ID I0BPU4_9BACL Unreviewed; 518 AA. AC I0BPU4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAR-2024, entry version 42. DE SubName: Full=Cytochrome C oxidase subunit II {ECO:0000313|EMBL:AFH64391.1}; DE SubName: Full=Glucan 1,4-alpha-maltohexaosidase {ECO:0000313|EMBL:AFK65320.1}; GN ORFNames=B2K_27485 {ECO:0000313|EMBL:AFH64391.1}; OS Paenibacillus mucilaginosus K02. OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH64391.1, ECO:0000313|Proteomes:UP000007392}; RN [1] {ECO:0000313|EMBL:AFK65320.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K02 {ECO:0000313|EMBL:AFK65320.1}; RA Lian B., Xiao B.; RT "Some potential microbial weathering related gene sequences of Bacillus RT mucilaginosus."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFH64391.1, ECO:0000313|Proteomes:UP000007392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K02 {ECO:0000313|EMBL:AFH64391.1, RC ECO:0000313|Proteomes:UP000007392}; RA Xiao B., Sun L., Xiao L., Lian B.; RT "Complete genome sequence of Paenibacillus mucilaginosus K02."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}. 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; CP003422; AFH64391.1; -; Genomic_DNA. DR EMBL; JN225126; AFK65320.1; -; Genomic_DNA. DR RefSeq; WP_014652230.1; NC_017672.3. DR AlphaFoldDB; I0BPU4; -. DR KEGG; pmw:B2K_27485; -. DR PATRIC; fig|997761.3.peg.5479; -. DR HOGENOM; CLU_024572_2_1_9; -. DR OrthoDB; 9805159at2; -. DR Proteomes; UP000007392; Chromosome. DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro. DR GO; GO:0005509; F:calcium ion binding; 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; IPR015237; Alpha-amylase_C_pro. DR InterPro; IPR006046; Alpha_amylase. 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; PF09154; Alpha-amy_C_pro; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR001021-2}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..518 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5038286485" FT DOMAIN 41..426 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 269 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT ACT_SITE 299 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1" FT BINDING 140 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 197 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 232 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 238 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 240 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 273 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 338 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 442 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" FT BINDING 465 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2" SQ SEQUENCE 518 AA; 57374 MW; A5162BD77E8C8567 CRC64; MSRIWSRRKT AKVIVSAALA FTLIASPGTE KAHAHHDGSN GVMMQYFEWY LPNDGTLWSK LQTNAAALKS AGVTAVWIPP AYKGGGSGDV GYGVYDMYDL GEFNQKGTVR TKYGTKDQLI SAVDTLHANG MQVYGDVVLN HRMNADATET VTAVEVNPSD RNSEISGEYS ISAWTQFHFP GRNNAYSSFK WKWYHFDGVD YDQSRNANKL FKLRGTGKSF DWEVDTENGN YDYLMGADLD WDHPEVISET RTWGNWFVNT AKLDGVRIDA VKHIKFDRMR DWLNGVRTDT GKSLFAVGEY WSGDINKLNN YMTKTSGAMS LFDVPLHYNL YAASNGSGGY DMRNILNNTL LKTNPTKAVT FVDNHDSQPG QALQSTVQGW FKPLAYALIL TRQEGYPSLF YGDYYGTSDG KIASFKTVLD KLLAARKTYA YGKQNDYLDH QDIIGWTREG DAAHANSGLA ALVTDGPGGS KRMYVGTGKA GQVWNDKTGN RTDTVTIDGS GYGTFPVNGG SVSVWAKQ //