LOCUS WP_120978626 821 aa linear BCT 23-APR-2025
DEFINITION glycoside hydrolase family 31 protein [Cohnella endophytica].
ACCESSION WP_120978626
VERSION WP_120978626.1
KEYWORDS RefSeq.
SOURCE Cohnella endophytica
ORGANISM Cohnella endophytica
Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales;
Paenibacillaceae; Cohnella.
REFERENCE 1 (residues 1 to 821)
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 821)
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 821)
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 821)
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 821)
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 821)
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 821)
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 821)
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..821
/organism="Cohnella endophytica"
/db_xref="taxon:2419778"
Protein 1..821
/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=94288
Region 13..100
/region_name="AGL_N"
/note="Alpha-glucosidase, N-terminal; pfam16338"
/db_xref="CDD:465098"
Region 147..252
/region_name="GH31_N"
/note="N-terminal domain of glycosyl hydrolase family 31
(GH31); cd14752"
/db_xref="CDD:270212"
Site 187
/site_type="active"
/db_xref="CDD:270212"
Region 233..700
/region_name="Glyco_hydro_31"
/note="Glycosyl hydrolases family 31; pfam01055"
/db_xref="CDD:460044"
Region 716..783
/region_name="DUF5110"
/note="Domain of unknown function (DUF5110); pfam17137"
/db_xref="CDD:465360"
ORIGIN
1 mkltgwekka dllyletetg iaklvpvser avrvvytqdr sfsvkesliv lnqgkksvrw
61 elreesdrli lrtsalkisi nkntcaftye dkdgclltke pdrggktlvp ievektvydd
121 qvtittgqga dgvrarvegs rktvdrsayh tklefewqeg ealyglgshe egvmdlrgth
181 qylyqqnmka vvpmlvstrg yavlwdscsy mafrddmhgs ylwtdvddem dyyflygpef
241 delvyeyrel tgsvpmlpkw algyaqsker yksqeeildi lreyrerklp ldllildwqs
301 wtgnwwgqks ldperfpdpe gmmrnlhedg arlmvsiwpi mnnngpdqee mreqgfllgn
361 qanydpfrpe arllywkqan eglfkhgida wwcdctepfe adwkgaikpe peervsinvn
421 efknyldpev inaysllhsr giyegqretd dtkrvvnltr sayagqqryg aitwsgdtaa
481 twttlrnqip aglnfcatgv pywtmdigaf fvgkkpemwf wngdydkgye ddgykelyvr
541 wfqlgaflpm frshgtdtpr evwrfgepgs vfydtlakfl klryrllpyl yaltgavtqd
601 hytmlralaf dfredpavrd igdqymfgpa flvnpvtkpm yyesgsrkle gvpstrrvyl
661 psgsgwydfw tgarleggmv ieaeapldil plfvragsiv pmspvvqstd elgsqpyeir
721 iypgrdgkfk lyedegdnyn yekgefasie mewldeertf kigsrqgdfp gmvrkrlmnl
781 vivgagggqg ngeaestmfd rtvtytgesv visfdsheaa s
//