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Conserved domains on  [gi|499660909|ref|WP_011341643|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Syntrophotalea carbinolica]

Protein Classification

N-acetyl-gamma-glutamyl-phosphate reductase( domain architecture ID 11414156)

N-acetyl-gamma-glutamyl-phosphate reductase catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to N-acetyl-L-glutamate 5-semialdehyde, as part of the L-arginine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-345 0e+00

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


:

Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 612.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIIRKSDFVFTALPHKAA 81
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPDELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  82 MAVVPAFLHAGKKVVDLSADYRLHDVDVYEAWYD-KHTSPELLDEAVYGLPELYRQQVVDARLVANPGCYPTSIALGLAP 160
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGfEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 161 LLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQVSFTPHLLPVNRG 240
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 241 ILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVIIVSVIDNLLKGAAS 320
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|....*
gi 499660909 321 QAVQNMNLMQAWSEDSGLSDLPLYP 345
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVPLYP 345
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-345 0e+00

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 612.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIIRKSDFVFTALPHKAA 81
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPDELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  82 MAVVPAFLHAGKKVVDLSADYRLHDVDVYEAWYD-KHTSPELLDEAVYGLPELYRQQVVDARLVANPGCYPTSIALGLAP 160
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGfEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 161 LLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQVSFTPHLLPVNRG 240
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 241 ILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVIIVSVIDNLLKGAAS 320
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|....*
gi 499660909 321 QAVQNMNLMQAWSEDSGLSDLPLYP 345
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-345 0e+00

N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273832 [Multi-domain]  Cd Length: 346  Bit Score: 536.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909    2 LKVAIVGASGYTGVELIRLLLNHPQVEIT-CVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIIRKSDFVFTALPHKA 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITyLVSSRESAGKPVSEVHPHLRGLVDLNLEPIDVEEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   81 AMAVVPAFLHAGKKVVDLSADYRLHDVDVYEAWY-DKHTSPELLDEAVYGLPELYRQQVVDARLVANPGCYPTSIALGLA 159
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYgFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  160 PLLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQVSFTPHLLPVNR 239
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  240 GILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVIIVSVIDNLLKGAA 319
Cdd:TIGR01850 241 GILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|....*.
gi 499660909  320 SQAVQNMNLMQAWSEDSGLSDLPLYP 345
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-345 2.62e-134

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 387.64  E-value: 2.62e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   1 MLKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRiDLTFDPVDVDTIIRKSDFVFTALPHKA 80
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQ-DLPNLVAVKDADFSDVDAVFCCLPHGT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  81 AMAVVpAFLHAGKKVVDLSADYRLHDVDVYEAWYDK-HTSPELLDEAVYGLPELYRQQVVDARLVANPGCYPTSIALGLA 159
Cdd:PLN02968 117 TQEII-KALPKDLKIVDLSADFRLRDIAEYEEWYGHpHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLV 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 160 PLLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQVSFTPHLLPVNR 239
Cdd:PLN02968 196 PLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSR 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 240 GILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVIIVSVIDNLLKGAA 319
Cdd:PLN02968 276 GMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKGAS 355

                        330       340
                 ....*....|....*....|....*.
gi 499660909 320 SQAVQNMNLMQAWSEDSGLSDLPLYP 345
Cdd:PLN02968 356 GQAVQNLNLMMGLPETTGLLQQPLFP 381
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 148-318 1.40e-103

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both, the arginine and lysine, biosynthetic pathways.


Pssm-ID: 467683  Cd Length: 171  Bit Score: 301.32  E-value: 1.40e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 148 GCYPTSIALGLAPLLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQ 227
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 228 VSFTPHLLPVNRGILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVII 307
Cdd:cd23934   81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                        170
                 ....*....|.
gi 499660909 308 VSVIDNLLKGA 318
Cdd:cd23934  161 VSAIDNLVKGA 171
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 3-141 1.56e-44

Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 148.83  E-value: 1.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909    3 KVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQN-AGASIDSVFPSLAGRIDLTFDPVDVDtIIRKSDFVFTALPHKAA 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEGGKDLVVEDVDPE-DFKDVDIVFFALPGGVS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   82 MAVVPAFLHAGKKVVDLSADYRLHdvdvyeawydkhtspellDEAVYGLPELYRQQVVDA 141
Cdd:pfam01118  80 KEIAPKLAEAGAKVIDLSSDFRMD------------------DDVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 3-141 1.83e-41

Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 140.76  E-value: 1.83e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909     3 KVAIVGASGYTGVELIRLLLNHPQVEITC-VTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIirKSDFVFTALPHKAA 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTAlAASSRSAGKKVSEAGPHLKGEVVLELDPPDFEEL--AVDIVFLALPHGVS 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499660909    82 MAVV---PAFLHAGKKVVDLSADYRLHdvdvyeawydkhtspellDEAVYGLPELYRQQVVDA 141
Cdd:smart00859  79 KESApllPRAAAAGAVVIDLSSAFRMD------------------DDVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-345 0e+00

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 612.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIIRKSDFVFTALPHKAA 81
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPDELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  82 MAVVPAFLHAGKKVVDLSADYRLHDVDVYEAWYD-KHTSPELLDEAVYGLPELYRQQVVDARLVANPGCYPTSIALGLAP 160
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGfEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 161 LLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQVSFTPHLLPVNRG 240
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 241 ILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVIIVSVIDNLLKGAAS 320
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|....*
gi 499660909 321 QAVQNMNLMQAWSEDSGLSDLPLYP 345
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-345 0e+00

N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273832 [Multi-domain]  Cd Length: 346  Bit Score: 536.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909    2 LKVAIVGASGYTGVELIRLLLNHPQVEIT-CVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIIRKSDFVFTALPHKA 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITyLVSSRESAGKPVSEVHPHLRGLVDLNLEPIDVEEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   81 AMAVVPAFLHAGKKVVDLSADYRLHDVDVYEAWY-DKHTSPELLDEAVYGLPELYRQQVVDARLVANPGCYPTSIALGLA 159
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYgFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  160 PLLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQVSFTPHLLPVNR 239
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  240 GILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVIIVSVIDNLLKGAA 319
Cdd:TIGR01850 241 GILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|....*.
gi 499660909  320 SQAVQNMNLMQAWSEDSGLSDLPLYP 345
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-345 2.62e-134

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 387.64  E-value: 2.62e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   1 MLKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRiDLTFDPVDVDTIIRKSDFVFTALPHKA 80
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQ-DLPNLVAVKDADFSDVDAVFCCLPHGT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  81 AMAVVpAFLHAGKKVVDLSADYRLHDVDVYEAWYDK-HTSPELLDEAVYGLPELYRQQVVDARLVANPGCYPTSIALGLA 159
Cdd:PLN02968 117 TQEII-KALPKDLKIVDLSADFRLRDIAEYEEWYGHpHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLV 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 160 PLLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQVSFTPHLLPVNR 239
Cdd:PLN02968 196 PLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSR 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 240 GILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVIIVSVIDNLLKGAA 319
Cdd:PLN02968 276 GMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKGAS 355

                        330       340
                 ....*....|....*....|....*.
gi 499660909 320 SQAVQNMNLMQAWSEDSGLSDLPLYP 345
Cdd:PLN02968 356 GQAVQNLNLMMGLPETTGLLQQPLFP 381
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 148-318 1.40e-103

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both, the arginine and lysine, biosynthetic pathways.


Pssm-ID: 467683  Cd Length: 171  Bit Score: 301.32  E-value: 1.40e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 148 GCYPTSIALGLAPLLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLAGKPVQ 227
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 228 VSFTPHLLPVNRGILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVII 307
Cdd:cd23934   81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                        170
                 ....*....|.
gi 499660909 308 VSVIDNLLKGA 318
Cdd:cd23934  161 VSAIDNLVKGA 171
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 2-147 2.95e-83

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both the arginine and lysine biosynthetic pathways.


Pssm-ID: 467521 [Multi-domain]  Cd Length: 170  Bit Score: 249.65  E-value: 2.95e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIIRKSDFVFTALPHKAA 81
Cdd:cd17895    1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTDLTFEPDDDEEIAEDADVVFLALPHGVS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499660909  82 MAVVPAFLHAGKKVVDLSADYRLHDVDVYEAWYD-KHTSPELLDEAVYGLPELYRQQVVDARLVANP 147
Cdd:cd17895   81 MELAPKLLEAGVKVIDLSADFRLKDPETYEKWYGfEHAAPELLKEAVYGLPELNREEIKKARLVANP 147
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 149-318 2.35e-53

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways.


