CPSM_RAT
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 03-AUG-2022, entry version 185.
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}.
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}.
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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 GlyGen; P07756; 3 sites.
DR iPTMnet; P07756; -.
DR PhosphoSitePlus; P07756; -.
DR SwissPalm; P07756; -.
DR jPOST; P07756; -.
DR PaxDb; P07756; -.
DR PRIDE; P07756; -.
DR Ensembl; ENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704.
DR GeneID; 497840; -.
DR KEGG; rno:497840; -.
DR UCSC; RGD:2395; rat.
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; IEPAGIH; -.
DR OrthoDB; 273358at2759; -.
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 tissues.
DR Genevisible; P07756; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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: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:0072341; F:modified amino acid binding; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0055081; P:anion homeostasis; IDA:RGD.
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:0046209; P:nitric oxide metabolic process; ISO:RGD.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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 Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 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 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 SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
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.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; ATP-binding; Glycoprotein; Ligase;
KW Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW 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
