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Conserved domains on  [gi|145698337|ref|NP_418394|]
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acetylglutamate kinase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

acetylglutamate kinase( domain architecture ID 10136257)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
 5-256 7.04e-146

AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK).


:

Pssm-ID: 239782 [Multi-domain]  Cd Length: 252  Bit Score: 407.95  E-value: 7.04e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   5 LIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTA 84
Cdd:cd04249    1 LVIKLGGALLETEAALEQLFSALSEYQQQHNRQLVIVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIPYITGALAGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  85 NKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQA 164
Cdd:cd04249   81 NKQLMAQAIKAGLKPVGLSLADGGMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPIISSIGADDQGQLMNVNADQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 165 ATALAATLGADLILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAEQLP 244
Cdd:cd04249  161 ATAIAQLLNADLVLLSDVSGVLDADKQLISELNAKQAAELIEQGVITDGMIVKVNAALDAAQSLRRGIDIASWQYPEQLT 240

                        250
                 ....*....|..
gi 145698337 245 ALFNGMPMGTRI 256
Cdd:cd04249  241 ALLAGEPVGTKI 252
 
Name Accession Description Interval E-value
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
 5-256 7.04e-146

AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239782 [Multi-domain]  Cd Length: 252  Bit Score: 407.95  E-value: 7.04e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   5 LIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTA 84
Cdd:cd04249    1 LVIKLGGALLETEAALEQLFSALSEYQQQHNRQLVIVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIPYITGALAGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  85 NKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQA 164
Cdd:cd04249   81 NKQLMAQAIKAGLKPVGLSLADGGMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPIISSIGADDQGQLMNVNADQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 165 ATALAATLGADLILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAEQLP 244
Cdd:cd04249  161 ATAIAQLLNADLVLLSDVSGVLDADKQLISELNAKQAAELIEQGVITDGMIVKVNAALDAAQSLRRGIDIASWQYPEQLT 240

                        250
                 ....*....|..
gi 145698337 245 ALFNGMPMGTRI 256
Cdd:cd04249  241 ALLAGEPVGTKI 252
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 1-258 7.05e-112

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 323.21  E-value: 7.05e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   1 MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGAL 80
Cdd:PRK00942  22 MGKTIVIKYGGNAMTDEELKEAFARDIVLLKQVGINP-VVVHGGGPQIDELLKKLGIESEFVNGLRVTDAETMEVVEMVL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  81 AGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQL--DEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMN 158
Cdd:PRK00942 101 AGKVNKELVSLINKHGGKAVGLSGKDGGLITAKKLeeDEDLGFVGEVTPVNPALLEALLEAGYIPVISPIGVGEDGETYN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 159 VNADQAATALAATLGAD-LILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASW 237
Cdd:PRK00942 181 INADTAAGAIAAALGAEkLILLTDVPGVLDDKGQLISELTASEAEELIEDGVITGGMIPKVEAALDAARGGVRSVHIIDG 260

                        250       260
                 ....*....|....*....|..
gi 145698337 238 RHAEQ-LPALFNGMPMGTRILA 258
Cdd:PRK00942 261 RVPHAlLLELFTDEGIGTMIVP 282
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 4-234 7.04e-84

acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273256 [Multi-domain]  Cd Length: 231  Bit Score: 250.28  E-value: 7.04e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337    4 PLIIKLGGVLLDSEeaLERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGT 83
Cdd:TIGR00761   1 TIVIKIGGAAISDL--LEAFASDIAFLRAVGIKP-VIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVLIGQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   84 ANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEE-LGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNAD 162
Cdd:TIGR00761  78 VNKELVALLNKHGINAIGLTGGDGQLFTARYLDKEdLGYVGEIKKVNKALIEALLKAGYIPVISSLALTAEGQALNVNAD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145698337  163 QAATALAATLGAD-LILLSDVSGILDGKGQ-RIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDI 234
Cdd:TIGR00761 158 TAAGALAAALGAEkLVLLTDVPGILNGDGQsLISEIPLDEIEQLIKQGIIKGGMIPKVNAALEALRGGVRSVHI 231
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 4-256 4.92e-72

