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Conserved domains on  [gi|6322390|ref|NP_012464|]
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acetyl-CoA:L-glutamate N-acetyltransferase [Saccharomyces cerevisiae S288C]

Protein Classification

acetylglutamate kinase( domain architecture ID 11475699)

acetylglutamate kinase catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate to form N-acetyl-L-glutamate 5-phosphate, which is the second step of arginine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF619-like super family cl14605
DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; ...
 423-538 5.31e-57

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.


The actual alignment was detected with superfamily member cd04266:

Pssm-ID: 417472  Cd Length: 108  Bit Score: 186.51  E-value: 5.31e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390  423 HDYIKRINGKIATIIVIGDYEGIAILTYEGSE---ENSFVYLDKFAVLPHLKGSLGISDIIFNLMFKKFPNEILWRSRKD 499
Cdd:cd04266   1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPDgstPEKIAYLDKFAVLPKAQGSDGIADILFNAMLDGFPNELIWRSRKD 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6322390  500 NVVNKWYFQRSVAVLDLSIdldpehcdekqSQFKLFYYG 538
Cdd:cd04266  81 NPVNKWYFERSVGVLKLSG-----------SQWKLFWTG 108
 
Name Accession Description Interval E-value
DUF619-NAGS-FABP cd04266
DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; ...
 423-538 5.31e-57

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: 186.51  E-value: 5.31e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390  423 HDYIKRINGKIATIIVIGDYEGIAILTYEGSE---ENSFVYLDKFAVLPHLKGSLGISDIIFNLMFKKFPNEILWRSRKD 499
Cdd:cd04266   1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPDgstPEKIAYLDKFAVLPKAQGSDGIADILFNAMLDGFPNELIWRSRKD 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6322390  500 NVVNKWYFQRSVAVLDLSIdldpehcdekqSQFKLFYYG 538
Cdd:cd04266  81 NPVNKWYFERSVGVLKLSG-----------SQWKLFWTG 108
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 364-563 1.53e-54

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: 182.07  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390    364 GVHIKTYDYKTLTQFNSIGLPKKFHVPEKGAkpssnspkLDINKFKSIIDQSFKRSLDLHDYIKRINGKIATIIVIGDYE 443
Cdd:pfam04768   1 DLQKELFTDSGAGTLIRRGYKVLRRTSLEEL--------IDIERLRNLIERSFDGRLSVADYLDRLKGRLFKIYVDEPYE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390    444 GIAILTYEGSeenSFVYLDKFAVLPHLKGSlGISDIIFNLMFKKFPNeILWRSRKDNVVNKWYFQRSVAVLdlsidldpe 523
Cdd:pfam04768  73 ALAIVTKEDG---GVPYLDKFAVSKSGWGN-GVSDNVFNAIKKDFPK-LVWRSREDNPNNKWYFERSDGSL--------- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 6322390    524 hcdeKQSQFKLFYYGnpqyakraLRDKKRLREFMRSVRDI 563
Cdd:pfam04768 139 ----LKNGWVLFWYG--------IKDLNEVSELVASFRDI 166
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 403-538 1.01e-15

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 79.32  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390   403 LDINKFKSIIDQSFKRSLDlHDYIKRIngKIATIIVIGDYEGIAILTyegsEENSFVYLDKFAVLPHLKGSlGISDIIFN 482
Cdd:PRK04531 262 LDLERLNLLIESSFGRTLK-PDYFDTT--QLLRAYVSENYRAAAILT----ETGGGPYLDKFAVLDDARGE-GLGRAVWN 333

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322390   483 LMFKKFPnEILWRSRKDNVVNKWYFQRsvavldlsidldpehCD--EKQSQFKLFYYG 538
Cdd:PRK04531 334 VMREETP-QLFWRSRHNNTINKFYYAE---------------SDgcIKQEKWKVFWYG 375
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
403-538 1.80e-14

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


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 75.90  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390  403 LDINKFKSIIDQSFKRSLDlHDYIKRIngKIATIIVIGDYEGIAILTyegsEENSFVYLDKFAVLPHLKGSlGISDIIFN 482
Cdd:COG5630 301 LDLPRLRDLIESSFGRKLV-EGYFDKT--KFYRAYVSESYRAAAILT----LEDGVPYLDKFAVLDDAQGE-GLGRAVWQ 372

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322390  483 LMFKKFPnEILWRSRKDNVVNKWYFQRSvavlDLSIdldpehcdeKQSQFKLFYYG 538
Cdd:COG5630 373 RMREENP-QLFWRSRHDNPVNGFYFAEA----DGCY---------KQEKWTVFWYG 414
 
Name Accession Description Interval E-value
DUF619-NAGS-FABP cd04266
DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; ...
 423-538 5.31e-57

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: 186.51  E-value: 5.31e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390  423 HDYIKRINGKIATIIVIGDYEGIAILTYEGSE---ENSFVYLDKFAVLPHLKGSLGISDIIFNLMFKKFPNEILWRSRKD 499
Cdd:cd04266   1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPDgstPEKIAYLDKFAVLPKAQGSDGIADILFNAMLDGFPNELIWRSRKD 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6322390  500 NVVNKWYFQRSVAVLDLSIdldpehcdekqSQFKLFYYG 538
Cdd:cd04266  81 NPVNKWYFERSVGVLKLSG-----------SQWKLFWTG 108
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 364-563 1.53e-54

