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Conserved domains on  [gi|1589248809|gb|TCV11464|]
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N-acetylglutamate kinase [Vibrio crassostreae]

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 ...
 8-259 2.46e-137

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: 386.77  E-value: 2.46e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   8 LIIKLGGAALSCGETLSKLFGAISAYQQQAQRPIVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALAGTA 87
Cdd:cd04249     1 LVIKLGGALLETEAALEQLFSALSEYQQQHNRQLVIVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIPYITGALAGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  88 NKLLQGQAIKDGINAVGLSLADGGLCKVSELNPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNADQA 167
Cdd:cd04249    81 NKQLMAQAIKAGLKPVGLSLADGGMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPIISSIGADDQGQLMNVNADQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 168 AVAVAGALDAELVLLSDVSGVLDGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVATWRYPEKLT 247
Cdd:cd04249   161 ATAIAQLLNADLVLLSDVSGVLDADKQLISELNAKQAAELIEQGVITDGMIVKVNAALDAAQSLRRGIDIASWQYPEQLT 240

                         250
                  ....*....|..
gi 1589248809 248 QLFSGKSIGTQF 259
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 ...
 8-259 2.46e-137

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: 386.77  E-value: 2.46e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   8 LIIKLGGAALSCGETLSKLFGAISAYQQQAQRPIVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALAGTA 87
Cdd:cd04249     1 LVIKLGGALLETEAALEQLFSALSEYQQQHNRQLVIVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIPYITGALAGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  88 NKLLQGQAIKDGINAVGLSLADGGLCKVSELNPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNADQA 167
Cdd:cd04249    81 NKQLMAQAIKAGLKPVGLSLADGGMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPIISSIGADDQGQLMNVNADQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 168 AVAVAGALDAELVLLSDVSGVLDGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVATWRYPEKLT 247
Cdd:cd04249   161 ATAIAQLLNADLVLLSDVSGVLDADKQLISELNAKQAAELIEQGVITDGMIVKVNAALDAAQSLRRGIDIASWQYPEQLT 240

                         250
                  ....*....|..
gi 1589248809 248 QLFSGKSIGTQF 259
Cdd:cd04249   241 ALLAGEPVGTKI 252
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 1-262 1.10e-112

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 325.52  E-value: 1.10e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   1 MSLNNQPLIIKLGGAALSCGETLSKLFGAISAYQQQAQRPiVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIA 80
Cdd:PRK00942   19 QRFMGKTIVIKYGGNAMTDEELKEAFARDIVLLKQVGINP-VVVHGGGPQIDELLKKLGIESEFVNGLRVTDAETMEVVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  81 GALAGTANKLLQGQAIKDGINAVGLSLADGGLCKVSEL--NPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQ 158
Cdd:PRK00942   98 MVLAGKVNKELVSLINKHGGKAVGLSGKDGGLITAKKLeeDEDLGFVGEVTPVNPALLEALLEAGYIPVISPIGVGEDGE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 159 LMNVNADQAAVAVAGALDAE-LVLLSDVSGVLDGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEV 237
Cdd:PRK00942  178 TYNINADTAAGAIAAALGAEkLILLTDVPGVLDDKGQLISELTASEAEELIEDGVITGGMIPKVEAALDAARGGVRSVHI 257

                         250       260
                  ....*....|....*....|....*.
gi 1589248809 238 ATWRYPEK-LTQLFSGKSIGTQFLPQ 262
Cdd:PRK00942  258 IDGRVPHAlLLELFTDEGIGTMIVPD 283
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 5-259 5.33e-84

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: 252.65  E-value: 5.33e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   5 NQPLIIKLGGAALSCGETLSKLFGAISAYQQQAQRPiVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALA 84
Cdd:COG0548    23 GKTFVIKYGGEAMEDEELKAALAQDIALLKSLGIRP-VLVHGGGPQINELLKRLGIESEFVNGLRVTDEETLEVVEMVLA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  85 GTANKLLQGQAIKDGINAVGLSLADGGLCKVSEL----NPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLM 160
Cdd:COG0548   102 GKVNKEIVALLSQGGGNAVGLSGKDGNLITARPLgvgdGVDLGHVGEVRRVDPELIRALLDAGYIPVISPIGYSPTGEVY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 161 NVNADQAAVAVAGALDAE-LVLLSDVSGVLDGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVAT 239
Cdd:COG0548   182 NINADTVAGAIAAALKAEkLILLTDVPGVLDDPGSLISELTAAEAEELIADGVISGGMIPKLEAALDAVRGGVKRVHIID 261

