ID   KGUA_PIG                Reviewed;         198 AA.
AC   P31006;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8 {ECO:0000269|PubMed:29515371};
DE   AltName: Full=GMP kinase;
GN   Name=GUK1; Synonyms=GUK;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-198, ACETYLATION AT GLY-2, AND SUBUNIT.
RC   TISSUE=Brain;
RX   PubMed=8097461; DOI=10.1111/j.1432-1033.1993.tb17757.x;
RA   Zschocke P.D., Schiltz E., Schulz G.E.;
RT   "Purification and sequence determination of guanylate kinase from pig
RT   brain.";
RL   Eur. J. Biochem. 213:263-269(1993).
RN   [2]
RP   FUNCTION, INTERACTION WITH RD3, CATALYTIC ACTIVITY, AND ACTIVITY
RP   REGULATION.
RX   PubMed=29515371; DOI=10.3389/fnmol.2018.00052;
RA   Wimberg H., Janssen-Bienhold U., Koch K.W.;
RT   "Control of the Nucleotide Cycle in Photoreceptor Cell Extracts by Retinal
RT   Degeneration Protein 3.";
RL   Front. Mol. Neurosci. 11:52-52(2018).
CC   -!- FUNCTION: Catalyzes the phosphorylation of GMP to GDP. Essential enzyme
CC       for recycling GMP and indirectly, cyclic GMP (cGMP). Involved in the
CC       cGMP metabolism in photoreceptors. {ECO:0000269|PubMed:29515371}.
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         Evidence={ECO:0000269|PubMed:29515371};
CC   -!- ACTIVITY REGULATION: Up-regulated by RD3.
CC       {ECO:0000269|PubMed:29515371}.
CC   -!- SUBUNIT: Monomer (PubMed:8097461). Interacts with RD3 (By similarity).
CC       {ECO:0000250|UniProtKB:Q16774, ECO:0000269|PubMed:8097461}.
CC   -!- SUBCELLULAR LOCATION: Photoreceptor inner segment
CC       {ECO:0000250|UniProtKB:Q64520}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q64520}. Note=Colocalizes with RD3 in
CC       photoreceptor inner segments and to a lesser extent in the outer
CC       plexiform layer. {ECO:0000250|UniProtKB:Q64520}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR   PIR; S23776; KIPGGU.
DR   AlphaFoldDB; P31006; -.
DR   SMR; P31006; -.
DR   STRING; 9823.ENSSSCP00000014875; -.
DR   iPTMnet; P31006; -.
DR   PaxDb; P31006; -.
DR   PeptideAtlas; P31006; -.
DR   PRIDE; P31006; -.
DR   eggNOG; KOG0707; Eukaryota.
DR   InParanoid; P31006; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004385; F:guanylate kinase activity; ISS:UniProtKB.
DR   GO; GO:0050145; F:nucleoside monophosphate kinase activity; EXP:Reactome.
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   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8097461"
FT   CHAIN           2..198
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170653"
FT   DOMAIN          4..186
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   BINDING         37..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   BINDING         171..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:8097461"
SQ   SEQUENCE   198 AA;  21921 MW;  09E9CC7130CCE1A7 CRC64;
     MGSPRPVVLS GPSGAGKSTL LKKLLQEHSS IFGFSVSHTT RDPRPGEENG KDYYFVTREV
     MQRDIAAGDF IEHAEFSGNL YGTSKAAVRA VQAMNRICVL DVDLQGVRNI KKTDLQPIYI
     FVQPPSLDVL EQRLRQRNTE TEESLAKRLA AAKADMESSK EPGLFDLIII NDSLDKAYWA
     LKEALSEEIK KAQATGHS