ID MDE5_SCHPO Reviewed; 513 AA.
AC O14154; Q874R5; Q96WR6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Alpha-amylase mde5;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE AltName: Full=Mei4-dependent protein 5;
DE AltName: Full=Meiotic expression up-regulated protein 30;
DE Flags: Precursor;
GN Name=mde5; Synonyms=meu30; ORFNames=SPAC25H1.09, SPAC4A8.01;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 191-513.
RC STRAIN=CD16-1;
RX PubMed=11376151; DOI=10.1093/nar/29.11.2327;
RA Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y.,
RA Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.;
RT "Comprehensive isolation of meiosis-specific genes identifies novel
RT proteins and unusual non-coding transcripts in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 29:2327-2337(2001).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P0C1B3};
CC Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high
CC concentrations. {ECO:0000250|UniProtKB:P0C1B3};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {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; CU329670; CAD62442.1; -; Genomic_DNA.
DR EMBL; AB054314; BAB60880.1; -; mRNA.
DR PIR; T38770; T38770.
DR RefSeq; XP_001713068.1; XM_001713016.2.
DR AlphaFoldDB; O14154; -.
DR SMR; O14154; -.
DR BioGRID; 280575; 10.
DR STRING; 284812.O14154; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GlyCosmos; O14154; 2 sites, No reported glycans.
DR PaxDb; 4896-SPAC25H1-09-1; -.
DR EnsemblFungi; SPAC25H1.09.1; SPAC25H1.09.1:pep; SPAC25H1.09.
DR PomBase; SPAC25H1.09; mde5.
DR VEuPathDB; FungiDB:SPAC25H1.09; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_7_2_1; -.
DR InParanoid; O14154; -.
DR OMA; AHNWLFT; -.
DR PhylomeDB; O14154; -.
DR PRO; PR:O14154; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; TAS:PomBase.
DR GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR GO; GO:0005509; F:calcium ion binding; NAS:PomBase.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IC:PomBase.
DR CDD; cd11319; AmyAc_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR015340; A_amylase_C_dom.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF223; ALPHA-AMYLASE MDE5; 1.
DR Pfam; PF09260; A_amylase_dom_C; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 2: Evidence at transcript level;
KW Calcium; Carbohydrate metabolism; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Reference proteome;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..513
FT /note="Alpha-amylase mde5"
FT /id="PRO_0000001357"
FT ACT_SITE 226
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT ACT_SITE 250
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 229..230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 318
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..60
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 171..184
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 260..304
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 454..488
FT /evidence="ECO:0000250"
SQ SEQUENCE 513 AA; 58716 MW; 455DD97FA428C182 CRC64;
MKHNEVFGWT LKVLSFLLVV IPANALDKHG WRKQSIYSLL TDRFASTNPK PCNPEDREYC
GGNWRGIIDK LDYIQGMGFT AIWISPIIKN IEGRTKYGEA YHGYWPQDLY TLNPHFGTEQ
DLIDLADALH DRGMYLMVDT VVNHMGSSDP RNIDYGIYRP FNQSSHYHPM CPIEQDKPLS
LEQCWIGTED MTLPDIDTEN PQIIETLYNF IHDQVKQFKI DGLRVDATKH VRRTFWPGFC
ESAGVYCQGE EWTGQADLFC EWQEYMDGLH NFPVQGVAAE SVIPLNDRAL RKTAIAMNLV
AHHCKDSTLL GLFLESQDAP RLAALNNDYT VLKNAMTLNL MSDGIPIVFY GQEQMFNGSH
DPVNRPALWD QGYNTDGPLY QYTSKVNKIR RDLINSEDGE IYIRSITHAI MIGDHVMVMY
KGPVITFITN YGAVDKEYLI KMPGSETMID LLTCTLIEVE GEVMRTSIKK GEPKILYPYQ
LAFRDGFCQE QITLQEIDDV FMGRNEINGP DRK
//