                         250       260
                  ....*....|....*....|.
gi 1589248809 240 WRYPEKLTQ-LFSGKSIGTQF 259
Cdd:COG0548   262 GRVPHALLLeLFTDDGIGTMI 282
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 7-234 1.38e-63

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: 198.66  E-value: 1.38e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   7 PLIIKLGGAALScgETLSKLFGAISAYQQQAQRPiVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALAGT 86
Cdd:TIGR00761   1 TIVIKIGGAAIS--DLLEAFASDIAFLRAVGIKP-VIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVLIGQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  87 ANKLLQGQAIKDGINAVGLSLADGGLCKVSELNPE-LGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNAD 165
Cdd:TIGR00761  78 VNKELVALLNKHGINAIGLTGGDGQLFTARYLDKEdLGYVGEIKKVNKALIEALLKAGYIPVISSLALTAEGQALNVNAD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589248809 166 QAAVAVAGALDAE-LVLLSDVSGVLDG-KGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRP 234
Cdd:TIGR00761 158 TAAGALAAALGAEkLVLLTDVPGILNGdGQSLISEIPLDEIEQLIKQGIIKGGMIPKVNAALEALRGGVRS 228
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 8-238 1.30e-36

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: 129.41  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   8 LIIKLGGAALSCGETLSKLFGAISAYQQQaQRPIVIVHGGGYLVDDLMNKLNLETVKKeglRVTPYDQIPVIAGALAGTA 87
Cdd:pfam00696   3 VVIKLGGSSLTDKERLKRLADEIAALLEE-GRKLVVVHGGGAFADGLLALLGLSPRFA---RLTDAETLEVATMDALGSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  88 NKLLQGQAIKDGINAVGLSLADGGLCKVSELNPELGAVgkaepgDSTVLQAILNAGALPIISS-IGLTEQGQLMNVNADQ 166
Cdd:pfam00696  79 GERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRI------DTEALEELLEAGVVPVITGfIGIDPEGELGRGSSDT 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589248809 167 AAVAVAGALDAE-LVLLSDVSGVLDGKGH------LIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVA 238
Cdd:pfam00696 153 LAALLAEALGADkLIILTDVDGVYTADPRkvpdakLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVIV 231
 
Name Accession Description Interval E-value
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
 8-259 2.46e-137

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: 386.77  E-value: 2.46e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   8 LIIKLGGAALSCGETLSKLFGAISAYQQQAQRPIVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALAGTA 87
Cdd:cd04249     1 LVIKLGGALLETEAALEQLFSALSEYQQQHNRQLVIVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIPYITGALAGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  88 NKLLQGQAIKDGINAVGLSLADGGLCKVSELNPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNADQA 167
Cdd:cd04249    81 NKQLMAQAIKAGLKPVGLSLADGGMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPIISSIGADDQGQLMNVNADQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 168 AVAVAGALDAELVLLSDVSGVLDGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVATWRYPEKLT 247
Cdd:cd04249   161 ATAIAQLLNADLVLLSDVSGVLDADKQLISELNAKQAAELIEQGVITDGMIVKVNAALDAAQSLRRGIDIASWQYPEQLT 240

                         250
                  ....*....|..
gi 1589248809 248 QLFSGKSIGTQF 259
Cdd:cd04249   241 ALLAGEPVGTKI 252
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 1-262 1.10e-112

