ID N1S5V1_FUSC4 Unreviewed; 1117 AA.
AC N1S5V1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=FOC4_g10000852 {ECO:0000313|EMBL:EMT73489.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT73489.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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}.
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DR EMBL; KB726232; EMT73489.1; -; Genomic_DNA.
DR AlphaFoldDB; N1S5V1; -.
DR STRING; 1229665.N1S5V1; -.
DR HOGENOM; CLU_000631_7_2_1; -.
DR Proteomes; UP000016929; 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; 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; 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; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000016929}.
FT DOMAIN 94..300
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 342..450
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 533..792
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 801..923
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT REGION 1083..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1117 AA; 125511 MW; D80FB6DAD3D98B0F CRC64;
MSVPDDPLNF IPADLFFPTV PNFQNPTEVV AVESSESIKP SDPLRYAAHI TLGGVNGDSQ
TQCLVQFVTP LIWRIRYDPK YTSLSDFEDT NTRTIVRVQE YRDSDARNAY PAGDEWFWRT
SFKQLSTDHW VLTSNEYQSK NGTATPKTSL HIFKSPFRIV ATRKLKTLEA DTSLLQSVGV
DTTSELEQII WQTTDQTFSY QKNSDIDAIN NVVLNVKKPG PAEYLGFGEQ GGKTVLKKPT
YLNYFCYDNF NYLKVYGQGA LDGREPLYQS SPFYLEMNGT PTYQNVTGVM IDNYSQVAID
LGKNDSNIIS IATRFNTFDA YILTADDVPA MIWQYTSIVG RPKLKPRYIL GHHQGCYGYA
NEGTVYNVVN AYRGSGIPLD GIHLDVDFQE RYRTFTSSTV NFPDSKRFFG NLKKQGIKAC
TNITPILTLR TVDEGAYKAL DAFWDQKDPK NPKTKYTKGL NSYPPTYWRY DGPNSNGPLA
KGVNPTSYGN DYYGQPQRLT FADYPGGPTY LDSYDFHANY NSGYPFHGGV SYGQTLGTPG
YYPDLNRADA REVWGKQYQD LFDDGLEFVW QDMTTPAVGR SYGDMLGFPS RLQMTDDSPI
SAPKTKTAIE LWSLYSYNLH KATYHGLSNL KGRENKRNFI IGRGSQTGMH RFAGLCTGDN
GSSWDFWKIS VAQVLALGYS GLTIAGVDMG GFTSDPTSNA SYPRWCNPEL FIRWYSGAFL
LPWYRNHYMQ HWDQQSNPPA KVFQEPWAFS DVLSNQYAHL IPQDQRVLYE AVVPICRYYV
QLRYSLIQVL YDCMFANMIN GLPIARAMLI TDPLDTSLFN TNESFIDTQY LLGHNILVCP
IVDPQVYNRD VYLPGTDLWY PSNLRVDNQN FGPDPILKHA ADLEQPVKGG RIISYGCSLP
AAFNRPDQVP FITPVYIRGG AIIPQLDVRQ FIGENDLNPP TIHFYPGGKK VTSYSMYLDD
GVSKDSAPNN LPQYKYQDPA KSKKPKGFYR EVKMTQESTS TARTLTIRHP WNGFDAKSTV
GDIYNLAVWT VKTGGAAPQV QVSFQDENGK TVDDARLSHN YDGNRGVLTV NVPVDLVPSL
DHPATTNGTL TNGSTNGASV NGHSKDRHIA VKITGLT
//
