AGALD_ASPFN
ID AGALD_ASPFN Reviewed; 655 AA.
AC B8N7Z0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable alpha-galactosidase D;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase D;
DE Flags: Precursor;
GN Name=aglD; ORFNames=AFLA_105840;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR EMBL; EQ963475; EED53209.1; -; Genomic_DNA.
DR RefSeq; XP_002376455.1; XM_002376414.1.
DR AlphaFoldDB; B8N7Z0; -.
DR SMR; B8N7Z0; -.
DR STRING; 5059.CADAFLAP00004320; -.
DR EnsemblFungi; EED53209; EED53209; AFLA_105840.
DR VEuPathDB; FungiDB:AFLA_105840; -.
DR eggNOG; KOG2366; Eukaryota.
DR HOGENOM; CLU_013093_3_0_1; -.
DR OMA; TLKYDNC; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..655
FT /note="Probable alpha-galactosidase D"
FT /id="PRO_0000395071"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 198..202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..155
FT /evidence="ECO:0000250"
SQ SEQUENCE 655 AA; 70844 MW; A393C1B52D478333 CRC64;
MLPKIFYLSL LPAALGHPHL QPRLDNGLAR TPQMGWNTYN HYSCSPNETI VRSNAQALVD
LGLASLGYRY VTTDCGWTVA DRLSDGSLTW NETLFPEGFP ALGKYLHDLD LLFGVYQDSG
IKLCGSPPDN VGNYEDQDAR TFASWEVDSL KYDNCYSDAA TGYPNVNYEP STSPQPRFAN
MSRALAAQNR SMVFQVCEWG IDFPARWAPA LGHSWRIGND IIPHWRAIYR TLNQAVPQTS
FAGPGQWPDL DMLFVGNDIL SIPEEQTHFS LWAILKSPLT IGAALKDDET SINDESLQIL
KQADIIGYNQ DSLGVSASLR RRWTEEGYEV WSGPLSGGRT VAALINWRNE SRDLTLDLPD
IGLQYAGTVK NIWDGTTAQN VKTSYTAKVQ GHGTILLELQ DTTASGQYPG DTFATSTGSS
TTFESIYGVT TSFRYNITVK LSEASSSSDV KIQSTASNKT ITAQVSASGT EASAQIPLLA
GSSNSITIVS PQSVDAITIT PPNGTYFPNT AFTTIGDADT VSCGAGYCQP VGSKIGNIST
NGTARAVIPA TAGTKYLAID YINNDVAFDS AWDWGSNSRN LTVSVNGNKP VRIEVPLSGQ
HSELFGPGKG WWDTATIGVL TEGWKDGDND VVIGNEGGES GFTSYGPDFV GLRVL
