ID W2TEG9_NECAM Unreviewed; 1506 AA.
AC W2TEG9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE Flags: Fragment;
GN ORFNames=NECAME_09737 {ECO:0000313|EMBL:ETN79596.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN79596.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
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 -!- 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; KI659424; ETN79596.1; -; Genomic_DNA.
DR RefSeq; XP_013301823.1; XM_013446369.1.
DR STRING; 51031.W2TEG9; -.
DR EnsemblMetazoa; NECAME_09737; NECAME_09737; NECAME_09737.
DR GeneID; 25349766; -.
DR KEGG; nai:NECAME_09737; -.
DR CTD; 25349766; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000053676; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
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; 2.
DR Pfam; PF02806; Alpha-amylase_C; 2.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 2.
DR SMART; SM00632; Aamy_C; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676}.
FT DOMAIN 204..526
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 535..619
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT DOMAIN 864..1254
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 1269..1353
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETN79596.1"
SQ SEQUENCE 1506 AA; 167719 MW; C7B7F981562D9EF5 CRC64;
DRGLIADQKR PCACPETQVD SGDGLPVCAE PGLTRDILVS RTSVRPKTCN QVTGRCKGGG
FESDDLMMQA KKIKYDVVGL TETRRRHSLN AVYEAGEELF LGTCDSRGVS GVGVLVNTSM
AKNTDSFEQR TTRIGRLWVR KCGPTPALTI FVAYALTSSY EEEEVDTLCM VLEKFYREDL
VFYKVIIGDF NAKVGPRRTP EELHIGTHGL QWNDQGERLS ESIMTTKTIH GNSQFQNVTS
ELARLCREAI KKDLKERRAE VPYTNVDFND WRCPKKNIEG SDYQYNAEAV RNCRLVGLLD
LDQGRPEVRE KLIAFLNHLI DLGIAGFRCD ASKHMWPGDL MLILNGTRNL REDIFGPNQR
PFIVHEVIDR GHEAIKVAEY TGLGRYTNFN FGGAVSAAAK GTTGWDLLSS LGPGYGYGNG
ADNDVLNFID NHDNQRDDHP YVVTYKNGDR YRLAVAYMMA WPYGYPRVMS SFYFDHRDQG
PPHSGSKTGY ATRSPIFVSH DETCNVTSGW VCEHRWPTIR EMAKFRSTVK GAAATQIVKD
NNRLAFARRG RGFFAINGNN EKWGRFFATT MPEGNYCDQY AGSLKNGKCT GRTIHVKKNG
QAFLRIGGKQ AVAFSLASRI GDPPVRPDLE DYSKTVILIK KNTHGGQYVF IRGGTSHAND
DECQPGLYQQ RNDKCAIPIM HNTTVPFVYN EYLSWSQGDE FLDFEGPEEE QGTYNGRAAS
GTPLAYSTNN PSEFEYNQHN KYGPSYWLVE LFVDCSKTDQ GWFELKGYLT PSHEWEPNIN
QGKCTGSIGG SAPFRSINHI AKCGAVNVFK WGSNECIVDP AYVAKESSPP KGGNVYFSPD
PLILYLPLIL NTEYDEPQTL PNRQAMVHLF EWKWTDIAAE CETFLQHYGY GAVQISPPNE
HISFVLNNDI PWYIRYQPVS YQLISRSGNE AQFKDMVNRC NKVGVRIIVD TVMNHMVGVS
QKSGVDGKSG SGGSSFDGTD GVEQFPGVPY TKSDFNDYRC HRDIQGSDYQ NSAQSVKNCR
LVGLLDLDQS NTEVRSKLIA YLDQLIDYGV AGFRRVILCD ASKHMWPDDL MVILNGTKNL
REDIFGLNQR PFVVHEVIDR GGEAVKCSDY IGIGRYTNFN FGAAVSSAAK GNSDWKLLSN
LGPGYAYGNL EDHDVLNFID NHDNQRDTSP YVVTYKDGDR YRMAVAYMLA WSYGYPRVMS
SYYFSQHDQG PPNSGAGNGY ATTSPTFNTD QTCNSASGWV CEHRWPTIRL IFCREMTKFR
SAVEGAAATE IFTDNQRIAF AREGKGFFAL NGNDRSWSKN FPTTMPAGTY CDQYAGSLEN
GKCTGTTVTV GQDGSAYLQI DSRNVIAFSL ASRIGAAPNP TTVPKGYLKT VILLKKDTYQ
GQSLFIRGGV SHANNNGTHD GQVSFGTPLA YSTNNPSDYE YQPYNKYGTG YWLVQLLVDC
SKSDQGWFEL KGYASPSIGW EPNIAQSACT GKIGGSAPFQ SVNHIAKCGA VNVFTWGSND
CVIDAI
//
