YFMD_SCHPO
ID YFMD_SCHPO Reviewed; 592 AA.
AC Q9UTE1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable 6-phosphofructo-2-kinase C222.13c;
DE EC=2.7.1.105;
GN ORFNames=SPAC222.13c;
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).
CC -!- FUNCTION: Synthesis of fructose 2,6-bisphosphate. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB60705.1; -; Genomic_DNA.
DR PIR; T50154; T50154.
DR RefSeq; NP_593152.1; NM_001018549.2.
DR AlphaFoldDB; Q9UTE1; -.
DR SMR; Q9UTE1; -.
DR BioGRID; 278435; 8.
DR STRING; 4896.SPAC222.13c.1; -.
DR iPTMnet; Q9UTE1; -.
DR MaxQB; Q9UTE1; -.
DR PaxDb; Q9UTE1; -.
DR PRIDE; Q9UTE1; -.
DR EnsemblFungi; SPAC222.13c.1; SPAC222.13c.1:pep; SPAC222.13c.
DR GeneID; 2541948; -.
DR KEGG; spo:SPAC222.13c; -.
DR PomBase; SPAC222.13c; -.
DR VEuPathDB; FungiDB:SPAC222.13c; -.
DR eggNOG; KOG0234; Eukaryota.
DR HOGENOM; CLU_006383_3_1_1; -.
DR InParanoid; Q9UTE1; -.
DR OMA; CIESDRY; -.
DR PhylomeDB; Q9UTE1; -.
DR PRO; PR:Q9UTE1; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; ISO:PomBase.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
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 SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..592
FT /note="Probable 6-phosphofructo-2-kinase C222.13c"
FT /id="PRO_0000318496"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /evidence="ECO:0000255"
FT ACT_SITE 266
FT /evidence="ECO:0000255"
FT ACT_SITE 527
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 300
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250"
SQ SEQUENCE 592 AA; 68640 MW; F0E96E375D343963 CRC64;
MSNTGSARTE EFTKGTGYEA TKPNNDTDDD AKQNYPSKEP HMKLGDYTEE TSFVDDSIFK
REELTPDRNS PANDVEKMEV PKPTPQWMKL KDEGKLGKHR KNRLRRPGRF PVRQESTIDI
PGLTVSKRTE NDSNNASYGI REKLIIILVG IPATGKSYIG SKLSRYYNWL KYNCRFFSVG
DKRREEGAST YSMSADFFDI KNEETFKFRE NVALETLEDL LHWMIHENGV IGILDATNST
HERRKHLYDR ISKEADIGIM FLESLCTDDI LFEENIKLKI KGPDYEGYDT ESALKDLRER
VDLYKKYYEP LDERDEQLPF LQYVKVINVG IKVVTHNIEG FLAGQAVYFM LNLNIQKRQI
WLTRPGESLD TVAGRIGGDA SLTPIGKQYA QDLANFMDRQ RVLWQLRYTN DLASTNKRFS
LSEASSFNVW SSVRKRAIET IEFFNPDSYN VKKIRLLNDL NLGSREGLTL REFSEKYPDE
FDVIKRKDYA YRFSGQGGES YLDVIHRLQP LIVEIERSSG NILVVSHRIV SNILMTYFLN
YHPEDIIDVG LPLHTLFCIE SDRYGTTCMA YRYDAANRQF IKDPMFDLRK RT
