ID   AGAL_SCHPO              Reviewed;         436 AA.
AC   Q9URZ0;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Alpha-galactosidase mel1;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase;
DE   AltName: Full=Melibiase;
DE   Flags: Precursor;
GN   Name=mel1; ORFNames=SPAC869.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15580593; DOI=10.1002/yea.1190;
RA   Goddard A., Ladds G., Davey J.;
RT   "Development of a semi-quantitative plate-based alpha-galactosidase gene
RT   reporter for Schizosaccharomyces pombe and its use to isolate a
RT   constitutively active Mam2.";
RL   Yeast 22:31-41(2005).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Secreted alpha-galactosidase required for catabolic
CC       conversion of melibiose to glucose and galactose.
CC       {ECO:0000269|PubMed:15580593}.
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: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:16823372}. Secreted {ECO:0000269|PubMed:15580593}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB60017.1; -; Genomic_DNA.
DR   PIR; T39118; T39118.
DR   RefSeq; NP_595012.1; NM_001020443.2.
DR   AlphaFoldDB; Q9URZ0; -.
DR   SMR; Q9URZ0; -.
DR   BioGRID; 279671; 1.
DR   STRING; 4896.SPAC869.07c.1; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   CLAE; MEL27A_SCHPO; -.
DR   MaxQB; Q9URZ0; -.
DR   PaxDb; Q9URZ0; -.
DR   PRIDE; Q9URZ0; -.
DR   EnsemblFungi; SPAC869.07c.1; SPAC869.07c.1:pep; SPAC869.07c.
DR   GeneID; 2543243; -.
DR   KEGG; spo:SPAC869.07c; -.
DR   PomBase; SPAC869.07c; mel1.
DR   VEuPathDB; FungiDB:SPAC869.07c; -.
DR   eggNOG; KOG2366; Eukaryota.
DR   HOGENOM; CLU_013093_1_0_1; -.
DR   InParanoid; Q9URZ0; -.
DR   OMA; AMTPTMG; -.
DR   PhylomeDB; Q9URZ0; -.
DR   Reactome; R-SPO-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q9URZ0; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IDA:PomBase.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IDA:PomBase.
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:0005995; P:melibiose catabolic process; IC:PomBase.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
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; IPR006215; Glyco_hydro_melibiase.
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   PRINTS; PR00748; MELIBIASE.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW   Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..436
FT                   /note="Alpha-galactosidase mel1"
FT                   /id="PRO_0000001006"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..156
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   436 AA;  49366 MW;  8B3EE243AE39BD50 CRC64;
     MISISFLNCF FLVFLFLFFS DVHGSYNGLG LKPQMGWNSW NKYACDIDES IILNNAKAIK
     EEGLLDLGYE YIVMDDCWSK HERNATTGRL EANPDKFPNG IGSMAKKLHD MGFKFGMYSS
     AGKYTCAGFP GSLNHEQIDA DTFADWGVDY LKYDNCFNEG KSGVPLISYE RYKRMSDALN
     KTGRPIFYSL CQWGEDFVWN WGNTIANSWR ISGDIFDTFS RKDVRCPCET IECFALQGDH
     CSVMNIISKA SFLSSKAGMN SGWNDLDSLE VGNGGMSFEE YKTHFTMWAI LKSPLILGND
     VSSMSPMDKL IVSNKELISI NQDIGTNPAA LIWKKKYGDE YIELFSGRLS NNDWVVAVLN
     AASEPLKMGI HLSDIFVDAL GNAEHDWLAT DLWNNNVKLV SDRIRANVAS HGVQVWRFQQ
     YKVKNTNDKF FSFNKH