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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   03-AUG-2022, entry version 148.
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}.
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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; 4896.SPAC25H1.09.1; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; O14154; -.
DR   PRIDE; O14154; -.
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; WIADITQ; -.
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; HDA: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   Gene3D; 2.60.40.1180; -; 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   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; 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
 
 
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