LOCUS       WP_015749847             761 aa            linear   BCT 23-APR-2025
DEFINITION  glycoside hydrolase family 31 protein [Nakamurella multipartita].
ACCESSION   WP_015749847
VERSION     WP_015749847.1
KEYWORDS    RefSeq.
SOURCE      Nakamurella multipartita
  ORGANISM  Nakamurella multipartita
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Nakamurellales;
            Nakamurellaceae; Nakamurella.
REFERENCE   1  (residues 1 to 761)
  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 761)
  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 761)
  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 761)
  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 761)
  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 761)
  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 761)
  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 761)
  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 11724728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Nakamurella multipartita"
                     /db_xref="taxon:53461"
     Protein         1..761
                     /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=83355
     Region          28..93
                     /region_name="AGL_N"
                     /note="Alpha-glucosidase, N-terminal; pfam16338"
                     /db_xref="CDD:465098"
     Region          192..495
                     /region_name="GH31_u1"
                     /note="glycosyl hydrolase family 31 (GH31);
                     uncharacterized subgroup; cd06595"
                     /db_xref="CDD:269881"
     Site            order(238,347,384,397,400,433,459)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269881"
     Region          613..672
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
ORIGIN      
        1 mpghrlpdpl pvspladpra vvagsryrit vltdgllrle yaedgvfedr asafalhrdl
       61 pvpaftvret daaleivter lhlvydrgpf ttsglsvqvr gnistyhsvw rygepaadlg
      121 gtartldnad grvplepgva srfgfalldd stslllepdg wvaprppgrt dlylfayghd
      181 yaaavralya vsgappvlpr walgnwwsry hrytaqayse lierfraqgl pfsvavidmd
      241 whlvdvdaah gsgwtgytwn relipepeql lewlhanglr itlnvhpadg vrafedaypa
      301 matalgrdaq agepiafdvt dreflaayle vlhrdlerqg vdfwwldwqs gphsrvigid
      361 plwmlnhfhf ldsvragpgl tfsryagpgs hrypvgfsgd tviswaslnf qpeftataan
      421 igygwwshdi gghmfgakdd eltarwvqyg vfspilrlhs ganpfihkep wtlepdaaav
      481 mtqslrlrhr lvpylhtmnh laaqgtplvr pmyweqpdra payrvshqfr fgtelivapi
      541 ttpadpisrl gavrvwlppg ewvdiacgrr ysgdrelvvh raladipvfa apgaivplda
      601 aavpdndpvn ptelellvvp gadgryelie ddgagrvart pirydaatgr vtigpaqgql
      661 dglpasrtwt vrspggdgsd pvtaapgeav vldlgaapvt dpgrelfdrl drarldhelk
      721 vqalaavtad rpagarighl halalprave savveilsal d
//