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LOCUS WP_000491412 750 aa linear BCT 01-MAR-2025 ACCESSION WP_000491412 VERSION WP_000491412.1 KEYWORDS RefSeq. SOURCE Shigella flexneri ORGANISM Shigella flexneri Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella. REFERENCE 1 (residues 1 to 750) AUTHORS Strobl,S., Maskos,K., Betz,M., Wiegand,G., Huber,R., Gomis-Ruth,F.X. and Glockshuber,R. TITLE Crystal structure of yellow meal worm alpha-amylase at 1.64 A resolution JOURNAL J Mol Biol 278 (3), 617-628 (1998) PUBMED 9600843 REFERENCE 2 (residues 1 to 750) AUTHORS Larson,S.B., Greenwood,A., Cascio,D., Day,J. and McPherson,A. TITLE Refined molecular structure of pig pancreatic alpha-amylase at 2.1 A resolution JOURNAL J Mol Biol 235 (5), 1560-1584 (1994) PUBMED 8107092 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 :: HMM Evidence Accession :: NF012356.6 Evidence Source :: EMBL-EBI Source Identifier :: PF00128.30 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..750 /organism="Shigella flexneri" /db_xref="taxon:623" Protein 1..750 /product="alpha-amylase family glycosyl hydrolase" /GO_function="GO:0003824 - catalytic activity [Evidence IEA]" /GO_process="GO:0005975 - carbohydrate metabolic process [Evidence IEA]" /calculated_mol_wt=85058 Region 216..640 /region_name="AmyAc_bac1_AmyA" /note="Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); cd11315" /db_xref="CDD:200454" Site order(268..269,272..273,312,315,390,434,436..437,439..440, 481,483,485,550..551,555) /site_type="active" /db_xref="CDD:200454" Site order(311,406,431) /site_type="other" /note="Ca binding site [ion binding]" /db_xref="CDD:200454" Site order(436,481,551) /site_type="active" /note="catalytic site [active]" /db_xref="CDD:200454" Region 651..738 /region_name="Alpha-amylase_C" /note="Alpha amylase, C-terminal all-beta domain; pfam02806" /db_xref="CDD:426991" ORIGIN 1 mfsikpgpgn lpidnptlls wnitdgdlns kfntleylnc itniinacgv ypqdlkdrei 61 istfhaekvi ndllkndyki slspdttyre lnkaaqssit apdrigegkt wvyqrdtmve 121 rgdnsgvhqy gpaehfthii sdkpspkdky vayainipdy elaadvynin vtspsgqqet 181 fkilinpehl rqtlerkslt avqksqceii tpkkpgeail hafnatyqqi renmsefars 241 hygyiqippv ttfradgpet peeekgywfh ayqpedlcti hnpmgdlqdf ialvkdakkf 301 gidiipdytf nfmgiggsgk ndldypsadi rakiskdies gipgywqgqv lipfikdpvt 361 kerkqihped ihltakdfea skdniskdew knlhalkeks lngmpkttpk sdqvimlqnq 421 yvremrkygv rglrydaakh skheqiersi tpplknyner lhntnlfnpk yhektvmnym 481 eylvtcqlne eqmssllyer ddlsaidfsl lmktikafsf ggdlltlask pgstissips 541 errilininh dfpnngnlfn dflfnhqqde qlamaymaal pfsrplvywd gqvlksttei 601 knydgstrvg geawlnkgcs tyqqlynefh alyidkagiw safegvfatk nvlafsrgds 661 vninhsphdg lviinkgnee vegtwpnklq priyknmgsn svniiinntr kiippckvft 721 lrggslnini prrsalllgk tgeppnylyl