位置:首页 > 蛋白库 > YIVH_SCHPO
YIVH_SCHPO
ID   YIVH_SCHPO              Reviewed;         449 AA.
AC   Q9UTK9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Putative 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase C144.17c;
DE   Includes:
DE     RecName: Full=6-phosphofructo-2-kinase;
DE              EC=2.7.1.105;
DE   Includes:
DE     RecName: Full=Fructose-2,6-bisphosphatase;
DE              EC=3.1.3.46;
GN   ORFNames=SPAC144.17c;
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   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).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579,
CC         ChEBI:CHEBI:456216; EC=2.7.1.105;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC       mutase 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; CAB59697.2; -; Genomic_DNA.
DR   PIR; T37684; T37684.
DR   RefSeq; NP_594678.2; NM_001020107.3.
DR   AlphaFoldDB; Q9UTK9; -.
DR   SMR; Q9UTK9; -.
DR   BioGRID; 279338; 34.
DR   STRING; 4896.SPAC144.17c.1; -.
DR   iPTMnet; Q9UTK9; -.
DR   MaxQB; Q9UTK9; -.
DR   PaxDb; Q9UTK9; -.
DR   PRIDE; Q9UTK9; -.
DR   DNASU; 2542894; -.
DR   EnsemblFungi; SPAC144.17c.1; SPAC144.17c.1:pep; SPAC144.17c.
DR   GeneID; 2542894; -.
DR   KEGG; spo:SPAC144.17c; -.
DR   PomBase; SPAC144.17c; -.
DR   VEuPathDB; FungiDB:SPAC144.17c; -.
DR   eggNOG; KOG0234; Eukaryota.
DR   HOGENOM; CLU_006383_0_2_1; -.
DR   InParanoid; Q9UTK9; -.
DR   OMA; FIEFICT; -.
DR   PhylomeDB; Q9UTK9; -.
DR   Reactome; R-SPO-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR   PRO; PR:Q9UTK9; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; ISM:PomBase.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10606; PTHR10606; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Hydrolase; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..449
FT                   /note="Putative 6-phosphofructo-2-kinase/fructose-2,6-
FT                   bisphosphatase C144.17c"
FT                   /id="PRO_0000318493"
FT   REGION          261..410
FT                   /note="Fructose-2,6-bisphosphatase"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000255"
FT   BINDING         59..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         116
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         144
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         181..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         207
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /evidence="ECO:0000250|UniProtKB:Q16875"
FT   BINDING         359..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         404..408
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   BINDING         408
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /evidence="ECO:0000250|UniProtKB:P07953"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   449 AA;  52011 MW;  4E6ED9A4C0617349 CRC64;
     MSRRNSIAVE QAINPNMLRA ANRSSEALLD NEKFGGVQPY STESGMLFHA GKLVIIMSGL
     PARGKSNIAV SIDRYLRWLG FNCRFYSLAK YIDERTREMT SSPVKSAASE NHVFSRNDTI
     ERCLADLEIF LLKEKGQVAI YDATNGTRRT RRILYDRFKN CGFKILFIES LCNKEDVINA
     NIQEAIHVSE EFRNWDLEMA EKEYCRRIDI LKCHYETIDE KDYSFVKMIN FAETIIANKS
     NEGYLLSRIL FLLMNMTLAR KRIFLVPKAS MRPLKLREPE DDIENRQFSE YVADRIRKSF
     PDVSFKNLHV LSCMEDSVMS PFRELGSVTS SMSSLSPILM DSFGDDLQKL KETYGEEEYN
     LYLVDPYRYR VKRKESFYDL AVRLEPLILE LGREQRDVLL IGSKSIIRVF YGYYMNVPAK
     DIPQLCLSSS SIYELIESST GMTVNEYDL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024