LOCUS       WP_157302615             798 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Chitinophaga oryziterrae].
ACCESSION   WP_157302615
VERSION     WP_157302615.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga oryziterrae
  ORGANISM  Chitinophaga oryziterrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 798)
  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 798)
  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 798)
  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 798)
  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 798)
  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 798)
  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 798)
  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 798)
  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..798
                     /organism="Chitinophaga oryziterrae"
                     /db_xref="taxon:1031224"
     Protein         1..798
                     /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=92766
     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          689..758
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mqvttssgky sakhypdtir ewkkegnyfy fytsetilev riisdkivrf ryaadgkfqr
       61 dfsyavsdrl eespvnfglr efeeafelyt dalrvfiard dmrltitdpd griinqdemg
      121 fhwqyylqkg gkivycskqi qegerfygmg dkptdlnlfd krienygtda ygyqkdtdpl
      181 yrnipfyygl hkgmgygiff dntfrtifdf gkeregttsf warggemnyy fiygpelmkv
      241 aeaytsitgt pelpplwalg yqqcrwsyyp dkrvkeiaae frkreipcdv ihldidymeg
      301 frcftwskeg fpepakmike ladqgfkivv iidpgikvdp eygiyqqgtq qdyfckradg
      361 almegdvwpg kcvfpdytnp evrkwwaglf kelvemgvkg vwndmnepav femgtfpedv
      421 rhnydgdavs hrkahniygh lmskataagm rkflmpnrpf visrscyaga qrwsslwtgd
      481 nvsswdhlwl asiqcqrlai sgisfagsdi ggfigepdge lylrwiqlav fhplmrthsa
      541 snetgfnqep fsfgpefevl nkkfiqlryq llpyiyttfr qyskygtpml rplsfvaqhd
      601 ektldrshef mmgdsllvth vsepgmkake lylpegqwyy yfndqvytga qlitiptpld
      661 emplfvkaga vipnydkiqy veqrelseem ilhvyysdqi vssslyedag dhygykngsy
      721 ndirfkqtsd kqhfelrkkf fgqykaaykr hnvqvhglpf katqyvvdgk tfklnnsnfa
      781 ggivkivver nfetlvik
//