ID A8AF94_CITK8 Unreviewed; 495 AA. AC A8AF94; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Glycosyl hydrolase family 13 catalytic domain-containing protein {ECO:0000259|SMART:SM00642}; GN OrderedLocusNames=CKO_01011 {ECO:0000313|EMBL:ABV12157.1}; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV12157.1, ECO:0000313|Proteomes:UP000008148}; RN [1] {ECO:0000313|EMBL:ABV12157.1, ECO:0000313|Proteomes:UP000008148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696 RC {ECO:0000313|Proteomes:UP000008148}; RG The Citrobacter koseri Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (AUG-2007) 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; CP000822; ABV12157.1; -; Genomic_DNA. DR RefSeq; WP_012131913.1; NC_009792.1. DR AlphaFoldDB; A8AF94; -. DR STRING; 290338.CKO_01011; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GeneID; 45135173; -. DR KEGG; cko:CKO_01011; -. DR HOGENOM; CLU_024572_2_0_6; -. DR OrthoDB; 9805159at2; -. DR Proteomes; UP000008148; Chromosome. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. 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 Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008148}. 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 495 AA; 56273 MW; 421665704BAD6E40 CRC64; MKNPTLLQYF HWYYPDGGKL WPELAERAGG LNDIGINMVW LPPAYKGASG GYSVGYDSYD LFDLGEFDQK GSVATKYGDK AQLLAAIEAL KQNDIAVLLD VVVNHKMGAD EKEAIRVQRV NEDNRTQIDD EIIECEGWTR YTFPARAGQY SQFIWDFKCF SGIDHIENPD EDGIFKIVND YTGDGWNDQV DDEMGNFDYL MGENIDFRNH AVTEEIKYWA RWVMAQTHCD GFRLDAVKHI PAWFYKEWIE HVQEVAPKPL FIVAEYWSHE VDKLQAYIDQ VDGKTMLFDA PLQMNFHEAS RQGRDYDMSQ IFTDTLVEAD PFHAVTLVAN HDTQPLQALE APVEAWFKPL AYALILLREN GVPSVFYPDL YGAHYEDTGG DGETYTIDMP VIGQLDQLIL ARQRFAHGIQ TLFFDHPNCV AFSRSGTDDD PGCVVVLSNG DDGEKTITLG ENYANKTWRD FLGNREERVT TDEKGEATFT CNGGCVSVWV IEDVL //