ID K2SQZ4_MACPH Unreviewed; 988 AA.
AC K2SQZ4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=MPH_03611 {ECO:0000313|EMBL:EKG19090.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG19090.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG19090.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG19090.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG19090.1}.
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DR EMBL; AHHD01000166; EKG19090.1; -; Genomic_DNA.
DR AlphaFoldDB; K2SQZ4; -.
DR STRING; 1126212.K2SQZ4; -.
DR VEuPathDB; FungiDB:MPH_03611; -.
DR eggNOG; KOG1066; Eukaryota.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; K2SQZ4; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000007129; 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; 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; IPR033403; DUF5110.
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 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.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:EKG19090.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..988
FT /note="alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003865167"
FT DOMAIN 97..342
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 399..727
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 735..823
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 842..892
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
FT REGION 213..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 111738 MW; D2E95DD5C92635D9 CRC64;
MPSAAPKSRR WTSFLLVVAV VCLLFTPAAS VKHENFKTCS QSGFCKRNRA FADNAQELSS
AWQSPYTLDP ASIAFNQGQL SATVLKKVND NDQVRLPLTL TFLESGTARF TLDEEKRQKG
DIELRHDSKA RKERYNEAEK WAIVGGLDVS TGAAISSEAD EGVTKVVYGP GGKFEAVIHH
SPLAVDFKRD GQTQVKFNDR GFLNLEHWRP KIEKEKKEGE EGAAEEAAPE PTEDESTWWD
ESFGGNTDSK PRGPEAVALD ITFPDYAHVY GIPEHASSLS LKETRGGDGA YSEPYRLYNA
DVFEYEMDSP MTLYGSIPFM QAHRKDSTVG VFWLNAAETW VDIVKSKSAA NALSLGVAGH
TDTKTHWISE SGLLDVFVFL GPEPKDVIKS YSELTGYTQL PQEFAIAYHQ CRWNYVTDED
VMDVDRKFDK HNIPYDVIWL DIEYTHEKKY FTWDPMTFPK TKEMHDQLDK HDRKLVAIID
PHIKNVADYP IVEELKSKEL AAKNKDGNQY EGWCWPGSSY WVDCFNPAAV DWWKSLFKYD
KFQGSAPNTF IWNDMNEPSV FNGPETTMPK DNMHFGNWEH RDVHNINGMT FHNATYEAII
ERKKGEVRRP FVLTRSFYAG SQRLGAMWTG DNQANWDHLA ASIPMTLNQG ISGFPFAGAD
VGGFFGNPEK DLLTRWYQAG AFYPFFRGHA HIDTRRREPY LAGSPYTEII TQALRLRYSL
MPTWYTAFHE ASVNGAPIIR PNYYVHPTDE KGFAIDDQLY LGSTGLLAKP VVTEGADSVD
IYIADDEPYY DYFDYTIYTG PGSKSIPAPL EKIPLLMQGG HIIPRRDRPR RSSGLMKYDP
YTLVVTIGKD GKAEGELYVD DGETFDYQQG AYIYRRFLFD KPTHALTSID ISTSGPKTAT
YLKSMAKVRV EKVVIVGAPD EWERLESVFV SEEGAKESQR RRKVPIKFTK GKDGKASFAV
VRDPKVSIAK GWKIDFGGEN EEHHGHAH
//