Pssm-ID: 467675  Cd Length: 166  Bit Score: 173.07  E-value: 2.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 149 CYPTSIALGLAPLLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGqlagKPVQV 228
Cdd:cd18125    1 CYATAALLALYPLLKAGLLKPTPITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNLG----GKHNV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 229 SFTPHLLPVNRGILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVRGSNYCNIGVVSDKRTGRVIIV 308
Cdd:cd18125   77 HFTPHVGPWVRGILMTIQCFTQKGWSLRQLHEAYREAYAGEPFVRVMPQGKGPDPKFVQGTNYADIGVELEEDTGRLVVM 156

                        170
                 ....*....|
gi 499660909 309 SVIDNLLKGA 318
Cdd:cd18125  157 SAIDNLVKGA 166
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 2-145 2.41e-53

N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; LysY (EC 1.2.1.103/EC 1.2.1.106) is involved in both the arginine and lysine biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LysY is the third enzyme in lysine biosynthesis from AAA. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor. Members in this subfamily belong to the type 1 AGPR family. They contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467527 [Multi-domain]  Cd Length: 170  Bit Score: 173.23  E-value: 2.41e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVdtiIRKSDFVFTALPHKAA 81
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNLRGRTLLKFVPPEE---LESCDVLFLALPHGES 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499660909  82 MAVVPAFLHAGKKVVDLSADYRLHDVDVYEAWYDK-HTSPELLDEAVYGLPELYRQQVVDARLVA 145
Cdd:cd24151   78 MKRIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGpHPRPELLERFVYGLPELHREELRGARYIA 142
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 148-318 3.91e-53

C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY; EC 1.2.1.103/EC 1.2.1.106) is involved in both, the arginine and lysine, biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LysY is the third enzyme in lysine biosynthesis from AAA. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor.


Pssm-ID: 467688  Cd Length: 174  Bit Score: 172.81  E-value: 3.91e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 148 GCYPTSIALGLAPLLENNLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGqLAGKPVQ 227
Cdd:cd23939    1 GCNATASILALYPLVKAGLLDDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELG-LLAREIS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 228 VSFTPHLLPVNRGILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGE----LPNILHVRGSNYCNIGVVSDKRTG 303
Cdd:cd23939   80 VSFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYRKAYGNEPFVRIVKDRKgiyrYPDPKLVIGSNFCDIGFELDEDNG 159

                        170
                 ....*....|....*
gi 499660909 304 RVIIVSVIDNLLKGA 318
Cdd:cd23939  160 RLVVFSAIDNLMKGA 174
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 3-141 1.56e-44

Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 148.83  E-value: 1.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909    3 KVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQN-AGASIDSVFPSLAGRIDLTFDPVDVDtIIRKSDFVFTALPHKAA 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEGGKDLVVEDVDPE-DFKDVDIVFFALPGGVS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   82 MAVVPAFLHAGKKVVDLSADYRLHdvdvyeawydkhtspellDEAVYGLPELYRQQVVDA 141
Cdd:pfam01118  80 KEIAPKLAEAGAKVIDLSSDFRMD------------------DDVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 3-141 1.83e-41

Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 140.76  E-value: 1.83e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909     3 KVAIVGASGYTGVELIRLLLNHPQVEITC-VTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIirKSDFVFTALPHKAA 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTAlAASSRSAGKKVSEAGPHLKGEVVLELDPPDFEEL--AVDIVFLALPHGVS 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499660909    82 MAVV---PAFLHAGKKVVDLSADYRLHdvdvyeawydkhtspellDEAVYGLPELYRQQVVDA 141
Cdd:smart00859  79 KESApllPRAAAAGAVVIDLSSAFRMD------------------DDVPYGLPEVNPEAIKKA 123
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 3-148 4.20e-36

N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. The model corresponds to the AGPR N-terminal NAD(P)-binding domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467525 [Multi-domain]  Cd Length: 154  Bit Score: 128.00  E-value: 4.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   3 KVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTIIRKSDFVFTALPHKAAM 82
Cdd:cd24149    2 RVGLIGARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVSGYTKSPIDYLNLSVEDIPEEVAAREVDAWVLALPNGVAK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499660909  83 AVVPAFLHAGKK--VVDLSADYRLHDvdvyeAWydkhtspelldeaVYGLPELYRQQVVDARLVANPG 148
Cdd:cd24149   82 PFVDAIDKANPKsvIVDLSADYRFDD-----AW-------------TYGLPELNRRRIAGAKRISNPG 131
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 3-147 2.99e-34

