LOCUS       WP_157306389             769 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Chitinophaga tropicalis].
ACCESSION   WP_157306389
VERSION     WP_157306389.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga tropicalis
  ORGANISM  Chitinophaga tropicalis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 769)
  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 769)
  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 769)
  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 769)
  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 769)
  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 769)
  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 769)
  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 769)
  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..769
                     /organism="Chitinophaga tropicalis"
                     /db_xref="taxon:2683588"
     Protein         1..769
                     /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=87299
     Region          34..109
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          118..230
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            144
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          211..651
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Region          667..732
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mlrrllmliv lsgilpavak gqefirngnv lqigntrlef ctpgmfrvsy stpleepwmv
       61 vrynwepvsl qvteekdqll vkttllqlkm rkqpfgidvy ttdgqllsaa gredshllqp
      121 dehffgfger mdfldqrgkk lrlevgrgkg mphitgaynv laanyspvpf fmstkgygif
      181 lhtsyasdwd mghtnkhsys frategpqey yfiygprftg ileqytsltg rsplmpfsaf
      241 glhvgtysgg twgheeltst tyvlelarrf reqgipidil fldstwrlfg kkggkgatsy
      301 ewretfhqpr rmfdslyamh ysmvglhirp rldngnylrl ldtantlgyt ypednnpgef
      361 inffdssavn wwwdhaamrv aglgakffkt degsafggla nessktgptg pearrlhnif
      421 pvayakaaye kfaahnhtrg mnhtregyag iqrypfifag dwpsewqyfe pvikaglnig
      481 lsgvgywahc mggfehpadp elyirwcqfg mlspvamlfg mdhpgykepw rygkealaif
      541 kqydelrysl lpylystawe qyqkgtplmr alvleyqdde nvynitdqym lgnsimvcpv
      601 tqkgastrvv ylpdgnwtdy wtgktyeghq hlnvltpldk lpifiktgsi ipfqpviqyt
      661 gqdqpdniil avypgadnsf alytddgksl eyqqgsyavt hisikggsiq inkpegsfqp
      721 rwktftlkvh speapsavkt dgswrydtqe kciyvtgisa traatiein
//