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 325.52  E-value: 1.10e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   1 MSLNNQPLIIKLGGAALSCGETLSKLFGAISAYQQQAQRPiVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIA 80
Cdd:PRK00942   19 QRFMGKTIVIKYGGNAMTDEELKEAFARDIVLLKQVGINP-VVVHGGGPQIDELLKKLGIESEFVNGLRVTDAETMEVVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  81 GALAGTANKLLQGQAIKDGINAVGLSLADGGLCKVSEL--NPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQ 158
Cdd:PRK00942   98 MVLAGKVNKELVSLINKHGGKAVGLSGKDGGLITAKKLeeDEDLGFVGEVTPVNPALLEALLEAGYIPVISPIGVGEDGE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 159 LMNVNADQAAVAVAGALDAE-LVLLSDVSGVLDGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEV 237
Cdd:PRK00942  178 TYNINADTAAGAIAAALGAEkLILLTDVPGVLDDKGQLISELTASEAEELIEDGVITGGMIPKVEAALDAARGGVRSVHI 257

                         250       260
                  ....*....|....*....|....*.
gi 1589248809 238 ATWRYPEK-LTQLFSGKSIGTQFLPQ 262
Cdd:PRK00942  258 IDGRVPHAlLLELFTDEGIGTMIVPD 283
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 8-259 1.45e-90

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: 268.22  E-value: 1.45e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   8 LIIKLGGAALSCGETLSKLFGAISAYQQQAQRPiVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALAGTA 87
Cdd:cd04238     1 VVIKYGGSAMKDEELKEAFADDIVLLKQVGINP-VIVHGGGPEINELLKRLGIESEFVNGLRVTDKETMEIVEMVLAGKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  88 NKLLQGQAIKDGINAVGLSLADGGLCKV---SELNPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNA 164
Cdd:cd04238    80 NKELVSLLNRAGGKAVGLSGKDGGLIKAekkEEKDIDLGFVGEVTEVNPELLETLLEAGYIPVIAPIAVDEDGETYNVNA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 165 DQAAVAVAGALDAE-LVLLSDVSGVLDGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVATWRYP 243
Cdd:cd04238   160 DTAAGAIAAALKAEkLILLTDVPGVLDDPGSLISELTPKEAEELIEDGVISGGMIPKVEAALEALEGGVRKVHIIDGRVP 239

                         250
                  ....*....|....*..
gi 1589248809 244 EKLTQ-LFSGKSIGTQF 259
Cdd:cd04238   240 HSLLLeLFTDEGIGTMI 256
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 5-259 5.33e-84

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: 252.65  E-value: 5.33e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   5 NQPLIIKLGGAALSCGETLSKLFGAISAYQQQAQRPiVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALA 84
Cdd:COG0548    23 GKTFVIKYGGEAMEDEELKAALAQDIALLKSLGIRP-VLVHGGGPQINELLKRLGIESEFVNGLRVTDEETLEVVEMVLA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  85 GTANKLLQGQAIKDGINAVGLSLADGGLCKVSEL----NPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLM 160
Cdd:COG0548   102 GKVNKEIVALLSQGGGNAVGLSGKDGNLITARPLgvgdGVDLGHVGEVRRVDPELIRALLDAGYIPVISPIGYSPTGEVY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 161 NVNADQAAVAVAGALDAE-LVLLSDVSGVLDGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVAT 239
Cdd:COG0548   182 NINADTVAGAIAAALKAEkLILLTDVPGVLDDPGSLISELTAAEAEELIADGVISGGMIPKLEAALDAVRGGVKRVHIID 261

                         250       260
                  ....*....|....*....|.
gi 1589248809 240 WRYPEKLTQ-LFSGKSIGTQF 259
Cdd:COG0548   262 GRVPHALLLeLFTDDGIGTMI 282
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 7-234 1.38e-63

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: 198.66  E-value: 1.38e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   7 PLIIKLGGAALScgETLSKLFGAISAYQQQAQRPiVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALAGT 86
Cdd:TIGR00761   1 TIVIKIGGAAIS--DLLEAFASDIAFLRAVGIKP-VIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVLIGQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  87 ANKLLQGQAIKDGINAVGLSLADGGLCKVSELNPE-LGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNAD 165
Cdd:TIGR00761  78 VNKELVALLNKHGINAIGLTGGDGQLFTARYLDKEdLGYVGEIKKVNKALIEALLKAGYIPVISSLALTAEGQALNVNAD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589248809 166 QAAVAVAGALDAE-LVLLSDVSGVLDG-KGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRP 234
Cdd:TIGR00761 158 TAAGALAAALGAEkLVLLTDVPGILNGdGQSLISEIPLDEIEQLIKQGIIKGGMIPKVNAALEALRGGVRS 228
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 9-229 2.65e-50