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467515 [Multi-domain]  Cd Length: 160  Bit Score: 123.45  E-value: 2.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   3 KVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAG-RIDLTFDPVDVdtiIRKSDFVFTALPHKAA 81
Cdd:cd02280    2 RVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIIsLQIQEFRPCEV---LNSADILVLALPHGAS 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499660909  82 MAVVPAFLHAGKKVVDLSADYRLHDVDVYEawydKHTSPELLDEAVYGLPELYRQQ-VVDARLVANP 147
Cdd:cd02280   79 AELVAAISNPQVKIIDLSADFRFTDPEVYR----RHPRPDLEGGWVYGLPELDREQrIANATRIANP 141
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 3-147 1.66e-33

N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate reductase (actinobacAGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC). There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The family includes N-acetyl-gamma-glutamyl-phosphate reductases mainly from actinobacteria. They belong to the type 1 AGPR family. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467524 [Multi-domain]  Cd Length: 164  Bit Score: 121.63  E-value: 1.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   3 KVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVDTiIRKSDFVFTALPHKAAM 82
Cdd:cd24148    2 RVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHLPPLADRVLEPTTPAV-LAGHDVVFLALPHGASA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499660909  83 AVVpAFLHAGKKVVDLSADYRLHDVDVYEAWYDKhtspELLDEAVYGLPEL--YRQQVVDARLVANP 147
Cdd:cd24148   81 AIA-AQLPPDVLVVDCGADHRLEDAAAWEKFYGG----EHAGGWTYGLPELpgAREALAGARRIAVP 142
argC_other TIGR01851
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ...
 49-329 8.81e-33

N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273833 [Multi-domain]  Cd Length: 310  Bit Score: 123.80  E-value: 8.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   49 LAGRIDLTFDPVDVD---------TIIRKSDFVFTALPHKAAMAVVPAFLHAGKKVVDLSADYRLHDvdvyeAWydkhts 119
Cdd:TIGR01851  21 LSGRDDIELLSIAPDrrkdaaeraKLLNAADVAILCLPDDAAREAVSLVDNPNTCIIDASTAYRTAD-----DW------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  120 pelldeaVYGLPEL---YRQQVVDARLVANPGCYPTSIALGLAPLLENNLIDAASLI-IDSKSGTSGAGRSA----KVGS 191
Cdd:TIGR01851  90 -------AYGFPELapgQREKIRNSKRIANPGCYPTGFIALMRPLVEAGILPADFPItINAVSGYSGGGKAMiadyEQGS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  192 LYCEVNEGFKAYGVA-SHRHTPEIEQTlGQLAGKPVqvsFTPHLLPVNRGILSTC---YASLVQPMDTAQLQQLYAQRYA 267
Cdd:TIGR01851 163 ADNPSLQPFRIYGLAlTHKHLPEMRVH-SGLALPPI---FTPAVGNFAQGMAVTIplhLQTLASKVSPADIHAALADYYQ 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499660909  268 GEIFVRVHPQGELP----NILHVRGSNYCNIG---VVSDKRTGRVIIVSVIDNLLKGAASQAVQNMNLM 329
Cdd:TIGR01851 239 GEQFVRVAPLDDVEtldnTFLDPQGLNGTNRLdlfVFGSDDGERALLVARLDNLGKGASGAAVQNLNIM 307
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 158-316 1.40e-27

Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase.


Pssm-ID: 397067 [Multi-domain]  Cd Length: 167  Bit Score: 105.86  E-value: 1.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  158 LAPLLENnLIDAASLIIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVAS-HRHTPEIEQTLGQLAGKPVQVSFTP---- 232
Cdd:pfam02774   1 LKPLRDA-LGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGEeHNGTPETREELKMVNETKKILGFTPkvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  233 --HLLPVNRGILSTCYASL-VQPMDTAQLQQLYAQryAGEIFVRVHPQGELPNILHVRG-SNYCNIGVV-SDKRTGR-VI 306
Cdd:pfam02774  80 tcVRVPVFRGHSETVTVKLkLKPIDVEEVYEAFYA--APGVFVVVRPEEDYPTPRAVRGgTNFVYVGRVrKDPDGDRgLK 157

                         170
                  ....*....|
gi 499660909  307 IVSVIDNLLK 316
Cdd:pfam02774 158 LVSVIDNLRK 167
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 148-318 2.08e-25

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family.


