LOCUS       WP_022251550             778 aa            linear   BCT 06-NOV-2025
DEFINITION  glycoside hydrolase family 31 protein [Segatella copri].
ACCESSION   WP_022251550
VERSION     WP_022251550.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 778)
  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 778)
  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 778)
  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 778)
  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 778)
  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 778)
  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 778)
  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 778)
  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 12177600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..778
                     /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=89223
     Region          28..113
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          127..240
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            156
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          221..653
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Region          669..736
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mknlklkltf lslcafataa haqqvkgnsv lytssqgnmr iemcsesmfr vtkvpaqqmp
       61 dnekwmvvny nfpqvdfsvd gkqiktsklq vsiqeapwri qvadasgkvl yeeltsgckd
      121 siynevkmnp dehffgfger mdridqrgqr vhlnvelgrg skpavggkdi lranycpvpl
      181 mlsnkgyavf fhtavpndwd mgwtnndkys fsapggdndy yfiygeqlet lihsyqqltg
      241 vaplmpraay glhigsysgg twhheskand tyvvnlidrl rqekipfdmm wldstwrlfa
      301 klgnggctfe fqdqfkdpkg midhayknhv amfglhirsl vdngkrnnll ttaqkkglti
      361 qdggtnaiin ffddkavdww wknaakkvtd lgakffktdv gsalnynnpn ieqkaahnlf
      421 piayakapye nfaklngqrg fdhtregyag iqrypfiwag dwgsewqwfe piirgginig
      481 lsgvgywshc mggfeqysay dtdlylrwvq mgmfspvsil fgmdhpryha pwtygeeaqk
      541 ifiqydslry allpyiytsa wdmyktsrpl mtplfydhlq dvntyqisdq ymfgrdmmvc
      601 pvtvknalsr pvyfpggdwl dfwtgerisg rqyksfltpi eimpiflrrg aiiprqeamq
      661 yvderpntni slliypsehs vyemyeddgk sldyqkgvya vtkmesrlaq newilnittp
      721 kgdykpvshy ysvsvyldkk pklvtvagkf vdgwkydekl rlltfdageg dmevvvkm
//