ID A0A059A3H4_EUCGR Unreviewed; 879 AA.
AC A0A059A3H4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
DE AltName: Full=Maltase {ECO:0000256|ARBA:ARBA00041343};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_K01953 {ECO:0000313|EMBL:KCW48231.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW48231.1};
RN [1] {ECO:0000313|EMBL:KCW48231.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW48231.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001657};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; KK198763; KCW48231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059A3H4; -.
DR STRING; 71139.A0A059A3H4; -.
DR EnsemblPlants; KCW48231; KCW48231; EUGRSUZ_K01953.
DR Gramene; KCW48231; KCW48231; EUGRSUZ_K01953.
DR InParanoid; A0A059A3H4; -.
DR OMA; YTHEKVV; -.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06602; GH31_MGAM_SI_GAA; 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; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
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 PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF133; ALPHA-GLUCOSIDASE; 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; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..879
FT /note="alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001567500"
FT DOMAIN 81..243
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 295..627
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 635..724
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT REGION 103..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KCW48231.1"
SQ SEQUENCE 879 AA; 96898 MW; B6815AD8D400D50D CRC64;
LKTCGVAETI IAIFLYLLSS TSEVRASVGE GEGTPGVIGY GHTVGSVTLN TSGTALTAKL
RLIKATTVYG PDVESLRLVA SFEASGRLRV RITDAERRRW EVPDDLIPRR PPSPPRRTPS
RPPPCPSGSH RCLSAASSDL VFDLRNTTPF SFAVSRRSSG DVLFETSTSD PSAFLVFKGQ
YLQLSSSLPP GRSSLYGIGE HTKPSLRLLP NQTLTLWNAD IRSAYLDVNL YGPHPLYMDV
RSSVGSSEGG GGGVGAGTSH GVLLLNSNGM DVVYTGDRIT YKVIDGYTEL IGRPTSMPYW
SFGFHQCRWG YKNVPDLEGV VAGYAKANIP LEVMWTDIDH MDANKDFTLD PINFPVEKMK
EFVSSLHENG QKYVLILDPG ISVNKTYGTY IRGMQADIFI KREGVPYLGR VWPGLVYFPD
FLHPSSESYW GGEIKSCPTY FNDPPPLPST LDNPPYKINN AGVHQPINNK TTPATSLHFG
NISEYNAHNL YGLLEAKATN KALVNVTGKR PFILSRSTFL SSGKHTAHWT GDNAATWDDL
AYSVPAILNF GLFGIPMVGA DICGFFWDTT EELCNRWIQL GAFYPFARDH SDINSIRQEL
YLWDSVAASV RKVLGLRYRL LPYLYTLMYE AYRKGIPIAP PQFFSFPEDK MTYLINSQFL
IGKGVMVTPI LQSGANTVDA YIPSGNWFNF FNYSNSVSTA LGMNVMLNAP PDHPHVHVRE
ANILAMQGEA MTTEVARRTT FELLVAVDKN GNSLGQVFLD DGEDVEMGGE GNKWTLVKFY
CEKIGNGVVV RSEVVNGEFA LIEKWVIDKV TILGLRKGTR MTKLRGHELY NKVEAKSGQR
TVTIVGKSSG GGEFVIAKVL GLSLLLGKRF KLEVKVPQS
//