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: 166.14  E-value: 2.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   9 IIKLGGAALScGETLSKLFGAISAYQQQAQRPIVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALAGTAN 88
Cdd:cd04250    18 VIKYGGNAMK-DEELKESFARDIVLLKYVGINPVVVHGGGPEINEMLKKLGIESEFVNGLRVTDEETMEIVEMVLVGKVN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  89 KLLQGQAIKDGINAVGLSLADGGL-------CKVSELNPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMN 161
Cdd:cd04250    97 KEIVSLINRAGGKAVGLSGKDGNLikakkkdATVIEEIIDLGFVGEVTEVNPELLETLLEAGYIPVIAPVGVGEDGETYN 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589248809 162 VNADQAAVAVAGALDAE-LVLLSDVSGVLDG---KGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAAN 229
Cdd:cd04250   177 INADTAAGAIAAALKAEkLILLTDVAGVLDDpndPGSLISEISLKEAEELIADGIISGGMIPKVEACIEALE 248
PLN02512 PLN02512
acetylglutamate kinase
 2-228 9.50e-41

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 142.52  E-value: 9.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   2 SLNNQPLIIKLGGAALSCGETLSKLFGAISAYQQQAQRPIViVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAG 81
Cdd:PLN02512   44 RFRGKTVVVKYGGAAMKDPELKAGVIRDLVLLSCVGLRPVL-VHGGGPEINSWLKKVGIEPQFKNGLRVTDAETMEVVEM 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  82 ALAGTANKLLQGQAIKDGINAVGLSLADGGL--CKVSELNPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQL 159
Cdd:PLN02512  123 VLVGKVNKSLVSLINKAGGTAVGLSGKDGRLlrARPSPNSADLGFVGEVTRVDPTVLRPLVDDGHIPVIATVAADEDGQA 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589248809 160 MNVNADQAAVAVAGALDAE-LVLLSDVSGVLDGK---GHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAA 228
Cdd:PLN02512  203 YNINADTAAGEIAAALGAEkLILLTDVAGVLEDKddpGSLVKELDIKGVRKLIADGKIAGGMIPKVECCVRSL 275
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 8-238 1.30e-36

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: 129.41  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   8 LIIKLGGAALSCGETLSKLFGAISAYQQQaQRPIVIVHGGGYLVDDLMNKLNLETVKKeglRVTPYDQIPVIAGALAGTA 87
Cdd:pfam00696   3 VVIKLGGSSLTDKERLKRLADEIAALLEE-GRKLVVVHGGGAFADGLLALLGLSPRFA---RLTDAETLEVATMDALGSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  88 NKLLQGQAIKDGINAVGLSLADGGLCKVSELNPELGAVgkaepgDSTVLQAILNAGALPIISS-IGLTEQGQLMNVNADQ 166
Cdd:pfam00696  79 GERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRI------DTEALEELLEAGVVPVITGfIGIDPEGELGRGSSDT 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589248809 167 AAVAVAGALDAE-LVLLSDVSGVLDGKGH------LIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVA 238
Cdd:pfam00696 153 LAALLAEALGADkLIILTDVDGVYTADPRkvpdakLIPEISYDELLELLASGLATGGMKVKLPAALEAARRGGIPVVIV 231
argB CHL00202
acetylglutamate kinase; Provisional
 5-260 4.21e-33

acetylglutamate kinase; Provisional


Pssm-ID: 133644 [Multi-domain]  Cd Length: 284  Bit Score: 121.82  E-value: 4.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   5 NQPLIIKLGGAALSCGETLSKLFGAISAYQQQAQRPiVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALA 84
Cdd:CHL00202   23 GRIMVIKYGGAAMKNLILKADIIKDILFLSCIGLKI-VVVHGGGPEINFWLKQLNISPKFWNGIRVTDKVTMEIVEMVLA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  85 GTANKLLQGQAIKDGINAVGLSLADGGLCKVSELN-PELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVN 163
Cdd:CHL00202  102 GKVNKDLVGSINANGGKAVGLCGKDANLIVARASDkKDLGLVGEIQQVDPQLIDMLLEKNYIPVIASVAADHDGQTYNIN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 164 ADQAAVAVAGALDAE-LVLLSDVSGVL---DGKGHLIPSLNQQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVAT 239
Cdd:CHL00202  182 ADVVAGEIAAKLNAEkLILLTDTPGILadiNDPNSLISTLNIKEARNLASTGIISGGMIPKVNCCIRALAQGVEAAHIID 261

