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Database: UniProt
Entry: X0HSB5_FUSOX
LinkDB: X0HSB5_FUSOX
Original site: X0HSB5_FUSOX 
ID   X0HSB5_FUSOX            Unreviewed;       963 AA.
AC   X0HSB5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE            EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
DE   AltName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN   ORFNames=FOPG_06643 {ECO:0000313|EMBL:EXL79337.1};
OS   Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL79337.1};
RN   [1] {ECO:0000313|EMBL:EXL79337.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL79337.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW808.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXL79337.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL79337.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Annotation of Fusarium oxysporum PHW808.";
RL   Submitted (MAY-2012) 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   -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC       {ECO:0000256|ARBA:ARBA00004833}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; JH658833; EXL79337.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0HSB5; -.
DR   HOGENOM; CLU_000631_7_0_1; -.
DR   Proteomes; UP000030676; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06603; GH31_GANC_GANAB_alpha; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
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   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR   Pfam; PF17137; DUF5110; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..963
FT                   /note="alpha-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004941111"
FT   DOMAIN          98..331
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          387..716
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          724..814
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          837..876
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
FT   REGION          216..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  109347 MW;  B83EE6B366C1DC59 CRC64;
     MRSNTASSFR WTALLLLLGT LTCLFQSAIA VKDKDFKKCD QSGFCKRNRA YADNAVAQGS
     NWKAPYEISA DSTVFEDGKL QAVVVKTINS HGETVRLPLT ISFLKSGAAR VTMDEEKRRN
     KDVVLRDDSP VRKERYDEAD DWVLVGGLDL DKEAQLAFQD KSQINIKYGP EAKQEAIIKF
     SPFEIDFRRD GNSHVKFNDR GLLNMEHWRP KIENKEGEEA AEDESTWWDE SFGGNTDTKP
     RGPESVALDI TFHGYEHVFG IPEHTGPLSL KQTRGGDGNY DEPYRMYNAD VFEYILDSPM
     TLYGSIPFMQ AHRKGSSVGV FWFNVAETWV DITKAKNQAN PLSLGVGGKT STHTHWISEA
     GLLDVFVLLG PTPQDLTKTY GELTGYTAMP QEFAIAYHQC RWNYISSDDV RNVDRNMDKH
     KIPYDVIWLD LEYTDDRKYF TWEPHSFPDP IDMGEHLDAH GRQLVVLLDP HIKKTDNYAA
     SEELVAQDLG VHDKEQKLYE GWCWPGASNW IDCFNPKAIE WWKTMLKFDK FKGTMSNTWM
     WNDMSEPSVF NGPEVTMPKD NIHHGGWEHR DVHNLNGLTF QNATFQALLH REKGELRRPF
     ILTRAFYAGS QKLGAMWTGD NQADWGHLAT SIPMTINQGI SGFPFAGADV GGFFGNPEKD
     LLVRWYQTGI WYPFFRAHAH IDARRREPYL LGEHYTPIAT AAIRLRYSLL PAWYTAFYNA
     AQDGSPIIRP MFWTHPSEEA GFALEDQFFV GSTGLLVKPV TEQNKESVDI WIPDDEVYYD
     YFTYDVQKTS KGKYLTVSAP LDKIPVLLRG GHIIPRRDIP RRSSALMRFD DYTLVVSASK
     SGAAEGELYV DDGDSFDYEQ GQYIHRKFTL SGNTLTSIEA EGRDTKSIKS GPWLKAMEKV
     HVDKIIIVGA PKTWDQKEVQ VESEGRTWTA KVQYHAAKGS RAAFAVVGRV GAKVGEDWSI
     KLA
//
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