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Conserved domains on  [gi|517454428|ref|WP_018625213|]
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acetylglutamate kinase [Kangiella aquimarina]

Protein Classification

acetylglutamate kinase( domain architecture ID 11480287)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 1-436 0e+00

acetylglutamate kinase; Provisional


:

Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 623.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   1 MTNHKVKETIIRLLNNMGSENEIRKYLKRFSSNEGMKFAIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLN 80
Cdd:PRK04531   1 QANMKTRQIIVRLLSSMASAKEISQYLKRFSQLDAERFAVIKVGGAVLRDDLEALASSLSFLQEVGLTPIVVHGAGPQLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  81 EQLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHNLVNALkntgvdaasfysgvfecaleseslglvgsiqsvhahdl 160
Cdd:PRK04531  81 AELDAAGIEKETVNGLRVTSPEALAIVRKVFQRSNLDLVEAV-------------------------------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 161 IESVRNGAIPVVSPLGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWLY 240
Cdd:PRK04531 123 ESSLRAGSIPVIASLGETPSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWIN 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 241 SGMKLKLQQIYQLLNHVSSATSVSITKPSLVAKELFTDRGSGTLVNKGEKIYQFDNWQELSKVKLTNLIESSFGYHLQPN 320
Cdd:PRK04531 203 GGMKLKLEQIKELLDRLPLESSVSITSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPD 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 321 YFQKTQLHKAYVTECYRAATIVTNDYAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFSMADG 400
Cdd:PRK04531 283 YFDTTQLLRAYVSENYRAAAILTETGGGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAESDG 362

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 517454428 401 FIRGKLWNVFWRGINEHSLIHSCVQQAMSRPRTVIS 436
Cdd:PRK04531 363 CIKQEKWKVFWYGLDDFEQIPKCVAHCANRPPTLES 398
 
Name Accession Description Interval E-value
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 1-436 0e+00

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 623.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   1 MTNHKVKETIIRLLNNMGSENEIRKYLKRFSSNEGMKFAIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLN 80
Cdd:PRK04531   1 QANMKTRQIIVRLLSSMASAKEISQYLKRFSQLDAERFAVIKVGGAVLRDDLEALASSLSFLQEVGLTPIVVHGAGPQLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  81 EQLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHNLVNALkntgvdaasfysgvfecaleseslglvgsiqsvhahdl 160
Cdd:PRK04531  81 AELDAAGIEKETVNGLRVTSPEALAIVRKVFQRSNLDLVEAV-------------------------------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 161 IESVRNGAIPVVSPLGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWLY 240
Cdd:PRK04531 123 ESSLRAGSIPVIASLGETPSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWIN 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 241 SGMKLKLQQIYQLLNHVSSATSVSITKPSLVAKELFTDRGSGTLVNKGEKIYQFDNWQELSKVKLTNLIESSFGYHLQPN 320
Cdd:PRK04531 203 GGMKLKLEQIKELLDRLPLESSVSITSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPD 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 321 YFQKTQLHKAYVTECYRAATIVTNDYAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFSMADG 400
Cdd:PRK04531 283 YFDTTQLLRAYVSENYRAAAILTETGGGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAESDG 362

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 517454428 401 FIRGKLWNVFWRGINEHSLIHSCVQQAMSRPRTVIS 436
Cdd:PRK04531 363 CIKQEKWKVFWYGLDDFEQIPKCVAHCANRPPTLES 398
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
2-433 0e+00

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


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 584.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   2 TNHKVKETIIRLLNNMGSENEIRKYLKRFSSNEGMKFAIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNE 81
Cdd:COG5630    2 NAKQTRQTIVRLLSNMGSAKEIEQYLKRFSQVDAERFAVVKVGGAVLRDDLDALASSLSFLQQVGLTPIVVHGAGPQLDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  82 QLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHNLVNALKNTGVDAASFYSGVFECA-LESESLGLVGSIQSVHAhDL 160
Cdd:COG5630   82 ALAAAGIETQRVDGLRVTSPEALEIVRRVFQQENLKLVEALEAMGTRARPIPSGVFEAEyLDRDTLGLVGEVTGVHL-AP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 161 IE-SVRNGAIPVVSPLGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWL 239
Cdd:COG5630  161 IEaSLRAGSIPIIASLGETPSGQILNINADVAARELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDHLMAQPWV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 240 YSGMKLKLQQIYQLLNHVSSATSVSITKPSLVAKELFTDRGSGTLVNKGEKIYQFDNWQELSKVKLTNLIESSFGYHLQP 319
Cdd:COG5630  241 NGGMRLKLEEIKDLLDDLPLTSSVSITRPSELAKELFTHKGSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 320 NYFQKTQLHKAYVTECYRAATIVTNDYAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFSMAD 399
Cdd:COG5630  321 GYFDKTKFYRAYVSESYRAAAILTLEDGVPYLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEAD 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 517454428 400 GFIRGKLWNVFWRGINEHSLIHSCVQQAMSRPRT 433
Cdd:COG5630  401 GCYKQEKWTVFWYGLDGFDEIQACVEHALARPPT 434
AAK_NAGK-fArgBP cd04252
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ...
 39-285 8.95e-113

