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Conserved domains on  [gi|157817440|ref|NP_001100523|]
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N-acetylglutamate synthase, mitochondrial [Rattus norvegicus]

Protein Classification

bifunctional acetylglutamate kinase/N-acetyl-gamma-glutamyl-phosphate reductase; amino acid kinase family protein( domain architecture ID 10223872)

bifunctional acetylglutamate kinase/N-acetyl-gamma-glutamyl-phosphate reductase contains an N-terminal N-Acetyl-L-glutamate kinase (NAGK) that catalyzes the phosphorylation of NAG, and a C-terminal reductase domain (ArgC) that catalyzes the third step or Arg biosynthesis from Glu| amino acid kinase (AAK) family protein catalyzes the phosphorylation of a variety of substrates including amino acids, using ATP as the source of the phosphoryl group

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAK super family cl00452
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 95-364 1.12e-153

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


The actual alignment was detected with superfamily member cd04236:

Pssm-ID: 444912 [Multi-domain]  Cd Length: 271  Bit Score: 439.66  E-value: 1.12e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  95 VQRDIQAFLNQCGASPGEARHWLTQFQTCYHSVDKPFAVVEVDEEVFGCPQAVSRLAFALAFLQRMDMKPLVVLGLPAPT 174
Cdd:cd04236    1 IYRDVKAFLHQKGGDPREARYWLTQFQIAMPNDWPAFAVLEVDHSVFRSLEMVQSLSFGLAFLQRMDMKLLVVMGLSAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 175 APSG-CLSFWEAKAQLAQSCKVLVNELRHNAATAVPFFGGGSVLSAAEPAPHASYGGIVAVETDLLQWCLESNSIPILCP 253
Cdd:cd04236   81 GTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTELLQWCLGSGHIPLVCP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 254 IGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNLPADLDLVTNAEWLSTKERQQIRLIVDVL 333
Cdd:cd04236  161 IGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWLSETEQNRIQDIATLL 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 157817440 334 SRLPHYSSAVITAASTLLTELFSNKGCGTLF 364
Cdd:cd04236  241 NALPSMSSAVITSAETLLTELFSHKGSGTLF 271
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 350-513 1.56e-64

NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region (pfam00696) in some fungal acetylglutamate kinase enzymes. it stabilizes the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain pfam00696.


:

Pssm-ID: 398437  Cd Length: 166  Bit Score: 207.11  E-value: 1.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  350 LLTELFSNKGCGTLFKNAERMLRVRSLDSL-DQGRLVNLVNASF-GKKLREDYLESLRPRLHSIYVSEGYNAAAILTVEp 427
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELiDIERLRNLIERSFdGRLSVADYLDRLKGRLFKIYVDEPYEALAIVTKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  428 vLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYEL 507
Cdd:pfam04768  81 -DGGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSEL 159


                  ....*.
gi 157817440  508 VNHAKG 513
Cdd:pfam04768 160 VASFRD 165
 
Name Accession Description Interval E-value
AAK_NAGS-Urea cd04236
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 95-364 1.12e-153

AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the urea cycle found in animals. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate; NAG is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Ureogenic NAGS activity is dependent on the concentration of glutamate (substrate) and arginine (activator). Domain architecture of ureogenic NAGS consists of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal DUF619 domain. Members of this CD belong to the protein superfamily, the Amino Acid Kinase Family (AAKF).


Pssm-ID: 239769 [Multi-domain]  Cd Length: 271  Bit Score: 439.66  E-value: 1.12e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  95 VQRDIQAFLNQCGASPGEARHWLTQFQTCYHSVDKPFAVVEVDEEVFGCPQAVSRLAFALAFLQRMDMKPLVVLGLPAPT 174
Cdd:cd04236    1 IYRDVKAFLHQKGGDPREARYWLTQFQIAMPNDWPAFAVLEVDHSVFRSLEMVQSLSFGLAFLQRMDMKLLVVMGLSAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 175 APSG-CLSFWEAKAQLAQSCKVLVNELRHNAATAVPFFGGGSVLSAAEPAPHASYGGIVAVETDLLQWCLESNSIPILCP 253
Cdd:cd04236   81 GTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTELLQWCLGSGHIPLVCP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 254 IGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNLPADLDLVTNAEWLSTKERQQIRLIVDVL 333
Cdd:cd04236  161 IGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWLSETEQNRIQDIATLL 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 157817440 334 SRLPHYSSAVITAASTLLTELFSNKGCGTLF 364
Cdd:cd04236  241 NALPSMSSAVITSAETLLTELFSHKGSGTLF 271
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 108-518 6.32e-92

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 286.56  E-value: 6.32e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 108 ASPGEARHWLTQFQtcyhSVD-KPFAVVEVDEEVFgcPQAVSRLAFALAFLQRMDMKPLVVLGlpapTAPSgclsfweAK 186
Cdd:PRK04531  18 ASAKEISQYLKRFS----QLDaERFAVIKVGGAVL--RDDLEALASSLSFLQEVGLTPIVVHG----AGPQ-------LD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 187 AQLAQSC--KVLVNELRHNAaTAVPFFGGGSVLSAaepaPHASYGGIVAVetdllqwcLESNSIPILCPIGETAARRSVL 264
Cdd:PRK04531  81 AELDAAGieKETVNGLRVTS-PEALAIVRKVFQRS----NLDLVEAVESS--------LRAGSIPVIASLGETPSGQILN 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 265 LDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNLPADLDLVTNAEWLSTKERQQIRLIVDVLSRLPHYSSAVI 344
Cdd:PRK04531 148 INADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWINGGMKLKLEQIKELLDRLPLESSVSI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 345 TAASTLLTELFSNKGCGTLFKNAERMLRVRSLDSLDQGRLVNLVNASFGKKLREDYLEslRPRLHSIYVSEGYNAAAILT 424
Cdd:PRK04531 228 TSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPDYFD--TTQLLRAYVSENYRAAAILT 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 425 VEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDS 504
Cdd:PRK04531 306 ETG---GGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAESDGCIKQEKWKVFWYGLDDFEQI 382

                        410
                 ....*....|....
gi 157817440 505 YELVNHAKGLPDSF 518
Cdd:PRK04531 383 PKCVAHCANRPPTL 396
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
108-518 6.90e-91

N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 285.06  E-value: 6.90e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 108 ASPGEARHWLTQFQtcyhSVDKP-FAVVEVDEEVFgcPQAVSRLAFALAFLQRMDMKPLVV-------------LGLPAP 173
Cdd:COG5630   18 GSAKEIEQYLKRFS----QVDAErFAVVKVGGAVL--RDDLDALASSLSFLQQVGLTPIVVhgagpqldaalaaAGIETQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 174 T------APSGCLSFweAKAQLAQSCKVLVNELRHNAATAVPFFGGgsvLSAAEPAPHASYG---GIVAVETDLLQWCLE 244
Cdd:COG5630   92 RvdglrvTSPEALEI--VRRVFQQENLKLVEALEAMGTRARPIPSG---VFEAEYLDRDTLGlvgEVTGVHLAPIEASLR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 245 SNSIPILCPIGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNLPADLDLVTNAEWLSTKERQ 324
Cdd:COG5630  167 AGSIPIIASLGETPSGQILNINADVAARELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDHLMAQPWVNGGMRL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 325 QIRLIVDVLSRLPHYSSAVITAASTLLTELFSNKGCGTLFKNAERMLRVRSLDSLDQGRLVNLVNASFGKKLREDYLESL 404
Cdd:COG5630  247 KLEEIKDLLDDLPLTSSVSITRPSELAKELFTHKGSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVEGYFDKT 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 405 RPrlHSIYVSEGYNAAAILTVEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDG 484
Cdd:COG5630  327 KF--YRAYVSESYRAAAILTLED---GVPYLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEADG 401

                        410       420       430
                 ....*....|....*....|....*....|....
gi 157817440 485 SFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSF 518
Cdd:COG5630  402 CYKQEKWTVFWYGLDGFDEIQACVEHALARPPTL 435
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 350-513 1.56e-64

NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region (pfam00696) in some fungal acetylglutamate kinase enzymes. it stabilizes the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain pfam00696.


Pssm-ID: 398437  Cd Length: 166  Bit Score: 207.11  E-value: 1.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  350 LLTELFSNKGCGTLFKNAERMLRVRSLDSL-DQGRLVNLVNASF-GKKLREDYLESLRPRLHSIYVSEGYNAAAILTVEp 427
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELiDIERLRNLIERSFdGRLSVADYLDRLKGRLFKIYVDEPYEALAIVTKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  428 vLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYEL 507
Cdd:pfam04768  81 -DGGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSEL 159


                  ....*.
gi 157817440  508 VNHAKG 513
Cdd:pfam04768 160 VASFRD 165
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 398-497 7.24e-58

DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans and fish; This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176267  Cd Length: 99  Bit Score: 187.58  E-value: 7.24e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 398 EDYLESLRPRLHSIYVSEGYNAAAILTVEPVlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 477
Cdd:cd04265    1 PDYFDSLQGRLHTIYLSEGYNAAAIVTNEEV-DGVPYLDKFAVSSSAQGEGTGEALWRRLRRDFPKLFWRSRSTNPINPW 79

                         90       100
                 ....*....|....*....|
gi 157817440 478 YFKHSDGSFSNKQWIFFWFG 497
Cdd:cd04265   80 YFKRCDGSFKNGHWTVFWYG 99
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 140-305 8.50e-04

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 41.20  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  140 VFGCPQAVSRLAFALAFLQRMDMKPLVV-------------LGLPA--PTAPSGCLSFWEAKAQLAQSCKVLVNELRHNA 204
Cdd:pfam00696  11 SLTDKERLKRLADEIAALLEEGRKLVVVhgggafadgllalLGLSPrfARLTDAETLEVATMDALGSLGERLNAALLAAG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  205 ATAVPFFGGGSVLSAAEPAPHAsyggIVAVETDLLQWCLESNSIPILCP-IGETAARRSVLLDSLEVTASLAKALQPTKI 283
Cdd:pfam00696  91 LPAVGLPAAQLLATEAGFIDDV----VTRIDTEALEELLEAGVVPVITGfIGIDPEGELGRGSSDTLAALLAEALGADKL 166

                         170       180
                  ....*....|....*....|....*...
gi 157817440  284 IFLNNSGGLRD------TSQKILSNVNL 305
Cdd:pfam00696 167 IILTDVDGVYTadprkvPDAKLIPEISY 194
 
Name Accession Description Interval E-value
AAK_NAGS-Urea cd04236
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 95-364 1.12e-153

AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the urea cycle found in animals. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate; NAG is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Ureogenic NAGS activity is dependent on the concentration of glutamate (substrate) and arginine (activator). Domain architecture of ureogenic NAGS consists of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal DUF619 domain. Members of this CD belong to the protein superfamily, the Amino Acid Kinase Family (AAKF).


Pssm-ID: 239769 [Multi-domain]  Cd Length: 271  Bit Score: 439.66  E-value: 1.12e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  95 VQRDIQAFLNQCGASPGEARHWLTQFQTCYHSVDKPFAVVEVDEEVFGCPQAVSRLAFALAFLQRMDMKPLVVLGLPAPT 174
Cdd:cd04236    1 IYRDVKAFLHQKGGDPREARYWLTQFQIAMPNDWPAFAVLEVDHSVFRSLEMVQSLSFGLAFLQRMDMKLLVVMGLSAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 175 APSG-CLSFWEAKAQLAQSCKVLVNELRHNAATAVPFFGGGSVLSAAEPAPHASYGGIVAVETDLLQWCLESNSIPILCP 253
Cdd:cd04236   81 GTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTELLQWCLGSGHIPLVCP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 254 IGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNLPADLDLVTNAEWLSTKERQQIRLIVDVL 333
Cdd:cd04236  161 IGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWLSETEQNRIQDIATLL 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 157817440 334 SRLPHYSSAVITAASTLLTELFSNKGCGTLF 364
Cdd:cd04236  241 NALPSMSSAVITSAETLLTELFSHKGSGTLF 271
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 108-518 6.32e-92

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 286.56  E-value: 6.32e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 108 ASPGEARHWLTQFQtcyhSVD-KPFAVVEVDEEVFgcPQAVSRLAFALAFLQRMDMKPLVVLGlpapTAPSgclsfweAK 186
Cdd:PRK04531  18 ASAKEISQYLKRFS----QLDaERFAVIKVGGAVL--RDDLEALASSLSFLQEVGLTPIVVHG----AGPQ-------LD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 187 AQLAQSC--KVLVNELRHNAaTAVPFFGGGSVLSAaepaPHASYGGIVAVetdllqwcLESNSIPILCPIGETAARRSVL 264
Cdd:PRK04531  81 AELDAAGieKETVNGLRVTS-PEALAIVRKVFQRS----NLDLVEAVESS--------LRAGSIPVIASLGETPSGQILN 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 265 LDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNLPADLDLVTNAEWLSTKERQQIRLIVDVLSRLPHYSSAVI 344
Cdd:PRK04531 148 INADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWINGGMKLKLEQIKELLDRLPLESSVSI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 345 TAASTLLTELFSNKGCGTLFKNAERMLRVRSLDSLDQGRLVNLVNASFGKKLREDYLEslRPRLHSIYVSEGYNAAAILT 424
Cdd:PRK04531 228 TSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPDYFD--TTQLLRAYVSENYRAAAILT 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 425 VEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDS 504
Cdd:PRK04531 306 ETG---GGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAESDGCIKQEKWKVFWYGLDDFEQI 382

                        410
                 ....*....|....
gi 157817440 505 YELVNHAKGLPDSF 518
Cdd:PRK04531 383 PKCVAHCANRPPTL 396
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
108-518 6.90e-91

N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 285.06  E-value: 6.90e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 108 ASPGEARHWLTQFQtcyhSVDKP-FAVVEVDEEVFgcPQAVSRLAFALAFLQRMDMKPLVV-------------LGLPAP 173
Cdd:COG5630   18 GSAKEIEQYLKRFS----QVDAErFAVVKVGGAVL--RDDLDALASSLSFLQQVGLTPIVVhgagpqldaalaaAGIETQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 174 T------APSGCLSFweAKAQLAQSCKVLVNELRHNAATAVPFFGGgsvLSAAEPAPHASYG---GIVAVETDLLQWCLE 244
Cdd:COG5630   92 RvdglrvTSPEALEI--VRRVFQQENLKLVEALEAMGTRARPIPSG---VFEAEYLDRDTLGlvgEVTGVHLAPIEASLR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 245 SNSIPILCPIGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNLPADLDLVTNAEWLSTKERQ 324
Cdd:COG5630  167 AGSIPIIASLGETPSGQILNINADVAARELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDHLMAQPWVNGGMRL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 325 QIRLIVDVLSRLPHYSSAVITAASTLLTELFSNKGCGTLFKNAERMLRVRSLDSLDQGRLVNLVNASFGKKLREDYLESL 404
Cdd:COG5630  247 KLEEIKDLLDDLPLTSSVSITRPSELAKELFTHKGSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVEGYFDKT 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 405 RPrlHSIYVSEGYNAAAILTVEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDG 484
Cdd:COG5630  327 KF--YRAYVSESYRAAAILTLED---GVPYLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEADG 401

                        410       420       430
                 ....*....|....*....|....*....|....
gi 157817440 485 SFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSF 518
Cdd:COG5630  402 CYKQEKWTVFWYGLDGFDEIQACVEHALARPPTL 435
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 350-513 1.56e-64

NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region (pfam00696) in some fungal acetylglutamate kinase enzymes. it stabilizes the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain pfam00696.


Pssm-ID: 398437  Cd Length: 166  Bit Score: 207.11  E-value: 1.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  350 LLTELFSNKGCGTLFKNAERMLRVRSLDSL-DQGRLVNLVNASF-GKKLREDYLESLRPRLHSIYVSEGYNAAAILTVEp 427
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELiDIERLRNLIERSFdGRLSVADYLDRLKGRLFKIYVDEPYEALAIVTKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  428 vLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYEL 507
Cdd:pfam04768  81 -DGGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSEL 159


                  ....*.
gi 157817440  508 VNHAKG 513
Cdd:pfam04768 160 VASFRD 165
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 398-497 7.24e-58

DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans and fish; This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176267  Cd Length: 99  Bit Score: 187.58  E-value: 7.24e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 398 EDYLESLRPRLHSIYVSEGYNAAAILTVEPVlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 477
Cdd:cd04265    1 PDYFDSLQGRLHTIYLSEGYNAAAIVTNEEV-DGVPYLDKFAVSSSAQGEGTGEALWRRLRRDFPKLFWRSRSTNPINPW 79

                         90       100
                 ....*....|....*....|
gi 157817440 478 YFKHSDGSFSNKQWIFFWFG 497
Cdd:cd04265   80 YFKRCDGSFKNGHWTVFWYG 99
DUF619-NAGS cd04264
DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic ...
 398-497 1.61e-57

DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic pathway and urea cycle found in humans and fish; DUF619-NAGS: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176266  Cd Length: 99  Bit Score: 186.42  E-value: 1.61e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 398 EDYLESLrPRLHSIYVSEGYNAAAILTVEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 477
Cdd:cd04264    1 PDYIDRL-QRLHAIYLSEGYNAAAIVTYEGVNNGVPYLDKFAVSSSAQGEGTSDALWRRLRRDFPKLFWRSRKTNPINPW 79

                         90       100
                 ....*....|....*....|
gi 157817440 478 YFKHSDGSFSNKQWIFFWFG 497
Cdd:cd04264   80 YFKRSDGSFKNGQWKVFWYG 99
AAK_NAGK-fArgBP cd04252
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ...
 147-363 1.31e-27

AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (fArgBP). The nuclear-encoded, mitochondrial polyprotein precursor with an N-terminal NAGK (ArgB) domain (this CD), a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved in the mitochondria into two distinct enzymes (NAGK-DUF619 and NAGPR). Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. This CD also includes some gamma-proteobacteria (Xanthomonas and Xylella) NAG kinases with an N-terminal NAGK (ArgB) domain (this CD) and a C-terminal DUF619 domain. The DUF619 domain is described as a putative distant homolog of the acetyltransferase, ArgA, predicted to function in NAG synthase association in fungi. Eukaryotic sequences have an N-terminal mitochondrial transit peptide. Members of this NAG kinase domain CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239785 [Multi-domain]  Cd Length: 248  Bit Score: 110.93  E-value: 1.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 147 VSRLAFALAFLQRMDMKPLVVLG----LPAPTAPSGC-------LSFWEAKAQ-------LAQSCKvLVNELRHNAATAV 208
Cdd:cd04252   14 LDELAASLSFLQHVGLYPIVVHGagpqLNEELEAAGVepeyvdgLRVTDPETLavarkvfLEENLK-LVEALERNGARAR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 209 PFFGGgsvLSAAEPAPHASY---GGIVAVETDLLQWCLESNSIPILCPIGETAARRSVLLDSLEVTASLAKALQPTKIIF 285
Cdd:cd04252   93 PITSG---VFEAEYLDKDKYglvGKITGVNKAPIEAAIRAGYLPILTSLAETPSGQLLNVNADVAAGELARVLEPLKIVF 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157817440 286 LNNSGGLRDTSQKILSNVNLPADLDLVTNAEWLSTKERQQIRLIVDVLSRLPHYSSAVITAASTLLTELFSNKGCGTL 363
Cdd:cd04252  170 LNETGGLLDGTGKKISAINLDEEYDDLMKQPWVKYGTKLKIKEIKELLDTLPRSSSVSITSPDDLQKELFTHSGAGTL 247
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 133-364 8.41e-25

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


Pssm-ID: 239033 [Multi-domain]  Cd Length: 248  Bit Score: 103.29  E-value: 8.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 133 VVEVDEEVFGCPQAVSRLAFALAFLQRMDMKPLVVLGLPAPTAPSGC-------------LSFWEAKAQLAQSCKVLVNE 199
Cdd:cd02115    1 VIKFGGSSVSSEERLRNLARILVKLASEGGRVVVVHGAGPQITDELLahgellgyarglrITDRETDALAAMGEGMSNLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 200 LRHNAATavpfFGGGSVLSAAEPAPHAS-----YGGIVAVETDLLQWCLESNSIPILCPIGETAA--RRSVLLDSLEVTA 272
Cdd:cd02115   81 IAAALEQ----HGIKAVPLDLTQAGFASpnqghVGKITKVSTDRLKSLLENGILPILSGFGGTDEkeTGTLGRGGSDSTA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 273 S-LAKALQPTKIIFLNNSGGLRDTSQ------KILSNVNlPADLDLVTNAEWlstkeRQQIRLIVDVLSRlpHYSSAVIT 345
Cdd:cd02115  157 AlLAAALKADRLVILTDVDGVYTADPrkvpdaKLLSELT-YEEAAELAYAGA-----MVLKPKAADPAAR--AGIPVRIA 228

                        250       260
                 ....*....|....*....|
gi 157817440 346 AASTLLT-ELFSNKGCGTLF 364
Cdd:cd02115  229 NTENPGAlALFTPDGGGTLI 248
DUF619-NAGS-FABP cd04266
DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; ...
 398-497 6.12e-20

DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; DUF619-NAGS-FABP: This family includes the DUF619 domain of N-acetylglutamate synthase (NAGS) of the fungal arginine-biosynthetic pathway (FABP). This NAGS (also known as arginine-requiring protein 2 or ARG2) consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. NAGS catalyzes the formation of NAG from acetylcoenzyme A and L-glutamate. The DUF619 domain, yet to be characterized, is predicted to function in NAGS association in fungi.


Pssm-ID: 176268  Cd Length: 108  Bit Score: 85.20  E-value: 6.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 398 EDYLESLRPRLHSIYVSEGYNAAAILTVEPVLGGTP----YLDKFVVSSSRQGQ-GSGQMLWECLRRDL-QTLFWRSRVT 471
Cdd:cd04266    1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPDGSTPekiaYLDKFAVLPKAQGSdGIADILFNAMLDGFpNELIWRSRKD 80

                         90       100
                 ....*....|....*....|....*...
gi 157817440 472 NPINPWYFKHSDGSFSNK--QWIFFWFG 497
Cdd:cd04266   81 NPVNKWYFERSVGVLKLSgsQWKLFWTG 108
DUF619-like cd03173
DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; ...
 399-497 1.15e-16

DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; DUF619-like: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. This subgroup also includes the DUF619 domain of the FABP N-acetylglutamate kinase (NAGK), the enzyme that catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-acetylglutamate phosphate reductase). The DUF619 domain function has yet to be characterized.


Pssm-ID: 176264  Cd Length: 98  Bit Score: 75.21  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 399 DYLESLRPRLHSIYVSEGYNAAAILTVEPvlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWY 478
Cdd:cd03173    2 SYLKRLKNGKFASYADEPLEGVAIVTYEG--NSIPYLDKFAVSDHLWLNNVTDNIFNLIRKDFPSLLWRVRENDANLKWY 79

                         90
                 ....*....|....*....
gi 157817440 479 FKHSDGSFSNKQWIFFWFG 497
Cdd:cd03173   80 FSKSVGSLDKNGFILFWYG 98
DUF619-NAGK-FABP cd04263
DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway; ...
 398-497 1.36e-12

DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway; DUF619-NAGK-FABP: DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (FABP). The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved into two distinct enzymes (NAGK-DUF619 and NAGPR) in the mitochondria. Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. Arg5,6 catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. It also binds and regulates the promoters of nuclear and mitochondrial genes, and may possibly regulate precursor mRNA metabolism. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176265  Cd Length: 98  Bit Score: 63.88  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 398 EDYLESLRPRLHSIYVSEGYNAAAIltVEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 477
Cdd:cd04263    1 ASYFDELKERPFKAYGDEPMEVLAI--VLPPSGEVATLATFTITKSGWLNNVADNIFTAIKKDHPKLVWTVREDDENLKW 78

                         90       100
                 ....*....|....*....|
gi 157817440 478 YFKHSDGSFSNKQWIFFWFG 497
Cdd:cd04263   79 HFEKADGSFTRNGKVLFWYG 98
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 229-364 1.17e-09

N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 59.28  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 229 GGIVAVETDLLQWCLESNSIPILCPIGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNlPAD 308
Cdd:COG0548  147 GEVRRVDPELIRALLDAGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELT-AAE 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817440 309 LDLVTNAEWLSTKERQQIRLIVDVLS-----------RLPHyssavitaasTLLTELFSNKGCGTLF 364
Cdd:COG0548  226 AEELIADGVISGGMIPKLEAALDAVRggvkrvhiidgRVPH----------ALLLELFTDDGIGTMI 282
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 228-363 7.36e-06

AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences in this CD have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239770 [Multi-domain]  Cd Length: 280  Bit Score: 47.94  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 228 YGGIV-AVETDLLQWCLESNSIPILCPIGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNLP 306
Cdd:cd04237  142 HTGEVrRIDADAIRRQLDQGSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDDDGELIRELTAQ 221

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 307 ADLDLVTNAEWLSTKERQQIRLIVDVLS---RLPHYSSAVITAAstLLTELFSNKGCGTL 363
Cdd:cd04237  222 EAEALLETGALLTNDTARLLQAAIEACRggvPRVHLISYAEDGA--LLLELFTRDGVGTL 279
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 194-364 7.60e-06

AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239771 [Multi-domain]  Cd Length: 256  Bit Score: 47.50  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 194 KVLVNELRHNAATAVPFFGGGSVLSAAEPAPHASY-----GGIVAVETDLLQWCLESNSIPILCPIGETAARRSVLLDSL 268
Cdd:cd04238   81 KELVSLLNRAGGKAVGLSGKDGGLIKAEKKEEKDIdlgfvGEVTEVNPELLETLLEAGYIPVIAPIAVDEDGETYNVNAD 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 269 EVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVNlPADLDLVTNAEWLSTKERQQIRLIVDVLSRLphYSSAVI---T 345
Cdd:cd04238  161 TAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELT-PKEAEELIEDGVISGGMIPKVEAALEALEGG--VRKVHIidgR 237

                        170
                 ....*....|....*....
gi 157817440 346 AASTLLTELFSNKGCGTLF 364
Cdd:cd04238  238 VPHSLLLELFTDEGIGTMI 256
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 243-363 3.28e-05

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 46.30  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 243 LESNSIPILCPIGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDTSQKILSNVnLPADLDlvtnaEWLSTKE 322
Cdd:PRK05279 165 LDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIREL-SPNEAQ-----ALLEALE 238

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157817440 323 RQQirLIVDVLSRLPHYSSAV---------ITAAS--TLLTELFSNKGCGTL 363
Cdd:PRK05279 239 DGD--YNSGTARFLRAAVKACrggvrrshlISYAEdgALLQELFTRDGIGTM 288
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 229-364 2.74e-04

AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239783 [Multi-domain]  Cd Length: 279  Bit Score: 42.88  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 229 GGIVAVETDLLQWCLESNSIPILCPIGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRDT---SQKILSNVNl 305
Cdd:cd04250  141 GEVTEVNPELLETLLEAGYIPVIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVLDDpndPGSLISEIS- 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817440 306 padldlVTNAEWLSTKERQQIRLIVDVLS-----------------RLPHyssavitaasTLLTELFSNKGCGTLF 364
Cdd:cd04250  220 ------LKEAEELIADGIISGGMIPKVEAciealeggvkaahiidgRVPH----------SLLLEIFTDEGIGTMI 279
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 140-305 8.50e-04

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 41.20  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  140 VFGCPQAVSRLAFALAFLQRMDMKPLVV-------------LGLPA--PTAPSGCLSFWEAKAQLAQSCKVLVNELRHNA 204
Cdd:pfam00696  11 SLTDKERLKRLADEIAALLEEGRKLVVVhgggafadgllalLGLSPrfARLTDAETLEVATMDALGSLGERLNAALLAAG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440  205 ATAVPFFGGGSVLSAAEPAPHAsyggIVAVETDLLQWCLESNSIPILCP-IGETAARRSVLLDSLEVTASLAKALQPTKI 283
Cdd:pfam00696  91 LPAVGLPAAQLLATEAGFIDDV----VTRIDTEALEELLEAGVVPVITGfIGIDPEGELGRGSSDTLAALLAEALGADKL 166

                         170       180
                  ....*....|....*....|....*...
gi 157817440  284 IFLNNSGGLRD------TSQKILSNVNL 305
Cdd:pfam00696 167 IILTDVDGVYTadprkvPDAKLIPEISY 194
argB CHL00202
acetylglutamate kinase; Provisional
 194-364 1.81e-03

acetylglutamate kinase; Provisional


Pssm-ID: 133644 [Multi-domain]  Cd Length: 284  Bit Score: 40.55  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 194 KVLVNELRHNAATAVPFFGGGSVLSAAEPA--PHASY-GGIVAVETDLLQWCLESNSIPILCPIGETAARRSVLLDSLEV 270
Cdd:CHL00202 106 KDLVGSINANGGKAVGLCGKDANLIVARASdkKDLGLvGEIQQVDPQLIDMLLEKNYIPVIASVAADHDGQTYNINADVV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817440 271 TASLAKALQPTKIIFLNNSGGlrdtsqkILSNVNLPADLDLVTNAEWLSTKERQQI-------RLIVDVLSRLPHYSSAV 343
Cdd:CHL00202 186 AGEIAAKLNAEKLILLTDTPG-------ILADINDPNSLISTLNIKEARNLASTGIisggmipKVNCCIRALAQGVEAAH 258

                        170       180
                 ....*....|....*....|....
gi 157817440 344 ITAAS---TLLTELFSNKGCGTLF 364
Cdd:CHL00202 259 IIDGKekhALLLEILTEKGIGSML 282
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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