DR KO; K15922; -. DR OMA; GVGRNKS; -. DR ProtClustDB; PRK10426; -. DR BioCyc; EcoCyc:EG11843-MONOMER; -. DR Genevestigator; P32138; -. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR InterPro; IPR011013; Glyco_hydro-type_carb-bd. DR InterPro; IPR000322; Glyco_hydro_31. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR22762; PTHR22762; 1. DR Pfam; PF01055; Glyco_hydro_31; 1. DR SUPFAM; SSF74650; Gal_mut_like; 1. DR SUPFAM; SSF51445; Glyco_hydro_cat; 1. DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; FALSE_NEG. DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; FALSE_NEG. PE 3: Inferred from homology; KW Complete proteome; Glycosidase; Hydrolase; Reference proteome. FT CHAIN 1 678 Alpha-glucosidase yihQ. FT /FTId=PRO_0000185372. FT ACT_SITE 405 405 Nucleophile (By similarity). FT ACT_SITE 408 408 By similarity. FT ACT_SITE 472 472 Proton donor (By similarity). FT CONFLICT 358 358 A -> R (in Ref. 1; AAB03011). FT CONFLICT 517 517 S -> T (in Ref. 1; AAB03011). SQ SEQUENCE 678 AA; 77275 MW; 85869F52BB72FEE7 CRC64; MDTPRPQLLD FQFHQNNDSF TLHFQQRLIL 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 KQWNQEGVQF LAYINPYVAS DKDLCEEAAQ HGYLAKDASG GDYLVEFGEF YGGVVDLTNP EAYAWFKEVI KKNMIELGCG GWMADFGEYL PTDTYLHNGV SAEIMHNAWP ALWAKCNYEA LEETGKLGEI LFFMRAGSTG SQKYSTMMWA GDQNVDWSLD DGLASVVPAA LSLAMTGHGL HHSDIGGYTT LFEMKRSKEL LLRWCDFSAF TPMMRTHEGN RPGDNWQFDG DAETIAHFAR MTTVFTTLKP YLKEAVALNA KSGLPVMRPL FLHYEDDAHT YTLKYQYLLG RDILVAPVHE EGRSDWTLYL PEDNWVHAWT GEAFRGGEVT VNAPIGKPPV FYRADSEWAA LFASLKSI //