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Conserved domains on  [gi|1906447529|ref|WP_189214422|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Actinokineospora fastidiosa]

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

CATH:  3.40.50.720
EC:  1.2.1.38
Gene Ontology:  GO:0051287|GO:0070401|GO:0008652|GO:0016620|GO:0003942
PubMed:  17316682
SCOP:  4000077

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]; ...
 3-340 2.57e-169

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: 474.56  E-value: 2.57e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADRVLAETTP-EVLKDHDVVFLALPHGHS 81
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPdELAAGCDVVFLALPHGVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529  82 AAIAAQLPD-DVLVIDCGADHRLNDPTAWDRWYGGEHA-----GAWPYGLPELpgGRDALVGARRIAVPGCYPTVSSLAL 155
Cdd:COG0002    81 MELAPELLEaGVKVIDLSADFRLKDPAVYEKWYGFEHAapellGEAVYGLPEL--NREEIKGARLIANPGCYPTAVLLAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 156 APALAAGLIDPE-VVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGaHRHTPEIAQNLGRAAGRPIAVSFTPVLAPL 234
Cdd:COG0002   159 APLLKAGLIDPDdIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGG-HRHTPEIEQELSRLAGEDVKVSFTPHLVPM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 235 PRGILATCSAQLTGGGD--EVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLIAVGAVDNLTKG 312
Cdd:COG0002   238 VRGILATIYARLKDGVTeeDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKG 317

                         330       340
                  ....*....|....*....|....*...
gi 1906447529 313 TAGAAVQSMNIALGLPETTGLSTVGVAP 340
Cdd:COG0002   318 AAGQAVQNMNLMFGLPETTGLELVPLYP 345
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 3-340 2.57e-169

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: 474.56  E-value: 2.57e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADRVLAETTP-EVLKDHDVVFLALPHGHS 81
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPdELAAGCDVVFLALPHGVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529  82 AAIAAQLPD-DVLVIDCGADHRLNDPTAWDRWYGGEHA-----GAWPYGLPELpgGRDALVGARRIAVPGCYPTVSSLAL 155
Cdd:COG0002    81 MELAPELLEaGVKVIDLSADFRLKDPAVYEKWYGFEHAapellGEAVYGLPEL--NREEIKGARLIANPGCYPTAVLLAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 156 APALAAGLIDPE-VVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGaHRHTPEIAQNLGRAAGRPIAVSFTPVLAPL 234
Cdd:COG0002   159 APLLKAGLIDPDdIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGG-HRHTPEIEQELSRLAGEDVKVSFTPHLVPM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 235 PRGILATCSAQLTGGGD--EVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLIAVGAVDNLTKG 312
Cdd:COG0002   238 VRGILATIYARLKDGVTeeDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKG 317

                         330       340
                  ....*....|....*....|....*...
gi 1906447529 313 TAGAAVQSMNIALGLPETTGLSTVGVAP 340
Cdd:COG0002   318 AAGQAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 3-340 1.03e-150

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: 427.38  E-value: 1.03e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAG-GNAGSALGEHQPHLLPLADRVLAETTPE-VLKDHDVVFLALPHGH 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSrESAGKPVSEVHPHLRGLVDLNLEPIDVEeILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529  81 SAAIAAQLPD-DVLVIDCGADHRLNDPTAWDRWYGGEHAGA-----WPYGLPELPggRDALVGARRIAVPGCYPTVSSLA 154
Cdd:TIGR01850  81 SAELAPELLAaGVKVIDLSADFRLKDPELYEKWYGFEHAGPellqkAVYGLPELH--REEIKGARLIANPGCYPTATLLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 155 LAPALAAGLIDPEVVVV-AVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGaHRHTPEIAQNLGRAAGRPIAVSFTPVLAP 233
Cdd:TIGR01850 159 LAPLLKEGLIDPTSIIVdAKSGVSGAGRKASEANHFPEVNENLRPYKVTG-HRHTPEIEQELGRLAGGKVKVSFTPHLVP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 234 LPRGILATCSAQLTGG--GDEVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLIAVGAVDNLTK 311
Cdd:TIGR01850 238 MTRGILATIYAKLKDGltEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVK 317

