ID AGLU_SACS2 Reviewed; 693 AA. AC P0CD66; O59645; DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot. DT 09-FEB-2010, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=Alpha-glucosidase; DE EC=3.2.1.20; DE AltName: Full=Maltase; GN Name=malA; OrderedLocusNames=SSO3051; ORFNames=C23_036; OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OS (Sulfolobus solfataricus). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=273057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=11427726; DOI=10.1073/pnas.141222098; RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.; RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001). CC -!- FUNCTION: Major soluble alpha-glucosidase. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D- CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}. 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; AE006641; AAK43151.1; -; Genomic_DNA. DR PIR; H90486; H90486. DR RefSeq; WP_009988431.1; NC_002754.1. DR PDB; 2G3M; X-ray; 2.55 A; A/B/C/D/E/F=5-693. DR PDB; 2G3N; X-ray; 2.55 A; A/B/C/D/E/F=5-693. DR PDBsum; 2G3M; -. DR PDBsum; 2G3N; -. DR AlphaFoldDB; P0CD66; -. DR SMR; P0CD66; -. DR STRING; 273057.SSO3051; -. DR CAZy; GH31; Glycoside Hydrolase Family 31. DR PaxDb; 273057-SSO3051; -. DR EnsemblBacteria; AAK43151; AAK43151; SSO3051. DR GeneID; 8762439; -. DR KEGG; sso:SSO3051; -. DR PATRIC; fig|273057.12.peg.3149; -. DR eggNOG; arCOG03663; Archaea. DR HOGENOM; CLU_000631_7_2_2; -. DR InParanoid; P0CD66; -. DR PhylomeDB; P0CD66; -. DR BRENDA; 3.2.1.20; 6163. DR EvolutionaryTrace; P0CD66; -. DR Proteomes; UP000001974; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR CDD; cd06604; GH31_glucosidase_II_MalA; 1. DR CDD; cd14752; GH31_N; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR030458; Glyco_hydro_31_AS. DR InterPro; IPR048395; Glyco_hydro_31_C. DR InterPro; IPR025887; Glyco_hydro_31_N_dom. DR InterPro; IPR000322; Glyco_hydro_31_TIM. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR NCBIfam; NF040948; alpha_gluc_MalA; 1. DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1. DR PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1. DR Pfam; PF13802; Gal_mutarotas_2; 1. DR Pfam; PF01055; Glyco_hydro_31_2nd; 1. DR Pfam; PF21365; Glyco_hydro_31_3rd; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Glycosidase; Hydrolase; Reference proteome. FT CHAIN 1..693 FT /note="Alpha-glucosidase" FT /id="PRO_0000185367" FT ACT_SITE 320 FT /evidence="ECO:0000250" FT ACT_SITE 323 FT /evidence="ECO:0000250" FT ACT_SITE 416 FT /note="Proton donor" FT /evidence="ECO:0000250" FT STRAND 5..8 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 10..19 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 38..41 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 78..83 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 104..109 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 112..118 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 124..132 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 135..143 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 155..166 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 189..201 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 206..211 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:2G3M" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 232..241 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 245..250 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 261..266 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 286..289 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 296..310 FT /evidence="ECO:0007829|PDB:2G3M" FT TURN 311..313 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:2G3M" FT TURN 322..324 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 328..337 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 348..351 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 357..361 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 364..367 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 368..371 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 375..389 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 397..400 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 406..408 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 421..435 FT /evidence="ECO:0007829|PDB:2G3M" FT TURN 436..438 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 452..455 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 461..470 FT /evidence="ECO:0007829|PDB:2G3M" FT TURN 471..473 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 490..492 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 495..525 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 529..531 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 533..536 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 541..545 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 550..552 FT /evidence="ECO:0007829|PDB:2G3M" FT TURN 553..555 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 556..558 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 563..567 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 569..572 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 574..579 FT /evidence="ECO:0007829|PDB:2G3M" FT TURN 580..582 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 585..593 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 596..598 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 600..610 FT /evidence="ECO:0007829|PDB:2G3M" FT HELIX 611..613 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 614..624 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 630..633 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 635..642 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 644..652 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 659..662 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 667..669 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 671..674 FT /evidence="ECO:0007829|PDB:2G3M" FT STRAND 677..693 FT /evidence="ECO:0007829|PDB:2G3M" SQ SEQUENCE 693 AA; 80441 MW; 27BB952C0A7B3858 CRC64; MQTIKIYENK GVYKVVIGEP FPPIEFPLEQ KISSNKSLSE LGLTIVQQGN KVIVEKSLDL KEHIIGLGEK AFELDRKRKR YVMYNVDAGA YKKYQDPLYV SIPLFISVKD GVATGYFFNS ASKVIFDVGL EEYDKVIVTI PEDSVEFYVI EGPRIEDVLE KYTELTGKPF LPPMWAFGYM ISRYSYYPQD KVVELVDIMQ KEGFRVAGVF LDIHYMDSYK LFTWHPYRFP EPKKLIDELH KRNVKLITIV DHGIRVDQNY SPFLSGMGKF CEIESGELFV GKMWPGTTVY PDFFREDTRE WWAGLISEWL SQGVDGIWLD MNEPTDFSRA IEIRDVLSSL PVQFRDDRLV TTFPDNVVHY LRGKRVKHEK VRNAYPLYEA MATFKGFRTS HRNEIFILSR AGYAGIQRYA FIWTGDNTPS WDDLKLQLQL VLGLSISGVP FVGCDIGGFQ GRNFAEIDNS MDLLVKYYAL ALFFPFYRSH KATDGIDTEP VFLPDYYKEK VKEIVELRYK FLPYIYSLAL EASEKGHPVI RPLFYEFQDD DDMYRIEDEY MVGKYLLYAP IVSKEESRLV TLPRGKWYNY WNGEIINGKS VVKSTHELPI YLREGSIIPL EGDELIVYGE TSFKRYDNAE ITSSSNEIKF SREIYVSKLT ITSEKPVSKI IVDDSKEIQV EKTMQNTYVA KINQKIRGKI NLE //