ID S8BSA4_9LAMI Unreviewed; 441 AA.
AC S8BSA4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|PIRNR:PIRNR001028};
GN ORFNames=M569_17388 {ECO:0000313|EMBL:EPS57430.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS57430.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS57430.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548,
CC ECO:0000256|PIRNR:PIRNR001028, ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR001028};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR001028,
CC ECO:0000256|RuleBase:RU003615}.
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:EPS57430.1}.
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DR EMBL; AUSU01010237; EPS57430.1; -; Genomic_DNA.
DR AlphaFoldDB; S8BSA4; -.
DR OrthoDB; 201664at2759; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; IPR013775; A-amylase_pln.
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:SF37; ALPHA-AMYLASE 1; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001028; Alph-amls_plant; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
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 Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW Signal {ECO:0000256|PIRNR:PIRNR001028}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT CHAIN 35..441
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT /id="PRO_5010605126"
FT DOMAIN 35..372
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 373..435
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ SEQUENCE 441 AA; 48763 MW; C127B524B14060AD CRC64;
MKLPMPGITS RSRFHARFTL VLLPIILLFS SADSDVLLQG FNWESCYRGG WYNSLIAVAP
QIAAAGVTHV WLPPPSQAVD PQGYLPGRLY DLDASKYGSK EELTALIKSL HDRGVKAVAD
VVINHRTAER KDARGIYCIF EGGTDDGRLD WGPAFICRDD AEYSDGTGNL DTGEGYAGAP
DIDHLNPTVQ AELSEWLNWL RHEIGFDGWR LDFVKGYSTG IAQIYVNNTD PRFVVGELWS
SLYYNTLDGR LEYNQDRHRD RIANWANSAG GGVKAFDFTT MGILRVAVQG ELWRLKDAPG
NPPGMMGISP EKSVTLVANH DSVDDQHWRF PPEKLILGYA YILTHPGTPM IFCDHFLAWS
NRDAILELTA IRARNGISET SKLEILIADA DLYVAKIEGK VITMIGSGMG MALGTLVPPT
FDLATSGDEY AIFEMNLASQ E
//
