ID KGUA_HUMAN Reviewed; 197 AA. AC Q16774; B1ANH1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 187. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8 {ECO:0000269|PubMed:31201273}; DE AltName: Full=GMP kinase; DE AltName: Full=Guanylate kinase 1 {ECO:0000312|HGNC:HGNC:4693}; GN Name=GUK1 {ECO:0000303|PubMed:8647247, ECO:0000312|HGNC:HGNC:4693}; GN Synonyms=GMK, GMPK {ECO:0000303|PubMed:31201273}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Retina; RX PubMed=8647247; DOI=10.1016/0014-5793(96)00365-1; RA Fitzgibbon J., Katsanis N., Wells D., Delhanty J., Vallins W., Hunt D.M.; RT "Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal RT localisation."; RL FEBS Lett. 385:185-188(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=8663313; DOI=10.1074/jbc.271.28.16734; RA Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.; RT "Cloning, characterization, and modeling of mouse and human guanylate RT kinases."; RL J. Biol. Chem. 271:16734-16740(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Ovary; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION AS DRUG-METABOLIZING ENZYME. RX PubMed=197968; DOI=10.1016/0006-2952(77)90071-5; RA Miller R.L., Adamczyk D.L., Spector T.; RT "Reassessment of the interactions of guanylate kinase and 6-thioguanosine RT 5'-phosphate."; RL Biochem. Pharmacol. 26:1573-1576(1977). RN [8] RP FUNCTION AS DRUG-METABOLIZING ENZYME. RX PubMed=6248551; DOI=10.1016/s0021-9258(20)79686-9; RA Miller W.H., Miller R.L.; RT "Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP RT kinase."; RL J. Biol. Chem. 255:7204-7207(1980). RN [9] RP FUNCTION AS DRUG-METABOLIZING ENZYME. RX PubMed=6306664; DOI=10.1073/pnas.80.13.4139; RA Field A.K., Davies M.E., DeWitt C., Perry H.C., Liou R., Germershausen J., RA Karkas J.D., Ashton W.T., Johnston D.B., Tolman R.L.; RT "9-([2-hydroxy-1-(hydroxymethyl)ethoxy]methyl)guanine: a selective RT inhibitor of herpes group virus replication."; RL Proc. Natl. Acad. Sci. U.S.A. 80:4139-4143(1983). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP INTERACTION WITH RD3. 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). RN [15] RP STRUCTURE BY NMR, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF RP SER-2; GLY-3; LEU-25; VAL-91; ARG-96; ARG-116; SER-121 AND SER-186, AND RP SUBUNIT. RX PubMed=31201273; DOI=10.1074/jbc.ra119.009251; RA Khan N., Shah P.P., Ban D., Trigo-Mourino P., Carneiro M.G., DeLeeuw L., RA Dean W.L., Trent J.O., Beverly L.J., Konrad M., Lee D., Sabo T.M.; RT "Solution structure and functional investigation of human guanylate kinase RT reveals allosteric networking and a crucial role for the enzyme in RT cancer."; RL J. Biol. Chem. 294:11920-11933(2019). CC -!- FUNCTION: Catalyzes the phosphorylation of GMP to GDP. Essential enzyme CC for recycling GMP and indirectly, cyclic GMP (cGMP) (PubMed:31201273). CC Involved in the cGMP metabolism in photoreceptors (By similarity). It CC may also have a role in the survival and growth progression of some CC tumors (PubMed:31201273). In addition to its physiological role, GUK1 CC is essential for convert prodrugs used for the treatment of cancers and CC viral infections into their pharmacologically active metabolites, most CC notably acyclovir, ganciclovir, and 6-thioguanine and its closely CC related analog 6-mercaptopurine (PubMed:197968, PubMed:6248551, CC PubMed:6306664). {ECO:0000250|UniProtKB:P46195, CC ECO:0000269|PubMed:197968, ECO:0000269|PubMed:31201273, CC ECO:0000269|PubMed:6248551, ECO:0000269|PubMed:6306664}. 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:31201273}; CC -!