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: 221.83  E-value: 4.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   4 PLIIKLGGVLLDSEEALERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGT 83
Cdd:COG0548   25 TFVIKYGGEAMEDEELKAALAQDIALLKSLGIRP-VLVHGGGPQINELLKRLGIESEFVNGLRVTDEETLEVVEMVLAGK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  84 ANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQL----DEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNV 159
Cdd:COG0548  104 VNKEIVALLSQGGGNAVGLSGKDGNLITARPLgvgdGVDLGHVGEVRRVDPELIRALLDAGYIPVISPIGYSPTGEVYNI 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 160 NADQAATALAATLGAD-LILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWR 238
Cdd:COG0548  184 NADTVAGAIAAALKAEkLILLTDVPGVLDDPGSLISELTAAEAEELIADGVISGGMIPKLEAALDAVRGGVKRVHIIDGR 263

                        250
                 ....*....|....*....
gi 145698337 239 HAEQLPA-LFNGMPMGTRI 256
Cdd:COG0548  264 VPHALLLeLFTDDGIGTMI 282
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-236 1.59e-34

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: 124.02  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337    3 NPLIIKLGGVLLDSEEALERLFSALVNYRESHqRPLVIVHGGGCVVDELMKGLNLPVKKKNglrVTPADQIDIITGALAG 82
Cdd:pfam00696   1 KRVVIKLGGSSLTDKERLKRLADEIAALLEEG-RKLVVVHGGGAFADGLLALLGLSPRFAR---LTDAETLEVATMDALG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   83 TANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELGHVglaqpgSPKLINSLLENGYLPVVSS-IGVTDEGQLMNVNA 161
Cdd:pfam00696  77 SLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRI------DTEALEELLEAGVVPVITGfIGIDPEGELGRGSS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  162 DQAATALAATLGAD-LILLSDVSGILDG------KGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDI 234
Cdd:pfam00696 151 DTLAALLAEALGADkLIILTDVDGVYTAdprkvpDAKLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVI 230


                  ..
gi 145698337  235 AS 236
Cdd:pfam00696 231 VN 232
 
Name Accession Description Interval E-value
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
 5-256 7.04e-146

AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239782 [Multi-domain]  Cd Length: 252  Bit Score: 407.95  E-value: 7.04e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   5 LIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTA 84
Cdd:cd04249    1 LVIKLGGALLETEAALEQLFSALSEYQQQHNRQLVIVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIPYITGALAGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  85 NKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQA 164
Cdd:cd04249   81 NKQLMAQAIKAGLKPVGLSLADGGMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPIISSIGADDQGQLMNVNADQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 165 ATALAATLGADLILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAEQLP 244
Cdd:cd04249  161 ATAIAQLLNADLVLLSDVSGVLDADKQLISELNAKQAAELIEQGVITDGMIVKVNAALDAAQSLRRGIDIASWQYPEQLT 240

                        250
                 ....*....|..
gi 145698337 245 ALFNGMPMGTRI 256
Cdd:cd04249  241 ALLAGEPVGTKI 252
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 1-258 7.05e-112

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 323.21  E-value: 7.05e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   1 MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGAL 80
Cdd:PRK00942  22 MGKTIVIKYGGNAMTDEELKEAFARDIVLLKQVGINP-VVVHGGGPQIDELLKKLGIESEFVNGLRVTDAETMEVVEMVL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  81 AGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQL--DEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMN 158
Cdd:PRK00942 101 AGKVNKELVSLINKHGGKAVGLSGKDGGLITAKKLeeDEDLGFVGEVTPVNPALLEALLEAGYIPVISPIGVGEDGETYN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 159 VNADQAATALAATLGAD-LILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASW 237
Cdd:PRK00942 181 INADTAAGAIAAALGAEkLILLTDVPGVLDDKGQLISELTASEAEELIEDGVITGGMIPKVEAALDAARGGVRSVHIIDG 260

                        250       260
                 ....*....|....*....|..
gi 145698337 238 RHAEQ-LPALFNGMPMGTRILA 258
Cdd:PRK00942 261 RVPHAlLLELFTDEGIGTMIVP 282
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 5-256 4.06e-87

