GUAA_HUMAN
ID GUAA_HUMAN Reviewed; 693 AA.
AC P49915; A8K639; B4DXV7; F8W720;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2 {ECO:0000269|PubMed:8089153};
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=GMPS;
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), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8089153; DOI=10.1016/s0021-9258(17)31590-9;
RA Hirst M., Haliday E., Nakamura J., Lou L.;
RT "Human GMP synthetase. Protein purification, cloning, and functional
RT expression of cDNA.";
RL J. Biol. Chem. 269:23830-23837(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
RX PubMed=11110714;
RA Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D.,
RA Rappaport E.F., Felix C.A.;
RT "t(3;11) translocation in treatment-related acute myeloid leukemia fuses
RT MLL with the GMPS (guanosine 5-prime monophosphate synthetase) gene.";
RL Blood 96:4360-4362(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318 AND SER-332, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-332, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15] {ECO:0007744|PDB:2VXO}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-693 IN COMPLEX WITH XMP,
RP SUBSTRATE-BINDING SITES, ACTIVE SITE, AND SUBUNIT.
RX PubMed=23816837; DOI=10.1016/j.jmb.2013.06.032;
RA Welin M., Lehtio L., Johansson A., Flodin S., Nyman T., Tresaugues L.,
RA Hammarstrom M., Graslund S., Nordlund P.;
RT "Substrate specificity and oligomerization of human GMP synthetase.";
RL J. Mol. Biol. 425:4323-4333(2013).
CC -!- FUNCTION: Catalyzes the conversion of xanthine monophosphate (XMP) to
CC GMP in the presence of glutamine and ATP through an adenyl-XMP
CC intermediate. {ECO:0000269|PubMed:8089153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC Evidence={ECO:0000269|PubMed:8089153};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11681;
CC Evidence={ECO:0000305|PubMed:8089153};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q4V7C6};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23816837}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8089153}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49915-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49915-2; Sequence=VSP_053933;
CC -!- DISEASE: Note=A chromosomal aberration involving GMPS is found in acute
CC myeloid leukemias. Translocation t(3,11)(q25,q23) with KMT2A/MLL1.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GMPSID229.html";
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DR EMBL; U10860; AAA60331.1; -; mRNA.
DR EMBL; AK291504; BAF84193.1; -; mRNA.
DR EMBL; AK302148; BAG63519.1; -; mRNA.
DR EMBL; AK315832; BAF98723.1; -; mRNA.
DR EMBL; AC067721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78741.1; -; Genomic_DNA.
DR EMBL; BC012178; AAH12178.1; -; mRNA.
DR CCDS; CCDS46941.1; -. [P49915-1]
DR PIR; A54847; A54847.
DR RefSeq; NP_003866.1; NM_003875.2. [P49915-1]
DR PDB; 2VPI; X-ray; 2.40 A; A/B=25-219.
DR PDB; 2VXO; X-ray; 2.50 A; A/B=20-693.
DR PDBsum; 2VPI; -.
DR PDBsum; 2VXO; -.
DR AlphaFoldDB; P49915; -.
DR SMR; P49915; -.
DR BioGRID; 114360; 122.
DR IntAct; P49915; 34.
DR MINT; P49915; -.
DR STRING; 9606.ENSP00000419851; -.
DR BindingDB; P49915; -.
DR ChEMBL; CHEMBL5721; -.
DR DrugBank; DB00993; Azathioprine.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00130; L-Glutamine.
DR MEROPS; C26.950; -.
DR GlyGen; P49915; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49915; -.
DR MetOSite; P49915; -.
DR PhosphoSitePlus; P49915; -.
DR SwissPalm; P49915; -.
DR BioMuta; GMPS; -.
DR DMDM; 1708072; -.
DR REPRODUCTION-2DPAGE; IPI00029079; -.
DR EPD; P49915; -.
DR jPOST; P49915; -.
DR MassIVE; P49915; -.
DR MaxQB; P49915; -.
DR PaxDb; P49915; -.
DR PeptideAtlas; P49915; -.
DR PRIDE; P49915; -.
DR ProteomicsDB; 29873; -.
DR ProteomicsDB; 56180; -. [P49915-1]
DR Antibodypedia; 33632; 262 antibodies from 33 providers.
DR DNASU; 8833; -.
DR Ensembl; ENST00000295920.7; ENSP00000295920.7; ENSG00000163655.16. [P49915-2]
DR Ensembl; ENST00000496455.7; ENSP00000419851.1; ENSG00000163655.16. [P49915-1]
DR GeneID; 8833; -.