                         330       340
                  ....*....|....*....|....*....
gi 1906447529 312 GTAGAAVQSMNIALGLPETTGLSTVGVAP 340
Cdd:TIGR01850 318 GAAGQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-333 2.50e-89

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 272.47  E-value: 2.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   2 TVRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADRVLAETTPEVLKDHDVVFLALPHGHS 81
Cdd:PLN02968   38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDLPNLVAVKDADFSDVDAVFCCLPHGTT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529  82 AAIAAQLPDDVLVIDCGADHRLNDPTAWDRWYGGEHAGAWP-----YGLPELPggRDALVGARRIAVPGCYPTVSSLALA 156
Cdd:PLN02968  118 QEIIKALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELqkeavYGLTELQ--REEIKSARLVANPGCYPTGIQLPLV 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 157 PALAAGLIDPEVVVV-AVSGTSGAGKALKPHLLGSEVMGSLSVYGVgGAHRHTPEIAQNLGRAAGRPIAVSFTPVLAPLP 235
Cdd:PLN02968  196 PLVKAGLIEPDNIIIdAKSGVSGAGRGAKEANLYTEIAEGIGAYGV-TRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMS 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 236 RGILATCSAQLTGG--GDEVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLIAVGAVDNLTKGT 313
Cdd:PLN02968  275 RGMQSTVYVHYAPGvtAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKGA 354

                         330       340
                  ....*....|....*....|
gi 1906447529 314 AGAAVQSMNIALGLPETTGL 333
Cdd:PLN02968  355 SGQAVQNLNLMMGLPETTGL 374
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 3-144 2.48e-82

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: 246.82  E-value: 2.48e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADRVLAETTPEVLKDHDVVFLALPHGHSA 82
Cdd:cd24148     1 IRVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHLPPLADRVLEPTTPAVLAGHDVVFLALPHGASA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906447529  83 AIAAQLPDDVLVIDCGADHRLNDPTAWDRWYGGEHAGAWPYGLPELPGGRDALVGARRIAVP 144
Cdd:cd24148    81 AIAAQLPPDVLVVDCGADHRLEDAAAWEKFYGGEHAGGWTYGLPELPGAREALAGARRIAVP 142
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 168-311 2.54e-29

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: 110.48  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 168 VVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGAHRHTPEIAQNLGRAAGRPIAVSFTP------VLAPLPRGILAT 241
Cdd:pfam02774  14 VIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGEEHNGTPETREELKMVNETKKILGFTPkvsatcVRVPVFRGHSET 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906447529 242 CSAQLTGGGDEVRAAYAKAYEH-EPFVHLLPEGRWPTTAAVLG-SNAVQLQ-VTVDPDLDR-LIAVGAVDNLTK 311
Cdd:pfam02774  94 VTVKLKLKPIDVEEVYEAFYAApGVFVVVRPEEDYPTPRAVRGgTNFVYVGrVRKDPDGDRgLKLVSVIDNLRK 167
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-138 1.16e-28

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: 107.25  E-value: 1.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529    4 RVAVAGASGYAGGEALRLLLGHPDVEIGALTAG-GNAGSALGEHQPHLLPLADRVLAETTPEVLkDHDVVFLALPHGHSA 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASsRSAGKKVSEAGPHLKGEVVLELDPPDFEEL-AVDIVFLALPHGVSK 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   83 AIAAQLPD----DVLVIDCGADHRLNDPtawdrwyggehagaWPYGLPELPggRDALVGA 138
Cdd:smart00859  80 ESAPLLPRaaaaGAVVIDLSSAFRMDDD--------------VPYGLPEVN--PEAIKKA 123
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 3-340 2.57e-169

