ID K9Y060_STAC7 Unreviewed; 494 AA.
AC K9Y060;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Glucan 1,4-alpha-maltohexaosidase {ECO:0000313|EMBL:AFZ37771.1};
DE EC=3.2.1.98 {ECO:0000313|EMBL:AFZ37771.1};
GN OrderedLocusNames=Sta7437_4301 {ECO:0000313|EMBL:AFZ37771.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ37771.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP003653; AFZ37771.1; -; Genomic_DNA.
DR RefSeq; WP_015195425.1; NC_019748.1.
DR AlphaFoldDB; K9Y060; -.
DR STRING; 111780.Sta7437_4301; -.
DR KEGG; scs:Sta7437_4301; -.
DR PATRIC; fig|111780.3.peg.4453; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_024572_2_0_3; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000010473; Chromosome.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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:AFZ37771.1};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000313|EMBL:AFZ37771.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 6..402
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 234
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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"
SQ SEQUENCE 494 AA; 56709 MW; 95DD8055B0EF0C9E CRC64;
MTEFNGVMMQ YFHWYNEPDG SLWNELAENA ADLAKAGITA VWLPPAYKGT AGGYDVGYGV
YDIFDLGEFD QKGSVRTKYG TKDEYVRAIK TAQEAGIHVY ADVVLNHKLG GDEQEEVEAT
PFNPNDRHHA IGEMQKVKVW THFTFPGRQG KYSSLEWHWW HFDAVDYNAY DGDANAIYLF
KDKKFDEQVD LEQGSFDYLM GCDLDMEHPE VRGELKYWGE WYMDTTNVDG FRFDAVKHVR
AGFFPEWLNH CRNYAGKQLF AVGEYWSNHI EALHHFIEVT GGDVALFDAP LHYNFSEASK
AGNNYDMRQI FDGTLVQQQP ALAVTLVENH DSQPLQSLES VVESWFKPLA YALILLRRDG
YPCIFYADYY GAHYKDTGND GQEYEIWIDQ HQWIIDKFLF ARQEYAFGDQ YDYFDHANCI
GWTRLGDEEH PGGMAVVLSN GGEGTKWMEV GKPNHTYIDL TEHIKEPIVT NDKGWAEFRC
PAGSVSVWVP KSAN
//
