ID CPSM_RAT Reviewed; 1500 AA. AC P07756; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 27-MAR-2024, entry version 193. DE RecName: Full=Carbamoyl-phosphate synthase [ammonia], mitochondrial; DE EC=6.3.4.16; DE AltName: Full=Carbamoyl-phosphate synthetase I; DE Short=CPSase I; DE Flags: Precursor; GN Name=Cps1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=2991241; DOI=10.1016/s0021-9258(17)39371-7; RA Nyunoya H., Broglie K.E., Widgren E.E., Lusty C.J.; RT "Characterization and derivation of the gene coding for mitochondrial RT carbamyl phosphate synthetase I of rat."; RL J. Biol. Chem. 260:9346-9356(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. RX PubMed=3038878; DOI=10.1016/s0021-9258(18)60973-1; RA Lagace M., Howell B.W., Burak R., Lusty C.J., Shore G.C.; RT "Rat carbamyl-phosphate synthetase I gene. Promoter sequence and tissue- RT specific transcriptional regulation in vitro."; RL J. Biol. Chem. 262:10415-10418(1987). RN [3] RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, ALLOSTERIC ACTIVATOR NAG BINDING RP SITE, KINETIC PARAMETERS, AND MUTAGENESIS OF THR-1391; THR-1394; TRP-1410; RP ASN-1437 AND ASN-1440. RX PubMed=19754428; DOI=10.1042/bj20090888; RA Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E., RA Yefimenko I., Rubio V., Cervera J.; RT "Structural insight on the control of urea synthesis: identification of the RT binding site for N-acetyl-L-glutamate, the essential allosteric activator RT of mitochondrial carbamoyl phosphate synthetase."; RL Biochem. J. 424:211-220(2009). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-189; SER-537; RP SER-540; SER-896; SER-898; SER-1036; SER-1090; SER-1093 AND SER-1431, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [5] RP PROTEOLYTIC CLEAVAGE. RX PubMed=23649895; DOI=10.1002/humu.22349; RA Diez-Fernandez C., Martinez A.I., Pekkala S., Barcelona B., RA Perez-Arellano I., Guadalajara A.M., Summar M., Cervera J., Rubio V.; RT "Molecular characterization of carbamoyl-phosphate synthetase (CPS1) RT deficiency using human recombinant CPS1 as a key tool."; RL Hum. Mutat. 34:1149-1159(2013). RN [6] RP GLYCOSYLATION AT SER-537; SER-1331 AND THR-1332. RX PubMed=24098488; DOI=10.1371/journal.pone.0076399; RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.; RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver RT mitochondria by combination of mass spectrometry and immunological RT methods."; RL PLoS ONE 8:E76399-E76399(2013). CC -!- FUNCTION: Involved in the urea cycle of ureotelic animals where the CC enzyme plays an important role in removing excess ammonia from the CC cell. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, CC ChEBI:CHEBI:456216; EC=6.3.4.16; CC Evidence={ECO:0000269|PubMed:19754428}; CC -!- ACTIVITY REGULATION: Requires N-acetyl-L-glutamate (NAG) as an CC allosteric activator. N-acetyl-L-beta-phenylglutamate (Phe-NAG) can CC also activate CPSase I, but with an activation constant that is 2-fold CC higher than that for NAG. {ECO:0000269|PubMed:19754428}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.06 mM for ATP {ECO:0000269|PubMed:19754428}; CC KM=6.43 mM for HCO(3)(-) {ECO:0000269|PubMed:19754428}; CC KM=1.07 mM for NH(4)(+) {ECO:0000269|PubMed:19754428}; CC Note=The activation constant Ka of N-acetyl-L-glutamate for the CC reaction is 0.11 mM.; CC -!- SUBUNIT: Can form homooligomers (monomers as predominant form and CC dimers). {ECO:0000250|UniProtKB:P31327}. CC -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P31327}. Cell membrane CC {ECO:0000250|UniProtKB:Q8C196}; Peripheral membrane protein CC {ECO:0000305}; Extracellular side {ECO:0000250|UniProtKB:Q8C196}. CC Note=Localizes to the cell surface of hepatocytes. CC {ECO:0000250|UniProtKB:Q8C196}. CC -!- TISSUE SPECIFICITY: Primarily in the liver and small intestine. CC -!- DOMAIN: The type-1 glutamine amidotransferase domain is defective. CC -!- PTM: 50% of the mature protein that was isolated had Leu-39 as its N- CC terminal residue and 50% had Ser-40 suggesting two adjacent processing CC sites. However, the possibility of proteolytic removal of Leu-39 during CC the isolation of the enzyme cannot be excluded. Undergoes proteolytic CC cleavage in the C-terminal region corresponding to the loss of CC approximately 12 AA residues from the C-terminus (PubMed:23649895). CC {ECO:0000269|PubMed:23649895}. CC -!- PTM: Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-1291 CC by SIRT5, leading to activation (By similarity). CC {ECO:0000250|UniProtKB:Q8C196}. CC -!- PTM: Glutarylated. Glutarylation levels increase during fasting. CC Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-892, CC Lys-915, Lys-1360 and Lys-1486, leading to activation. CC {ECO:0000250|UniProtKB:P31327}. 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; M12335; AAB59717.1; -; Genomic_DNA. DR EMBL; M11710; AAB59717.1; JOINED; mRNA. DR EMBL; M12318; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12319; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12320; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12321; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12322; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12323; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12324; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12325; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12326; AAB59717.1; JOINED; mRNA. DR EMBL; M12327; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; M12328; AAB59717.1; JOINED; Genomic_DNA. DR EMBL; J02805; AAA40959.1; -; Genomic_DNA. DR PIR; A28481; SYRTCA. DR RefSeq; NP_058768.1; NM_017072.2. DR RefSeq; XP_017452081.1; XM_017596592.1. DR AlphaFoldDB; P07756; -. DR SMR; P07756; -. DR