ID   K9P7U5_CYAGP            Unreviewed;       548 AA.
AC   K9P7U5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Glycosidase {ECO:0000313|EMBL:AFY28639.1};
GN   OrderedLocusNames=Cyagr_1474 {ECO:0000313|EMBL:AFY28639.1};
OS   Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Cyanobium.
OX   NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY28639.1, ECO:0000313|Proteomes:UP000010388};
RN   [1] {ECO:0000313|Proteomes:UP000010388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
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; CP003495; AFY28639.1; -; Genomic_DNA.
DR   RefSeq; WP_015109091.1; NC_019675.1.
DR   AlphaFoldDB; K9P7U5; -.
DR   STRING; 292564.Cyagr_1474; -.
DR   KEGG; cgc:Cyagr_1474; -.
DR   PATRIC; fig|292564.3.peg.1401; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_024572_2_1_3; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000010388; Chromosome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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   Glycosidase {ECO:0000313|EMBL:AFY28639.1};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Hydrolase {ECO:0000313|EMBL:AFY28639.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          55..451
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        282
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        312
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         154
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         211
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         245
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         251
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         286
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         351
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         487
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   548 AA;  62061 MW;  4AD421EEE6746699 CRC64;
     MASLFEALKQ EVLAVEKDPA LDTGTATVTL LQEWLASHEA EISARKLAAP TEFNGTLMQW
     FHWYSDGDGG HWRRLRQEAP ALARAGITAL WLPPAGKGGS VWDVGYGTYD LFDLGEFDQK
     GTVRTKYGTK QEYLEAIQAC RGVGIQVYAD VVFNHKLNAD EQEQYRATPY DPADRNRPLG
     EERTISAWTR FRFDGRGNHY SSMQWHWYHF DAVDHNSLDP DFKAIWRTQG AGFEGNVDLE
     KGNYDYLMGS DLNVNHPEVR GELKHWGLWT LDHVGADGFR LDAIKHIASD FFLDWISSLE
     EHAQRDLFVV GEYWTYNIES LHWYAANTGG HMSLFDAPLH MNFHQASRSG GNYDMRRLLD
     GTLMQQLPLL AVTLVENHDT QPLQSLESVV EAWFKPLAYA VILLRDQGYP CIFHADYYGA
     DYTDRKDGQE YRIVLPSHRF LIDRFLLARG HCAYGPQYDY LDHVNTIGWT RLGTSGHPGA
     MAVLMSDGPA GHKWMEVGKR HTTFRDLTGH IQTPITTNGD GWAEWHCPGG SVSVWVEADA
     LTAMGVTL
//