GenomeNet

Database: UniProt
Entry: Q1HFV4_EMEND
LinkDB: Q1HFV4_EMEND
Original site: Q1HFV4_EMEND 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system