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: 259.36  E-value: 4.06e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   5 LIIKLGGVLLDSEEALERLFSALVNYReSHQRPLVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTA 84
Cdd:cd04238    1 VVIKYGGSAMKDEELKEAFADDIVLLK-QVGINPVIVHGGGPEINELLKRLGIESEFVNGLRVTDKETMEIVEMVLAGKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  85 NKTLLAWAKKHQIAAVGLFLGDGDSVKVTQL---DEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNA 161
Cdd:cd04238   80 NKELVSLLNRAGGKAVGLSGKDGGLIKAEKKeekDIDLGFVGEVTEVNPELLETLLEAGYIPVIAPIAVDEDGETYNVNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 162 DQAATALAATLGAD-LILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHA 240
Cdd:cd04238  160 DTAAGAIAAALKAEkLILLTDVPGVLDDPGSLISELTPKEAEELIEDGVISGGMIPKVEAALEALEGGVRKVHIIDGRVP 239

                        250
                 ....*....|....*..
gi 145698337 241 EQLPA-LFNGMPMGTRI 256
Cdd:cd04238  240 HSLLLeLFTDEGIGTMI 256
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 4-234 7.04e-84

acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273256 [Multi-domain]  Cd Length: 231  Bit Score: 250.28  E-value: 7.04e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337    4 PLIIKLGGVLLDSEeaLERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGT 83
Cdd:TIGR00761   1 TIVIKIGGAAISDL--LEAFASDIAFLRAVGIKP-VIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVLIGQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   84 ANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEE-LGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNAD 162
Cdd:TIGR00761  78 VNKELVALLNKHGINAIGLTGGDGQLFTARYLDKEdLGYVGEIKKVNKALIEALLKAGYIPVISSLALTAEGQALNVNAD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145698337  163 QAATALAATLGAD-LILLSDVSGILDGKGQ-RIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDI 234
Cdd:TIGR00761 158 TAAGALAAALGAEkLVLLTDVPGILNGDGQsLISEIPLDEIEQLIKQGIIKGGMIPKVNAALEALRGGVRSVHI 231
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 4-256 4.92e-72

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: 221.83  E-value: 4.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   4 PLIIKLGGVLLDSEEALERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGT 83
Cdd:COG0548   25 TFVIKYGGEAMEDEELKAALAQDIALLKSLGIRP-VLVHGGGPQINELLKRLGIESEFVNGLRVTDEETLEVVEMVLAGK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  84 ANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQL----DEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNV 159
Cdd:COG0548  104 VNKEIVALLSQGGGNAVGLSGKDGNLITARPLgvgdGVDLGHVGEVRRVDPELIRALLDAGYIPVISPIGYSPTGEVYNI 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 160 NADQAATALAATLGAD-LILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWR 238
Cdd:COG0548  184 NADTVAGAIAAALKAEkLILLTDVPGVLDDPGSLISELTAAEAEELIADGVISGGMIPKLEAALDAVRGGVKRVHIIDGR 263

                        250
                 ....*....|....*....
gi 145698337 239 HAEQLPA-LFNGMPMGTRI 256
Cdd:COG0548  264 VPHALLLeLFTDDGIGTMI 282
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 6-256 1.57e-44

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: 150.29  E-value: 1.57e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   6 IIKLGGVLLDSEEALERLFSALVNYReSHQRPLVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALaGTAN 85
Cdd:cd02115    1 VIKFGGSSVSSEERLRNLARILVKLA-SEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDALAAMGE-GMSN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  86 KTLLAWAKKHQIAAVGLFLGDGDSvkvtqLDEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDE---GQLMNVNAD 162
Cdd:cd02115   79 LLIAAALEQHGIKAVPLDLTQAGF-----ASPNQGHVGKITKVSTDRLKSLLENGILPILSGFGGTDEketGTLGRGGSD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 163 QAATALAATLGAD-LILLSDVSGILDG------KGQRIAEMTAAKAEQLIEQGIitdgMIVKVNAAlDAARTLGRPVDIA 235
Cdd:cd02115  154 STAALLAAALKADrLVILTDVDGVYTAdprkvpDAKLLSELTYEEAAELAYAGA----MVLKPKAA-DPAARAGIPVRIA 228

