ID Q7QBU5_ANOGA Unreviewed; 496 AA. AC Q7QBU5; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 5. DT 24-JAN-2024, entry version 145. 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 Name=1273652 {ECO:0000313|EnsemblMetazoa:AGAP002318-PA}; GN ORFNames=AgaP_AGAP002318 {ECO:0000313|EMBL:EAA07514.5}; OS Anopheles gambiae (African malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Anophelinae; Anopheles. OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA07514.5}; RN [1] {ECO:0000313|EMBL:EAA07514.5, ECO:0000313|Proteomes:UP000007062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST {ECO:0000313|EMBL:EAA07514.5, RC ECO:0000313|Proteomes:UP000007062}; RX PubMed=12364791; DOI=10.1126/science.1076181; RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W., RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., RA Collins F.H., Hoffman S.L.; RT "The genome sequence of the malaria mosquito Anopheles gambiae."; RL Science 298:129-149(2002). RN [2] {ECO:0000313|EMBL:EAA07514.5} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA07514.5}; RG The Anopheles Genome Sequencing Consortium; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EAA07514.5} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA07514.5}; RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003; RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.; RT "The Anopheles gambiae genome: an update."; RL Trends Parasitol. 20:49-52(2004). RN [4] {ECO:0000313|EMBL:EAA07514.5} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA07514.5}; RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5; RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F., RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.; RT "Update of the Anopheles gambiae PEST genome assembly."; RL Genome Biol. 8:R5.1-R5.13(2007). RN [5] {ECO:0000313|EMBL:EAA07514.5} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA07514.5}; RG VectorBase; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EnsemblMetazoa:AGAP002318-PA} RP IDENTIFICATION. RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP002318-PA}; RG EnsemblMetazoa; RL Submitted (JAN-2021) to UniProtKB. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAAB01008859; EAA07514.5; -; Genomic_DNA. DR RefSeq; XP_312654.5; XM_312654.5. DR AlphaFoldDB; Q7QBU5; -. DR STRING; 7165.Q7QBU5; -. DR PaxDb; 7165-AGAP002318-PA; -. DR EnsemblMetazoa; AGAP002318-RA; AGAP002318-PA; AGAP002318. DR GeneID; 1273652; -. DR KEGG; aga:AgaP_AGAP002318; -. DR VEuPathDB; VectorBase:AGAP002318; -. DR eggNOG; KOG2212; Eukaryota. DR HOGENOM; CLU_013336_2_1_1; -. DR InParanoid; Q7QBU5; -. DR OMA; ACTGNTI; -. DR OrthoDB; 3249969at2759; -. DR Proteomes; UP000007062; Chromosome 2R. 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 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134}; KW Chloride {ECO:0000256|ARBA:ARBA00023214}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; 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 Reference proteome {ECO:0000313|Proteomes:UP000007062}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..17 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 18..496 FT /note="Alpha-amylase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014588327" FT DOMAIN 28..398 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT DOMAIN 407..495 FT /note="Alpha-amylase C-terminal" FT /evidence="ECO:0000259|SMART:SM00632" SQ SEQUENCE 496 AA; 54746 MW; 965ADE9C71C71FA1 CRC64; MRAAVVLLAA CATLAAAQFN THQWADRSGI VHLFEWKWDD IAAECENFLA PRGYAGVQVS PPTENAVIGG NFRRPWWERY QPMSYRLETR SGSEAQFASM VRRCNDVGVR IYVDLVINHM ADLVGGGGTA GSTANRPNFS FPGVPFSVTD FNPPCIITNY NDPIMVRNCQ LVSLPDLNQG VPWVRDKIVE LMNHLIGLGV AGFRVDAVKH MWPGDLQAIY SRMNNLPTSH GFPPNARPFL TQEVIDLGGE AVTRDEYTHL GTITEFRHSA EIGRVFRGRN PFRHLTNWGT GWGFLPSHLA LVFIDNHDNQ RGHGGGGSDV LTYKVPRNYK MATAFMLAHP FGIVRVMSSF SFSDSEQGPP QDANGNLLSP TFNPDNSCGP GWVCEHRWRQ IYNMIGFRNA VAGTQINDWW DNGNYQMAFC RGARGFIAFN LESFDLNQSL QTCLPAGTYC DVISGDLVNG ACTGNTITVG GDGRAQIVLP ANAYDGVLAI HINSRV //