Pssm-ID: 467684  Cd Length: 178  Bit Score: 100.37  E-value: 2.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 148 GCYPTSIALGLAPLLENNLIDA-ASLIIDSKSGTSGAGRsaKVGSLYCEVNEG----FKAYGVA-SHRHTPEIeQTLGQL 221
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPAdYPLSIHAVSGYSGGGK--KMIEQYEAAEAAdlppPRPYGLGlEHKHLPEM-QKHAGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 222 AGKPVqvsFTPHLLPVNRGILSTC---YASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVR-----GSNYCN 293
Cdd:cd23935   78 ARPPI---FTPAVGNFYQGMLVTVplhLDLLEKGVSAAEVHEALAEHYAGERFVKVMPLDEPDALGFLDpqalnGTNNLE 154

                        170       180
                 ....*....|....*....|....*.
gi 499660909 294 IGV-VSDKrtGRVIIVSVIDNLLKGA 318
Cdd:cd23935  155 LFVfGNDK--GQALLVARLDNLGKGA 178
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 148-318 2.69e-23

C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. This model corresponds to the AGPR C-terminal catalytic domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467685  Cd Length: 161  Bit Score: 94.24  E-value: 2.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 148 GCYPTSIALGLAPLLENNLIDAASLIIdskSGTSGAGR--SAK--VGSLycevNEGFKAYGVASHRHTPEIEQTLGQlag 223
Cdd:cd23936    1 GCYATGAQLALAPLLDDLDGPPSVFGV---SGYSGAGTkpSPKndPEVL----ADNLIPYSLVGHIHEREVSRHLGT--- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 224 kpvQVSFTPHLLPVNRGILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVhpQGELPNILHVRGSNYCNI-GVVSDKRT 302
Cdd:cd23936   71 ---PVAFMPHVAPWFQGITLTISIPLKKSMTADEIRELYQEAYAGEPLIKV--TKEIPLVRDNAGKHGVVVgGFTVHPDG 145

                        170
                 ....*....|....*.
gi 499660909 303 GRVIIVSVIDNLLKGA 318
Cdd:cd23936  146 KRVVVVATIDNLLKGA 161
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 3-147 3.01e-22

N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and N-acetyl-gamma-glutamyl-phosphate reductase (AGPR); Aspartate-beta-semialdehyde dehydrogenase (ASADH, EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the second step of the aspartate biosynthetic pathway, an essential enzyme found in bacteria, fungi, and higher plants. ASADH catalyses the formation of L-aspartate-beta-semialdehyde (ASA) by the reductive dephosphorylation of L-beta-aspartyl phosphate (BAP), utilizing the reducing power of NADPH. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. N-acetyl-gamma-glutamyl-phosphate reductase (AGPR, EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, reversibly catalyses the NADPH-dependent reduction of N-acetyl-gamma-glutamyl phosphate; the third step of arginine biosynthesis. ASADH and AGPR proteins contain an N-terminal Rossmann fold NAD(P)H binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467516 [Multi-domain]  Cd Length: 145  Bit Score: 90.89  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   3 KVAIVGASGYTGVELIRLLLNHP-QVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVdtiIRKSDFVFTALPHKAA 81
Cdd:cd02281    2 KVGVVGATGYVGGEFLRLLLEHPfPLFEIVLLAASSAGAKKKYFHPKLWGRVLVEFTPEEV---LEQVDIVFTALPGGVS 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499660909  82 MAVVPAFLHAGKKVVDLSADYRlhdvdvyeawydkhtspeLLDEAVYGLPELYRQQVV---DARLVANP 147
Cdd:cd02281   79 AKLAPELSEAGVLVIDNASDFR------------------LDKDVPLVVPEVNREHIGelkGTKIIANP 129
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-331 2.82e-18

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 84.49  E-value: 2.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   1 MLKVAIVGASGYTGVELIRLLLNHPQVEITCVT-SRQNAGAS-IDSVFPSLAGRI-----DLTFDPVDVDTiIRKSDFVF 73
Cdd:PRK08664   3 KLKVGILGATGMVGQRFVQLLANHPWFEVTALAaSERSAGKTyGEAVRWQLDGPIpeevaDMEVVSTDPEA-VDDVDIVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  74 TALPHKAAMAVVPAFLHAGKKVVDLSADYRLHDvDVyeawydkhtsPELLDEAVYGLPELYRQQ----VVDARLVANPGC 149
Cdd:PRK08664  82 SALPSDVAGEVEEEFAKAGKPVFSNASAHRMDP-DV----------PLVIPEVNPEHLELIEVQrkrrGWDGFIVTNPNC 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 150 YPTSIALGLAPLLENNL--IDAASL--IidsksgtSGAGRSakvgslycevnegfkayGVAShrhtPEI----------E 215
Cdd:PRK08664 151 STIGLVLALKPLMDFGIerVHVTTMqaI-------SGAGYP-----------------GVPS----MDIvdnvipyiggE 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 216 QT---------LGQLAGKPVQ-----VSFTPHLLPVNRGILSTCYASLVQPMDTAQLQQLYaQRYAGEI----------- 270
Cdd:PRK08664 203 EEkieketlkiLGKFEGGKIVpadfpISATCHRVPVIDGHTEAVFVKFKEDVDPEEIREAL-ESFKGLPqelglpsapkk 281

