ID P91982_CAEEL Unreviewed; 713 AA.
AC P91982;
DT 01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=C50B6.7 {ECO:0000313|EMBL:CAB02856.1,
GN ECO:0000313|WormBase:C50B6.7}, CELE_C50B6.7
GN {ECO:0000313|EMBL:CAB02856.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB02856.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAB02856.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB02856.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; BX284605; CAB02856.1; -; Genomic_DNA.
DR PIR; T20090; T20090.
DR RefSeq; NP_506303.1; NM_073902.3.
DR AlphaFoldDB; P91982; -.
DR SMR; P91982; -.
DR STRING; 6239.C50B6.7.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EPD; P91982; -.
DR PaxDb; 6239-C50B6-7; -.
DR PeptideAtlas; P91982; -.
DR EnsemblMetazoa; C50B6.7.1; C50B6.7.1; WBGene00008220.
DR GeneID; 179813; -.
DR KEGG; cel:CELE_C50B6.7; -.
DR UCSC; C50B6.7; c. elegans.
DR AGR; WB:WBGene00008220; -.
DR WormBase; C50B6.7; CE08876; WBGene00008220; -.
DR eggNOG; KOG2212; Eukaryota.
DR GeneTree; ENSGT00940000167534; -.
DR HOGENOM; CLU_013336_3_0_1; -.
DR InParanoid; P91982; -.
DR OMA; WHNYKSG; -.
DR OrthoDB; 3249969at2759; -.
DR PhylomeDB; P91982; -.
DR Reactome; R-CEL-189085; Digestion of dietary carbohydrate.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00008220; Expressed in larva and 2 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
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:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 1: Evidence at protein level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|EPD:P91982,
KW ECO:0007829|PeptideAtlas:P91982};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..713
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004161938"
FT DOMAIN 32..418
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 427..511
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 713 AA; 78658 MW; 6076FAA0143058F6 CRC64;
MLKHLFLFLF IKSSIAYNFY WYDKTQTLQN RQTMVHLFEW KWADVAKECE NFLQYYGYGA
VQVSPPMEHL KAFPNNNYPW WVRYQPVSYK LDSRSGNEQE FQDMVNRCNK VGVRIIVDIV
MNHMVGIGQK SGNGVGSSGS SSFDGTHGVQ SFPGVPYSLG DFNNPKCDGD IQGSDYQNSA
EHVKDCRLVG LLDLNQASAT VRAKIVAYLN KLVDMGVAGF RHDASKHMWP QDILNILNDV
KDLRSDIYGS NQRPFAVHEV IDRGGEAVKC GDYFGNGRYT NFNFGAAVSA AAKQQSDWKY
LANLGPGYGY GNNEDHDVLN FIDNHDNQRD SSPYVVTYKD GQKYNLAVGF MLAWPYGYPR
VMSSFAFSYS DQSPPNSGAS NDYATTSPTF NGDQTCNSNS GWVCEHRWPA IRQMAKFRSA
VQGTAAADIV TDTRRIAFAR DGKGFFALNQ QDGAWTKIFA TNLPAGDYCD HFSGGLDNGK
CVGTKITVRD DHTSYLSVPS NSIVAISLDS KLTPYTPPAP PSGYSTTVIL LKKDTNPGQN
IFVRGGTSQA HNGKCSTGPY QQSSDPCAIP MYHATTVPFV FAEYLTWSQQ DNYLDFEGAE
INQGTHDGAA AFGTPLAYST NDKTAIEYQP YNKYGPGYWI AVLRMDCSKA EQGWFEVKGY
ETPDIGWEGD IKQGSCSGSV GGSAPFSSIN HVAKCGAVNV FTWGSASCVI DSA
//
