GenomeNet

Database: RefSeq
Entry: WP_120978626
LinkDB: WP_120978626
Original site: WP_120978626 
LOCUS       WP_120978626             821 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Cohnella endophytica].
ACCESSION   WP_120978626
VERSION     WP_120978626.1
KEYWORDS    RefSeq.
SOURCE      Cohnella endophytica
  ORGANISM  Cohnella endophytica
            Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (residues 1 to 821)
  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 821)
  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 821)
  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 821)
  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 821)
  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 821)
  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 821)
  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 821)
  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..821
                     /organism="Cohnella endophytica"
                     /db_xref="taxon:2419778"
     Protein         1..821
                     /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=94288
     Region          13..100
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          147..252
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            187
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          233..700
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Region          716..783
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mkltgwekka dllyletetg iaklvpvser avrvvytqdr sfsvkesliv lnqgkksvrw
       61 elreesdrli lrtsalkisi nkntcaftye dkdgclltke pdrggktlvp ievektvydd
      121 qvtittgqga dgvrarvegs rktvdrsayh tklefewqeg ealyglgshe egvmdlrgth
      181 qylyqqnmka vvpmlvstrg yavlwdscsy mafrddmhgs ylwtdvddem dyyflygpef
      241 delvyeyrel tgsvpmlpkw algyaqsker yksqeeildi lreyrerklp ldllildwqs
      301 wtgnwwgqks ldperfpdpe gmmrnlhedg arlmvsiwpi mnnngpdqee mreqgfllgn
      361 qanydpfrpe arllywkqan eglfkhgida wwcdctepfe adwkgaikpe peervsinvn
      421 efknyldpev inaysllhsr giyegqretd dtkrvvnltr sayagqqryg aitwsgdtaa
      481 twttlrnqip aglnfcatgv pywtmdigaf fvgkkpemwf wngdydkgye ddgykelyvr
      541 wfqlgaflpm frshgtdtpr evwrfgepgs vfydtlakfl klryrllpyl yaltgavtqd
      601 hytmlralaf dfredpavrd igdqymfgpa flvnpvtkpm yyesgsrkle gvpstrrvyl
      661 psgsgwydfw tgarleggmv ieaeapldil plfvragsiv pmspvvqstd elgsqpyeir
      721 iypgrdgkfk lyedegdnyn yekgefasie mewldeertf kigsrqgdfp gmvrkrlmnl
      781 vivgagggqg ngeaestmfd rtvtytgesv visfdsheaa s
//
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