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LOCUS WP_004151861 707 aa linear BCT 31-DEC-2024 ACCESSION WP_004151861 VERSION WP_004151861.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 707) AUTHORS Coines,J., Raich,L. and Rovira,C. TITLE Modeling catalytic reaction mechanisms in glycoside hydrolases JOURNAL Curr Opin Chem Biol 53, 183-191 (2019) PUBMED 31731209 REFERENCE 2 (residues 1 to 707) AUTHORS Naumoff,D.G. TITLE Hierarchical classification of glycoside hydrolases JOURNAL Biochemistry (Mosc) 76 (6), 622-635 (2011) PUBMED 21639842 REFERENCE 3 (residues 1 to 707) 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 707) 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 16044983 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..707 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..707 /product="alpha-galactosidase" /EC_number="3.2.1.22" /GO_function="GO:0004557 - alpha-galactosidase activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]" /GO_process="GO:0000272 - polysaccharide catabolic process [Evidence IEA]" /calculated_mol_wt=79802 Region 24..232 /region_name="Glyco_hydro_36N" /note="Glycosyl hydrolase family 36 N-terminal domain; pfam16875" /db_xref="CDD:465291" Region 253..592 /region_name="AmyAc_family" /note="Alpha amylase catalytic domain family; cl38930" /db_xref="CDD:476817" Site order(299,330,374,439,443,483,502,505) /site_type="active" /db_xref="CDD:269892" Region 609..692 /region_name="Glyco_hydro_36C" /note="Glycosyl hydrolase family 36 C-terminal domain; pfam16874" /db_xref="CDD:465290" ORIGIN 1 msdslihlqs agadvviktr pfaeivywgp hlshfspqda dsltrpvang rldvdspvtl 61 maelghglfg apgieghrqg ldasplftts evrhegqtlt lvsedpqagl rlqseialda 121 sgvlsvrhgv tnlraspwqv drlavtlpva erarevmafh grwirefqph rltlehdsfv 181 lenrrgrtsh ehfpalitgs rafsemqgev wgvhlawsgn hrlraevktd grrylqaeal 241 ylpgemalae getlwtpyly asysanglng msqqfhrylr eriirfpgnk prpvhlntwe 301 giyfdhdpdy imrmadeaaa lgverfiidd gwfkgrnddw aalgdwylde kkypygltpv 361 idhvkslgme fgiwvepemi npdsdlyrah pdwvlalpgy tpltgrhqfv lnlnipeafd 421 yllermswll gehavdyvkw dmnrelvqpg hqgraaadaq trqfyrlldt lvarfphief 481 escssgggri dyevlkrshr fwasdnndal erntiqrgms yffppevmga hignrhchat 541 frqhsiafrg ltalfghmgl eldpvsadee eragyrkyaa lhkqwrdvih hgvqwridmp 601 dattlahgvv spdkaqaifl vsqlampdyt lmaplrlagl easaryqvtl ldhpniqitg 661 egghtmrklp awmttpqtvs gewlqqagla lpildpesai liglqrv