YQ29_SCHPO
ID YQ29_SCHPO Reviewed; 478 AA.
AC Q10427; Q9UUN0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Uncharacterized glycosyl hydrolase C11E10.09c;
DE EC=3.2.1.-;
GN ORFNames=SPCC11E10.09c, SPCC188.01c;
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).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; CU329672; CAB57851.1; -; Genomic_DNA.
DR PIR; T40860; T40860.
DR RefSeq; NP_588205.1; NM_001023195.2.
DR AlphaFoldDB; Q10427; -.
DR SMR; Q10427; -.
DR BioGRID; 275622; 5.
DR STRING; 4896.SPCC11E10.09c.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR MaxQB; Q10427; -.
DR PaxDb; Q10427; -.
DR EnsemblFungi; SPCC11E10.09c.1; SPCC11E10.09c.1:pep; SPCC11E10.09c.
DR PomBase; SPCC11E10.09c; -.
DR VEuPathDB; FungiDB:SPCC11E10.09c; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_7_2_1; -.
DR InParanoid; Q10427; -.
DR OMA; AHNWLFT; -.
DR PhylomeDB; Q10427; -.
DR PRO; PR:Q10427; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0009986; C:cell surface; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046379; P:extracellular polysaccharide metabolic process; IC:PomBase.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..478
FT /note="Uncharacterized glycosyl hydrolase C11E10.09c"
FT /id="PRO_0000054345"
FT ACT_SITE 216
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 219..220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 308
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 478 AA; 55442 MW; 3C65EAD005DF7D3E CRC64;
MNLICSILPK KEPSYLKLWR KQVIYQVLTD RFALDEDNFY AKASGNLYLG GTWKGITRNL
DYIKSLGCTA IWISPIVKNI SETTDCGQAY HGYWAQDMTQ LNENFGTEED LKELVNAIHE
KNMLCMVDIV VNHMGHAGSK PVNFLLYQPF NSGKYYHNWQ FVQNYDDPHE TITGWLGDSH
VNLPDIRTEK NEVRKFFQNW VSDLIKRYQF DGIRLDTAKH VEKSFFPTFI EAANVFTTGE
VFHGDPKVVG DYQKYLPSTL NFPLFFQLRE TFLDPKHSMF SFYDKAVLDV RHYFKDVTVL
CNFLENHDFP RFFHETKDIA LALNALTALI FMDGIPIIYY GQEQMFDGGS DPDNREGLWK
SKYNTSNPMF RHLSSMIRTR QNLVETYPEF TYVLSFQLYI DDSVYVFTRP GVIIAISNEG
STSSFKVEID LKEHWKEVPS SFTDILTQKT IPCKDHKLKI KSKSGLPKIL ISSDPSFL
