KGUA_SCHPO
ID KGUA_SCHPO Reviewed; 202 AA.
AC Q9P6I5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase;
GN ORFNames=SPBC1198.05;
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).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:456216; EC=2.7.4.8;
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR EMBL; CU329671; CAB91180.1; -; Genomic_DNA.
DR RefSeq; NP_595074.1; NM_001020980.2.
DR AlphaFoldDB; Q9P6I5; -.
DR SMR; Q9P6I5; -.
DR STRING; 4896.SPBC1198.05.1; -.
DR iPTMnet; Q9P6I5; -.
DR MaxQB; Q9P6I5; -.
DR PaxDb; Q9P6I5; -.
DR PRIDE; Q9P6I5; -.
DR EnsemblFungi; SPBC1198.05.1; SPBC1198.05.1:pep; SPBC1198.05.
DR GeneID; 2539674; -.
DR KEGG; spo:SPBC1198.05; -.
DR PomBase; SPBC1198.05; -.
DR VEuPathDB; FungiDB:SPBC1198.05; -.
DR eggNOG; KOG0707; Eukaryota.
DR HOGENOM; CLU_001715_0_1_1; -.
DR InParanoid; Q9P6I5; -.
DR OMA; EWAVVHG; -.
DR PhylomeDB; Q9P6I5; -.
DR Reactome; R-SPO-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-SPO-9748787; Azathioprine ADME.
DR PRO; PR:Q9P6I5; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004385; F:guanylate kinase activity; ISS:UniProtKB.
DR GO; GO:0046037; P:GMP metabolic process; IC:PomBase.
DR GO; GO:0006183; P:GTP biosynthetic process; IC:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006163; P:purine nucleotide metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR017665; Guanylate_kinase.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03263; guanyl_kin; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..202
FT /note="Guanylate kinase"
FT /id="PRO_0000170654"
FT DOMAIN 18..200
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
SQ SEQUENCE 202 AA; 22395 MW; 4A395B71FDCCAF92 CRC64;
MTPQLSSSVA SKLVTLKLKP VVVFGPSGVG KSTLLKRLLK DHGDKLGFSV SHTTRTPRAG
EKDGIDYHFV TKEEFQKLVA EEKFVEWAVF SGNMYGTSIM AIQELEAVNK KAILDIDLQG
VLQVKASPID AQYVFLAPPS IEQLEVRLRG RGTENESAIL QRLERARAEI EYSEKPGNFD
ALIVNDDVEK AYKQLEAICL SD