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: 331.26  E-value: 8.95e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  39 AIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHNL 118
Cdd:cd04252    1 AVIKVGGAIIEDDLDELAASLSFLQHVGLYPIVVHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAVARKVFLEENLKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 119 VNALKNTGVDAASFYSGVFECA-LESESLGLVGSIQSVHAhDLIE-SVRNGAIPVVSPLGETEQGQIVNINADTATLALA 196
Cdd:cd04252   81 VEALERNGARARPITSGVFEAEyLDKDKYGLVGKITGVNK-APIEaAIRAGYLPILTSLAETPSGQLLNVNADVAAGELA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 197 KTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWLYSGMKLKLQQIYQLLNHVSSATSVSITKPSLVAKELF 276
Cdd:cd04252  160 RVLEPLKIVFLNETGGLLDGTGKKISAINLDEEYDDLMKQPWVKYGTKLKIKEIKELLDTLPRSSSVSITSPDDLQKELF 239


                 ....*....
gi 517454428 277 TDRGSGTLV 285
Cdd:cd04252  240 THSGAGTLI 248
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 38-255 5.58e-55

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: 182.48  E-value: 5.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   38 FAIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARKVFISE-NH 116
Cdd:TIGR00761   1 TIVIKIGGAAISDLLEAFASDIAFLRAVGIKPVIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVLIGQvNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  117 NLVNALKNTGVDAASFYSG---VFEC-ALESESLGLVGSIQSVHAHDLIESVRNGAIPVVSPLGETEQGQIVNINADTAT 192
Cdd:TIGR00761  81 ELVALLNKHGINAIGLTGGdgqLFTArYLDKEDLGYVGEIKKVNKALIEALLKAGYIPVISSLALTAEGQALNVNADTAA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517454428  193 LALAKTIEPYKVVFLTSTGGILDADE-KLIPAISLQnDYHYLMQQSWLYSGMKLKLQQIYQLLN 255
Cdd:TIGR00761 161 GALAAALGAEKLVLLTDVPGILNGDGqSLISEIPLD-EIEQLIKQGIIKGGMIPKVNAALEALR 223
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 271-425 3.53e-43

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


Pssm-ID: 398437  Cd Length: 166  Bit Score: 149.33  E-value: 3.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  271 VAKELFTDRGSGTLVNKGEKIYQFDNWQELSKV-KLTNLIESSFGYHLQ-PNYFQ--KTQLHKAYVTECYRAATIVT-ND 345
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELIDIeRLRNLIERSFDGRLSvADYLDrlKGRLFKIYVDEPYEALAIVTkED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  346 YAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFSMADGFIRGKLWNVFWRGINEHSLIHSCVQ 425
Cdd:pfam04768  82 GGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSELVA 161
 
Name Accession Description Interval E-value
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 1-436 0e+00

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 623.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   1 MTNHKVKETIIRLLNNMGSENEIRKYLKRFSSNEGMKFAIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLN 80
Cdd:PRK04531   1 QANMKTRQIIVRLLSSMASAKEISQYLKRFSQLDAERFAVIKVGGAVLRDDLEALASSLSFLQEVGLTPIVVHGAGPQLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  81 EQLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHNLVNALkntgvdaasfysgvfecaleseslglvgsiqsvhahdl 160
Cdd:PRK04531  81 AELDAAGIEKETVNGLRVTSPEALAIVRKVFQRSNLDLVEAV-------------------------------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 161 IESVRNGAIPVVSPLGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWLY 240
Cdd:PRK04531 123 ESSLRAGSIPVIASLGETPSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWIN 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 241 SGMKLKLQQIYQLLNHVSSATSVSITKPSLVAKELFTDRGSGTLVNKGEKIYQFDNWQELSKVKLTNLIESSFGYHLQPN 320
Cdd:PRK04531 203 GGMKLKLEQIKELLDRLPLESSVSITSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPD 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 321 YFQKTQLHKAYVTECYRAATIVTNDYAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFSMADG 400
Cdd:PRK04531 283 YFDTTQLLRAYVSENYRAAAILTETGGGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAESDG 362

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 517454428 401 FIRGKLWNVFWRGINEHSLIHSCVQQAMSRPRTVIS 436
Cdd:PRK04531 363 CIKQEKWKVFWYGLDDFEQIPKCVAHCANRPPTLES 398
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
2-433 0e+00

