ID   AGALB_ASPCL             Reviewed;         448 AA.
AC   A1C5D3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable alpha-galactosidase B;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase B;
DE   Flags: Precursor;
GN   Name=aglB; ORFNames=ACLA_003130;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; DS027004; EAW14901.1; -; Genomic_DNA.
DR   RefSeq; XP_001276327.1; XM_001276326.1.
DR   AlphaFoldDB; A1C5D3; -.
DR   SMR; A1C5D3; -.
DR   STRING; 5057.CADACLAP00000129; -.
DR   EnsemblFungi; EAW14901; EAW14901; ACLA_003130.
DR   GeneID; 4708471; -.
DR   KEGG; act:ACLA_003130; -.
DR   VEuPathDB; FungiDB:ACLA_003130; -.
DR   eggNOG; KOG2366; Eukaryota.
DR   HOGENOM; CLU_013093_2_2_1; -.
DR   OMA; NAFGCDI; -.
DR   OrthoDB; 964130at2759; -.
DR   Proteomes; UP000006701; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR000111; Glyco_hydro_27/36_CS.
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; 2.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..448
FT                   /note="Probable alpha-galactosidase B"
FT                   /id="PRO_0000393214"
FT   ACT_SITE        156
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        248
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         226..230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..78
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..158
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  49135 MW;  212C7A414488080A CRC64;
     MSRFHLPLAA AVVLVSCLWS ANALVRPDGV GKLPALGWNS WNAFGCDIDD AKIMTAAKEI
     VNLGLKDLGY EYINIDDCWS VKSGRDKTTK RIVPDPAKFP DGIAGVADRI HDLGLKVGIY
     SSAGLTTCAG YPASLGYEEI DAQTFAEWGI DYLKYDNCGV PSNWTDAYTF CVPDPGSAST
     NGTCPDNENP APQGYDWSTS LTAQRHQRMR DALLGVEHTI FYSLCEWGQA DVSAWGNATG
     NSWRMSGDIT PSWDRIAAIA NENSFLLNHV DFWGHSDPDM LEVGNGDLTL AENRAHFALW
     AAMKSPLIIG TALDGIDPAH LEILLNKYLI AFHQDPVIGR PAYPYKWGYS PDWTFDPAHP
     AEYWSGPSST LDGTLVLMLN SEGSRQTRTA VWKEIPELKD ALGRKGRRQT GFRVTDVWTG
     KDLGCVRDHY TVTLESHDVA ALLVGKGC