LOCUS       WP_034939160             790 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Erwinia mallotivora].
ACCESSION   WP_034939160
VERSION     WP_034939160.1
KEYWORDS    RefSeq.
SOURCE      Erwinia mallotivora
  ORGANISM  Erwinia mallotivora
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Erwinia.
REFERENCE   1  (residues 1 to 790)
  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 790)
  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 790)
  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 790)
  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 790)
  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 790)
  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 790)
  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 790)
  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 13163290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Erwinia mallotivora"
                     /db_xref="taxon:69222"
     Protein         1..790
                     /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=90830
     Region          29..>100
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          149..>785
                     /region_name="PLN02763"
                     /note="hydrolase, hydrolyzing O-glycosyl compounds"
                     /db_xref="CDD:215408"
     Region          257..574
                     /region_name="GH31_glycosidase_Aec37"
                     /note="E.coli Aec37-like; cd06599"
                     /db_xref="CDD:269885"
     Site            order(306,419,474,487,490,523,549)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269885"
ORIGIN      
        1 mktlkhwtla qsdahhlqli vdgrhhlcly vleenlirva vkrqgefnpd rswsiapqgd
       61 vpwegrsres lagfslpaft vseqadslvl ttrqlrvtvh qplwlewhyl dphgewqflt
      121 gdrttsayll nahgdgvahy lrrqpderyy glgekagdlq rngrryemrn ldamgynaat
      181 tdplykhipf tltrrdnisf glyydnlsnt qldlgneldn yhqpyrrwqa esgdidyylf
      241 tgcrvldvtk afvrltgktl fgpkwslgys gstmhytdap daqqqlmnfi rlcreqaipc
      301 dsfqlssgyt sinnkryvfn wnrekvpqpq qmsaafhaag lhlaanikpc llqdhpqyqa
      361 vaaqglfird sesdqpersa fwddegshld ftnpatitww qqgvtrqlle mgidstwndn
      421 neyevwdgea rchgfgrsla ikdirpvmpl lmmrasmeaq qrfapekrpf lisrsgcagm
      481 qryvqtwsgd nrtswqtlry nirmglgmsl sglynlghdv ggfagdkpda elfvrwvqng
      541 vmhprftihs wnddhtvnep wmypavtpai rdaielryrl lpylytllwq ahaddepmlr
      601 ptfldhenda qtfvegdefm lgrdllvasv vepgqrqrsl wlpdnltgwy dfysgewysg
      661 gqwvtlaapl eklpllvrag aglplsqhlr avnvaednqr elklfplkgv gsaegllfed
      721 dgeswgyqqg nalwlnwrmt cddrairlti tteghfqpgw kklhitlphq ehrrlwvngt
      781 ecdtwplnea
//