                         250       260
                  ....*....|....*....|..
gi 1589248809 240 WRYPEK-LTQLFSGKSIGTQFL 260
Cdd:CHL00202  262 GKEKHAlLLEILTEKGIGSMLV 283
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 9-259 8.48e-31

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: 114.85  E-value: 8.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   9 IIKLGGAALSCGETLSKLFGAISAYQQQAQRPIViVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALaGTAN 88
Cdd:cd02115     1 VIKFGGSSVSSEERLRNLARILVKLASEGGRVVV-VHGAGPQITDELLAHGELLGYARGLRITDRETDALAAMGE-GMSN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  89 KLLQGQAIKDGINAVGLSLADGGLckvseLNPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQ---GQLMNVNAD 165
Cdd:cd02115    79 LLIAAALEQHGIKAVPLDLTQAGF-----ASPNQGHVGKITKVSTDRLKSLLENGILPILSGFGGTDEketGTLGRGGSD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 166 QAAVAVAGALDAE-LVLLSDVSGVLDG------KGHLIPSLNQQQADDLIAGKvitdGMIVKVQAALEAAnDLGRPIEVA 238
Cdd:cd02115   154 STAALLAAALKADrLVILTDVDGVYTAdprkvpDAKLLSELTYEEAAELAYAG----AMVLKPKAADPAA-RAGIPVRIA 228

                         250       260
                  ....*....|....*....|.
gi 1589248809 239 TWRYPEKLtQLFSGKSIGTQF 259
Cdd:cd02115   229 NTENPGAL-ALFTPDGGGTLI 248
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
7-229 3.87e-30

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


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 113.46  E-value: 3.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   7 PLIIKLGGAALSCGETLSKLFGAISAYQQQaqrpIVIVHGGGYLVDDLMNKLNLETVK---KEGL--RVTPYDQIPVIAG 81
Cdd:PRK14058    1 MIVVKIGGSVGIDPEDALIDVASLWADGER----VVLVHGGSDEVNELLERLGIEPRFvtsPSGVtsRYTDRETLEVFIM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  82 ALAgTANKLLQGQAIKDGINAVGLSLADGGLCK---------VSELNPEL---GAVGKAEPGDSTVLQAILNAGALPIIS 149
Cdd:PRK14058   77 AMA-LINKQLVERLQSLGVNAVGLSGLDGGLLEgkrkkavrvVEEGKKKIirgDYTGKIEEVNTDLLKLLLKAGYLPVVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 150 SIGLTEQGQLMNVNADQAAVAVAGALDAE-LVLLSDVSGVL---DGKGHLIPSLNQQQADDLIagKVITDGMIVKVQAAL 225
Cdd:PRK14058  156 PPALSEEGEPLNVDGDRAAAAIAGALKAEaLVLLSDVPGLLrdpPDEGSLIERITPEEAEELS--KAAGGGMKKKVLMAA 233


                  ....
gi 1589248809 226 EAAN 229
Cdd:PRK14058  234 EAVE 237
AAK_NAGK-fArgBP cd04252
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ...
 9-257 1.41e-26

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: 103.61  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   9 IIKLGGAALScgETLSKLFGAISAYQQQAQRPIViVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVIAGALAGTAN 88
Cdd:cd04252     2 VIKVGGAIIE--DDLDELAASLSFLQHVGLYPIV-VHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAVARKVFLEENL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  89 KLLQgqAIKD-GINAVGLSladGGLCKVSELNPEL-GAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNADQ 166
Cdd:cd04252    79 KLVE--ALERnGARARPIT---SGVFEAEYLDKDKyGLVGKITGVNKAPIEAAIRAGYLPILTSLAETPSGQLLNVNADV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 167 AAVAVAGALDA-ELVLLSDVSGVLDGKGHLIPSLN-QQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVATWRYPE 244
Cdd:cd04252   154 AAGELARVLEPlKIVFLNETGGLLDGTGKKISAINlDEEYDDLMKQPWVKYGTKLKIKEIKELLDTLPRSSSVSITSPDD 233