                        250       260
                 ....*....|....*....|.
gi 145698337 236 SWRHAEQLpALFNGMPMGTRI 256
Cdd:cd02115  229 NTENPGAL-ALFTPDGGGTLI 248
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 6-226 1.63e-42

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: 146.11  E-value: 1.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   6 IIKLGGVLLDSEEALERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTAN 85
Cdd:cd04250   18 VIKYGGNAMKDEELKESFARDIVLLKYVGINP-VVVHGGGPEINEMLKKLGIESEFVNGLRVTDEETMEIVEMVLVGKVN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  86 KTLLAWAKKHQIAAVGLFLGDGDSVKVTQLD-------EELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMN 158
Cdd:cd04250   97 KEIVSLINRAGGKAVGLSGKDGNLIKAKKKDatvieeiIDLGFVGEVTEVNPELLETLLEAGYIPVIAPVGVGEDGETYN 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145698337 159 VNADQAATALAATLGAD-LILLSDVSGILDG---KGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAAR 226
Cdd:cd04250  177 INADTAAGAIAAALKAEkLILLTDVAGVLDDpndPGSLISEISLKEAEELIADGIISGGMIPKVEACIEALE 248
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-236 1.59e-34

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: 124.02  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337    3 NPLIIKLGGVLLDSEEALERLFSALVNYRESHqRPLVIVHGGGCVVDELMKGLNLPVKKKNglrVTPADQIDIITGALAG 82
Cdd:pfam00696   1 KRVVIKLGGSSLTDKERLKRLADEIAALLEEG-RKLVVVHGGGAFADGLLALLGLSPRFAR---LTDAETLEVATMDALG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   83 TANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELGHVglaqpgSPKLINSLLENGYLPVVSS-IGVTDEGQLMNVNA 161
Cdd:pfam00696  77 SLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRI------DTEALEELLEAGVVPVITGfIGIDPEGELGRGSS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  162 DQAATALAATLGAD-LILLSDVSGILDG------KGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDI 234
Cdd:pfam00696 151 DTLAALLAEALGADkLIILTDVDGVYTAdprkvpDAKLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVI 230


                  ..
gi 145698337  235 AS 236
Cdd:pfam00696 231 VN 232
PLN02512 PLN02512
acetylglutamate kinase
 5-225 2.19e-32

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 120.18  E-value: 2.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   5 LIIKLGGVLLDSEEALERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTA 84
Cdd:PLN02512  50 VVVKYGGAAMKDPELKAGVIRDLVLLSCVGLRP-VLVHGGGPEINSWLKKVGIEPQFKNGLRVTDAETMEVVEMVLVGKV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  85 NKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEE--LGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNAD 162
Cdd:PLN02512 129 NKSLVSLINKAGGTAVGLSGKDGRLLRARPSPNSadLGFVGEVTRVDPTVLRPLVDDGHIPVIATVAADEDGQAYNINAD 208

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145698337 163 QAATALAATLGAD-LILLSDVSGILDGK---GQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAA 225
Cdd:PLN02512 209 TAAGEIAAALGAEkLILLTDVAGVLEDKddpGSLVKELDIKGVRKLIADGKIAGGMIPKVECCVRSL 275
argB CHL00202
acetylglutamate kinase; Provisional
 5-224 2.63e-31

acetylglutamate kinase; Provisional


Pssm-ID: 133644 [Multi-domain]  Cd Length: 284  Bit Score: 116.82  E-value: 2.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   5 LIIKLGGVLLDSEEALERLFSALVNYRESHQRPlVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTA 84
Cdd:CHL00202  26 MVIKYGGAAMKNLILKADIIKDILFLSCIGLKI-VVVHGGGPEINFWLKQLNISPKFWNGIRVTDKVTMEIVEMVLAGKV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  85 NKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDE-ELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQ 163
Cdd:CHL00202 105 NKDLVGSINANGGKAVGLCGKDANLIVARASDKkDLGLVGEIQQVDPQLIDMLLEKNYIPVIASVAADHDGQTYNINADV 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145698337 164 AATALAATLGAD-LILLSDVSGILDGKGQR---IAEMTAAKAEQLIEQGIITDGMIVKVNAALDA 224
Cdd:CHL00202 185 VAGEIAAKLNAEkLILLTDTPGILADINDPnslISTLNIKEARNLASTGIISGGMIPKVNCCIRA 249
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 6-249 7.00e-22

AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239784 [Multi-domain]  Cd Length: 257  Bit Score: 91.28  E-value: 7.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   6 IIKLGGVLLDSeeaLERLFSALVNYREshqrPLVIVHGGGCVVDELMKGLNLP---VKKKNGL--RVTPADQIDIITGAL 80
Cdd:cd04251    2 VVKIGGSVVSD---LDKVIDDIANFGE----RLIVVHGGGNYVNEYLKRLGVEpkfVTSPSGIrsRYTDKETLEVFVMVM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  81 aGTANKTLLAWAKKHQIAAVGLFLGDG--------DSVKVTQLDEEL----GHVGLAQPGSPKLINSLLENGYLPVVSSI 148
Cdd:cd04251   75 -GLINKKIVARLHSLGVKAVGLTGLDGrlleakrkEIVRVNERGRKMiirgGYTGKVEKVNSDLIEALLDAGYLPVVSPV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 149 GVTDEGQLMNVNADQAATALAATLGAD-LILLSDVSGILdGKGQRIAEMTAAKAEQLIEQgiITDGMIVKVNAALDAART 227
Cdd:cd04251  154 AYSEEGEPLNVDGDRAAAAIAAALKAErLILLTDVEGLY-LDGRVIERITVSDAESLLEK--AGGGMKRKLLAAAEAVEG 230

                        250       260
                 ....*....|....*....|..
gi 145698337 228 LGRPVDIASWRHAEQLPALFNG 249
Cdd:cd04251  231 GVREVVIGDARADSPISSALNG 252
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
4-225 3.75e-21

[LysW]-aminoadipate/[LysW]-glutamate kinase;


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 89.57  E-value: 3.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   4 PLIIKLGG-VLLDSEEALERLFSalvNYRESHQrpLVIVHGGGCVVDELMKGLNLPVKK---KNGL--RVTPADQIDIIT 77
Cdd:PRK14058   1 MIVVKIGGsVGIDPEDALIDVAS---LWADGER--VVLVHGGSDEVNELLERLGIEPRFvtsPSGVtsRYTDRETLEVFI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  78 GALAgTANKTLLAWAKKHQIAAVGLFLGDGDSV------KVTQLDE------ELGHVGLAQPGSPKLINSLLENGYLPVV 145
Cdd:PRK14058  76 MAMA-LINKQLVERLQSLGVNAVGLSGLDGGLLegkrkkAVRVVEEgkkkiiRGDYTGKIEEVNTDLLKLLLKAGYLPVV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 146 SSIGVTDEGQLMNVNADQAATALAATLGAD-LILLSDVSGIL---DGKGQRIAEMTAAKAEQLIEQgiITDGMIVKVNAA 221
Cdd:PRK14058 155 APPALSEEGEPLNVDGDRAAAAIAGALKAEaLVLLSDVPGLLrdpPDEGSLIERITPEEAEELSKA--AGGGMKKKVLMA 232


                 ....
gi 145698337 222 LDAA 225
Cdd:PRK14058 233 AEAV 236
AAK_NAGK-fArgBP cd04252
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ...
 6-256 2.31e-19

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: 84.35  E-value: 2.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   6 IIKLGGVLLdsEEALERLFSALVNYRESHQRPLViVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIitgalagtAN 85
Cdd:cd04252    2 VIKVGGAII--EDDLDELAASLSFLQHVGLYPIV-VHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAV--------AR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  86 KTLLAWAKKhQIAAVGLFLGDGDSV-----KVTQLDEEL-GHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNV 159
Cdd:cd04252   71 KVFLEENLK-LVEALERNGARARPItsgvfEAEYLDKDKyGLVGKITGVNKAPIEAAIRAGYLPILTSLAETPSGQLLNV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 160 NADQAATALAATLG-ADLILLSDVSGILDGKGQRIAEMT-AAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASW 237
Cdd:cd04252  150 NADVAAGELARVLEpLKIVFLNETGGLLDGTGKKISAINlDEEYDDLMKQPWVKYGTKLKIKEIKELLDTLPRSSSVSIT 229

