LOCUS WP_025708138 824 aa linear BCT 21-APR-2025
DEFINITION glycoside hydrolase family 31 protein [Paenibacillus graminis].
ACCESSION WP_025708138
VERSION WP_025708138.1
KEYWORDS RefSeq.
SOURCE Paenibacillus graminis
ORGANISM Paenibacillus graminis
Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales;
Paenibacillaceae; Paenibacillus.
REFERENCE 1 (residues 1 to 824)
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 824)
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 824)
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 824)
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 824)
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 824)
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 824)
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 824)
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 11724808
Evidence Source :: NCBI SPARCLE
##Evidence-For-Name-Assignment-END##
COMPLETENESS: full length.
FEATURES Location/Qualifiers
source 1..824
/organism="Paenibacillus graminis"
/db_xref="taxon:189425"
Protein 1..824
/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=93969
Region 35..123
/region_name="AGL_N"
/note="Alpha-glucosidase, N-terminal; pfam16338"
/db_xref="CDD:465098"
Region 136..250
/region_name="GH31_N"
/note="N-terminal domain of glycosyl hydrolase family 31
(GH31); cd14752"
/db_xref="CDD:270212"
Site 170
/site_type="active"
/db_xref="CDD:270212"
Region 231..670
/region_name="Glyco_hydro_31"
/note="Glycosyl hydrolases family 31; pfam01055"
/db_xref="CDD:460044"
Region 704..>739
/region_name="DUF5110"
/note="Domain of unknown function (DUF5110); pfam17137"
/db_xref="CDD:465360"
ORIGIN
1 messeairpe kmgplvmket wntpgsfvsw erseniyivr gerggivfvf lndemfrmkv
61 frnkvpdltt taavlaescv phlfpveend gqltfttsai rliiektsll lrvenmdgkv
121 imqqnltsws prgashaeyd mqpdshfygl gekasfldkr gerytnwntd vfaphlpeie
181 alyesiplli hmhgalsygl fldntgrsdf dmrshgvaft igcstgaydi yfingpemkd
241 vvkrytsltg rialppkwai gyhqsrysym nqqevlqlar tfreknipcd viyldihymd
301 eyrvftfdpv hfpepdkmia elrglgvrii pivdpgvkkd pnyevykqgv lekhfcrrle
361 gdiffgevwp gisafpdfsd vrtaewwgdl hkyytdlgiq giwndmnepa vfnesktmdl
421 dvmhfnngrp vtheeyhnly gmmmskatye glaehmgger pfvltragya giqryaavwt
481 gdnrsfwehm amampmvlnm glsglafsgp diggfahhts aqllvrwtqm gvffpycrnh
541 ssigtlrqep wsfgeevegi lrefiglryr wmphlynlfh eaemtglpvi rplileyprd
601 phvtnlcdqf llgenvliap vyrpdtehrs vylpeglwid ywdgevhegg rhilaaaplr
661 impmyvkagt fvaegplkqy aledtaesvi fhlygaears gffaaftlye ddghsfsykk
721 ghyseisvha ageegglrlg wtytvreyap rrdmlrfalc ypnfaaasvd glpevsleql
781 eegrtgwarn gkngaliiqv ndaarggelr iqavraeeel nrke
//