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499660909 271 FVRVHPQGELPN-ILHVrgsNYCN-----IGVVSDKRTGRVIIVSVIDNLLKGAASQAVQNMNLMQA 331
Cdd:PRK08664 282 PIILFEEPDRPQpRLDR---DAGDgmavsVGRLREDGIFDIKFVVLGHNTVRGAAGASVLNAELLKK 345
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 149-314 5.48e-18

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 80.26  E-value: 5.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 149 CYPTSIALGLAPLLENNLIDAASliIDSKSGTSGAGRSAKVGSLYCEVNEGFKAYGVASHRHTPEIEQTLGQLaGKPVQV 228
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEIL--VVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGEI-GKPIKV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 229 SFTPHLLPVNRGILSTCYASLVQPMDTAQLQQLYAQRYAGEIFVRVHPQGELPNILHVR-GSNYCNIGVVSDKRTGR--V 305
Cdd:cd18122   78 DGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVgGVYGVPVGRQREFAFDDnkL 157


                 ....*....
gi 499660909 306 IIVSVIDNL 314
Cdd:cd18122  158 KVFSAVDNE 166
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 2-109 2.12e-13

N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of ASADH enzymes that has a similar overall fold and domain organization but sharing very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain. Family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.


Pssm-ID: 467518  Cd Length: 162  Bit Score: 67.13  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVT-SRQNAGAS--------IDSVFPSLAGriDLTFDPVDvDTIIRKSDFV 72
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGaSERSAGKKygdavrwkQDTPIPEEVA--DMVVKECE-PEEFKDCDIV 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499660909  73 FTALPHKAAMAVVPAFLHAGKKVVDLSADYRLhDVDV 109
Cdd:cd02315   78 FSALDSDVAGEIEPAFAKAGIPVFSNASNHRM-DPDV 113
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 2-109 3.01e-09

N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar proteins; Archaeal NADP-dependent MCR (EC 1.2.1.75) catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA. Sequence comparison suggests that the archaeal malonyl-CoA reductase gene (mcr) has evolved from the duplication of a common ancestral aspartate beta-semialdehyde dehydrogenase (ASADH) gene (asd). MCR contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain.


Pssm-ID: 467526  Cd Length: 163  Bit Score: 55.41  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGA---------SIDSVFPSLAGRIDLTFDPVDVDTIirksDFV 72
Cdd:cd24150    2 LKAAILGATGLVGIEYVRMLSNHPYIKPAYLAGKGSVGKpygevvrwqTVGQVPKEIADMEIKPTDPKLMDDV----DII 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499660909  73 FTALPHKAAMAVVPAFLHAGKKVVDLSADYRLhDVDV 109
Cdd:cd24150   78 FSPLPQGAAGPVEEQFAKEGFPVISNSPDHRF-DPDV 113
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 2-109 6.64e-08

N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 protein and similar proteins; The family includes aspartate beta-semialdehyde dehydrogenase (ASADH), NADP-dependent malonyl-CoA reductase (MCR), and USG-1 protein. They contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain and are members of the GAPDH superfamily of proteins. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. NADP-dependent MCR (EC 1.2.1.75) is mainly found in Archaea. It catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA. Sequence comparison suggests that the archaeal MCR gene (mcr) has evolved from the duplication of a common ancestral ASADH gene (asd). The biological function of USG-1 protein and homologs remains unclear. They are homologs to ASADH but lack the conserved active site residues of the ASADH protein C-terminal catalytic domain.


Pssm-ID: 467523 [Multi-domain]  Cd Length: 142  Bit Score: 51.18  E-value: 6.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQV--EITCVTSRQNAGASIDsvFPSLAGRIDLTFDPVdvdtiIRKSDFVFTALPHK 79
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEPDPlfELRALASEESAGKKAE--FAGEAIMVQEADPID-----FLGLDIVFLCAGAG 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 499660909  80 AAMAVVPAFLHAGKKVVDLSADYRLhDVDV 109
Cdd:cd24147   74 VSAKFAPEAARAGVLVIDNAGALRM-DPDV 102
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 3-148 1.21e-07

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family.


