LOCUS WP_113614136 800 aa linear BCT 23-APR-2025
DEFINITION glycoside hydrolase family 31 protein [Chitinophaga flava].
ACCESSION WP_113614136
VERSION WP_113614136.1
KEYWORDS RefSeq.
SOURCE Chitinophaga flava
ORGANISM Chitinophaga flava
Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE 1 (residues 1 to 800)
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 800)
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 800)
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 800)
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 800)
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 800)
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 800)
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 800)
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..800
/organism="Chitinophaga flava"
/db_xref="taxon:2259036"
Protein 1..800
/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=92480
Region 27..117
/region_name="AGL_N"
/note="Alpha-glucosidase, N-terminal; pfam16338"
/db_xref="CDD:465098"
Region 137..249
/region_name="GH31_N"
/note="N-terminal domain of glycosyl hydrolase family 31
(GH31); cd14752"
/db_xref="CDD:270212"
Site 169
/site_type="active"
/db_xref="CDD:270212"
Region 230..672
/region_name="Glyco_hydro_31"
/note="Glycosyl hydrolases family 31; pfam01055"
/db_xref="CDD:460044"
Region 688..>735
/region_name="DUF5110"
/note="Domain of unknown function (DUF5110); pfam17137"
/db_xref="CDD:465360"
ORIGIN
1 mqvetsssky gikhypdair ewkkegnyfc fytsetilev rviadkiirf ryaadgtfqr
61 dfsyatsdtl eespitfgik eweetfeiyt dvlkvfiard nlrititdkd gkvinqdemg
121 fhwqhylqkg gkivycsklv qedecfyglg dkptelnlrg krlenygtda ygyqkdtdpl
181 yrnipfyygl hngigygiff dntfrtifdf gkeredacsf warggemnyy fiygpelldv
241 asaytritgt pelppiwtlg yhqcrwsyyp dkrvreiaae frnrripcdv iyldidymeg
301 frcftwskey fpdpaglird laaqgfkivv iidpgikvdp dytiyqegik nnyfckradg
361 almegdvwpg kcvfpdftnp evrewwsslf kglaetgvrg vwndmnepav femgtfpedv
421 rhdydgeevs hrrahnvygh lmskataagm kkyllpnrpf litrscyaga qrwssvwtgd
481 nvsswehlwl atiqcqrlsv sgisfagsdi ggfigepdge lytrwiqlas fhplmrthsa
541 snetgfnqep wsfgpeyeki vtkfislryq llpymyttfw qyatngtpml rplafvaqhd
601 pathncshef mlgdallish vseegmkekn vylpegkwyy fwndkvytgr qnitvptple
661 emplfvkaga vvprypemqy thetpvteml lhvyygegvv ksvlyedagd hygykngqyn
721 vinfkqvsta dqfvlkkkyy vnyevsythh riflhglpfq aatvtvdgtv islnsdnyls
781 dgsisfiadr gfeqivinrg
//