DR KEGG; hsa:8833; -.
DR MANE-Select; ENST00000496455.7; ENSP00000419851.1; NM_003875.3; NP_003866.1.
DR UCSC; uc003faq.4; human. [P49915-1]
DR CTD; 8833; -.
DR DisGeNET; 8833; -.
DR GeneCards; GMPS; -.
DR HGNC; HGNC:4378; GMPS.
DR HPA; ENSG00000163655; Tissue enhanced (testis).
DR MIM; 600358; gene.
DR neXtProt; NX_P49915; -.
DR OpenTargets; ENSG00000163655; -.
DR PharmGKB; PA28763; -.
DR VEuPathDB; HostDB:ENSG00000163655; -.
DR eggNOG; KOG1622; Eukaryota.
DR GeneTree; ENSGT00390000006591; -.
DR HOGENOM; CLU_014340_0_2_1; -.
DR InParanoid; P49915; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 392369at2759; -.
DR PhylomeDB; P49915; -.
DR TreeFam; TF106132; -.
DR BRENDA; 6.3.5.2; 2681.
DR PathwayCommons; P49915; -.
DR Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR SignaLink; P49915; -.
DR SIGNOR; P49915; -.
DR UniPathway; UPA00189; UER00296.
DR BioGRID-ORCS; 8833; 585 hits in 1076 CRISPR screens.
DR ChiTaRS; GMPS; human.
DR EvolutionaryTrace; P49915; -.
DR GeneWiki; GMP_synthase; -.
DR GenomeRNAi; 8833; -.
DR Pharos; P49915; Tbio.
DR PRO; PR:P49915; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P49915; protein.
DR Bgee; ENSG00000163655; Expressed in left testis and 166 other tissues.
DR ExpressionAtlas; P49915; baseline and differential.
DR Genevisible; P49915; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IDA:UniProtKB.
DR GO; GO:0003921; F:GMP synthase activity; IDA:MGI.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IDA:MGI.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; TAS:ProtInc.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Chromosomal rearrangement; Cytoplasm; Direct protein sequencing;
KW Glutamine amidotransferase; GMP biosynthesis; Ligase; Nucleotide-binding;
KW Phosphoprotein; Proto-oncogene; Purine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..693
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140257"
FT DOMAIN 27..216
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 217..435
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT ACT_SITE 104
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605,
FT ECO:0000269|PubMed:23816837"
FT ACT_SITE 190
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605,
FT ECO:0000269|PubMed:23816837"
FT ACT_SITE 192
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605,
FT ECO:0000269|PubMed:23816837"
FT BINDING 244..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886"
FT BINDING 337
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000269|PubMed:23816837"
FT BINDING 522
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000269|PubMed:23816837"
FT BINDING 610
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000269|PubMed:23816837"
FT BINDING 685
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000269|PubMed:23816837"
FT BINDING 691
FT /ligand="XMP"
FT /ligand_id="ChEBI:CHEBI:57464"
FT /evidence="ECO:0000269|PubMed:23816837"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 10..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053933"
FT CONFLICT 261
FT /note="N -> D (in Ref. 2; BAG63519)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="H -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2VPI"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2VPI"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2VPI"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2VPI"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2VPI"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2VPI"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:2VPI"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2VPI"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:2VPI"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:2VPI"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 333..354
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 416..425
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 442..446
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 459..470
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 492..504
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 507..520
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 523..536
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 540..553
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 557..563
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 582..601
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 613..617
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 643..649
FT /evidence="ECO:0007829|PDB:2VXO"
FT TURN 654..656
FT /evidence="ECO:0007829|PDB:2VXO"
FT HELIX 659..671
FT /evidence="ECO:0007829|PDB:2VXO"
FT STRAND 675..681
FT /evidence="ECO:0007829|PDB:2VXO"
SQ SEQUENCE 693 AA; 76715 MW; 1CDA0DD3B244728D CRC64;
MALCNGDSKL ENAGGDLKDG HHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPV LGICYGMQMM NKVFGGTVHK
KSVREDGVFN ISVDNTCSLF RGLQKEEVVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE
SKKLYGAQFH PEVGLTENGK VILKNFLYDI AGCSGTFTVQ NRELECIREI KERVGTSKVL
VLLSGGVDST VCTALLNRAL NQEQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMNLKPE
EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR
ILGRELGLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH
TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW
ESLIFLARLI PRMCHNVNRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP ATPGNEIPVE
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