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: 474.56  E-value: 2.57e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADRVLAETTP-EVLKDHDVVFLALPHGHS 81
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPdELAAGCDVVFLALPHGVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529  82 AAIAAQLPD-DVLVIDCGADHRLNDPTAWDRWYGGEHA-----GAWPYGLPELpgGRDALVGARRIAVPGCYPTVSSLAL 155
Cdd:COG0002    81 MELAPELLEaGVKVIDLSADFRLKDPAVYEKWYGFEHAapellGEAVYGLPEL--NREEIKGARLIANPGCYPTAVLLAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 156 APALAAGLIDPE-VVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGaHRHTPEIAQNLGRAAGRPIAVSFTPVLAPL 234
Cdd:COG0002   159 APLLKAGLIDPDdIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGG-HRHTPEIEQELSRLAGEDVKVSFTPHLVPM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 235 PRGILATCSAQLTGGGD--EVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLIAVGAVDNLTKG 312
Cdd:COG0002   238 VRGILATIYARLKDGVTeeDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKG 317

                         330       340
                  ....*....|....*....|....*...
gi 1906447529 313 TAGAAVQSMNIALGLPETTGLSTVGVAP 340
Cdd:COG0002   318 AAGQAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 3-340 1.03e-150

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: 427.38  E-value: 1.03e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAG-GNAGSALGEHQPHLLPLADRVLAETTPE-VLKDHDVVFLALPHGH 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSrESAGKPVSEVHPHLRGLVDLNLEPIDVEeILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529  81 SAAIAAQLPD-DVLVIDCGADHRLNDPTAWDRWYGGEHAGA-----WPYGLPELPggRDALVGARRIAVPGCYPTVSSLA 154
Cdd:TIGR01850  81 SAELAPELLAaGVKVIDLSADFRLKDPELYEKWYGFEHAGPellqkAVYGLPELH--REEIKGARLIANPGCYPTATLLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 155 LAPALAAGLIDPEVVVV-AVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGaHRHTPEIAQNLGRAAGRPIAVSFTPVLAP 233
Cdd:TIGR01850 159 LAPLLKEGLIDPTSIIVdAKSGVSGAGRKASEANHFPEVNENLRPYKVTG-HRHTPEIEQELGRLAGGKVKVSFTPHLVP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 234 LPRGILATCSAQLTGG--GDEVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLIAVGAVDNLTK 311
Cdd:TIGR01850 238 MTRGILATIYAKLKDGltEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVK 317

                         330       340
                  ....*....|....*....|....*....
gi 1906447529 312 GTAGAAVQSMNIALGLPETTGLSTVGVAP 340
Cdd:TIGR01850 318 GAAGQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-333 2.50e-89

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 272.47  E-value: 2.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   2 TVRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADRVLAETTPEVLKDHDVVFLALPHGHS 81
Cdd:PLN02968   38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDLPNLVAVKDADFSDVDAVFCCLPHGTT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529  82 AAIAAQLPDDVLVIDCGADHRLNDPTAWDRWYGGEHAGAWP-----YGLPELPggRDALVGARRIAVPGCYPTVSSLALA 156
Cdd:PLN02968  118 QEIIKALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELqkeavYGLTELQ--REEIKSARLVANPGCYPTGIQLPLV 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 157 PALAAGLIDPEVVVV-AVSGTSGAGKALKPHLLGSEVMGSLSVYGVgGAHRHTPEIAQNLGRAAGRPIAVSFTPVLAPLP 235
Cdd:PLN02968  196 PLVKAGLIEPDNIIIdAKSGVSGAGRGAKEANLYTEIAEGIGAYGV-TRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMS 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 236 RGILATCSAQLTGG--GDEVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLIAVGAVDNLTKGT 313
Cdd:PLN02968  275 RGMQSTVYVHYAPGvtAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKGA 354

