LOCUS       WP_007922107             822 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Ktedonobacter racemifer].
ACCESSION   WP_007922107
VERSION     WP_007922107.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 822)
  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 822)
  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 822)
  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 822)
  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 822)
  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 822)
  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 822)
  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 822)
  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..822
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..822
                     /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=91195
     Region          36..124
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          152..270
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            189
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          251..693
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Region          709..776
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mematpatts ahlislsplg yhalgtasml etttskvclr agsatvevta lapdlfrvgf
       61 fphgrpasyg seaviprewe pgfvtirege gevtiatsva tahlsldplr igftdqagra
      121 fatddpelgm gwltpeqaps ldmvnplail gtptrvykrh qqgaryfgcg ertgelektg
      181 thqlfwnidp prghtalqnn lyvsipftma madgqawglf ldsparvefd lahedsqrsw
      241 fgaengdlvy yvfcgptpqa vleryteltg rtplpplwsl gngqsrfsye taeevralar
      301 afrerdipcd tlyldidcld gyrvftwdnt rfpdpeglls elremgfhvv civdagvkvd
      361 enyevytegr erdlycktpq gddyqnavwp gvcvfpdftn pqarawwgdl hqglldagit
      421 giwsdmnepa lfiplnstmp sdvihpgggk arlhtqvhna ygslmvqaar egllrlrpqq
      481 rpfvisrsgy agvqrhaliw tgdnsstweh lamsltqlln lglsgvgwag tdvggfygdt
      541 sgelltrwte fgifqpfcrn hsekqtrhqe pwvfgepyts tirdllklrq rllpylytlf
      601 aechrtgapl lrplfwhype dtdaygasdq flcgdallva pitrpgaeyr hvylptgtwf
      661 hywtgerfeg pahilahapl gqpafyvran taiplwpamn yvgqapadpl tlilypapgs
      721 gsatlyedag dgyayteged arrailceve dklirvtlga qegtyasasq rfllelrevs
      781 tapaeinlgd qpiawyydhe qrrvsinlaa taheqvidia ls
//