IntAct; P07756; 1. DR STRING; 10116.ENSRNOP00000019021; -. DR CarbonylDB; P07756; -. DR GlyCosmos; P07756; 3 sites, No reported glycans. DR GlyGen; P07756; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P07756; -. DR PhosphoSitePlus; P07756; -. DR SwissPalm; P07756; -. DR jPOST; P07756; -. DR PaxDb; 10116-ENSRNOP00000019021; -. DR Ensembl; ENSRNOT00000019023.6; ENSRNOP00000019021.4; ENSRNOG00000013704.6. DR Ensembl; ENSRNOT00055017561; ENSRNOP00055014140; ENSRNOG00055010377. DR Ensembl; ENSRNOT00060033638; ENSRNOP00060027534; ENSRNOG00060019455. DR Ensembl; ENSRNOT00065050086; ENSRNOP00065041155; ENSRNOG00065028982. DR GeneID; 497840; -. DR KEGG; rno:497840; -. DR UCSC; RGD:2395; rat. DR AGR; RGD:2395; -. DR CTD; 1373; -. DR RGD; 2395; Cps1. DR eggNOG; KOG0370; Eukaryota. DR GeneTree; ENSGT00940000157192; -. DR HOGENOM; CLU_000513_0_2_1; -. DR InParanoid; P07756; -. DR OMA; FPFNKFP; -. DR OrthoDB; 309at2759; -. DR PhylomeDB; P07756; -. DR Reactome; R-RNO-70635; Urea cycle. DR SABIO-RK; P07756; -. DR PRO; PR:P07756; -. DR Proteomes; UP000002494; Chromosome 9. DR Bgee; ENSRNOG00000013704; Expressed in liver and 16 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD. DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD. DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0005524; F:ATP binding; IDA:RGD. DR GO; GO:0005509; F:calcium ion binding; IPI:RGD. DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IDA:RGD. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0004175; F:endopeptidase activity; IDA:RGD. DR GO; GO:0016595; F:glutamate binding; IPI:RGD. DR GO; GO:0046872; F:metal ion binding; ISO:RGD. DR GO; GO:0072341; F:modified amino acid binding; ISO:RGD. DR GO; GO:0005543; F:phospholipid binding; IDA:RGD. DR GO; GO:0030955; F:potassium ion binding; ISO:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD. DR GO; GO:0036094; F:small molecule binding; ISO:RGD. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; ISO:RGD. DR GO; GO:0071242; P:cellular response to ammonium ion; ISO:RGD. DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD. DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEP:RGD. DR GO; GO:0071400; P:cellular response to oleic acid; IEP:RGD. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD. DR GO; GO:0050667; P:homocysteine metabolic process; ISO:RGD. DR GO; GO:0001889; P:liver development; IEP:RGD. DR GO; GO:0007494; P:midgut development; IEP:RGD. DR GO; GO:0055081; P:monoatomic anion homeostasis; IDA:RGD. DR GO; GO:0046209; P:nitric oxide metabolic process; ISO:RGD. DR GO; GO:0014075; P:response to amine; IEP:RGD. DR GO; GO:0043200; P:response to amino acid; IEP:RGD. DR GO; GO:0051591; P:response to cAMP; IEP:RGD. DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD. DR GO; GO:0032094; P:response to food; IEP:RGD. DR GO; GO:0033762; P:response to glucagon; IEP:RGD. DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD. DR GO; GO:0060416; P:response to growth hormone; IEP:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD. DR GO; GO:0034201; P:response to oleic acid; IEP:RGD. DR GO; GO:0042594; P:response to starvation; IEP:RGD. DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD. DR GO; GO:0009636; P:response to toxic substance; IEP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0010043; P:response to zinc ion; IEP:RGD. DR GO; GO:0019433; P:triglyceride catabolic process; ISO:RGD. DR GO; GO:0000050; P:urea cycle; IDA:RGD. DR GO; GO:0042311; P:vasodilation; ISO:RGD. DR CDD; cd01744; GATase1_CPSase; 1. DR CDD; cd01423; MGS_CPS_I_III; 1. DR Gene3D; 3.40.50.20; -; 2. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2. DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1. DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_01209; CPSase_S_chain; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR006275; CarbamoylP_synth_lsu. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf. DR InterPro; IPR006274; CarbamoylP_synth_ssu. DR InterPro; IPR002474; CarbamoylP_synth_ssu_N. DR InterPro; IPR036480; CarbP_synth_ssu_N_sf. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR035686; CPSase_GATase1. DR InterPro; IPR017926; GATASE. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR NCBIfam; TIGR01369; CPSaseII_lrg; 1. DR NCBIfam; TIGR01368; CPSaseIIsmall; 1. DR PANTHER; PTHR11405:SF57; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 1. DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF00988; CPSase_sm_chain; 1. DR Pfam; PF00117; GATase; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR PRINTS; PR00099; CPSGATASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM01097; CPSase_sm_chain; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1. DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 2. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 2. DR PROSITE; PS00867; CPSASE_2; 2. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51855; MGS; 1. DR Genevisible; P07756; RN. PE 1: Evidence at protein level; KW Acetylation; Allosteric enzyme; ATP-binding; Cell membrane; Glycoprotein; KW Ligase; Membrane; Mitochondrion; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transit peptide; Urea cycle. FT TRANSIT 1..38 FT /note="Mitochondrion" FT CHAIN 39..1500 FT /note="Carbamoyl-phosphate synthase [ammonia], FT mitochondrial" FT /id="PRO_0000029899" FT DOMAIN 219..404 FT /note="Glutamine amidotransferase type-1" FT DOMAIN 551..743 FT /note="ATP-grasp 1" FT DOMAIN 1093..1284 FT /note="ATP-grasp 2" FT DOMAIN 1355..1500 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" FT REGION 39..218 FT /note="Anthranilate phosphoribosyltransferase homolog" FT BINDING 1391 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT BINDING 1394 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT BINDING 1410 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT BINDING 1437 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT BINDING 1440 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT BINDING 1449 FT /ligand="N-acetyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:44337" FT /ligand_note="allosteric activator" FT MOD_RES 55 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 55 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 55 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 57 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 57 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 119 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 119 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 157 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 157 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 171 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 171 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 176 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 182 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 189 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 197 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 207 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 207 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 207 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 210 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 210 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 214 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 214 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 214 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 219 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 219 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 228 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 228 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 237 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 279 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 280 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 280 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 287 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 287 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 307 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 307 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 307 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 310 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 310 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 400 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 402 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 402 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 412 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 412 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 412 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 453 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 453 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 458 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 458 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 458 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 522 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 522 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 527 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 527 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 527 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 532 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 532 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 537 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 540 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 553 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 553 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 553 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 560 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 560 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 575 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 575 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 603 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 603 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 612 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 612 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 630 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 728 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 751 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 751 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 757 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 757 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 757 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 772 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 772 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 793 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 793 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 793 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 811 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 811 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 831 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 831 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 841 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 841 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 856 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 856 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 869 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 875 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 875 