                        250
                 ....*....|....*....
gi 145698337 238 RHAEQLPALFNGMPMGTRI 256
Cdd:cd04252  230 SPDDLQKELFTHSGAGTLI 248
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 6-218 2.89e-10

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 59.68  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   6 IIKLGGVLLdsEEALERLFSALVNYRESHQRPLViVHGGGCVVDELMKGLNLPVKKKNGLRVTpADQIDIITGALAGTAN 85
Cdd:PRK04531  40 VIKVGGAVL--RDDLEALASSLSFLQEVGLTPIV-VHGAGPQLDAELDAAGIEKETVNGLRVT-SPEALAIVRKVFQRSN 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  86 KTLlawakkhqIAAVGlflgdgdsvkvtqldeelghvglaqpgspklinSLLENGYLPVVSSIGVTDEGQLMNVNADQAA 165
Cdd:PRK04531 116 LDL--------VEAVE---------------------------------SSLRAGSIPVIASLGETPSGQILNINADVAA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145698337 166 TALAATLG-ADLILLSDVSGILDGKGQRIAEMT-AAKAEQLIEQGIITDGMIVKV 218
Cdd:PRK04531 155 NELVSALQpYKIIFLTGTGGLLDADGKLISSINlSTEYDHLMQQPWINGGMKLKL 209
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
6-256 1.15e-07

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 51.37  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   6 IIKLGG-VLLDS-------EEALERLFSALvnyRESHQRPLVIVHGGGC----VVDELmkGLNLPVKKKN--GLRVTPAD 71
Cdd:COG1608    3 VLKLGGsVITDKdkpetvrRDALERIAREI---AAALDLDLVIVHGGGSfghpVAKKY--GLHGTLGTEDaeGVSETHRA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  72 QI---DIITGALAgtanktllawakKHQIAAVGL-----FLGDGDsvKVTQLDEElghvglaqpgspkLINSLLENGYLP 143
Cdd:COG1608   78 MRelnRIVVDALL------------EAGVPAVSVppssfAVRDNG--RILSFDTE-------------PIKEMLEEGFVP 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 144 VVSSIGVTDEG---------QLMN-----VNADQaatalaatlgadLILLSDVSGILD--GKGQRIAEMTAAKAEQLIEQ 207
Cdd:COG1608  131 VLHGDVVFDAErgftilsgdEIVVylakeLKPER------------VGLATDVDGVYDddPKGKLIPEITRSNFDEVLDA 198

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145698337 208 GI------ITDGMIVKVNAALDAARTlGRPVDIASWRHAEQL-PALFNGMPMGTRI 256
Cdd:COG1608  199 LGgsagtdVTGGMAGKVEELLELAKP-GVEVYIFNGNKPGNLsAALRGEEVRGTRI 253
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 38-207 2.03e-06

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 48.22  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  38 LVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDI-----------ITGALAGTANKTLLAWAkkhQIAAV-GLF-- 103
Cdd:PRK05279  59 LVLVHGARPQIEEQLAARGIEPRYHKGLRVTDAAALECvkqaagelrldIEARLSMGLPNTPMAGA---HIRVVsGNFvt 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 104 ---LG--DG-D---SVKVTQLDEELghvglaqpgspklINSLLENGYLPVVSSIGVTDEGQLMNVNADQAATALAATLGA 174
Cdd:PRK05279 136 arpLGvdDGvDyqhTGEVRRIDAEA-------------IRRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKA 202

                        170       180       190
                 ....*....|....*....|....*....|....
gi 145698337 175 D-LILLSDVSGILDGKGQRIAEMTAAKAEQLIEQ 207
Cdd:PRK05279 203 DkLIFFTESQGVLDEDGELIRELSPNEAQALLEA 236
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 38-226 2.33e-05