                         330       340
                  ....*....|....*....|
gi 1906447529 314 AGAAVQSMNIALGLPETTGL 333
Cdd:PLN02968  355 SGQAVQNLNLMMGLPETTGL 374
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 3-144 2.48e-82

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: 246.82  E-value: 2.48e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADRVLAETTPEVLKDHDVVFLALPHGHSA 82
Cdd:cd24148     1 IRVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHLPPLADRVLEPTTPAVLAGHDVVFLALPHGASA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906447529  83 AIAAQLPDDVLVIDCGADHRLNDPTAWDRWYGGEHAGAWPYGLPELPGGRDALVGARRIAVP 144
Cdd:cd24148    81 AIAAQLPPDVLVVDCGADHRLEDAAAWEKFYGGEHAGGWTYGLPELPGAREALAGARRIAVP 142
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 145-313 2.82e-70

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: 216.58  E-value: 2.82e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 145 GCYPTVSSLALAPALAAGLIDPE-VVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGaHRHTPEIAQNLGRAAGRPI 223
Cdd:cd23934     1 GCYPTAALLALAPLLKAGLIEPDdIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGG-HRHTPEIEQELSKLAGEDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 224 AVSFTPVLAPLPRGILATCSAQLTGGG--DEVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLI 301
Cdd:cd23934    80 EVSFTPHLVPMTRGILATIYAKLKDGVtaEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLI 159

                         170
                  ....*....|..
gi 1906447529 302 AVGAVDNLTKGT 313
Cdd:cd23934   160 VVSAIDNLVKGA 171
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 4-144 1.11e-44

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: 150.41  E-value: 1.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   4 RVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPlADRVLAETTPEVLKDHDVVFLALPHGHSAA 83
Cdd:cd02280     2 RVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLII-SLQIQEFRPCEVLNSADILVLALPHGASAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906447529  84 IAAQLPD-DVLVIDCGADHRLNDPTAWDRWYGGEHAGAWPYGLPELPgGRDALVGARRIAVP 144
Cdd:cd02280    81 LVAAISNpQVKIIDLSADFRFTDPEVYRRHPRPDLEGGWVYGLPELD-REQRIANATRIANP 141
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 3-144 2.26e-44

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: 149.89  E-value: 2.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADRVLAETTPEVLKDH-DVVFLALPHGHS 81
Cdd:cd17895     1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTDLTFEPDDDEEIAEDaDVVFLALPHGVS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906447529  82 AAIAAQLPD-DVLVIDCGADHRLNDPTAWDRWYGGEHagAWP-------YGLPELPggRDALVGARRIAVP 144
Cdd:cd17895    81 MELAPKLLEaGVKVIDLSADFRLKDPETYEKWYGFEH--AAPellkeavYGLPELN--REEIKKARLVANP 147
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 146-313 2.52e-43

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: 147.26  E-value: 2.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 146 CYPTVSSLALAPALAAGLIDPE-VVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGaHRHTPEIAQNLGraaGRPiA 224
Cdd:cd18125     1 CYATAALLALYPLLKAGLLKPTpITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSG-HRHTPEIAQNLG---GKH-N 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 225 VSFTPVLAPLPRGILATCSAQLTGGG--DEVRAAYAKAYEHEPFVHLLPEGRWPTTAAVLGSNAVQLQVTVDPDLDRLIA 302
Cdd:cd18125    76 VHFTPHVGPWVRGILMTIQCFTQKGWslRQLHEAYREAYAGEPFVRVMPQGKGPDPKFVQGTNYADIGVELEEDTGRLVV 155

                         170
                  ....*....|.
gi 1906447529 303 VGAVDNLTKGT 313
Cdd:cd18125   156 MSAIDNLVKGA 166
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 3-142 3.35e-36