                         250
                  ....*....|...
gi 1589248809 245 KLTQLFSGKSIGT 257
Cdd:cd04252   234 LQKELFTHSGAGT 246
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 9-253 2.31e-24

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: 97.82  E-value: 2.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   9 IIKLGGAALScgeTLSKLFGAISAYQQQAqrpiVIVHGGGYLVDDLMNKLNLETV---KKEGL--RVTPYDQIPVIAGAL 83
Cdd:cd04251     2 VVKIGGSVVS---DLDKVIDDIANFGERL----IVVHGGGNYVNEYLKRLGVEPKfvtSPSGIrsRYTDKETLEVFVMVM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  84 aGTANKLLQGQAIKDGINAVGLSLADGGLCK--------VSELNPEL----GAVGKAEPGDSTVLQAILNAGALPIISSI 151
Cdd:cd04251    75 -GLINKKIVARLHSLGVKAVGLTGLDGRLLEakrkeivrVNERGRKMiirgGYTGKVEKVNSDLIEALLDAGYLPVVSPV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 152 GLTEQGQLMNVNADQAAVAVAGALDAE-LVLLSDVSGVLdGKGHLIPSLNQQQADDLIagKVITDGMIVKVQAALEAAND 230
Cdd:cd04251   154 AYSEEGEPLNVDGDRAAAAIAAALKAErLILLTDVEGLY-LDGRVIERITVSDAESLL--EKAGGGMKRKLLAAAEAVEG 230

                         250       260
                  ....*....|....*....|...
gi 1589248809 231 LGRPIEVATWRYPEKLTQLFSGK 253
Cdd:cd04251   231 GVREVVIGDARADSPISSALNGG 253
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 9-257 4.96e-23

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 96.66  E-value: 4.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   9 IIKLGGAALScgETLSKLFGAISAYQQQAQRPIViVHGGGYLVDDLMNKLNLETVKKEGLRVTpYDQIPVIAGALAGTAN 88
Cdd:PRK04531   40 VIKVGGAVLR--DDLEALASSLSFLQEVGLTPIV-VHGAGPQLDAELDAAGIEKETVNGLRVT-SPEALAIVRKVFQRSN 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  89 KLLqgqaikdgINAVGLSLAdgglckvselnpelgavgkaepgdstvlqailnAGALPIISSIGLTEQGQLMNVNADQAA 168
Cdd:PRK04531  116 LDL--------VEAVESSLR---------------------------------AGSIPVIASLGETPSGQILNINADVAA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 169 VAVAGALD-AELVLLSDVSGVLDGKGHLIPSLN-QQQADDLIAGKVITDGMIVKVQAALEAANDLGRPIEVATWRYPEKL 246
Cdd:PRK04531  155 NELVSALQpYKIIFLTGTGGLLDADGKLISSINlSTEYDHLMQQPWINGGMKLKLEQIKELLDRLPLESSVSITSPSDLA 234

                         250
                  ....*....|.
gi 1589248809 247 TQLFSGKSIGT 257
Cdd:PRK04531  235 KELFTHKGSGT 245
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 9-257 3.82e-13

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: 67.29  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   9 IIKLGGAALSC---GET-----LSKLFGAISAYqqqAQRPIVIVHGGG---------YLVDDLMNKLNLETVKKEGLRVT 71
Cdd:cd04241     3 ILKLGGSVITDkdrPETireenLERIARELAEA---IDEKLVLVHGGGsfghpkakeYGLPDGDGSFSAEGVAETHEAML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  72 PYDQIpvIAGALagtankllqgqaIKDGINAVGLSLADgglCKVSElnpelgaVGKAEPGDSTVLQAILNAGALPII-SS 150
Cdd:cd04241    80 ELNSI--VVDAL------------LEAGVPAVSVPPSS---FFVTE-------NGRIVSFDLEVIKELLDRGFVPVLhGD 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 151 IGLTEQGQLMNVNADQAAVAVAGALDAELV-LLSDVSGVLD---GKGHLIPSLNQQQADDLIA-----GKVITDGMIVKV 221
Cdd:cd04241   136 VVLDEGGGITILSGDDIVVELAKALKPERViFLTDVDGVYDkppPDAKLIPEIDVGSLEDILAalgsaGTDVTGGMAGKI 215

