LOCUS WP_127200468 821 aa linear BCT 14-JUL-2025
DEFINITION glycoside hydrolase family 31 protein [Paenibacillus zeisoli].
ACCESSION WP_127200468
VERSION WP_127200468.1
KEYWORDS RefSeq.
SOURCE Paenibacillus zeisoli
ORGANISM Paenibacillus zeisoli
Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales;
Paenibacillaceae; Paenibacillus.
REFERENCE 1 (residues 1 to 821)
AUTHORS Lovering,A.L., Lee,S.S., Kim,Y.W., Withers,S.G. and Strynadka,N.C.
TITLE Mechanistic and structural analysis of a family 31
alpha-glycosidase and its glycosyl-enzyme intermediate
JOURNAL J Biol Chem 280 (3), 2105-2115 (2005)
PUBMED 15501829
REFERENCE 2 (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 3 (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 4 (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]
REFERENCE 5 (residues 1 to 821)
AUTHORS Henrissat,B.
TITLE A classification of glycosyl hydrolases based on amino acid
sequence similarities
JOURNAL Biochem J 280 (Pt 2) (Pt 2), 309-316 (1991)
PUBMED 1747104
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 11605355
Evidence Source :: NCBI SPARCLE
##Evidence-For-Name-Assignment-END##
COMPLETENESS: full length.
FEATURES Location/Qualifiers
source 1..821
/organism="Paenibacillus zeisoli"
/db_xref="taxon:2496267"
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=92387
Region 127..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..766
/region_name="DUF5110"
/note="Domain of unknown function (DUF5110); pfam17137"
/db_xref="CDD:465360"
ORIGIN
1 mhtseeihpd qigiedtqay rslgpmtgss shesgasftv cgkggnlsfw rvspqvlrva
61 cslhgdsaqm vpsqallpqr slegfdikdh qreliirtge fhvvldketl siqirhgsdl
121 dcgnysfsyt esrlrcrggm keeaaifglg ettgylnkrg drytmwnsdi ldphvpdmes
181 lyqsipllih htgqsslglf idhpgrmtvd mresgdnydv etidgemdly iiageglrev
241 vssytaltgr mqipplwslg yqqsrfsymn qdevlelart frakeipcdv iyldihymdn
301 ykvfsfdpeq fpdpegmmne laqmglrvvp vvnpgvkide gykvyeegva erhfcqlpdg
361 elyrghvwpg psmfpdftee rtrewwgalh qfyvdhgisg iwndmnepsv fnsptktmde
421 evlhgnngqp rthgelhnly gmlmckatke gldtllqger sfvltragya giqryaavwt
481 gdnrsywqhm emfmamgmnl glsgvafcga dvggfmhhas gellvrwtql gaftpffrnh
541 saiesrkqep wsfgeqveei crkfielrys llpymytlfh eaaetglpvm rplvleypqd
601 rqtfnlsdqf llggqllvap icrpgaehrs vylpegvwyd ywtgsrhegg yhhlahaaid
661 riplfvksga vipmtsglqh tegavwtnln vhiygkgigt dpgqsvtgey tlyeddgith
721 ayeagefsrl kvdflesngv meisagydya aisgsgnere ilftihqlsf ipekieglne
781 arslshlevq tagwyydrqg nhlfvkvplm aghgvkvsvl g
//