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: 128.55  E-value: 3.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHLLPLADrvLAETTPEVLKDHDVVFLALPHGHSA 82
Cdd:cd24151     1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNLRGRTL--LKFVPPEELESCDVLFLALPHGESM 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906447529  83 A-IAAQLPDDVLVIDCGADHRLNDPTAWDRWYGGEHA-----GAWPYGLPELpgGRDALVGARRIA 142
Cdd:cd24151    79 KrIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPrpellERFVYGLPEL--HREELRGARYIA 142
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 164-313 5.40e-33

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: 120.42  E-value: 5.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 164 IDPEVVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGaHRHTPEIAQNLGRAAgRPIAVSFTPVLAPLPRGILATCS 243
Cdd:cd23939    21 DDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTG-HRHTAEIEQELGLLA-REISVSFTAHSVDMVRGILATAH 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906447529 244 AQLTGGGDE--VRAAYAKAYEHEPFVHLLPEG----RWPTTAAVLGSNAVQLQVTVDPDLDRLIAVGAVDNLTKGT 313
Cdd:cd23939    99 VFLKEGVTEkdLWKAYRKAYGNEPFVRIVKDRkgiyRYPDPKLVIGSNFCDIGFELDEDNGRLVVFSAIDNLMKGA 174
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 168-311 2.54e-29

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: 110.48  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 168 VVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYGVGGAHRHTPEIAQNLGRAAGRPIAVSFTP------VLAPLPRGILAT 241
Cdd:pfam02774  14 VIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGEEHNGTPETREELKMVNETKKILGFTPkvsatcVRVPVFRGHSET 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906447529 242 CSAQLTGGGDEVRAAYAKAYEH-EPFVHLLPEGRWPTTAAVLG-SNAVQLQ-VTVDPDLDR-LIAVGAVDNLTK 311
Cdd:pfam02774  94 VTVKLKLKPIDVEEVYEAFYAApGVFVVVRPEEDYPTPRAVRGgTNFVYVGrVRKDPDGDRgLKLVSVIDNLRK 167
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-138 1.16e-28

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: 107.25  E-value: 1.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529    4 RVAVAGASGYAGGEALRLLLGHPDVEIGALTAG-GNAGSALGEHQPHLLPLADRVLAETTPEVLkDHDVVFLALPHGHSA 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASsRSAGKKVSEAGPHLKGEVVLELDPPDFEEL-AVDIVFLALPHGVSK 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   83 AIAAQLPD----DVLVIDCGADHRLNDPtawdrwyggehagaWPYGLPELPggRDALVGA 138
Cdd:smart00859  80 ESAPLLPRaaaaGAVVIDLSSAFRMDDD--------------VPYGLPEVN--PEAIKKA 123
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 4-138 4.08e-26

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: 100.68  E-value: 4.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   4 RVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGN-AGSALGEHQPHLLPLADRVLAETTPEVLKDHDVVFLALPHGHSA 82
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEGGKDLVVEDVDPEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1906447529  83 AIAAQLPD-DVLVIDCGADHRLNDptawdrwyggehagAWPYGLPELpgGRDALVGA 138
Cdd:pfam01118  81 EIAPKLAEaGAKVIDLSSDFRMDD--------------DVPYGLPEV--NREAIKQA 121
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 4-144 4.21e-25

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: 98.59  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   4 RVAVAGASGYAGGEALRLLLGHP-DVEIGALTAGGNAGSALGEHQPHLLPLadRVLAETTPEVLKDHDVVFLALPHGHSA 82
Cdd:cd02281     2 KVGVVGATGYVGGEFLRLLLEHPfPLFEIVLLAASSAGAKKKYFHPKLWGR--VLVEFTPEEVLEQVDIVFTALPGGVSA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906447529  83 AIAAQLPD-DVLVIDCGADHRLNdptawdrwyggehaGAWPYGLPELPGGR-DALVGARRIAVP 144
Cdd:cd02281    80 KLAPELSEaGVLVIDNASDFRLD--------------KDVPLVVPEVNREHiGELKGTKIIANP 129
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 4-145 5.87e-25