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


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 584.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   2 TNHKVKETIIRLLNNMGSENEIRKYLKRFSSNEGMKFAIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNE 81
Cdd:COG5630    2 NAKQTRQTIVRLLSNMGSAKEIEQYLKRFSQVDAERFAVVKVGGAVLRDDLDALASSLSFLQQVGLTPIVVHGAGPQLDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  82 QLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHNLVNALKNTGVDAASFYSGVFECA-LESESLGLVGSIQSVHAhDL 160
Cdd:COG5630   82 ALAAAGIETQRVDGLRVTSPEALEIVRRVFQQENLKLVEALEAMGTRARPIPSGVFEAEyLDRDTLGLVGEVTGVHL-AP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 161 IE-SVRNGAIPVVSPLGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWL 239
Cdd:COG5630  161 IEaSLRAGSIPIIASLGETPSGQILNINADVAARELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDHLMAQPWV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 240 YSGMKLKLQQIYQLLNHVSSATSVSITKPSLVAKELFTDRGSGTLVNKGEKIYQFDNWQELSKVKLTNLIESSFGYHLQP 319
Cdd:COG5630  241 NGGMRLKLEEIKDLLDDLPLTSSVSITRPSELAKELFTHKGSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 320 NYFQKTQLHKAYVTECYRAATIVTNDYAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFSMAD 399
Cdd:COG5630  321 GYFDKTKFYRAYVSESYRAAAILTLEDGVPYLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEAD 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 517454428 400 GFIRGKLWNVFWRGINEHSLIHSCVQQAMSRPRT 433
Cdd:COG5630  401 GCYKQEKWTVFWYGLDGFDEIQACVEHALARPPT 434
AAK_NAGK-fArgBP cd04252
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ...
 39-285 8.95e-113

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: 331.26  E-value: 8.95e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  39 AIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHNL 118
Cdd:cd04252    1 AVIKVGGAIIEDDLDELAASLSFLQHVGLYPIVVHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAVARKVFLEENLKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 119 VNALKNTGVDAASFYSGVFECA-LESESLGLVGSIQSVHAhDLIE-SVRNGAIPVVSPLGETEQGQIVNINADTATLALA 196
Cdd:cd04252   81 VEALERNGARARPITSGVFEAEyLDKDKYGLVGKITGVNK-APIEaAIRAGYLPILTSLAETPSGQLLNVNADVAAGELA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 197 KTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWLYSGMKLKLQQIYQLLNHVSSATSVSITKPSLVAKELF 276
Cdd:cd04252  160 RVLEPLKIVFLNETGGLLDGTGKKISAINLDEEYDDLMKQPWVKYGTKLKIKEIKELLDTLPRSSSVSITSPDDLQKELF 239


                 ....*....
gi 517454428 277 TDRGSGTLV 285
Cdd:cd04252  240 THSGAGTLI 248
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 26-285 4.21e-55

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: 184.47  E-value: 4.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  26 YLKRFSsneGMKFaIIKVGGAILKDD--IDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEV 103
Cdd:COG0548   17 YIQAFR---GKTF-VIKYGGEAMEDEelKAALAQDIALLKSLGIRPVLVHGGGPQINELLKRLGIESEFVNGLRVTDEET 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 104 LKVARKVFISE-NHNLVNALKNTGVDAA--SFYSGVFECA-----LESESLGLVGSIQSVHAhDLIESV-RNGAIPVVSP 174
Cdd:COG0548   93 LEVVEMVLAGKvNKEIVALLSQGGGNAVglSGKDGNLITArplgvGDGVDLGHVGEVRRVDP-ELIRALlDAGYIPVISP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 175 LGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQnDYHYLMQQSWLYSGMKLKLQQIYQLL 254
Cdd:COG0548  172 IGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTAA-EAEELIADGVISGGMIPKLEAALDAV 250

                        250       260       270
                 ....*....|....*....|....*....|..
gi 517454428 255 NH-VSSATSVSITKPSLVAKELFTDRGSGTLV 285
Cdd:COG0548  251 RGgVKRVHIIDGRVPHALLLELFTDDGIGTMI 282
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 38-255 5.58e-55

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: 182.48  E-value: 5.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   38 FAIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARKVFISE-NH 116
Cdd:TIGR00761   1 TIVIKIGGAAISDLLEAFASDIAFLRAVGIKPVIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVLIGQvNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  117 NLVNALKNTGVDAASFYSG---VFEC-ALESESLGLVGSIQSVHAHDLIESVRNGAIPVVSPLGETEQGQIVNINADTAT 192
Cdd:TIGR00761  81 ELVALLNKHGINAIGLTGGdgqLFTArYLDKEDLGYVGEIKKVNKALIEALLKAGYIPVISSLALTAEGQALNVNADTAA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517454428  193 LALAKTIEPYKVVFLTSTGGILDADE-KLIPAISLQnDYHYLMQQSWLYSGMKLKLQQIYQLLN 255
Cdd:TIGR00761 161 GALAAALGAEKLVLLTDVPGILNGDGqSLISEIPLD-EIEQLIKQGIIKGGMIPKVNAALEALR 223
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 40-285 5.87e-54