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: 44.47  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  38 LVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGAlAGTANKTLLA----------WAKKHQIAAVGLF---- 103
Cdd:cd04237   52 LVLVHGARPQIDQRLAERGLEPRYHRGLRITDAAALECVKEA-AGAVRLEIEAllsmglpnspMAGARIRVVSGNFvtar 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 104 -LGDGDSVkvtqldeELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQAATALAATLGAD-LILLSD 181
Cdd:cd04237  131 pLGVVDGV-------DFGHTGEVRRIDADAIRRQLDQGSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADkLIFLTD 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 145698337 182 VSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVK-VNAALDAAR 226
Cdd:cd04237  204 GPGLLDDDGELIRELTAQEAEALLETGALLTNDTARlLQAAIEACR 249
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 6-256 2.36e-05

AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239774 [Multi-domain]  Cd Length: 252  Bit Score: 44.56  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   6 IIKLGG-VLLDS-------EEALERLFSALVNYREshqRPLVIVHGGGC----VVDELMKGLNLPVKKKNGLRVTPADQI 73
Cdd:cd04241    3 ILKLGGsVITDKdrpetirEENLERIARELAEAID---EKLVLVHGGGSfghpKAKEYGLPDGDGSFSAEGVAETHEAML 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  74 ---DIITGALAgtanktllawakKHQIAAVGLFLGdgdSVKVTqldeELGHVGLAqpgSPKLINSLLENGYLPVVSSIGV 150
Cdd:cd04241   80 elnSIVVDALL------------EAGVPAVSVPPS---SFFVT----ENGRIVSF---DLEVIKELLDRGFVPVLHGDVV 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 151 TDEGQLMNV-NADQAATALAATLGAD-LILLSDVSGILD---GKGQRIAEMTAAKAEQLIEQGI-----ITDGMIVKVNA 220
Cdd:cd04241  138 LDEGGGITIlSGDDIVVELAKALKPErVIFLTDVDGVYDkppPDAKLIPEIDVGSLEDILAALGsagtdVTGGMAGKIEE 217

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 145698337 221 ALDAARtLGRPVDIASWRHAEQLPALFNGMPMGTRI 256
Cdd:cd04241  218 LLELAR-RGIEVYIFNGDKPENLYRALLGNFIGTRI 252
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 133-257 4.22e-05

AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.


Pssm-ID: 239775 [Multi-domain]  Cd Length: 251  Bit Score: 43.59  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 133 INSLLENGYLPVV--------SSIGVTDEGQL------MnVNADQaatalaatlgadLILLSDVSGILDGKG------QR 192
Cdd:cd04242  116 LETLLELGVIPIInendtvatEEIRFGDNDRLsalvagL-VNADL------------LILLSDVDGLYDKNPrenpdaKL 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145698337 193 IAEMTAAKAEqlIEQGII-------TDGMIVKVNAALDAARtLGRPVDIASWRHAEQLPALFNGMPMGTRIL 257
Cdd:cd04242  183 IPEVEEITDE--IEAMAGgsgssvgTGGMRTKLKAARIATE-AGIPVVIANGRKPDVLLDILAGEAVGTLFL 251
N-Ac-Glu-synth TIGR01890
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ...
 38-206 6.09e-05

amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273856 [Multi-domain]  Cd Length: 429  Bit Score: 43.63  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337   38 LVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDI-----------ITGALAGTANKTLLAWAKkhqiaaVGLFLGD 106
Cdd:TIGR01890  51 LVLVHGARPQIERILAARGRTPHYHRGLRVTDEASLEQaqqaagtlrlaIEARLSMSLSNTPMAGSR------LPVVSGN 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  107 GDSVKVTQLDE--ELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQAATALAATLGAD-LILLSDVS 183
Cdd:TIGR01890 125 FVTARPIGVIEgvDYEHTGVIRKIDTEGIRRQLDAGSIVLLSPLGHSPTGETFNLDMEDVATSVAISLKADkLIYFTLSP 204