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: 98.34  E-value: 5.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   4 RVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGEHQPHlLPLADRVLAETTPEVLKDH--DVVFLALPHGHS 81
Cdd:cd24149     2 RVGLIGARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVSGYTKS-PIDYLNLSVEDIPEEVAARevDAWVLALPNGVA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906447529  82 A----AIAAQLPDDVlVIDCGADHRLNDptawdrwyggehagAWPYGLPELPggRDALVGARRIAVPG 145
Cdd:cd24149    81 KpfvdAIDKANPKSV-IVDLSADYRFDD--------------AWTYGLPELN--RRRIAGAKRISNPG 131
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 145-312 9.71e-16

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: 74.17  E-value: 9.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 145 GCYPTVSSLALAPALAAGLIDPE--VVVVAVSGTSGAGKAL--KPHLLGSEVMGSLSVYGVGGAHRHTPEIAQNLGRAAg 220
Cdd:cd23935     1 GCYATGAILLLRPLVEAGLLPADypLSIHAVSGYSGGGKKMieQYEAAEAADLPPPRPYGLGLEHKHLPEMQKHAGLAR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 221 RPIavsFTPVLAPLPRGILATC---SAQLTGG--GDEVRAAYAKAYEHEPFVHLLP--EGRWPTTA---AVLGSNAVQLQ 290
Cdd:cd23935    80 PPI---FTPAVGNFYQGMLVTVplhLDLLEKGvsAAEVHEALAEHYAGERFVKVMPldEPDALGFLdpqALNGTNNLELF 156

                         170       180
                  ....*....|....*....|..
gi 1906447529 291 VTVDPDlDRLIAVGAVDNLTKG 312
Cdd:cd23935   157 VFGNDK-GQALLVARLDNLGKG 177
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 145-312 3.76e-12

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: 63.42  E-value: 3.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 145 GCYPTVSSLALAPALAAGLIDPevVVVAVSGTSGAG---------KALKPHLLGSEVMGslsvygvggaHRHTPEIAQNL 215
Cdd:cd23936     1 GCYATGAQLALAPLLDDLDGPP--SVFGVSGYSGAGtkpspkndpEVLADNLIPYSLVG----------HIHEREVSRHL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 216 GRAagrpiaVSFTPVLAPLPRGILATCSAQL--TGGGDEVRAAYAKAYEHEPFVHLlpEGRWPTTAAVLGSNAVQLQ-VT 292
Cdd:cd23936    69 GTP------VAFMPHVAPWFQGITLTISIPLkkSMTADEIRELYQEAYAGEPLIKV--TKEIPLVRDNAGKHGVVVGgFT 140

                         170       180
                  ....*....|....*....|
gi 1906447529 293 VDPDLDRLIAVGAVDNLTKG 312
Cdd:cd23936   141 VHPDGKRVVVVATIDNLLKG 160
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 167-309 7.10e-11

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: 60.23  E-value: 7.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529 167 EVVVVAVSGTSGAGKALKPHLLGSEVMGSLSVYgVGGAHRHTPEIAQNLGRAaGRPIAVSFTPVLAPLPRGILATCSAQL 246
Cdd:cd18122    21 EILVVTVQAVSGAGPKTKGPILKSEVRAIIPNI-PKNETKHAPETGKVLGEI-GKPIKVDGIAVRVPATLGHLVTVTVKL 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906447529 247 --TGGGDEVRAAYAKAYEHEPFVHLLPEG-RWPTTAAVLGSNAVQL--QVTVDPDLDRLIAVGAVDNL 309
Cdd:cd18122    99 ekTATLEQIAEAVAEAVEEVQISAEDGLTyAKVSTRSVGGVYGVPVgrQREFAFDDNKLKVFSAVDNE 166
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 3-79 6.03e-10

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: 57.12  E-value: 6.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGALTA-GGNAGSALGE----HQPHLLP--LADRVLAETTPEVLKDHDVVFLA 75
Cdd:cd02315     1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGAsERSAGKKYGDavrwKQDTPIPeeVADMVVKECEPEEFKDCDIVFSA 80