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: 180.40  E-value: 5.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  40 IIKVGGAILKDDI--DNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARKVFISE-NH 116
Cdd:cd04238    2 VIKYGGSAMKDEElkEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNGLRVTDKETMEIVEMVLAGKvNK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 117 NLVNALKNTGVDAASFySG----VFEC---ALESESLGLVGSIQSVHAhDLIES-VRNGAIPVVSPLGETEQGQIVNINA 188
Cdd:cd04238   82 ELVSLLNRAGGKAVGL-SGkdggLIKAekkEEKDIDLGFVGEVTEVNP-ELLETlLEAGYIPVIAPIAVDEDGETYNVNA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 189 DTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLqNDYHYLMQQSWLYSGMKLKLQQIYQLLNH-VSSATSVSITK 267
Cdd:cd04238  160 DTAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTP-KEAEELIEDGVISGGMIPKVEAALEALEGgVRKVHIIDGRV 238

                        250
                 ....*....|....*...
gi 517454428 268 PSLVAKELFTDRGSGTLV 285
Cdd:cd04238  239 PHSLLLELFTDEGIGTMI 256
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 25-288 3.72e-52

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 176.84  E-value: 3.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  25 KYLKRFSsnegMKFAIIKVGGAILKDD--IDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSE 102
Cdd:PRK00942  16 PYIQRFM----GKTIVIKYGGNAMTDEelKEAFARDIVLLKQVGINPVVVHGGGPQIDELLKKLGIESEFVNGLRVTDAE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 103 VLKVARKVFI-SENHNLVNALKNTGVDAASFySG----VFEC--ALESESLGLVGSIQSVHAhDLIES-VRNGAIPVVSP 174
Cdd:PRK00942  92 TMEVVEMVLAgKVNKELVSLINKHGGKAVGL-SGkdggLITAkkLEEDEDLGFVGEVTPVNP-ALLEAlLEAGYIPVISP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 175 LGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQnDYHYLMQQSWLYSGMKLKLQQIYQLL 254
Cdd:PRK00942 170 IGVGEDGETYNINADTAAGAIAAALGAEKLILLTDVPGVLDDKGQLISELTAS-EAEELIEDGVITGGMIPKVEAALDAA 248

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 517454428 255 NH-VSSATSVSITKPSLVAKELFTDRGSGTLVNKG 288
Cdd:PRK00942 249 RGgVRSVHIIDGRVPHALLLELFTDEGIGTMIVPD 283
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 26-285 5.45e-48

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: 165.76  E-value: 5.45e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  26 YLKRFSSnegmKFAIIKVGGAILKDDI--DNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEV 103
Cdd:cd04250    8 YIQKFRG----KTVVIKYGGNAMKDEElkESFARDIVLLKYVGINPVVVHGGGPEINEMLKKLGIESEFVNGLRVTDEET 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 104 LKVARKVFISE-NHNLVNALKNTGVDAASFySGV-----------FECALESESLGLVGSIQSVHAhDLIES-VRNGAIP 170
Cdd:cd04250   84 MEIVEMVLVGKvNKEIVSLINRAGGKAVGL-SGKdgnlikakkkdATVIEEIIDLGFVGEVTEVNP-ELLETlLEAGYIP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 171 VVSPLGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDA---DEKLIPAISLQnDYHYLMQQSWLYSGMKLKL 247
Cdd:cd04250  162 VIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVLDDpndPGSLISEISLK-EAEELIADGIISGGMIPKV 240

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 517454428 248 QQIYQLLNH-VSSATSVSITKPSLVAKELFTDRGSGTLV 285
Cdd:cd04250  241 EACIEALEGgVKAAHIIDGRVPHSLLLEIFTDEGIGTMI 279
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 271-425 3.53e-43

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


Pssm-ID: 398437  Cd Length: 166  Bit Score: 149.33  E-value: 3.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  271 VAKELFTDRGSGTLVNKGEKIYQFDNWQELSKV-KLTNLIESSFGYHLQ-PNYFQ--KTQLHKAYVTECYRAATIVT-ND 345
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELIDIeRLRNLIERSFDGRLSvADYLDrlKGRLFKIYVDEPYEALAIVTkED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  346 YAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFSMADGFIRGKLWNVFWRGINEHSLIHSCVQ 425
Cdd:pfam04768  82 GGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSELVA 161
AAK_NAGS-Urea cd04236
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 18-284 6.40e-38

