ID   AGAL8_EMENI             Reviewed;         499 AA.
AC   C8VJZ7;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Putative alpha-galactosidase 8;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase 8;
DE   AltName: Full=Melibiase 8;
DE   Flags: Precursor;
GN   Name=agl8; ORFNames=AN11361;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=15285616;
RA   Naumov D.G.;
RT   "Phylogenetic analysis of alpha-galactosidases of the GH27 family.";
RL   Mol. Biol. (Mosk.) 38:463-476(2004).
CC   -!- FUNCTION: Putative alpha-galactosidase involved in the degradation of
CC       simple oligosaccharides like melibiose, raffinose and stachyose, and of
CC       polymeric galacto(gluco)mannans. {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}.
CC   -!- CAUTION: Could be the product of a pseudogene. It is unsure wether the
CC       two stop codons at positions 140 and 230 are real or are due to
CC       sequencing errors (PubMed:15285616). {ECO:0000305|PubMed:15285616}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF84131.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=CBF84131.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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; AACD01000048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN001306; CBF84131.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; C8VJZ7; -.
DR   SMR; C8VJZ7; -.
DR   STRING; 227321.C8VJZ7; -.
DR   HOGENOM; CLU_2904182_0_0_1; -.
DR   InParanoid; C8VJZ7; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR   GO; GO:0046477; P:glycosylceramide catabolic process; IBA:GO_Central.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR   CDD; cd14792; GH27; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11452; PTHR11452; 2.
DR   Pfam; PF16499; Melibiase_2; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   5: Uncertain;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..499
FT                   /note="Putative alpha-galactosidase 8"
FT                   /id="PRO_0000392533"
FT   ACT_SITE        238
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        303
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   499 AA;  56049 MW;  7708819E68A79358 CRC64;
     MELEKFKPWR DSHSEHIPVP LTSRQNIIII LLILFSHYHH WYWRCRRPTD RWSLLAVCHK
     HHQRAPNSLP TSKSLHSFLH SARGWNSWGI QATPNTIPSY PKEELGRVLN QKFIISQCTM
     LTDPATQDAG YDLCSLDGGW YSSITDKFGC ITYNASLFDI SALSRYLHGK GLRMGLYSQP
     GTPCKARHGT NVTVGSAFID HVDKNNNCYF DYENPNTQLY RELITLWVSW GVDMIKLDYV
     TPGSTFQDTC MPGNLNASAI AYHCAIEKSG RKFQLDVSSD VCRSQPYWGT WNSNADSIRV
     DTDINPYDSD DFFFFYMQHC TVEDYRQFVN LQVVDAQNDK PVTLRGNLDN LFVGNPAKVK
     GVTDKQRNTL MRIWIGASSN LFLGSDMRIL DDLGRWLITS PSSIAAADFC AMYPMQPRNP
     GTGSNQAVQL QACITGPSEH GEAYVLLTNL GPNLGDGGYV TVGGGEQKMS VTLADMGPSR
     SSANRLDLSP RPIHVLILL