LOCUS       WP_010989370             763 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Listeria monocytogenes].
ACCESSION   WP_010989370
VERSION     WP_010989370.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales;
            Listeriaceae; Listeria.
REFERENCE   1  (residues 1 to 763)
  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 763)
  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 763)
  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 763)
  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 763)
  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 763)
  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 763)
  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 763)
  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 11724808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..763
                     /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=86370
     Region          35..130
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          134..248
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            168
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          229..670
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Region          684..>732
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mdastsfail psnvkqktaf erkvnqvkaa swtnncltgt ldigqfscyf vnekiarvtv
       61 npfgevdltp siaaihdnek qaakftetnd cyelhfadke vivcknpfqi imkqagkrif
      121 qteglainrd kehqisiqse pgtaifglge ktgalnkags iismwntdvy sphnkdtvel
      181 yqsipfmiad takttyglfy dnshrtefdf qsfeemytvl aeggqanlyi ifgedvkevv
      241 anytdltgkt plppkwslgy hqsrysytse eeveriantf kekeipldcv fmdihymddf
      301 rvftfnpdtf pngpeliarl reqnidvvpi vdpgikkdvd ysvyqegikn nyfctklegs
      361 iyygdvwpgv safpdflstt vqhwwgslhk fytdlgirgi wndmnepsvf nesktmdldv
      421 vhnldgknvt hkeahnlygl ymskatfegl krlvpnerpf sltragyagv qrysavwtgd
      481 nrshwehlem slpmimnlgl sgvaftgadv ggfssdctke mlirwtqaga flpyfrnhcv
      541 qdsiyqepwa fgadaekivk qyielryafl pyiytefqkt aesglplvrp lymefkderd
      601 liqvndqfml genilvapiv regqakrlvr lpkglwfnyw tkeqfvggdy iiadapidtm
      661 piyikagtil pvgssvqntk etqeltlevy ldsetatgyv ynddgksyqy esgavskttl
      721 tatfkngevl inathqgean lqqkvttiqv fgekidkitr agi
//