AGLU_SACS2
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 25-MAY-2022, entry version 68.
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; Crenarchaeota; 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}.
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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 EnsemblBacteria; AAK43151; AAK43151; SSO3051.
DR GeneID; 44128770; -.
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 OMA; QGVDCFK; -.
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 Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 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