                         170       180
                  ....*....|....*....|...
gi 145698337  184 GILDGKGQRIAEMTAAKAEQLIE 206
Cdd:TIGR01890 205 GISDPDGTLAAELSPQEVESLAE 227
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 131-256 7.38e-04

AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239768  Cd Length: 308  Bit Score: 40.19  E-value: 7.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 131 KLINSLLENGYLPVVSSIG----VTDEGQLMNV-----------------NADQaatalaatlgadLILLSDVSGI-LD- 187
Cdd:cd04235  172 EAIKTLVDNGVIVIAAGGGgipvVREGGGLKGVeavidkdlasallaeeiNADL------------LVILTDVDNVyINf 239

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145698337 188 GK-GQR-IAEMTAAKAEQLIEQGIITDG-MIVKVNAALDAARTLGRPVDIASwrhAEQLPALFNGMpMGTRI 256
Cdd:cd04235  240 GKpNQKaLEQVTVEELEKYIEEGQFAPGsMGPKVEAAIRFVESGGKKAIITS---LENAEAALEGK-AGTVI 307
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 176-254 1.53e-03

AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia.


Pssm-ID: 239789 [Multi-domain]  Cd Length: 284  Bit Score: 38.95  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 176 LILLSDVSGILDG----KGQRIAEMTAAKAEQLIEQG----IITDGMIVKVNAALDAARTlGRPVDIASWRHAEQLPALF 247
Cdd:cd04256  196 LILLSDVDGLYDGppgsDDAKLIHTFYPGDQQSITFGtksrVGTGGMEAKVKAALWALQG-GTSVVITNGMAGDVITKIL 274


                 ....*..
gi 145698337 248 NGMPMGT 254
Cdd:cd04256  275 EGKKVGT 281
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 176-254 2.06e-03

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 39.32  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337 176 LILLSDVSGILDG-----KGQRIAEMTAAKAEQLIEQGIITD----GMIVKVNAALDAARTlGRPVDIASWRHAEQLPAL 246
Cdd:PLN02418 193 LILLSDVEGLYTGppsdpSSKLIHTYIKEKHQDEITFGEKSRvgrgGMTAKVKAAVNAASA-GIPVVITSGYALDNIRKV 271


                 ....*...
gi 145698337 247 FNGMPMGT 254
Cdd:PLN02418 272 LRGERVGT 279
AAK_NAGS-Urea cd04236
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 13-193 3.37e-03

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: 37.90  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  13 LLDSEEALERLFSALVNYRESHQRPLViVHGGGCVVDELMKGLNLPVKKKnglRVTpadqidiitgalagTANKTLLAWA 92
Cdd:cd04236   46 VFRSLEMVQSLSFGLAFLQRMDMKLLV-VMGLSAPDGTNMSDLELQAARS---RLV--------------KDCKTLVEAL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  93 KKHQIAAVGLFLGDGdsvkVTQLDEELGHVglAQPGSPKLINSLLE----NGYLPVVSSIGVTDEGQLMNVNADQAATAL 168
Cdd:cd04236  108 QANSAAAHPLFSGES----VLQAEEPEPGA--SKGPSVSVDTELLQwclgSGHIPLVCPIGETSSGRSVSLDSSEVTTAI 181

                        170       180
                 ....*....|....*....|....*.
gi 145698337 169 AATLG-ADLILLSDVSGILDGKGQRI 193
Cdd:cd04236  182 AKALQpIKVIFLNRSGGLRDQKHKVL 207
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 176-254 4.82e-03

delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130164 [Multi-domain]  Cd Length: 715  Bit Score: 37.97  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698337  176 LILLSDVSGILDG-KGQRIAEM--TAAKAEQlieQGIIT---------DGMIVKVNAALDAARTlGRPVDIASWRHAEQL 243
Cdd:TIGR01092 185 LILLSDVEGLYDGpPSDDDSKLidTFYKEKH---QGEITfgtksrlgrGGMTAKVKAAVWAAYG-GTPVIIASGTAPKNI 260

                          90
                  ....*....|.
gi 145698337  244 PALFNGMPMGT 254
Cdd:TIGR01092 261 TKVVEGKKVGT 271
 
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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