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1589248809 222 QAALEAAnDLGRPIEVATWRYPEKLTQLFSGKSIGT 257
Cdd:cd04241   216 EELLELA-RRGIEVYIFNGDKPENLYRALLGNFIGT 250
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 41-228 2.66e-10

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 60.16  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  41 IVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVI---AGAL---------AGTANKLLQGQAIK----------- 97
Cdd:PRK05279   59 LVLVHGARPQIEEQLAARGIEPRYHKGLRVTDAAALECVkqaAGELrldiearlsMGLPNTPMAGAHIRvvsgnfvtarp 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  98 ----DGINaVGLSladgglckvselnpelGAVGKAepgDSTVLQAILNAGALPIISSIGLTEQGQLMNVNADQAAVAVAG 173
Cdd:PRK05279  139 lgvdDGVD-YQHT----------------GEVRRI---DAEAIRRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAI 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589248809 174 ALDAE-LVLLSDVSGVLDGKGHLIPSLNQQQADDLIAgKVITDGMIVKVQAALEAA 228
Cdd:PRK05279  199 ALKADkLIFFTESQGVLDEDGELIRELSPNEAQALLE-ALEDGDYNSGTARFLRAA 253
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
9-257 8.05e-10

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 57.54  E-value: 8.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809   9 IIKLGGAALSC--------GETLSKLFGAISAYqqqAQRPIVIVHGGG---------YLVDDLMNKLNletvkKEGLRVT 71
Cdd:COG1608     3 VLKLGGSVITDkdkpetvrRDALERIAREIAAA---LDLDLVIVHGGGsfghpvakkYGLHGTLGTED-----AEGVSET 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  72 PYDqipviagalAGTANKLLQGQAIKDGINAVGLSLADGGLCKvselnpelgaVGKAEPGDSTVLQAILNAGALPII--- 148
Cdd:COG1608    75 HRA---------MRELNRIVVDALLEAGVPAVSVPPSSFAVRD----------NGRILSFDTEPIKEMLEEGFVPVLhgd 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 149 --------SSIglteqgqlmnVNADQAAVAVAGALDAELV-LLSDVSGVLD--GKGHLIPSLNQQQADDL---IAGKVIT 214
Cdd:COG1608   136 vvfdaergFTI----------LSGDEIVVYLAKELKPERVgLATDVDGVYDddPKGKLIPEITRSNFDEVldaLGGSAGT 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1589248809 215 D---GMIVKVQAALEAAnDLGRPIEVATWRYPEKLTQLFSGKSI-GT 257
Cdd:COG1608   206 DvtgGMAGKVEELLELA-KPGVEVYIFNGNKPGNLSAALRGEEVrGT 251
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 41-227 6.94e-09

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: 55.25  E-value: 6.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809  41 IVIVHGGGYLVDDLMNKLNLETVKKEGLRVTPYDQIPVI---AGAL---------AGTANKLLQGQAIK-DGINAVG--- 104
Cdd:cd04237    52 LVLVHGARPQIDQRLAERGLEPRYHRGLRITDAAALECVkeaAGAVrleieallsMGLPNSPMAGARIRvVSGNFVTarp 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 105 LSLADGglckvselnPELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNADQAAVAVAGALDAE-LVLLS 183
Cdd:cd04237   132 LGVVDG---------VDFGHTGEVRRIDADAIRRQLDQGSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADkLIFLT 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1589248809 184 DVSGVLDGKGHLIPSLNQQQADDLI-AGKVITDGMIVKVQAALEA 227
Cdd:cd04237   203 DGPGLLDDDGELIRELTAQEAEALLeTGALLTNDTARLLQAAIEA 247
AAK_NAGS-Urea cd04236
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 132-259 2.75e-07