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: 138.82  E-value: 6.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  18 GSENEIRKYLKRFS---SNEGMKFAIIKVGGAILK--DDIDNLVSSLSFLQQVGLTPIVVHGA----GPQLNEQLEQEri 88
Cdd:cd04236   14 GDPREARYWLTQFQiamPNDWPAFAVLEVDHSVFRslEMVQSLSFGLAFLQRMDMKLLVVMGLsapdGTNMSDLELQA-- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  89 eaqfiegkrvtnsevlkvARKVFISENHNLVNALKNTGVDAASFYSG----VFECALESESLGLVGSIQSvhahDLIE-S 163
Cdd:cd04236   92 ------------------ARSRLVKDCKTLVEALQANSAAAHPLFSGesvlQAEEPEPGASKGPSVSVDT----ELLQwC 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 164 VRNGAIPVVSPLGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWLYSGM 243
Cdd:cd04236  150 LGSGHIPLVCPIGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWLSETE 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 517454428 244 KLKLQQIYQLLNHVSSATSVSITKPSLVAKELFTDRGSGTL 284
Cdd:cd04236  230 QNRIQDIATLLNALPSMSSAVITSAETLLTELFSHKGSGTL 270
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 319-413 2.14e-37

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


Pssm-ID: 176267  Cd Length: 99  Bit Score: 131.73  E-value: 2.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 319 PNYFQKTQ--LHKAYVTECYRAATIVTN--DYAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFY 394
Cdd:cd04265    1 PDYFDSLQgrLHTIYLSEGYNAAAIVTNeeVDGVPYLDKFAVSSSAQGEGTGEALWRRLRRDFPKLFWRSRSTNPINPWY 80

                         90
                 ....*....|....*....
gi 517454428 395 FSMADGFIRGKLWNVFWRG 413
Cdd:cd04265   81 FKRCDGSFKNGHWTVFWYG 99
DUF619-NAGS cd04264
DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic ...
 319-413 1.15e-35

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


Pssm-ID: 176266  Cd Length: 99  Bit Score: 127.10  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 319 PNYFQKTQ-LHKAYVTECYRAATIVTN---DYAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFY 394
Cdd:cd04264    1 PDYIDRLQrLHAIYLSEGYNAAAIVTYegvNNGVPYLDKFAVSSSAQGEGTSDALWRRLRRDFPKLFWRSRKTNPINPWY 80

                         90
                 ....*....|....*....
gi 517454428 395 FSMADGFIRGKLWNVFWRG 413
Cdd:cd04264   81 FKRSDGSFKNGQWKVFWYG 99
argB CHL00202
acetylglutamate kinase; Provisional
 26-285 4.55e-35

acetylglutamate kinase; Provisional


Pssm-ID: 133644 [Multi-domain]  Cd Length: 284  Bit Score: 131.45  E-value: 4.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  26 YLKRFSSnegmKFAIIKVGGAILKDDI--DNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEV 103
Cdd:CHL00202  17 YIQKFRG----RIMVIKYGGAAMKNLIlkADIIKDILFLSCIGLKIVVVHGGGPEINFWLKQLNISPKFWNGIRVTDKVT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 104 LKVARKVFISE-NHNLVNALKNTGVDAASFySG-----VFECALESESLGLVGSIQSVHAHDLIESVRNGAIPVVSPLGE 177
Cdd:CHL00202  93 MEIVEMVLAGKvNKDLVGSINANGGKAVGL-CGkdanlIVARASDKKDLGLVGEIQQVDPQLIDMLLEKNYIPVIASVAA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 178 TEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGIL-DAD--EKLIPAISLQnDYHYLMQQSWLYSGMKLKLQ-QIYQL 253
Cdd:CHL00202 172 DHDGQTYNINADVVAGEIAAKLNAEKLILLTDTPGILaDINdpNSLISTLNIK-EARNLASTGIISGGMIPKVNcCIRAL 250

                        250       260       270
                 ....*....|....*....|....*....|..
gi 517454428 254 LNHVSSATSVSITKPSLVAKELFTDRGSGTLV 285
Cdd:CHL00202 251 AQGVEAAHIIDGKEKHALLLEILTEKGIGSML 282
PLN02512 PLN02512
acetylglutamate kinase
 26-285 3.92e-32

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 124.03  E-value: 3.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  26 YLKRFSSnegmKFAIIKVGGAILKDDI--DNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEV 103
Cdd:PLN02512  41 FIQRFRG----KTVVVKYGGAAMKDPElkAGVIRDLVLLSCVGLRPVLVHGGGPEINSWLKKVGIEPQFKNGLRVTDAET 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 104 LKVARKVFISE-NHNLVN--------ALKNTGVDAasfysGVFECALESES--LGLVGSIQSVHAHDLIESVRNGAIPVV 172
Cdd:PLN02512 117 MEVVEMVLVGKvNKSLVSlinkaggtAVGLSGKDG-----RLLRARPSPNSadLGFVGEVTRVDPTVLRPLVDDGHIPVI 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 173 SPLGETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILDADEK---LIPAISLqNDYHYLMQQSWLYSGMKLKLQ- 248
Cdd:PLN02512 192 ATVAADEDGQAYNINADTAAGEIAAALGAEKLILLTDVAGVLEDKDDpgsLVKELDI-KGVRKLIADGKIAGGMIPKVEc 270