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 49.91  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   3 KVAIVGASGYTGVELIRLLLNHPQVEITcvtsrqnagaSIDSvfpslagriDLTFDPVDVDTIIRKSDFVFTALPHKAAM 82
Cdd:cd17896    2 KVFIDGEAGTTGLQIRERLAGRSDIELL----------SIPE---------DKRKDPAARAELLNAADIAILCLPDDAAR 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499660909  83 AVVPAFLHAGKKVVDLSADYRLHDvdvyeAWydkhtspelldeaVYGLPEL---YRQQVVDARLVANPG 148
Cdd:cd17896   63 EAVALVTNPRTRIIDASTAHRTAP-----GW-------------AYGFPELspeQREKIATSKRVANPG 113
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 2-96 1.52e-07

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 49.87  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGaSIDSVFPSLAGRIDLTFDPVDVDTIIRKSDFV--FTAlpHK 79
Cdd:cd02274    1 IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSG-LLGGDAGGLAGIGTGVIVSLDLELAAADADVVidFTT--PE 77

                         90
                 ....*....|....*..
gi 499660909  80 AAMAVVPAFLHAGKKVV 96
Cdd:cd02274   78 ATLENLEAAAKAGVPLV 94
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 2-96 4.91e-06

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 47.42  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNA-GASIDSVFPSLAGRIDLTFDPVDVDTIIrksDfvFTAlpHKA 80
Cdd:COG0289    1 IKIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPGSpGQDAGELALGVPVTDDLEEALAKADVVI---D--FTH--PEA 73

                         90
                 ....*....|....*.
gi 499660909  81 AMAVVPAFLHAGKKVV 96
Cdd:COG0289   74 TLENLEAALEAGVPVV 89
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 2-96 5.90e-06

Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 44.92  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909    2 LKVAIVGASGYTGVELIRLLLNHPQVEITCVTSRQNAGASIDSVFPSLAGRIDLTFDPVDVdtiIRKSDFV--FTAlpHK 79
Cdd:pfam01113   1 IKIAVAGASGRMGRELIKAVLEAPDLELVAAVDRPGSSLLGSDAGELAPLGVPVTDDLEEV---LADADVLidFTT--PE 75

                          90
                  ....*....|....*..
gi 499660909   80 AAMAVVPAFLHAGKKVV 96
Cdd:pfam01113  76 ATLENLEFALKHGVPLV 92
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 4-324 6.78e-06

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 47.35  E-value: 6.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   4 VAIVGASGYTGVELIRLLLNHPQ---VEITCVTSRQNAGASIdsvfpSLAGRiDLTFDPVDVdTIIRKSDFVFTALPHKA 80
Cdd:PRK06728   8 VAVVGATGAVGQKIIELLEKETKfniAEVTLLSSKRSAGKTV-----QFKGR-EIIIQEAKI-NSFEGVDIAFFSAGGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  81 AMAVVPAFLHAGKKVVDLSADYRL-HDVDVYEAWYDKHTSPElldeavyglpelyrqqvvDARLVANPGCYPTSIALGLA 159
Cdd:PRK06728  81 SRQFVNQAVSSGAIVIDNTSEYRMaHDVPLVVPEVNAHTLKE------------------HKGIIAVPNCSALQMVTALQ 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 160 PLLENNLIDaaSLIIDSKSGTSGAGRSA---------------KVGSLYCEVNEGFKAYGVA---------------SHR 209
Cdd:PRK06728 143 PIRKVFGLE--RIIVSTYQAVSGSGIHAiqelkeqaksilageEVESTILPAKKDKKHYPIAfnvlpqvdiftdndfTFE 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 210 HTPEIEQTLGQLAGKPVQVSFTPHLLPVNRGILSTCYASLVQPMDTAQLQQLYAQryAGEIFVRVHPQGEL-PNILHVRG 288
Cdd:PRK06728 221 EVKMIQETKKILEDPNLKMAATCVRVPVISGHSESVYIELEKEATVAEIKEVLFD--APGVILQDNPSEQLyPMPLYAEG 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 499660909 289 SNYCNIGVVS---DKRTG-RVIIVSviDNLLKGAASQAVQ 324
Cdd:PRK06728 299 KIDTFVGRIRkdpDTPNGfHLWIVS--DNLLKGAAWNSVQ 336
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 2-145 2.27e-05

N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes Escherichia coli USG-1 protein, Pseudomonas aeruginosa USG-1 homolog proteins and similar proteins. Although their biological function remains unknown, they are homologs to aspartate beta-semialdehyde dehydrogenase (ASADH) which contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. However, USG-1 proteins lack the conserved active site residues of the ASADH protein C-terminal domain.