- ACTIVITY REGULATION: Up-regulated by RD3. CC {ECO:0000250|UniProtKB:P46195}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=20.7 uM for GMP {ECO:0000269|PubMed:31201273}; CC Note=kcat is 58.5 sec(-1) with GMP as substrate. CC {ECO:0000269|PubMed:31201273}; CC -!- SUBUNIT: Monomer (PubMed:31201273). Interacts with RD3 CC (PubMed:29515371). {ECO:0000269|PubMed:29515371, CC ECO:0000269|PubMed:31201273}. 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q16774-1; Sequence=Displayed; CC Name=2; CC IsoId=Q16774-2; Sequence=VSP_043778; CC Name=3; CC IsoId=Q16774-3; Sequence=VSP_043778, VSP_047372; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8663313}. CC -!- SIMILARITY: Belongs to the guanylate kinase 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; L76200; AAC37598.1; -; mRNA. DR EMBL; U66895; AAC50659.1; -; mRNA. DR EMBL; AK303845; BAG64788.1; -; mRNA. DR EMBL; AL359510; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471098; EAW69856.1; -; Genomic_DNA. DR EMBL; BC006249; AAH06249.1; -; mRNA. DR EMBL; BC009914; AAH09914.1; -; mRNA. DR CCDS; CCDS1568.1; -. [Q16774-1] DR CCDS; CCDS53481.1; -. [Q16774-2] DR CCDS; CCDS55689.1; -. [Q16774-3] DR PIR; S68864; S68864. DR RefSeq; NP_000849.1; NM_000858.5. [Q16774-1] DR RefSeq; NP_001152862.1; NM_001159390.1. [Q16774-2] DR RefSeq; NP_001152863.1; NM_001159391.1. [Q16774-1] DR RefSeq; NP_001229768.1; NM_001242839.1. [Q16774-1] DR RefSeq; NP_001229769.1; NM_001242840.1. [Q16774-3] DR PDB; 6NUI; NMR; -; A=1-197. DR PDBsum; 6NUI; -. DR AlphaFoldDB; Q16774; -. DR SMR; Q16774; -. DR BioGRID; 109242; 55. DR IntAct; Q16774; 9. DR STRING; 9606.ENSP00000355689; -. DR ChEMBL; CHEMBL4989; -. DR DrugBank; DB00787; Acyclovir. DR DrugBank; DB01972; Guanosine-5'-Monophosphate. DR DrugBank; DB00577; Valaciclovir. DR iPTMnet; Q16774; -. DR MetOSite; Q16774; -. DR PhosphoSitePlus; Q16774; -. DR BioMuta; GUK1; -. DR DMDM; 2497498; -. DR EPD; Q16774; -. DR jPOST; Q16774; -. DR MassIVE; Q16774; -. DR MaxQB; Q16774; -. DR PaxDb; 9606-ENSP00000355689; -. DR PeptideAtlas; Q16774; -. DR ProteomicsDB; 3255; -. DR ProteomicsDB; 61062; -. [Q16774-1] DR ProteomicsDB; 61063; -. [Q16774-2] DR Pumba; Q16774; -. DR Antibodypedia; 34661; 280 antibodies from 23 providers. DR DNASU; 2987; -. DR Ensembl; ENST00000366728.6; ENSP00000355689.2; ENSG00000143774.18. [Q16774-3] DR Ensembl; ENST00000366730.5; ENSP00000355691.1; ENSG00000143774.18. [Q16774-1] DR Ensembl; ENST00000453943.6; ENSP00000401832.2; ENSG00000143774.18. [Q16774-2] DR GeneID; 2987; -. DR KEGG; hsa:2987; -. DR MANE-Select; ENST00000453943.6; ENSP00000401832.2; NM_001159390.2; NP_001152862.1. [Q16774-2] DR UCSC; uc001hsi.4; human. [Q16774-1] DR AGR; HGNC:4693; -. DR CTD; 2987; -. DR DisGeNET; 2987; -. DR GeneCards; GUK1; -. DR HGNC; HGNC:4693; GUK1. DR HPA; ENSG00000143774; Tissue enhanced (brain). DR MIM; 139270; gene. DR neXtProt; NX_Q16774; -. DR OpenTargets; ENSG00000143774; -. DR PharmGKB; PA29072; -. DR VEuPathDB; HostDB:ENSG00000143774; -. DR eggNOG; KOG0707; Eukaryota. DR GeneTree; ENSGT00940000155815; -. DR HOGENOM; CLU_001715_0_2_1; -. DR InParanoid; Q16774; -. DR OMA; EWAVVHG; -. DR OrthoDB; 324675at2759; -. DR PhylomeDB; Q16774; -. DR TreeFam; TF314473; -. DR BioCyc; MetaCyc:HS07104-MONOMER; -. DR BRENDA; 2.7.4.8; 2681. DR PathwayCommons; Q16774; -. DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates. DR Reactome; R-HSA-9748787; Azathioprine ADME. DR SABIO-RK; Q16774; -. DR SignaLink; Q16774; -. DR BioGRID-ORCS; 2987; 758 hits in 1135 CRISPR screens. DR ChiTaRS; GUK1; human. DR GeneWiki; GUK1; -. DR GenomeRNAi; 2987; -. DR Pharos; Q16774; Tbio. DR PRO; PR:Q16774; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q16774; Protein. DR Bgee; ENSG00000143774; Expressed in right frontal lobe and 212 other cell types or tissues. DR ExpressionAtlas; Q16774; baseline and differential. 