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 517454428 249 QIYQLLNHVSSATSVSITKPSLVAKELFTDRGSGTLV 285
Cdd:PLN02512 271 CVRSLAQGVKTAHIIDGRVPHSLLLEILTDEGAGTMI 307
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 40-285 5.70e-30

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: 116.77  E-value: 5.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  40 IIKVGGAILK--DDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHN 117
Cdd:cd02115    1 VIKFGGSSVSseERLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDALAAMGEGMSNLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 118 LVNALKNTGVDAASFysGVFECALESESLGLVGSIQSVHAHDLIESVRNGAIPVVSPLGETEQ---GQIVNINADTATLA 194
Cdd:cd02115   81 IAAALEQHGIKAVPL--DLTQAGFASPNQGHVGKITKVSTDRLKSLLENGILPILSGFGGTDEketGTLGRGGSDSTAAL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 195 LAKTIEPYKVVFLTSTGGILDAD------EKLIPAISLQnDYHYLMQQSWlysgMKLKLQQIYQLLNHvssATSVSITKP 268
Cdd:cd02115  159 LAAALKADRLVILTDVDGVYTADprkvpdAKLLSELTYE-EAAELAYAGA----MVLKPKAADPAARA---GIPVRIANT 230

                        250
                 ....*....|....*...
gi 517454428 269 S-LVAKELFTDRGSGTLV 285
Cdd:cd02115  231 EnPGALALFTPDGGGTLI 248
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 38-285 9.15e-25

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: 103.02  E-value: 9.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  38 FAIIKVGGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARK----VFIS 113
Cdd:cd04237   21 FVIAFGGEAVAHPNFDNIVHDIALLHSLGIRLVLVHGARPQIDQRLAERGLEPRYHRGLRITDAAALECVKEaagaVRLE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 114 ENHNLVNALKNTGVDAASF--YSGVFECA-----LESESLGLVGSIQSVHAHDLIESVRNGAIPVVSPLGETEQGQIVNI 186
Cdd:cd04237  101 IEALLSMGLPNSPMAGARIrvVSGNFVTArplgvVDGVDFGHTGEVRRIDADAIRRQLDQGSIVLLSPLGYSPTGEVFNL 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 187 NA-DTATlALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYLMQQSWLYSGMKLKLQQIYQ-LLNHVSSATSVS 264
Cdd:cd04237  181 SMeDVAT-AVAIALKADKLIFLTDGPGLLDDDGELIRELTAQEAEALLETGALLTNDTARLLQAAIEaCRGGVPRVHLIS 259

                        250       260
                 ....*....|....*....|.
gi 517454428 265 ITKPSLVAKELFTDRGSGTLV 285
Cdd:cd04237  260 YAEDGALLLELFTRDGVGTLI 280
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 37-256 1.30e-24

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: 101.29  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   37 KFAIIKVGGAIL--KDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIegkRVTNSEVLKVARKVFISE 114
Cdd:pfam00696   1 KRVVIKLGGSSLtdKERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFA---RLTDAETLEVATMDALGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  115 NHNLVNALKNTGVDAASFYSGVFECALESESLGLVgsIQSVHAHDLIESVRNGAIPVVSPL-GETEQGQIVNINADTATL 193
Cdd:pfam00696  78 LGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDV--VTRIDTEALEELLEAGVVPVITGFiGIDPEGELGRGSSDTLAA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517454428  194 ALAKTIEPYKVVFLTSTGGILDAD------EKLIPAISLQNDYHYLMQQsWLYSGMKLKLQQIYQLLNH 256
Cdd:pfam00696 156 LLAEALGADKLIILTDVDGVYTADprkvpdAKLIPEISYDELLELLASG-LATGGMKVKLPAALEAARR 223
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
 40-248 2.01e-21

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: 92.86  E-value: 2.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  40 IIKVGGAILKDD--IDNLVSSLSFLQQVGLTPIV-VHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLK-VARKVFISEN 115
Cdd:cd04249    2 VIKLGGALLETEaaLEQLFSALSEYQQQHNRQLViVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIPyITGALAGTAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 116 HNLVNALKNTGVDAA--SFYSG-VFECALESESLGLVGSIQSVHAHDLIESVRNGAIPVVSPLGETEQGQIVNINADTAT 192
Cdd:cd04249   82 KQLMAQAIKAGLKPVglSLADGgMTAVTQLDPELGAVGKATANDPSLLNDLLKAGFLPIISSIGADDQGQLMNVNADQAA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517454428 193 LALAKTIEPyKVVFLTSTGGILDADEKLIPAISlQNDYHYLMQQSWLYSGMKLKLQ 248
Cdd:cd04249  162 TAIAQLLNA-DLVLLSDVSGVLDADKQLISELN-AKQAAELIEQGVITDGMIVKVN 215
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
40-226 2.31e-20

