ID A0A1Z4RKV3_9CHRO Unreviewed; 494 AA.
AC A0A1Z4RKV3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:BAZ43088.1};
GN ORFNames=NIES4102_00840 {ECO:0000313|EMBL:BAZ43088.1};
OS Chondrocystis sp. NIES-4102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Chondrocystis.
OX NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ43088.1, ECO:0000313|Proteomes:UP000217698};
RN [1] {ECO:0000313|EMBL:BAZ43088.1, ECO:0000313|Proteomes:UP000217698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ43088.1,
RC ECO:0000313|Proteomes:UP000217698};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; AP018281; BAZ43088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4RKV3; -.
DR KEGG; chon:NIES4102_00840; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000217698; 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; IPR015237; Alpha-amylase_C_pro.
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 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000217698};
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; 56563 MW; 70B861B41F954390 CRC64;
MAEFNGVMMQ YFHWYNEPDG SLWNQLAADA EDLAKAGITA VWLPPAYKGS AGGYDVGYGV
YDMFDLGEFD QKGSVRTKYG TKEEYLKAIR IAQDAGVHVY ADVVLNHKLG GDQDEEVEAT
PFNPNDRHHA IGDLQKVKVW THFTFPGRQG KYSSLEWHWW HFDAVDYNAY DGDANAIYLF
KDKQFDDQVD LEQGSFDYLM GCDLDVEHPE VRGELKYWGE WYIDTTGVDG FRFDAVKHVK
AGFFPDWLNH VRHYAGKQLF AVGEYWSTHI EALHHFIDVT GGDVALFDAP LHYNFSEASK
SGNDYDMRQI FDNSLVKDQP TLAVTLVENH DSQPLQSLES VVESWFKPIA YALILLRRDG
YPCIFYADYY GAHYKDWGND GQEHEVWLDS HKWIIDKFLE ARQNYAYGDQ YDYFDHGNCL
GWTRIGDEKH PGGMAVVVSN SDDGHKWMET GTPNQTYIDI TEHINDPVVT NEDGWAEFLC
PAGSVSVWVP KESD
//