                  ....
gi 1906447529  76 LPHG 79
Cdd:cd02315    81 LDSD 84
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-77 6.72e-09

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 56.37  E-value: 6.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   1 MTVRVAVAGASGYAGGEALRLLLGHPDVEIGALTAG-GNAGSALGE----HQPHLLP--LADRVLAETTPEVLKDHDVVF 73
Cdd:PRK08664    2 MKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASeRSAGKTYGEavrwQLDGPIPeeVADMEVVSTDPEAVDDVDIVF 81


                  ....
gi 1906447529  74 LALP 77
Cdd:PRK08664   82 SALP 85
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 2-104 4.77e-08

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: 51.94  E-value: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   2 TVRVAVAGASGYAGGEALRLLLGHPDVEIGALTAGGNAGSALGE----HQPHLLP--LADRVLAETTPEVLKDHDVVFLA 75
Cdd:cd24150     1 TLKAAILGATGLVGIEYVRMLSNHPYIKPAYLAGKGSVGKPYGEvvrwQTVGQVPkeIADMEIKPTDPKLMDDVDIIFSP 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1906447529  76 LPHGHSAAIAAQLPDDVL-VIDCGADHRLN 104
Cdd:cd24150    81 LPQGAAGPVEEQFAKEGFpVISNSPDHRFD 110
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 4-145 1.01e-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: 50.29  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   4 RVAVAGASGYAGGEALRLLLGHPDVEIgaLTaggnagsalgehqphlLPLADRVLAETTPEVLKDHDVVFLALPHGHS-A 82
Cdd:cd17896     2 KVFIDGEAGTTGLQIRERLAGRSDIEL--LS----------------IPEDKRKDPAARAELLNAADIAILCLPDDAArE 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906447529  83 AIAAQLPDDVLVIDCGADHRLNDptawdrwyggehagAWPYGLPEL-PGGRDALVGARRIAVPG 145
Cdd:cd17896    64 AVALVTNPRTRIIDASTAHRTAP--------------GWAYGFPELsPEQREKIATSKRVANPG 113
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 3-106 2.22e-04

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: 40.78  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDV--EIGALTAGGNAGsalgehQPHLLPLADRVLAETTPEVLKDHDVVFLALPHGH 80
Cdd:cd24147     1 LRVGVVGATGAVGSEILQLLAEEPDPlfELRALASEESAG------KKAEFAGEAIMVQEADPIDFLGLDIVFLCAGAGV 74

                          90       100
                  ....*....|....*....|....*..
gi 1906447529  81 SAAIAAQLPD-DVLVIDCGADHRLNDP 106
Cdd:cd24147    75 SAKFAPEAARaGVLVIDNAGALRMDPD 101
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 308-326 3.62e-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: 37.20  E-value: 3.62e-03
                          10
                  ....*....|....*....
gi 1906447529 308 NLTKGTAGAAVQSMNIALG 326
Cdd:cd17896   114 NLGKGASGAAVQNMNLMLG 132
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 3-69 4.64e-03

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: 36.44  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEIGAL---TAGGNAGSALGEHQPHLLPLADR---VLAE-------TTPEVLKDH 69
Cdd:pfam01113   1 IKIAVAGASGRMGRELIKAVLEAPDLELVAAvdrPGSSLLGSDAGELAPLGVPVTDDleeVLADadvlidfTTPEATLEN 80
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 3-69 5.91e-03

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: 37.79  E-value: 5.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906447529   3 VRVAVAGASGYAGGEALRLLLGHPDVEI-GALTAGGNAGSALGEHQPHLLPLAD--RVLAE-------TTPEVLKDH 69
Cdd:COG0289     1 IKIAVAGASGRMGRELIRAVLEAPDLELvAAIDRPGSPGQDAGELALGVPVTDDleEALAKadvvidfTHPEATLEN 77
 
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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