ID E6WLB3_PANSA Unreviewed; 492 AA. AC E6WLB3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 62. DE SubName: Full=Glucan 1,4-alpha-maltohexaosidase {ECO:0000313|EMBL:ADU72198.1}; DE EC=3.2.1.98 {ECO:0000313|EMBL:ADU72198.1}; GN OrderedLocusNames=Pat9b_4889 {ECO:0000313|EMBL:ADU72198.1}; OS Pantoea sp. (strain At-9b). OG Plasmid pPAT9B02 {ECO:0000313|EMBL:ADU72198.1, OG ECO:0000313|Proteomes:UP000001624}. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU72198.1, ECO:0000313|Proteomes:UP000001624}; RN [1] {ECO:0000313|EMBL:ADU72198.1, ECO:0000313|Proteomes:UP000001624} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-9b {ECO:0000313|EMBL:ADU72198.1, RC ECO:0000313|Proteomes:UP000001624}; RC PLASMID=Plasmid pPAT9B02 {ECO:0000313|Proteomes:UP000001624}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.; RT "Complete sequence plasmid2 of Pantoea sp. At-9b."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002435; ADU72198.1; -; Genomic_DNA. DR RefSeq; WP_013512027.1; NC_014839.1. DR AlphaFoldDB; E6WLB3; -. DR KEGG; pao:Pat9b_4889; -. DR HOGENOM; CLU_024572_2_0_6; -. DR OrthoDB; 9805159at2; -. DR Proteomes; UP000001624; Plasmid pPAT9B02. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0033927; F:glucan 1,4-alpha-maltohexaosidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11318; AmyAc_bac_fung_AmyA; 1. DR Gene3D; 2.40.30.140; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR013776; A-amylase_thermo. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1. DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 4: Predicted; KW Calcium {ECO:0000256|PIRSR:PIRSR001021-2}; KW Glycosidase {ECO:0000313|EMBL:ADU72198.1}; KW Hydrolase {ECO:0000313|EMBL:ADU72198.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}; KW Plasmid {ECO:0000313|EMBL:ADU72198.1}. FT DOMAIN 4..402 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 235 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT ACT_SITE 265 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT BINDING 104 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 198 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 206 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 239 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" SQ SEQUENCE 492 AA; 56247 MW; 2EC1CF03E008224D CRC64; MKNPTLLQAF HWYYPEGGQL WPKLAERAAH MSESGINMIW LPPAYKGASG GSSVGYDTYD LFDLGEFDQK GSIATKYGDK AQLHTAIEAL HQHQIAVLMD VVVNHKMGAD ERERILVNRV DEQDRSQIHE EVVECDAWTR YTFPVRAGKY SKFIWDYKCF SGVDHIENPD EDGVFKIVND YTGEGWNDQV DNELGNFDYL MGSNIDFRNR SATEEIKYWA RWMMETTQCD GFRLDAVKHI PAWFYKEWID HVQEVSEKQL FIVAEYWSFE LDKLQQYINQ VEGKTLLFDA PLHMKFHEAS KQGSSYDMSQ IFSGTLVEAD PFHAVTIVAN HDTQPLQALE APVEAWFKPL AYALILLREN GVPCVFYPDL YGASYEDIGS DGEKHKVEMP VIDKLDRLMI ARQRFAHGVQ TLWFDHPNCI AFSRSGTEDE TGCVVIMSNG DYGEKTLMLG ENYAGKNWRD FLGNRDETIT TNEQGEAVFT CSGGSVSVWV ID //