ID Q1HFV4_EMEND Unreviewed; 874 AA.
AC Q1HFV4;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Probable alpha/beta-glucosidase agdC {ECO:0000256|ARBA:ARBA00014002};
DE EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=AN0941-2 {ECO:0000313|EMBL:ABF50846.1};
OS Emericella nidulans (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425 {ECO:0000313|EMBL:ABF50846.1};
RN [1] {ECO:0000313|EMBL:ABF50846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC A4 Glasgow {ECO:0000313|EMBL:ABF50846.1};
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Has both alpha- and beta-glucosidase activity.
CC {ECO:0000256|ARBA:ARBA00025512}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; DQ490470; ABF50846.1; -; mRNA.
DR AlphaFoldDB; Q1HFV4; -.
DR SMR; Q1HFV4; -.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:AspGD.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016052; P:carbohydrate catabolic process; IDA:AspGD.
DR GO; GO:0005982; P:starch metabolic process; IEP:AspGD.
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; 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:SF67; ALPHA/BETA-GLUCOSIDASE AGDC-RELATED; 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 2: Evidence at transcript level;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185}.
FT DOMAIN 107..214
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 263..667
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 675..763
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT REGION 441..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 98043 MW; 13F8419DBB4E8C70 CRC64;
MLGFLLFLPL VGAAVIGPRA NSQICPGYKA SHAKHNSHTF TADLTLAGKP CDTYGTDLKD
LKLLVEYQTD ERLHVMIYDA NEQVYQVPES VLPRVGNGNG TEKDSALKFD YVEEPFSFTV
SRNGDVLFDT SASNLIFQSQ YLNLRTWLPN DPHLYGLGEH TDSLRLETNN YTRTLWNRDS
YGVPSHSNLY GAHPVYYDHR GSAGTHGVFL ANSNGMDIKI NKTLDGKQYL EYNILGGVLD
FYFFTGSTPK EASTQYAKVV GLPAMQSYWT FGFHQCKYGY RDVYEVAEVV YNYSQAGIPL
ETMWTDIDYM ELRRVFTLDP ERFPLGKMRE LVDYLHDHNQ HYIVMVDPAV STSDNPGYRR
GVEQDIFLKT QNGSLYKGAV WPGVTVYPDW FHPAIQDYWN GEFNKFFDPE TGIDIDGLWI
DMNEAANMCT FPCTDPERYS IENDLPPAPP AVRPSNPRPL PGFPDDFQPG SSKRLSKRAH
GDKLGLPGRN LLSPPYSIKN AAGALSQNTI QTNIGHAGGY VEYDTHNLYG TMMSSASRIA
MQQRRPDVRP LIITRSTYAG AGAHVGHWLG DNLSTWKLYR ASIAQVLAFA SMFQIPMVGA
DVCGFGSNTT EELCARWASL GAFYTFYRNH NEIGNIPQEY YYWESVTESA TKAINIRYQL
LDYVYTAFHR QSKTGEPFLQ PLFYLYPEDK NTFAIDLQFF YGDAILISPV TEKNSTSVNA
YFPKDIFYDW YTGAVIQGQG ANIILSNINI THIPIHIRGG NIVPIRSSGA MTTTELRKKG
FQLIIASGID GTASGSLYLD DGDSLEQTDT ANIEFEYRSG VLYIKGQFIH DVPVKIESVI
LLGQTTTAGA GRHNQKQVIE TNLELTAPTR VKLA
//