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


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 90.34  E-value: 2.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  40 IIKVGGAILKDDIDNLVSSLSfLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGK-----RVTNSEVLKVARKVFISE 114
Cdd:PRK14058   3 VVKIGGSVGIDPEDALIDVAS-LWADGERVVLVHGGSDEVNELLERLGIEPRFVTSPsgvtsRYTDRETLEVFIMAMALI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 115 NHNLVNALKNTGVDAASFySGVFECALESESLGLV----------------GSIQSVHAhDLIES-VRNGAIPVVSPLGE 177
Cdd:PRK14058  82 NKQLVERLQSLGVNAVGL-SGLDGGLLEGKRKKAVrvveegkkkiirgdytGKIEEVNT-DLLKLlLKAGYLPVVAPPAL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517454428 178 TEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGIL---DADEKLIPAISL 226
Cdd:PRK14058 160 SEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLrdpPDEGSLIERITP 211
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 44-285 4.75e-18

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 85.97  E-value: 4.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  44 GGAILKDDIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARKVfISENH-----NL 118
Cdd:PRK05279  34 GEAIAHGNFSNIVHDIALLHSLGIRLVLVHGARPQIEEQLAARGIEPRYHKGLRVTDAAALECVKQA-AGELRldieaRL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 119 VNALKNTGVDAA--SFYSGVFECAlesESLGLV--------GSIQSVHAHDLIESVRNGAIPVVSPLGETEQGQIVNINA 188
Cdd:PRK05279 113 SMGLPNTPMAGAhiRVVSGNFVTA---RPLGVDdgvdyqhtGEVRRIDAEAIRRQLDSGAIVLLSPLGYSPTGESFNLTM 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 189 -DTATlALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQNDYHYL--MQQSWLYSGMKLKLQQIYQ-LLNHVSSATSVS 264
Cdd:PRK05279 190 eEVAT-QVAIALKADKLIFFTESQGVLDEDGELIRELSPNEAQALLeaLEDGDYNSGTARFLRAAVKaCRGGVRRSHLIS 268

                        250       260
                 ....*....|....*....|.
gi 517454428 265 ITKPSLVAKELFTDRGSGTLV 285
Cdd:PRK05279 269 YAEDGALLQELFTRDGIGTMI 289
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 39-247 3.14e-17

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: 80.88  E-value: 3.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  39 AIIKVGGAILkDDIDNLVSSLsflQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEG-----KRVTNSEVLKVARKVFIS 113
Cdd:cd04251    1 IVVKIGGSVV-SDLDKVIDDI---ANFGERLIVVHGGGNYVNEYLKRLGVEPKFVTSpsgirSRYTDKETLEVFVMVMGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 114 ENHNLVNALKNTGVDAASFySGVFECALESESLGLV----------------GSIQSVhAHDLIES-VRNGAIPVVSPLG 176
Cdd:cd04251   77 INKKIVARLHSLGVKAVGL-TGLDGRLLEAKRKEIVrvnergrkmiirggytGKVEKV-NSDLIEAlLDAGYLPVVSPVA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517454428 177 ETEQGQIVNINADTATLALAKTIEPYKVVFLTSTGGILdADEKLIPAISLqNDYHYLMQQswLYSGMKLKL 247
Cdd:cd04251  155 YSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLY-LDGRVIERITV-SDAESLLEK--AGGGMKRKL 221
N-Ac-Glu-synth TIGR01890
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ...
 40-287 7.35e-17

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: 82.15  E-value: 7.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428   40 IIKVGGAILKD-DIDNLVSSLSFLQQVGLTPIVVHGAGPQLNEQLEQERIEAQFIEGKRVTNSEVLKVARKVFISENHN- 117
Cdd:TIGR01890  21 VVGLGGELVEGgNLGNIVADIALLHSLGVRLVLVHGARPQIERILAARGRTPHYHRGLRVTDEASLEQAQQAAGTLRLAi 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  118 ---LVNALKNTGVDAA--SFYSGVFecaLESESLGLV--------GSIQSVHAHDLIESVRNGAIPVVSPLGETEQGQIV 184
Cdd:TIGR01890 101 earLSMSLSNTPMAGSrlPVVSGNF---VTARPIGVIegvdyehtGVIRKIDTEGIRRQLDAGSIVLLSPLGHSPTGETF 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  185 NINADTATLALAKTIEPYKVVFLTSTGGILDADEKLIPAISLQnDYHYLMQqswlysgmKLKLQQIYQLLNHVSSATSVS 264
Cdd:TIGR01890 178 NLDMEDVATSVAISLKADKLIYFTLSPGISDPDGTLAAELSPQ-EVESLAE--------RLGSETTRRLLSAAVKACRGG 248

                         250       260       270
                  ....*....|....*....|....*....|.
gi 517454428  265 ITKPSLVA--------KELFTDRGSGTLVNK 287
Cdd:TIGR01890 249 VHRSHIVSyaedgsllQELFTRDGIGTSISK 279
DUF619-NAGS-FABP cd04266
DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; ...
 338-413 3.38e-14