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: 50.23  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 132 DSTVLQAILNAGALPIISSIGLTEQGQLMNVNADQAAVAVAGALDA-ELVLLSDVSGVLDGKGHLIPSLN-QQQADDLIA 209
Cdd:cd04236   142 DTELLQWCLGSGHIPLVCPIGETSSGRSVSLDSSEVTTAIAKALQPiKVIFLNRSGGLRDQKHKVLPQVHlPADLPSLSD 221

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1589248809 210 GKVITDGMIVKVQAALEAANDLGRPIEVATWRYPEKLTQLFSGKSIGTQF 259
Cdd:cd04236   222 AEWLSETEQNRIQDIATLLNALPSMSSAVITSAETLLTELFSHKGSGTLF 271
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
 136-260 3.29e-07

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: 50.13  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 136 LQAILNAGALPIIS---SIGLTEqgqLMNVNADQAAVAVAGALDAE-LVLLSDVSGVLDGKGH------LIPSLNQ--QQ 203
Cdd:cd04242   116 LETLLELGVIPIINendTVATEE---IRFGDNDRLSALVAGLVNADlLILLSDVDGLYDKNPRenpdakLIPEVEEitDE 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 204 ADDLIAG---KVITDGMIVKVQAALEAANdLGRPIEVATWRYPEKLTQLFSGKSIGTQFL 260
Cdd:cd04242   193 IEAMAGGsgsSVGTGGMRTKLKAARIATE-AGIPVVIANGRKPDVLLDILAGEAVGTLFL 251
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
 165-259 2.62e-06

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 48.18  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 165 DQAAVAVAGALDAE-LVLLSDVSGVLDG-----KGHLIPSLNQQQADDLIA----GKVITDGMIVKVQAALEAANDlGRP 234
Cdd:PLN02418  178 DSLAALLALELKADlLILLSDVEGLYTGppsdpSSKLIHTYIKEKHQDEITfgekSRVGRGGMTAKVKAAVNAASA-GIP 256

                          90       100
                  ....*....|....*....|....*
gi 1589248809 235 IEVATWRYPEKLTQLFSGKSIGTQF 259
Cdd:PLN02418  257 VVITSGYALDNIRKVLRGERVGTLF 281
PLN02825 PLN02825
amino-acid N-acetyltransferase
 121-208 3.97e-06

amino-acid N-acetyltransferase


Pssm-ID: 215441 [Multi-domain]  Cd Length: 515  Bit Score: 47.46  E-value: 3.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 121 ELGAVGKAEPGDSTVLQAILNAGALPIISSIGLTEQGQLMNVNADQAAVAVAGALDAE-LVLLSDvSGVLDGKGHLIPSL 199
Cdd:PLN02825  147 DFGATGEVKKIDVSRIKERLDSNCIVLLSNLGYSSSGEVLNCNTYEVATACALAIGADkLICIVD-GPILDENGRLIRFM 225


                  ....*....
gi 1589248809 200 NQQQADDLI 208
Cdd:PLN02825  226 TLEEADMLI 234
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
 165-259 3.05e-04

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: 41.82  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 165 DQAAVAVAGALDAEL-VLLSDVSGVLDG-----KGHLIPS-LNQQQADDLIAG---KVITDGMIVKVQAALEAANDlGRP 234
Cdd:TIGR01092 170 DSLAALLALELKADLlILLSDVEGLYDGppsddDSKLIDTfYKEKHQGEITFGtksRLGRGGMTAKVKAAVWAAYG-GTP 248

                          90       100
                  ....*....|....*....|....*
gi 1589248809 235 IEVATWRYPEKLTQLFSGKSIGTQF 259
Cdd:TIGR01092 249 VIIASGTAPKNITKVVEGKKVGTLF 273
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
 165-259 1.56e-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: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589248809 165 DQAAVAVAGALDAEL-VLLSDVSGVLDGK-----GHLIPSLNQQQADDLIAG---KVITDGMIVKVQAALEAANDlGRPI 235
Cdd:cd04256   181 DSLAARLAVELKADLlILLSDVDGLYDGPpgsddAKLIHTFYPGDQQSITFGtksRVGTGGMEAKVKAALWALQG-GTSV 259

                          90       100
                  ....*....|....*....|....
gi 1589248809 236 EVATWRYPEKLTQLFSGKSIGTQF 259
Cdd:cd04256   260 VITNGMAGDVITKILEGKKVGTFF 283
 
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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