ID A0A2V0P434_9CHLO Unreviewed; 424 AA.
AC A0A2V0P434;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
GN ORFNames=Rsub_04950 {ECO:0000313|EMBL:GBF91845.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF91845.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF91845.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF91845.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF91845.1}.
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DR EMBL; BDRX01000027; GBF91845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0P434; -.
DR STRING; 307507.A0A2V0P434; -.
DR InParanoid; A0A2V0P434; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR012850; A-amylase_bs_C.
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:SF48; ALPHA-AMYLASE ISOZYME 3C; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001021; Alph-amls_thrmst; 2.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00810; Alpha-amyl_C2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:GBF91845.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT DOMAIN 17..358
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 359..422
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
SQ SEQUENCE 424 AA; 47557 MW; B11EC15DE4064303 CRC64;
MFGALFGGAS RRDRRDAVLF QGFGWDSCQK GGWYTKLKQQ LPELKAAGVT HLWLPPPSHS
VSPQGYMPGQ LYNLEASKYG GKKELKELTS AAKKQGIACV ADVVINHRCA DIQENGVYNH
YSDDTDHKGR RIDWGRWAIT CDDPHFNGSG NRDTGADYAA APDLDHANPE LRAALRDWLH
WLQHDIGFEG WRLDFVKGYA PKFVDEYVSS TVGAAALNVG EFWVDMEWQG GELAADQDRA
RQVLCDWVNA NNKSCSAFDF PLKGVLQEAA KRTQYWRLRD ARGKAPGLVG WWPEHAVTFV
DNHDTGSSQQ HWPFPSHLVG VGYAYILTHP GIPCVFYEHF FDWGEELRGT IKGLLEVRRR
AGIKAGARLD IRAAEADFYF AVVDGRVAVK LGPRLDMGPH LPRAEDGWQQ VAAGTEFCVW
EKKK
//