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: 182.07  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390    364 GVHIKTYDYKTLTQFNSIGLPKKFHVPEKGAkpssnspkLDINKFKSIIDQSFKRSLDLHDYIKRINGKIATIIVIGDYE 443
Cdd:pfam04768   1 DLQKELFTDSGAGTLIRRGYKVLRRTSLEEL--------IDIERLRNLIERSFDGRLSVADYLDRLKGRLFKIYVDEPYE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390    444 GIAILTYEGSeenSFVYLDKFAVLPHLKGSlGISDIIFNLMFKKFPNeILWRSRKDNVVNKWYFQRSVAVLdlsidldpe 523
Cdd:pfam04768  73 ALAIVTKEDG---GVPYLDKFAVSKSGWGN-GVSDNVFNAIKKDFPK-LVWRSREDNPNNKWYFERSDGSL--------- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 6322390    524 hcdeKQSQFKLFYYGnpqyakraLRDKKRLREFMRSVRDI 563
Cdd:pfam04768 139 ----LKNGWVLFWYG--------IKDLNEVSELVASFRDI 166
DUF619-NAGS cd04264
DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic ...
 423-538 3.84e-36

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: 130.18  E-value: 3.84e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390  423 HDYIKRINGKIATIIVIGdYEGIAILTYEGSEENsFVYLDKFAVLPHLKGsLGISDIIFNLMFKKFPnEILWRSRKDNVV 502
Cdd:cd04264   1 PDYIDRLQRLHAIYLSEG-YNAAAIVTYEGVNNG-VPYLDKFAVSSSAQG-EGTSDALWRRLRRDFP-KLFWRSRKTNPI 76

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6322390  503 NKWYFQRSVAVLdlsidldpehcdeKQSQFKLFYYG 538
Cdd:cd04264  77 NPWYFKRSDGSF-------------KNGQWKVFWYG 99
DUF619-like cd03173
DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; ...
 423-538 1.93e-31

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: 117.20  E-value: 1.93e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390  423 HDYIKRI-NGKIATIIVIGdYEGIAILTYEGseeNSFVYLDKFAVLPHLkGSLGISDIIFNLMFKKFPnEILWRSRKDNV 501
Cdd:cd03173   1 ASYLKRLkNGKFASYADEP-LEGVAIVTYEG---NSIPYLDKFAVSDHL-WLNNVTDNIFNLIRKDFP-SLLWRVRENDA 74

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6322390  502 VNKWYFQRSVAVLDLsidldpehcdekqSQFKLFYYG 538
Cdd:cd03173  75 NLKWYFSKSVGSLDK-------------NGFILFWYG 98
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 424-538 7.63e-16

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: 73.17  E-value: 7.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390  424 DYIKRINGKIATIIVIGDYEGIAILTYEgsEENSFVYLDKFAVLPHLKGsLGISDIIFNLMFKKFPnEILWRSRKDNVVN 503
Cdd:cd04265   2 DYFDSLQGRLHTIYLSEGYNAAAIVTNE--EVDGVPYLDKFAVSSSAQG-EGTGEALWRRLRRDFP-KLFWRSRSTNPIN 77

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6322390  504 KWYFQrsvavldlsidldpeHCD--EKQSQFKLFYYG 538
Cdd:cd04265  78 PWYFK---------------RCDgsFKNGHWTVFWYG 99
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 403-538 1.01e-15

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 79.32  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390   403 LDINKFKSIIDQSFKRSLDlHDYIKRIngKIATIIVIGDYEGIAILTyegsEENSFVYLDKFAVLPHLKGSlGISDIIFN 482
Cdd:PRK04531 262 LDLERLNLLIESSFGRTLK-PDYFDTT--QLLRAYVSENYRAAAILT----ETGGGPYLDKFAVLDDARGE-GLGRAVWN 333

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322390   483 LMFKKFPnEILWRSRKDNVVNKWYFQRsvavldlsidldpehCD--EKQSQFKLFYYG 538
Cdd:PRK04531 334 VMREETP-QLFWRSRHNNTINKFYYAE---------------SDgcIKQEKWKVFWYG 375
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
403-538 1.80e-14

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


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 75.90  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322390  403 LDINKFKSIIDQSFKRSLDlHDYIKRIngKIATIIVIGDYEGIAILTyegsEENSFVYLDKFAVLPHLKGSlGISDIIFN 482
Cdd:COG5630 301 LDLPRLRDLIESSFGRKLV-EGYFDKT--KFYRAYVSESYRAAAILT----LEDGVPYLDKFAVLDDAQGE-GLGRAVWQ 372

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322390  483 LMFKKFPnEILWRSRKDNVVNKWYFQRSvavlDLSIdldpehcdeKQSQFKLFYYG 538
Cdd:COG5630 373 RMREENP-QLFWRSRHDNPVNGFYFAEA----DGCY---------KQEKWTVFWYG 414
 
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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