LOCUS WP_196989360 828 aa linear BCT 23-APR-2025
DEFINITION glycoside hydrolase family 31 protein [Panacibacter microcysteis].
ACCESSION WP_196989360
VERSION WP_196989360.1
KEYWORDS RefSeq.
SOURCE Panacibacter microcysteis
ORGANISM Panacibacter microcysteis
Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
Chitinophagales; Chitinophagaceae; Panacibacter.
REFERENCE 1 (residues 1 to 828)
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 828)
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 828)
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 828)
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 828)
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 828)
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 828)
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 828)
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..828
/organism="Panacibacter microcysteis"
/db_xref="taxon:2793269"
Protein 1..828
/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=93619
Region 43..128
/region_name="AGL_N"
/note="Alpha-glucosidase, N-terminal; pfam16338"
/db_xref="CDD:465098"
Region 150..256
/region_name="GH31_N"
/note="N-terminal domain of glycosyl hydrolase family 31
(GH31); cd14752"
/db_xref="CDD:270212"
Site 177
/site_type="active"
/db_xref="CDD:270212"
Region 237..677
/region_name="Glyco_hydro_31"
/note="Glycosyl hydrolases family 31; pfam01055"
/db_xref="CDD:460044"
Region 693..761
/region_name="DUF5110"
/note="Domain of unknown function (DUF5110); pfam17137"
/db_xref="CDD:465360"
ORIGIN
1 mksylrqais ivllflavet saqifqagai tafkkspgsi sgkttnaifd vhvynnnivr
61 vrvskeksfr nfsyalvtne ipvytnvvvt ekgnsiilst avieleikkt pglafvfrnk
121 ngkiinedea qngavsfsgn kvtafkklis derfiglgea lgnidrrgtg vtlnntdnyk
181 yadprvpmys sipfymgihq kevyglffnn shkaffnfgs stpytsvtfd ggemdyffly
241 dtsvarvveh ytsltgrmqm pplwslgyqq srctyypqdq vmwiaetfrr rqipldgivl
301 dadyqlgyep frtnterfpd mpglaaqlak mhieltasvy pgvhidstyd sytdgirqni
361 fikttdglpf qteiaplkvh lpdytdpkar qwwiskmqwm ktngikgywn dmnepatans
421 ylpedlvfdf dghkattaea knvygfqmar ssyeaavnnl gnqrpfiltr sgfagvqrys
481 alwsgdnlat degllnsill nnqlglsglp fvgydvggyi gdgsknlyir wieagvfspy
541 crnhreffgt anepwaygee aeaisktyin fryrlmpyiy samytaskng iplhrslain
601 ypfdaniyqn syqyqflfgq dmlvapltsn ekskqvylpq gdwydlftdn kiagaqvvnt
661 dcpgyklplf ikasaiipvq givqstkdkp tdtlflhvyn gqvdntytyy eddgtsldyk
721 kemyyqrdis fhpaarqiti aakrgayksh fnyiqlllhg fddnlqsltv ngsqqsvlnn
781 ghalldpldn lgdiydkgyy kslqeavnkk tirtvtiqht gnninilw
//