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LOCUS WP_010989902 591 aa linear BCT 26-JUL-2024 ACCESSION WP_010989902 VERSION WP_010989902.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 591) AUTHORS Kumar,V. TITLE Identification of the sequence motif of glycoside hydrolase 13 family members JOURNAL Bioinformation 6 (2), 61-63 (2011) PUBMED 21544166 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 591) AUTHORS Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and Henrissat,B. TITLE Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins JOURNAL Protein Eng Des Sel 19 (12), 555-562 (2006) PUBMED 17085431 REFERENCE 3 (residues 1 to 591) AUTHORS MacGregor,E.A., Janecek,S. and Svensson,B. TITLE Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes JOURNAL Biochim Biophys Acta 1546 (1), 1-20 (2001) PUBMED 11257505 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 11139521 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..591 /organism="Listeria monocytogenes" /db_xref="taxon:1639" Protein 1..591 /product="glycoside hydrolase family 13 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=68489 Region 1..124 /region_name="Alpha-amylase_N" /note="Alpha amylase, N-terminal ig-like domain; pfam02903" /db_xref="CDD:397170" Region 137..518 /region_name="AmyAc_CMD" /note="Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; cd11338" /db_xref="CDD:200477" Site order(208,210,250,306,339..340,368,370,434..435,479,483) /site_type="active" /db_xref="CDD:200477" Site order(308,342..347,350,370..371,392,418) /site_type="other" /note="homodimer interface [polypeptide binding]" /db_xref="CDD:200477" Site order(339,368,435) /site_type="active" /note="catalytic site [active]" /db_xref="CDD:200477" ORIGIN 1 mekagiyhqp assyaysyda ktlhirirtk rldiskvtli aadpylwkdg kwqsesytmr 61 kiaeteehdy wffaitpehr rlqygflltd tegettfygg rgffeptean latmdyyfkf 121 pfihavdtfe apewvrntiw yqifperfan gnpaispent lpwgskdpnt tdffggdieg 181 iiehldylae lgingvyltp vfeaptnhky dtidykkidp hfgdketfrk lvkeahkrgi 241 rimldavfnh igdtspewqd vvekeeksay rdwfhihsfp vrqnengnie geptlsydtf 301 aftthmpkln tanpevqkyl ldiatywire fdidgwrldv anevdhafwk efkkaaqaek 361 ediyilgeiw hdswiwllgd efhavmnypf tqtiienfie ekitpeqmvs gineqymryp 421 nqvnevmfnm ldshdtaril tranndedkv kqalafmfah tgspciyygt eigmdggndp 481 gcrkcmewde akqnqdmlaf tkqlialrkd nqaiitsgel twleassetg itafskelng 541 eklhflfnqt kkdqdftisf antaidiwnn qavsdnltip akgflviken s