GenomeNet

Database: RefSeq
Entry: WP_113614136
LinkDB: WP_113614136
Original site: WP_113614136 
LOCUS       WP_113614136             800 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Chitinophaga flava].
ACCESSION   WP_113614136
VERSION     WP_113614136.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga flava
  ORGANISM  Chitinophaga flava
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 800)
  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 800)
  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 800)
  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 800)
  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 800)
  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 800)
  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 800)
  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 800)
  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..800
                     /organism="Chitinophaga flava"
                     /db_xref="taxon:2259036"
     Protein         1..800
                     /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=92480
     Region          27..117
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          137..249
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            169
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          230..672
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Region          688..>735
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mqvetsssky gikhypdair ewkkegnyfc fytsetilev rviadkiirf ryaadgtfqr
       61 dfsyatsdtl eespitfgik eweetfeiyt dvlkvfiard nlrititdkd gkvinqdemg
      121 fhwqhylqkg gkivycsklv qedecfyglg dkptelnlrg krlenygtda ygyqkdtdpl
      181 yrnipfyygl hngigygiff dntfrtifdf gkeredacsf warggemnyy fiygpelldv
      241 asaytritgt pelppiwtlg yhqcrwsyyp dkrvreiaae frnrripcdv iyldidymeg
      301 frcftwskey fpdpaglird laaqgfkivv iidpgikvdp dytiyqegik nnyfckradg
      361 almegdvwpg kcvfpdftnp evrewwsslf kglaetgvrg vwndmnepav femgtfpedv
      421 rhdydgeevs hrrahnvygh lmskataagm kkyllpnrpf litrscyaga qrwssvwtgd
      481 nvsswehlwl atiqcqrlsv sgisfagsdi ggfigepdge lytrwiqlas fhplmrthsa
      541 snetgfnqep wsfgpeyeki vtkfislryq llpymyttfw qyatngtpml rplafvaqhd
      601 pathncshef mlgdallish vseegmkekn vylpegkwyy fwndkvytgr qnitvptple
      661 emplfvkaga vvprypemqy thetpvteml lhvyygegvv ksvlyedagd hygykngqyn
      721 vinfkqvsta dqfvlkkkyy vnyevsythh riflhglpfq aatvtvdgtv islnsdnyls
      781 dgsisfiadr gfeqivinrg
//
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