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; IDA:UniProtKB. DR GO; GO:0006185; P:dGDP biosynthetic process; IMP:UniProtKB. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006163; P:purine nucleotide metabolic process; IDA:UniProtKB. DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB. DR CDD; cd00071; GMPK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03263; guanyl_kin; 1. DR PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1. DR PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR Genevisible; Q16774; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Kinase; Nucleotide-binding; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..197 FT /note="Guanylate kinase" FT /id="PRO_0000170651" 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 137 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330" FT VAR_SEQ 1 FT /note="M -> MLRRPLAGLAAAALGRAPPDGM (in isoform 2 and FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043778" FT VAR_SEQ 159..197 FT /note="SKEPGLFDVVIINDSLDQAYAELKEALSEEIKKAQRTGA -> RNQESSKDR FT RLRLAVCSRHPGPIQDQGSSIEPPPWQAIRQLCALGQHVEWRRCCPCGWNILG (in FT isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_047372" FT MUTAGEN 2 FT /note="S->L: Increases in kcat with GMP as substrate." FT /evidence="ECO:0000269|PubMed:31201273" FT MUTAGEN 3 FT /note="G->A: Increases in kcat with GMP as substrate." FT /evidence="ECO:0000269|PubMed:31201273" FT MUTAGEN 25 FT /note="L->P: Leads to aggregation. Increases in kcat with FT GMP as substrate." FT /evidence="ECO:0000269|PubMed:31201273" FT MUTAGEN 91 FT /note="V->M: Increases in kcat with GMP as substrate." FT /evidence="ECO:0000269|PubMed:31201273" FT MUTAGEN 96 FT /note="R->H: Increases in kcat with GMP as substrate." FT /evidence="ECO:0000269|PubMed:31201273" FT MUTAGEN 116 FT /note="R->Q: Increases in kcat with GMP as substrate." FT /evidence="ECO:0000269|PubMed:31201273" FT MUTAGEN 121 FT /note="S->F: Increases in kcat with GMP as substrate." FT /evidence="ECO:0000269|PubMed:31201273" FT MUTAGEN 186 FT /note="S->Y: Increases in kcat with GMP as substrate." FT /evidence="ECO:0000269|PubMed:31201273" FT STRAND 7..10 FT /evidence="ECO:0007829|PDB:6NUI" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 17..27 FT /evidence="ECO:0007829|PDB:6NUI" FT TURN 28..31 FT /evidence="ECO:0007829|PDB:6NUI" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:6NUI" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:6NUI" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 58..67 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 69..72 FT /evidence="ECO:0007829|PDB:6NUI" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:6NUI" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 85..93 FT /evidence="ECO:0007829|PDB:6NUI" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 104..110 FT /evidence="ECO:0007829|PDB:6NUI" FT TURN 111..114 FT /evidence="ECO:0007829|PDB:6NUI" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 127..135 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 142..158 FT /evidence="ECO:0007829|PDB:6NUI" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:6NUI" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 174..184 FT /evidence="ECO:0007829|PDB:6NUI" FT HELIX 186..193 FT /evidence="ECO:0007829|PDB:6NUI" SQ SEQUENCE 197 AA; 21726 MW; C49573212A0DA825 CRC64; MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL DVDLQGVRNI KATDLRPIYI SVQPPSLHVL EQRLRQRNTE TEESLVKRLA AAQADMESSK EPGLFDVVII NDSLDQAYAE LKEALSEEIK KAQRTGA //