LOCUS       WP_144136861             797 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Blautia wexlerae].
ACCESSION   WP_144136861
VERSION     WP_144136861.1
KEYWORDS    RefSeq.
SOURCE      Blautia wexlerae
  ORGANISM  Blautia wexlerae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Arumapperuma,T., Li,J., Hornung,B., Soler,N.M.,
            Goddard-Borger,E.D., Terrapon,N. and Williams,S.J.
  TITLE     A subfamily classification to choreograph the diverse activities
            within glycoside hydrolase family 31
  JOURNAL   J Biol Chem 299 (4), 103038 (2023)
   PUBMED   36806678
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Rose,D.R., Chaudet,M.M. and Jones,K.
  TITLE     Structural Studies of the Intestinal alpha-Glucosidases,
            Maltase-glucoamylase and Sucrase-isomaltase
  JOURNAL   J Pediatr Gastroenterol Nutr 66 Suppl 3, S11-S13 (2018)
   PUBMED   29762369
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Okuyama,M., Saburi,W., Mori,H. and Kimura,A.
  TITLE     alpha-Glucosidases and alpha-1,4-glucan lyases: structures,
            functions, and physiological actions
  JOURNAL   Cell Mol Life Sci 73 (14), 2727-2751 (2016)
   PUBMED   27137181
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Lombard,V., Golaconda Ramulu,H., Drula,E., Coutinho,P.M. and
            Henrissat,B.
  TITLE     The carbohydrate-active enzymes database (CAZy) in 2013
  JOURNAL   Nucleic Acids Res 42 (Database issue), D490-D495 (2014)
   PUBMED   24270786
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Ernst,H.A., Lo Leggio,L., Willemoes,M., Leonard,G., Blum,P. and
            Larsen,S.
  TITLE     Structure of the Sulfolobus solfataricus alpha-glucosidase:
            implications for domain conservation and substrate recognition in
            GH31
  JOURNAL   J Mol Biol 358 (4), 1106-1124 (2006)
   PUBMED   16580018
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Rigden,D.J.
  TITLE     Iterative database searches demonstrate that glycoside hydrolase
            families 27, 31, 36 and 66 share a common evolutionary origin with
            family 13
  JOURNAL   FEBS Lett 523 (1-3), 17-22 (2002)
   PUBMED   12123797
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   8  (residues 1 to 797)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11724728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Blautia wexlerae"
                     /db_xref="taxon:418240"
     Protein         1..797
                     /product="glycoside hydrolase family 31 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=91927
     Region          25..88
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          190..494
                     /region_name="GH31_u1"
                     /note="glycosyl hydrolase family 31 (GH31);
                     uncharacterized subgroup; cd06595"
                     /db_xref="CDD:269881"
     Site            order(235,345,383,396,399,432,458)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269881"
     Region          613..681
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mdlkkfvleg npvcrkeavi vgdhfritml ttalirfeys edggfedrat qmvcnrdfpv
       61 pefrvsdsge elhiytkdle ihydrqkfsp sglmirvagg kaservwhyg depkdllgta
      121 rtldeadgei plshgimsrn gfsvlddsht mamgedgmve prqgnradfy ffgyghryve
      181 clqdfyrlcg ktpllprytf gnwwsryhky teteykelve rfekeevpfs vavvdmdwhl
      241 vedvppvygs gwtgytwnkk ffpnppefmd wlhkhgykit lnvhpadgvr ayeeayprva
      301 ekmgidpask epvlfdmtdp kfietyfeel hhpmeeegvd fwwldwqqgt vtkvpgldpl
      361 wmlnhyhyld skwkgkralt fsryagpgsh rypvgfsgdt fitweslkfq pyftanasni
      421 gfgwwshdig ghmfgyrdde ltarwvqlgv fspmnrlhst dnpfngkepw kynqivetvm
      481 knflklrhkl vpylytmnrr asraglplvq pmyylepere etyevpnnyy fgtemmvspi
      541 tdkldpvtgl agaktwipqg iwydffngra ykggrkvdlw rdiyempvlv regsiiplkd
      601 megydnsien peklevlvyp gesgefvlwe dggdtpedld enwvstrmtk tadengtvfi
      661 veaaqgntav ipqkrswkir fcniqdkpqe vtvngqvykd aefaedekih gtivllkdvp
      721 adaqvkvtfa adaavyqrdy aeevyeilek aqityaqkte vykvvkelgt eavpvlvsmn
      781 lnpsllgvlm eiltmgi
//