GenomeNet

Database: UniProt/SWISS-PROT
Entry: MDE5_SCHPO
LinkDB: MDE5_SCHPO
Original site: MDE5_SCHPO 
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   22-NOV-2017, entry version 133.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
RT   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
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units.
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
CC       high concentrations. {ECO:0000250|UniProtKB:P0C1B3};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000305}.
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   ProteinModelPortal; O14154; -.
DR   SMR; O14154; -.
DR   BioGrid; 280575; 10.
DR   MINT; MINT-4670941; -.
DR   STRING; 4896.SPAC25H1.09.1; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; O14154; -.
DR   EnsemblFungi; SPAC25H1.09.1; SPAC25H1.09.1:pep; SPAC25H1.09.
DR   KEGG; spo:SPAC25H1.09; -.
DR   EuPathDB; FungiDB:SPAC25H1.09; -.
DR   PomBase; SPAC25H1.09; mde5.
DR   HOGENOM; HOG000165530; -.
DR   InParanoid; O14154; -.
DR   KO; K01176; -.
DR   OMA; NDQKYFH; -.
DR   OrthoDB; EOG092C1HLH; -.
DR   PhylomeDB; O14154; -.
DR   PRO; PR:O14154; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
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   InterPro; IPR013777; A-amylase-like.
DR   InterPro; IPR015340; A_amylase_DUF1966_C.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF09260; DUF1966; 1.
DR   PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase;
KW   Metal-binding; Reference proteome; Signal.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    513       Alpha-amylase mde5.
FT                                /FTId=PRO_0000001357.
FT   REGION      229    230       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   ACT_SITE    226    226       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P56271}.
FT   ACT_SITE    250    250       Proton donor.
FT                                {ECO:0000250|UniProtKB:P56271}.
FT   METAL       143    143       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   METAL       182    182       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P56271}.
FT   METAL       195    195       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P56271}.
FT   METAL       226    226       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   METAL       230    230       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   METAL       250    250       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     105    105       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     144    144       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     224    224       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     254    254       Substrate; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     318    318       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     365    365       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   SITE        318    318       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   CARBOHYD    162    162       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    357    357       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     52     60       {ECO:0000250|UniProtKB:P56271}.
FT   DISULFID    171    184       {ECO:0000250|UniProtKB:P56271}.
FT   DISULFID    260    304       {ECO:0000250|UniProtKB:P56271}.
FT   DISULFID    454    488       {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
//
DBGET integrated database retrieval system