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 875 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 889 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 889 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 889 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 892 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 892 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 892 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 896 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 898 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 908 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 908 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 915 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 915 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 915 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 919 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 919 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 919 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 935 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1036 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1074 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1074 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1074 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1079 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1090 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1093 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1100 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1100 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1149 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1168 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1168 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1168 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1183 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1183 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1183 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1203 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1222 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1224 FT /note="N6-glutaryllysine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1232 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1232 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1269 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1269 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1291 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1291 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1356 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1356 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1356 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1360 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1360 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1431 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1444 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1444 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1471 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1471 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1479 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1479 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1479 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1486 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT MOD_RES 1486 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P31327" FT MOD_RES 1486 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8C196" FT CARBOHYD 537 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000269|PubMed:24098488" FT CARBOHYD 1331 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000269|PubMed:24098488" FT CARBOHYD 1332 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000269|PubMed:24098488" FT MUTAGEN 1391 FT /note="T->V: 400-fold increase in the activation constant FT of NAG. 3-fold decrease in the reaction rate at saturation FT of NAG." FT /evidence="ECO:0000269|PubMed:19754428" FT MUTAGEN 1394 FT /note="T->A: 900-fold increase in the activation constant FT of NAG. 3-fold decrease in the reaction rate at saturation FT of NAG." FT /evidence="ECO:0000269|PubMed:19754428" FT MUTAGEN 1410 FT /note="W->K: 60-fold increase in the activation constant of FT NAG." FT /evidence="ECO:0000269|PubMed:19754428" FT MUTAGEN 1437 FT /note="N->D: 70-fold increase in the activation constant of FT NAG." FT /evidence="ECO:0000269|PubMed:19754428" FT MUTAGEN 1440 FT /note="N->D: 110-fold increase in the activation constant FT of NAG. Modifies the specificity for the activator: Binds FT Phe-NAG considerably better than NAG." FT /evidence="ECO:0000269|PubMed:19754428" SQ SEQUENCE 1500 AA; 164580 MW; 038E8F893DE1C34D CRC64; MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSHDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML GKIEFEGQSV DFVDPNKQNL IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA EVHLVPWNHD FTQMDYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK GKGTTITSVL PKPALVASRV EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD AVYFLPITPQ FVTEVIKAER PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES IMATEDRQLF SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR KELSEPSSTR IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT EETLRQAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV STDFDECDKL YFEELSLERI LDIYHQEACN GCIISVGGQI PNNLAVPLYK NGVKIMGTSP LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN VVFSEDEMKR FLEEATRVSQ EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI IPSDYVAIKA PMFSWPRLRD ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN NNTKFVHDNY VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA //