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Conserved domains on  [gi|23308587|ref|NP_694551|]
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N-acetylglutamate synthase, mitochondrial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 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 ...
 102-371 1.13e-164

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: 467.78  E-value: 1.13e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 102 VQRDIQAFLNQCGASPGEARHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAPT 181
Cdd:cd04236   1 IYRDVKAFLHQKGGDPREARYWLTQFQIAMPNDWPAFAVLEVDHSVFRSLEMVQSLSFGLAFLQRMDMKLLVVMGLSAPD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 182 APSG-CLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDLLQWCLESGSIPILCP 260
Cdd:cd04236  81 GTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTELLQWCLGSGHIPLVCP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 261 IGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVL 340
Cdd:cd04236 161 IGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWLSETEQNRIQDIATLL 240

                       250       260       270
                ....*....|....*....|....*....|.
gi 23308587 341 SRLPHHSSAVITAASTLLTELFSNKGSGTLF 371
Cdd:cd04236 241 NALPSMSSAVITSAETLLTELFSHKGSGTLF 271
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 357-520 3.55e-65

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: 209.03  E-value: 3.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   357 LLTELFSNKGSGTLFKNAERMLRVRSLDKL-DQGRLVDLVNASF-GKKLRDDYLASLRPRLHSIYVSEGYNAAAILTMEp 434
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELiDIERLRNLIERSFdGRLSVADYLDRLKGRLFKIYVDEPYEALAIVTKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   435 vLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYEL 514
Cdd:pfam04768  81 -DGGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSEL 159


                  ....*.
gi 23308587   515 VNHAKG 520
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 ...
 102-371 1.13e-164

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: 467.78  E-value: 1.13e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 102 VQRDIQAFLNQCGASPGEARHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAPT 181
Cdd:cd04236   1 IYRDVKAFLHQKGGDPREARYWLTQFQIAMPNDWPAFAVLEVDHSVFRSLEMVQSLSFGLAFLQRMDMKLLVVMGLSAPD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 182 APSG-CLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDLLQWCLESGSIPILCP 260
Cdd:cd04236  81 GTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTELLQWCLGSGHIPLVCP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 261 IGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVL 340
Cdd:cd04236 161 IGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWLSETEQNRIQDIATLL 240

                       250       260       270
                ....*....|....*....|....*....|.
gi 23308587 341 SRLPHHSSAVITAASTLLTELFSNKGSGTLF 371
Cdd:cd04236 241 NALPSMSSAVITSAETLLTELFSHKGSGTLF 271
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 115-525 6.22e-97

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 299.66  E-value: 6.22e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  115 ASPGEARHWLTQFQtchhSAD-KPFAVIEVDEEVLkcQQGVSSLAFALAFLQRMDMKPLVVLGlpapTAPSgclsfweAK 193
Cdd:PRK04531  18 ASAKEISQYLKRFS----QLDaERFAVIKVGGAVL--RDDLEALASSLSFLQEVGLTPIVVHG----AGPQ-------LD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  194 AQLAKSC--KVLVDALRHNAAAAvPFFGGGSVLRAaepaPHASYGGIVSVetdllqwcLESGSIPILCPIGETAARRSVL 271
Cdd:PRK04531  81 AELDAAGieKETVNGLRVTSPEA-LAIVRKVFQRS----NLDLVEAVESS--------LRAGSIPVIASLGETPSGQILN 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  272 LDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVI 351
Cdd:PRK04531 148 INADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWINGGMKLKLEQIKELLDRLPLESSVSI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  352 TAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLAslRPRLHSIYVSEGYNAAAILT 431
Cdd:PRK04531 228 TSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPDYFD--TTQLLRAYVSENYRAAAILT 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  432 MEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDS 511
Cdd:PRK04531 306 ETG---GGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAESDGCIKQEKWKVFWYGLDDFEQI 382

                        410
                 ....*....|....
gi 23308587  512 YELVNHAKGLPDSF 525
Cdd:PRK04531 383 PKCVAHCANRPPTL 396
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
115-527 1.40e-95

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


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 297.39  E-value: 1.40e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 115 ASPGEARHWLTQFQtchhSADKP-FAVIEVDEEVLkcQQGVSSLAFALAFLQRMDMKPLVVLG--------LPA---PTA 182
Cdd:COG5630  18 GSAKEIEQYLKRFS----QVDAErFAVVKVGGAVL--RDDLDALASSLSFLQQVGLTPIVVHGagpqldaaLAAagiETQ 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 183 PSGCLSFWEAKAqLAKSCKV-------LVDALRHNAAAAVPFFGGgsvLRAAEPAPHASYG---GIVSVETDLLQWCLES 252
Cdd:COG5630  92 RVDGLRVTSPEA-LEIVRRVfqqenlkLVEALEAMGTRARPIPSG---VFEAEYLDRDTLGlvgEVTGVHLAPIEASLRA 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 253 GSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQ 332
Cdd:COG5630 168 GSIPIIASLGETPSGQILNINADVAARELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDHLMAQPWVNGGMRLK 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 333 MRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLR 412
Cdd:COG5630 248 LEEIKDLLDDLPLTSSVSITRPSELAKELFTHKGSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVEGYFDKTK 327

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 413 PrlHSIYVSEGYNAAAILTMEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGS 492
Cdd:COG5630 328 F--YRAYVSESYRAAAILTLED---GVPYLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEADGC 402

                       410       420       430
                ....*....|....*....|....*....|....*
gi 23308587 493 FSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHK 527
Cdd:COG5630 403 YKQEKWTVFWYGLDGFDEIQACVEHALARPPTLKD 437
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 357-520 3.55e-65

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: 209.03  E-value: 3.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   357 LLTELFSNKGSGTLFKNAERMLRVRSLDKL-DQGRLVDLVNASF-GKKLRDDYLASLRPRLHSIYVSEGYNAAAILTMEp 434
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELiDIERLRNLIERSFdGRLSVADYLDRLKGRLFKIYVDEPYEALAIVTKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   435 vLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYEL 514
Cdd:pfam04768  81 -DGGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSEL 159


                  ....*.
gi 23308587   515 VNHAKG 520
Cdd:pfam04768 160 VASFRD 165
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 405-504 1.13e-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: 189.51  E-value: 1.13e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 405 DDYLASLRPRLHSIYVSEGYNAAAILTMEPVlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 484
Cdd:cd04265   1 PDYFDSLQGRLHTIYLSEGYNAAAIVTNEEV-DGVPYLDKFAVSSSAQGEGTGEALWRRLRRDFPKLFWRSRSTNPINPW 79

                        90       100
                ....*....|....*....|
gi 23308587 485 YFKHSDGSFSNKQWIFFWFG 504
Cdd:cd04265  80 YFKRCDGSFKNGHWTVFWYG 99
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 147-302 1.39e-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: 43.51  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   147 VLKCQQGVSSLAFALAFLQRMDMKPLVV-------------LGLPA--PTAPSGCLSFWEAKAQLAKSCKVLVDALRHNA 211
Cdd:pfam00696  11 SLTDKERLKRLADEIAALLEEGRKLVVVhgggafadgllalLGLSPrfARLTDAETLEVATMDALGSLGERLNAALLAAG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   212 AAAVPFFGGGSVLRAAEPAPHAsyggIVSVETDLLQWCLESGSIPILCP-IGETAARRSVLLDSLEVTASLAKALRPTKI 290
Cdd:pfam00696  91 LPAVGLPAAQLLATEAGFIDDV----VTRIDTEALEELLEAGVVPVITGfIGIDPEGELGRGSSDTLAALLAEALGADKL 166

                         170
                  ....*....|..
gi 23308587   291 IFLNNTGGLRDS 302
Cdd:pfam00696 167 IILTDVDGVYTA 178
 
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 ...
 102-371 1.13e-164

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: 467.78  E-value: 1.13e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 102 VQRDIQAFLNQCGASPGEARHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAPT 181
Cdd:cd04236   1 IYRDVKAFLHQKGGDPREARYWLTQFQIAMPNDWPAFAVLEVDHSVFRSLEMVQSLSFGLAFLQRMDMKLLVVMGLSAPD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 182 APSG-CLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDLLQWCLESGSIPILCP 260
Cdd:cd04236  81 GTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTELLQWCLGSGHIPLVCP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 261 IGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVL 340
Cdd:cd04236 161 IGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWLSETEQNRIQDIATLL 240

                       250       260       270
                ....*....|....*....|....*....|.
gi 23308587 341 SRLPHHSSAVITAASTLLTELFSNKGSGTLF 371
Cdd:cd04236 241 NALPSMSSAVITSAETLLTELFSHKGSGTLF 271
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 115-525 6.22e-97

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 299.66  E-value: 6.22e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  115 ASPGEARHWLTQFQtchhSAD-KPFAVIEVDEEVLkcQQGVSSLAFALAFLQRMDMKPLVVLGlpapTAPSgclsfweAK 193
Cdd:PRK04531  18 ASAKEISQYLKRFS----QLDaERFAVIKVGGAVL--RDDLEALASSLSFLQEVGLTPIVVHG----AGPQ-------LD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  194 AQLAKSC--KVLVDALRHNAAAAvPFFGGGSVLRAaepaPHASYGGIVSVetdllqwcLESGSIPILCPIGETAARRSVL 271
Cdd:PRK04531  81 AELDAAGieKETVNGLRVTSPEA-LAIVRKVFQRS----NLDLVEAVESS--------LRAGSIPVIASLGETPSGQILN 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  272 LDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVI 351
Cdd:PRK04531 148 INADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWINGGMKLKLEQIKELLDRLPLESSVSI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  352 TAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLAslRPRLHSIYVSEGYNAAAILT 431
Cdd:PRK04531 228 TSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPDYFD--TTQLLRAYVSENYRAAAILT 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  432 MEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDS 511
Cdd:PRK04531 306 ETG---GGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAESDGCIKQEKWKVFWYGLDDFEQI 382

                        410
                 ....*....|....
gi 23308587  512 YELVNHAKGLPDSF 525
Cdd:PRK04531 383 PKCVAHCANRPPTL 396
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
115-527 1.40e-95

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


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 297.39  E-value: 1.40e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 115 ASPGEARHWLTQFQtchhSADKP-FAVIEVDEEVLkcQQGVSSLAFALAFLQRMDMKPLVVLG--------LPA---PTA 182
Cdd:COG5630  18 GSAKEIEQYLKRFS----QVDAErFAVVKVGGAVL--RDDLDALASSLSFLQQVGLTPIVVHGagpqldaaLAAagiETQ 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 183 PSGCLSFWEAKAqLAKSCKV-------LVDALRHNAAAAVPFFGGgsvLRAAEPAPHASYG---GIVSVETDLLQWCLES 252
Cdd:COG5630  92 RVDGLRVTSPEA-LEIVRRVfqqenlkLVEALEAMGTRARPIPSG---VFEAEYLDRDTLGlvgEVTGVHLAPIEASLRA 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 253 GSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQ 332
Cdd:COG5630 168 GSIPIIASLGETPSGQILNINADVAARELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDHLMAQPWVNGGMRLK 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 333 MRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLR 412
Cdd:COG5630 248 LEEIKDLLDDLPLTSSVSITRPSELAKELFTHKGSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVEGYFDKTK 327

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 413 PrlHSIYVSEGYNAAAILTMEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGS 492
Cdd:COG5630 328 F--YRAYVSESYRAAAILTLED---GVPYLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEADGC 402

                       410       420       430
                ....*....|....*....|....*....|....*
gi 23308587 493 FSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHK 527
Cdd:COG5630 403 YKQEKWTVFWYGLDGFDEIQACVEHALARPPTLKD 437
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 357-520 3.55e-65

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: 209.03  E-value: 3.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   357 LLTELFSNKGSGTLFKNAERMLRVRSLDKL-DQGRLVDLVNASF-GKKLRDDYLASLRPRLHSIYVSEGYNAAAILTMEp 434
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELiDIERLRNLIERSFdGRLSVADYLDRLKGRLFKIYVDEPYEALAIVTKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   435 vLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYEL 514
Cdd:pfam04768  81 -DGGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSEL 159


                  ....*.
gi 23308587   515 VNHAKG 520
Cdd:pfam04768 160 VASFRD 165
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 405-504 1.13e-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: 189.51  E-value: 1.13e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 405 DDYLASLRPRLHSIYVSEGYNAAAILTMEPVlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 484
Cdd:cd04265   1 PDYFDSLQGRLHTIYLSEGYNAAAIVTNEEV-DGVPYLDKFAVSSSAQGEGTGEALWRRLRRDFPKLFWRSRSTNPINPW 79

                        90       100
                ....*....|....*....|
gi 23308587 485 YFKHSDGSFSNKQWIFFWFG 504
Cdd:cd04265  80 YFKRCDGSFKNGHWTVFWYG 99
DUF619-NAGS cd04264
DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic ...
 405-504 2.82e-58

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: 188.73  E-value: 2.82e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 405 DDYLASLrPRLHSIYVSEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 484
Cdd:cd04264   1 PDYIDRL-QRLHAIYLSEGYNAAAIVTYEGVNNGVPYLDKFAVSSSAQGEGTSDALWRRLRRDFPKLFWRSRKTNPINPW 79

                        90       100
                ....*....|....*....|
gi 23308587 485 YFKHSDGSFSNKQWIFFWFG 504
Cdd:cd04264  80 YFKRSDGSFKNGQWKVFWYG 99
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 140-371 3.57e-32

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: 124.09  E-value: 3.57e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 140 VIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAPTAPSGC-------------LSFWEAKAQLAKSCKVLVDA 206
Cdd:cd02115   1 VIKFGGSSVSSEERLRNLARILVKLASEGGRVVVVHGAGPQITDELLahgellgyarglrITDRETDALAAMGEGMSNLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 207 LRHNAAAavpfFGGGSVLRAAEPAPHAS-----YGGIVSVETDLLQWCLESGSIPILCPIGETAA--RRSVLLDSLEVTA 279
Cdd:cd02115  81 IAAALEQ----HGIKAVPLDLTQAGFASpnqghVGKITKVSTDRLKSLLENGILPILSGFGGTDEkeTGTLGRGGSDSTA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 280 S-LAKALRPTKIIFLNNTGGLRDS------SHKVLSNVNlPADLDLVCNAEWvstkeRQQMRLIVDVLSRlpHHSSAVIT 352
Cdd:cd02115 157 AlLAAALKADRLVILTDVDGVYTAdprkvpDAKLLSELT-YEEAAELAYAGA-----MVLKPKAADPAAR--AGIPVRIA 228

                       250       260
                ....*....|....*....|
gi 23308587 353 AASTLLT-ELFSNKGSGTLF 371
Cdd:cd02115 229 NTENPGAlALFTPDGGGTLI 248
AAK_NAGK-fArgBP cd04252
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ...
 139-370 3.89e-32

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: 123.64  E-value: 3.89e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 139 AVIEVDEEVLkcQQGVSSLAFALAFLQRMDMKPLVVLG----LPAPTAPSGC-------LSFWEAKAQ-------LAKSC 200
Cdd:cd04252   1 AVIKVGGAII--EDDLDELAASLSFLQHVGLYPIVVHGagpqLNEELEAAGVepeyvdgLRVTDPETLavarkvfLEENL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 201 KvLVDALRHNAAAAVPFFGGgsvLRAAEPAPHASY---GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEV 277
Cdd:cd04252  79 K-LVEALERNGARARPITSG---VFEAEYLDKDKYglvGKITGVNKAPIEAAIRAGYLPILTSLAETPSGQLLNVNADVA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 278 TASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTL 357
Cdd:cd04252 155 AGELARVLEPLKIVFLNETGGLLDGTGKKISAINLDEEYDDLMKQPWVKYGTKLKIKEIKELLDTLPRSSSVSITSPDDL 234

                       250
                ....*....|...
gi 23308587 358 LTELFSNKGSGTL 370
Cdd:cd04252 235 QKELFTHSGAGTL 247
DUF619-NAGS-FABP cd04266
DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; ...
 405-504 6.43e-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: 84.82  E-value: 6.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 405 DDYLASLRPRLHSIYVSEGYNAAAILTMEPVLGGTP----YLDKFVVSSSRQGQ-GSGQMLWECLRRDL-QTLFWRSRVT 478
Cdd:cd04266   1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPDGSTPekiaYLDKFAVLPKAQGSdGIADILFNAMLDGFpNELIWRSRKD 80

                        90       100
                ....*....|....*....|....*...
gi 23308587 479 NPINPWYFKHSDGSFSNK--QWIFFWFG 504
Cdd:cd04266  81 NPVNKWYFERSVGVLKLSgsQWKLFWTG 108
DUF619-like cd03173
DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; ...
 406-504 1.50e-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: 1.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 406 DYLASLRPRLHSIYVSEGYNAAAILTMEPvlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWY 485
Cdd:cd03173   2 SYLKRLKNGKFASYADEPLEGVAIVTYEG--NSIPYLDKFAVSDHLWLNNVTDNIFNLIRKDFPSLLWRVRENDANLKWY 79

                        90
                ....*....|....*....
gi 23308587 486 FKHSDGSFSNKQWIFFWFG 504
Cdd:cd03173  80 FSKSVGSLDKNGFILFWYG 98
DUF619-NAGK-FABP cd04263
DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway; ...
 405-504 3.44e-11

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: 59.64  E-value: 3.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 405 DDYLASLRPRLHSIYVSEGYNAAAILTmePVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 484
Cdd:cd04263   1 ASYFDELKERPFKAYGDEPMEVLAIVL--PPSGEVATLATFTITKSGWLNNVADNIFTAIKKDHPKLVWTVREDDENLKW 78

                        90       100
                ....*....|....*....|
gi 23308587 485 YFKHSDGSFSNKQWIFFWFG 504
Cdd:cd04263  79 HFEKADGSFTRNGKVLFWYG 98
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 236-371 1.24e-10

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: 62.36  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 236 GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNlPAD 315
Cdd:COG0548 147 GEVRRVDPELIRALLDAGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELT-AAE 225

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308587 316 LDLVCNAEWVSTKERQQMRLIVDVLS-----------RLPHhssavitaasTLLTELFSNKGSGTLF 371
Cdd:COG0548 226 AEELIADGVISGGMIPKLEAALDAVRggvkrvhiidgRVPH----------ALLLELFTDDGIGTMI 282
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 201-371 2.55e-08

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: 55.21  E-value: 2.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 201 KVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASY-----GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSL 275
Cdd:cd04238  81 KELVSLLNRAGGKAVGLSGKDGGLIKAEKKEEKDIdlgfvGEVTEVNPELLETLLEAGYIPVIAPIAVDEDGETYNVNAD 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 276 EVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNlPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPhhSSAVI---T 352
Cdd:cd04238 161 TAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELT-PKEAEELIEDGVISGGMIPKVEAALEALEGGV--RKVHIidgR 237

                       170
                ....*....|....*....
gi 23308587 353 AASTLLTELFSNKGSGTLF 371
Cdd:cd04238 238 VPHSLLLELFTDEGIGTMI 256
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 236-371 1.94e-06

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: 49.43  E-value: 1.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 236 GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDS---SHKVLSNVNl 312
Cdd:cd04250 141 GEVTEVNPELLETLLEAGYIPVIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVLDDpndPGSLISEIS- 219

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 313 PADLDLVCNAEWVSTKERQQMRLIVDVLS-----------RLPHhssavitaasTLLTELFSNKGSGTLF 371
Cdd:cd04250 220 LKEAEELIADGIISGGMIPKVEACIEALEggvkaahiidgRVPH----------SLLLEIFTDEGIGTMI 279
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 235-370 7.70e-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: 47.55  E-value: 7.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587 235 YGGIV-SVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLP 313
Cdd:cd04237 142 HTGEVrRIDADAIRRQLDQGSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDDDGELIRELTAQ 221

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308587 314 ADLDLVCNAEWVSTKERQQMRLIVDVLSR-------LPHHSSavitaaSTLLTELFSNKGSGTL 370
Cdd:cd04237 222 EAEALLETGALLTNDTARLLQAAIEACRGgvprvhlISYAED------GALLLELFTRDGVGTL 279
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 235-370 2.13e-05

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 47.07  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  235 YGGIV-SVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVnLP 313
Cdd:PRK05279 149 HTGEVrRIDAEAIRRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIREL-SP 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308587  314 ADLDlvcnaEWVSTKERQQmrLIVDVLSRLPHHSSAV---------ITAAS--TLLTELFSNKGSGTL 370
Cdd:PRK05279 228 NEAQ-----ALLEALEDGD--YNSGTARFLRAAVKACrggvrrshlISYAEdgALLQELFTRDGIGTM 288
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 236-373 3.83e-05

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 45.48  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  236 GGIVSVETDLLQWCLESGSIPILCPIG------------ETAArrsvlldslevtASLAKALRPTKIIFLNNTGGLRDSS 303
Cdd:PRK00942 145 GEVTPVNPALLEALLEAGYIPVISPIGvgedgetyninaDTAA------------GAIAAALGAEKLILLTDVPGVLDDK 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  304 HKVLSNVNlPADLD---------------LVCNAEWVSTKERQqmrliVDVLS-RLPHhssavitaasTLLTELFSNKGS 367
Cdd:PRK00942 213 GQLISELT-ASEAEeliedgvitggmipkVEAALDAARGGVRS-----VHIIDgRVPH----------ALLLELFTDEGI 276


                 ....*.
gi 23308587  368 GTLFKN 373
Cdd:PRK00942 277 GTMIVP 282
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 147-302 1.39e-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: 43.51  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   147 VLKCQQGVSSLAFALAFLQRMDMKPLVV-------------LGLPA--PTAPSGCLSFWEAKAQLAKSCKVLVDALRHNA 211
Cdd:pfam00696  11 SLTDKERLKRLADEIAALLEEGRKLVVVhgggafadgllalLGLSPrfARLTDAETLEVATMDALGSLGERLNAALLAAG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587   212 AAAVPFFGGGSVLRAAEPAPHAsyggIVSVETDLLQWCLESGSIPILCP-IGETAARRSVLLDSLEVTASLAKALRPTKI 290
Cdd:pfam00696  91 LPAVGLPAAQLLATEAGFIDDV----VTRIDTEALEELLEAGVVPVITGfIGIDPEGELGRGSSDTLAALLAEALGADKL 166

                         170
                  ....*....|..
gi 23308587   291 IFLNNTGGLRDS 302
Cdd:pfam00696 167 IILTDVDGVYTA 178
argB CHL00202
acetylglutamate kinase; Provisional
 201-316 3.04e-03

acetylglutamate kinase; Provisional


Pssm-ID: 133644 [Multi-domain]  Cd Length: 284  Bit Score: 39.78  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308587  201 KVLVDALRHNAAAAVPFFGGGSVLRAAEPA--PHASY-GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEV 277
Cdd:CHL00202 106 KDLVGSINANGGKAVGLCGKDANLIVARASdkKDLGLvGEIQQVDPQLIDMLLEKNYIPVIASVAADHDGQTYNINADVV 185

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 23308587  278 TASLAKALRPTKIIFLNNTGGlrdsshkVLSNVNLPADL 316
Cdd:CHL00202 186 AGEIAAKLNAEKLILLTDTPG-------ILADINDPNSL 217
 
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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