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


Pssm-ID: 176268  Cd Length: 108  Bit Score: 68.25  E-value: 3.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 338 AATIVTNDYA-----------------IPYLDKFVVEDSAKGeGLGTA--VWNRMLLDNP-QLFWRASANNPINKFYFSM 397
Cdd:cd04266   12 ATVIIAGDYEgaailtwegpdgstpekIAYLDKFAVLPKAQG-SDGIAdiLFNAMLDGFPnELIWRSRKDNPVNKWYFER 90

                         90
                 ....*....|....*...
gi 517454428 398 ADGFI--RGKLWNVFWRG 413
Cdd:cd04266   91 SVGVLklSGSQWKLFWTG 108
DUF619-like cd03173
DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; ...
 329-413 1.01e-11

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


Pssm-ID: 176264  Cd Length: 98  Bit Score: 60.96  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 329 KAYVTECYRAATIVTN-DYAIPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFSMADGFIRGKLW 407
Cdd:cd03173   13 ASYADEPLEGVAIVTYeGNSIPYLDKFAVSDHLWLNNVTDNIFNLIRKDFPSLLWRVRENDANLKWYFSKSVGSLDKNGF 92


                 ....*.
gi 517454428 408 NVFWRG 413
Cdd:cd03173   93 ILFWYG 98
DUF619-NAGK-FABP cd04263
DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway; ...
 320-413 1.18e-08

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


Pssm-ID: 176265  Cd Length: 98  Bit Score: 52.32  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 320 NYFQ--KTQLHKAYVTECYRAATIVTNDYA-IPYLDKFVVEDSAKGEGLGTAVWNRMLLDNPQLFWRASANNPINKFYFS 396
Cdd:cd04263    2 SYFDelKERPFKAYGDEPMEVLAIVLPPSGeVATLATFTITKSGWLNNVADNIFTAIKKDHPKLVWTVREDDENLKWHFE 81

                         90
                 ....*....|....*..
gi 517454428 397 MADGFIRGKLWNVFWRG 413
Cdd:cd04263   82 KADGSFTRNGKVLFWYG 98
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
 38-253 6.01e-08

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: 53.42  E-value: 6.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  38 FAIIKVGGAIL----------KDDIDNLVSSLSflQQVGLTPIVVHGAG----PQLNEQLEQERIEAQFIEGKRVTNSEV 103
Cdd:cd04241    1 MIILKLGGSVItdkdrpetirEENLERIARELA--EAIDEKLVLVHGGGsfghPKAKEYGLPDGDGSFSAEGVAETHEAM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 104 LKVARKVfisenhnlVNALKNTGVDAASFYSgvFECALESESLGLVGSIQSVHahdliESVRNGAIPV----VSPlgETE 179
Cdd:cd04241   79 LELNSIV--------VDALLEAGVPAVSVPP--SSFFVTENGRIVSFDLEVIK-----ELLDRGFVPVlhgdVVL--DEG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 180 QGQIVnINADTATLALAKTIEPYKVVFLTSTGGILDA---DEKLIPAI---SLQNDYHYLMQQSWLYSG-MKLKLQQIYQ 252
Cdd:cd04241  142 GGITI-LSGDDIVVELAKALKPERVIFLTDVDGVYDKpppDAKLIPEIdvgSLEDILAALGSAGTDVTGgMAGKIEELLE 220


                 .
gi 517454428 253 L 253
Cdd:cd04241  221 L 221
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
39-285 1.13e-07

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 52.53  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428  39 AIIKVGGAIL----------KDDIDNLVSSLSFLQQVGLtpIVVHGAG----PQLNEQLEQERIEAQFIEGKRVTNSEVL 104
Cdd:COG1608    2 IVLKLGGSVItdkdkpetvrRDALERIAREIAAALDLDL--VIVHGGGsfghPVAKKYGLHGTLGTEDAEGVSETHRAMR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 105 KVARKVfisenhnlVNALKNTGVDAASFYSgvFECALESESLGLVGSIQSVHahdliESVRNGAIPVVSplGE----TEQ 180
Cdd:COG1608   80 ELNRIV--------VDALLEAGVPAVSVPP--SSFAVRDNGRILSFDTEPIK-----EMLEEGFVPVLH--GDvvfdAER 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517454428 181 GQIVnINADTATLALAKTIEPYKVVFLTSTGGILDAD--EKLIPAISLQNDYHYLMQqswLYS--------GMKLKLQQI 250
Cdd:COG1608  143 GFTI-LSGDEIVVYLAKELKPERVGLATDVDGVYDDDpkGKLIPEITRSNFDEVLDA---LGGsagtdvtgGMAGKVEEL 218

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 517454428 251 YQLlnhVSSATSVSIT---KPSLVAKELFTDRGSGTLV 285
Cdd:COG1608  219 LEL---AKPGVEVYIFngnKPGNLSAALRGEEVRGTRI 253
 
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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