Pssm-ID: 467520 [Multi-domain]  Cd Length: 144  Bit Score: 43.76  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLLNH--PQVEITCVTSRQNAGASIdsvfpSLAGRiDLTFDPVDVDTIiRKSDFVFTALPHK 79
Cdd:cd17894    1 YRIAVVGATGLVGKELLELLEERgfPVGRLRLLDSEESAGELV-----EFGGE-PLDVQDLDEFDF-SDVDLVFFAGPAE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499660909  80 AAMAVVPAFLHAGKKVVDLSADYRLH-DVDVYEAWYDKHTSPELLDEAVYGLPELYRQQVVDARLVA 145
Cdd:cd17894   74 VARAYAPRARAAGCLVIDLSGALRSDpDVPLVVPGVNPEALAAAAERRVVAVPNNRRGAALNAVEIA 140
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 2-324 2.51e-05

Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439906 [Multi-domain]  Cd Length: 333  Bit Score: 45.41  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLLL--NHPQVEITCVTSRQNAGASIdsvfpSLAGRiDLTFDPVDvDTIIRKSDFVFTALPHK 79
Cdd:COG0136    1 YNVAVVGATGAVGRVLLELLEerDFPVGELRLLASSRSAGKTV-----SFGGK-ELTVEDAT-DFDFSGVDIALFSAGGS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909  80 AAMAVVPAFLHAGKKVVDLSADYRLHDvDVyeawydkhtsPeLLdeavygLPELYRQQVVDAR---LVANPGCyPTSIAL 156
Cdd:COG0136   74 VSKEYAPKAAAAGAVVIDNSSAFRMDP-DV----------P-LV------VPEVNPEALADHLpkgIIANPNC-STIQML 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 157 -GLAPLLENNLID--------AAsliidsksgtSGAGRSAkvgslyceVNEgfkaygvashrhtpEIEQTLGQLAGKPVQ 227
Cdd:COG0136  135 vALKPLHDAAGIKrvvvstyqAV----------SGAGAAA--------MDE--------------LAEQTAALLNGEEIE 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909 228 VSFTPH-----LLP-----------------VN--RGIL--------STC-------------YASLVQPMDTAQLQQLY 262
Cdd:COG0136  183 PEVFPHpiafnLIPqidvflengytkeemkmVNetRKILgdpdipvsATCvrvpvfrghseavNIEFERPVSLEEARELL 262

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499660909 263 AQryAGEIFVRVHPQ-GELPNILHVRGSNYCNIGVV----SDKRTGRVIIVSviDNLLKGAASQAVQ 324
Cdd:COG0136  263 AA--APGVKVVDDPAeNDYPTPLDASGTDEVFVGRIrkdlSVPNGLNLWVVA--DNLRKGAALNAVQ 325
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 2-106 3.88e-03

N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase 2 (ASADH2) and similar proteins; The family corresponds to a new branch of bacterial ASADH enzymes that has a similar overall fold and domain organization but sharing less sequence homology with the other bacterial ASADHs. The second isoform of ASADH in Vibrio cholerae is one of the prototypes of this family. It also includes ASADHs from Streptococcus pneumoniae, Mycobacterium tuberculosis, Thermus thermophilus, as well as from eukaryotes. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain.


Pssm-ID: 467519 [Multi-domain]  Cd Length: 142  Bit Score: 37.03  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499660909   2 LKVAIVGASGYTGVELIRLL--LNHPQVEITCVTSRQNAGASIdsvfpSLAGRiDLTFDPVDVDTiIRKSDFVFTALPHK 79
Cdd:cd02316    1 YNVAIVGATGAVGQEMLKVLeeRNFPVSELRLLASARSAGKTL-----EFKGK-ELTVEELTEDS-FKGVDIALFSAGGS 73

                         90       100
                 ....*....|....*....|....*..
gi 499660909  80 AAMAVVPAFLHAGKKVVDLSADYRLHD 106
Cdd:cd02316   74 VSKEFAPIAAEAGAVVIDNSSAFRMDP 100
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 308-329 6.19e-03

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family.


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 36.43  E-value: 6.19e-03
                         10        20
                 ....*....|....*....|..
gi 499660909 308 VSVIDNLLKGAASQAVQNMNLM 329
Cdd:cd17896  109 VANPGNLGKGASGAAVQNMNLM 130
 
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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