NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515667391|ref|WP_017099991|]
View 

MULTISPECIES: N-acetyl-gamma-glutamyl-phosphate reductase [Vibrio]

Protein Classification

NAGSA dehydrogenase family protein( domain architecture ID 11493209)

NAGSA (N-acetyl-glutamate semialdehyde) dehydrogenase family protein such as N-acetyl-gamma-glutamyl-phosphate reductase (also called NAGSA dehydrogenase) that 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:  3.30.360.10
EC:  1.2.1.-
Gene Ontology:  GO:0051287|GO:0070401|GO:0008652|GO:0046983|GO:0016620
PubMed:  10613839
SCOP:  4000077

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-333 1.26e-165

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: 465.13  E-value: 1.26e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391    2 LKTTIIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIAALHGKLAGLIDMPVQPLtNPEEVAKQSDVIFLATA 81
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRES--AGKPVSEVHPHLRGLVDLNLEPI-DVEEILEDADVVFLALP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   82 HEVSHDLAPIFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAVAGCYPTASQL 161
Cdd:TIGR01850  78 HGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  162 AIKPLVEAKLLDENQWpVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHLG------CDVIFTPHLG 233
Cdd:TIGR01850 158 ALAPLLKEGLIDPTSI-IVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHLV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  234 NFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGWKVQG--QHIIVVSAIDNLL 310
Cdd:TIGR01850 237 PMTRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEgGYPSTKAVIGSNFCDIGFAVDErtGRVVVVSAIDNLV 316

                         330       340
                  ....*....|....*....|...
gi 515667391  311 KGASSQAMQCLNLRYGFAPLTAL 333
Cdd:TIGR01850 317 KGAAGQAVQNMNLMFGFDETTGL 339
 
Name Accession Description Interval E-value
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-333 1.26e-165

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: 465.13  E-value: 1.26e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391    2 LKTTIIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIAALHGKLAGLIDMPVQPLtNPEEVAKQSDVIFLATA 81
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRES--AGKPVSEVHPHLRGLVDLNLEPI-DVEEILEDADVVFLALP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   82 HEVSHDLAPIFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAVAGCYPTASQL 161
Cdd:TIGR01850  78 HGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  162 AIKPLVEAKLLDENQWpVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHLG------CDVIFTPHLG 233
Cdd:TIGR01850 158 ALAPLLKEGLIDPTSI-IVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHLV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  234 NFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGWKVQG--QHIIVVSAIDNLL 310
Cdd:TIGR01850 237 PMTRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEgGYPSTKAVIGSNFCDIGFAVDErtGRVVVVSAIDNLV 316

                         330       340
                  ....*....|....*....|...
gi 515667391  311 KGASSQAMQCLNLRYGFAPLTAL 333
Cdd:TIGR01850 317 KGAAGQAVQNMNLMFGFDETTGL 339
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-333 8.22e-165

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: 463.00  E-value: 8.22e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   2 LKTTIIGASGYTGAELALMINRHPELTLSglYVSANSvDAGKPIAALHGKLAGLIDMPVQPLTnPEEVAKQSDVIFLATA 81
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIV--ALTSRS-NAGKPVSEVHPHLRGLTDLVFEPPD-PDELAAGCDVVFLALP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  82 HEVSHDLAPIFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAVAGCYPTASQL 161
Cdd:COG0002   77 HGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 162 AIKPLVEAKLLDENqWPVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHL------GCDVIFTPHLG 233
Cdd:COG0002  157 ALAPLLKAGLIDPD-DIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELsrlageDVKVSFTPHLV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 234 NFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGWKVQ--GQHIIVVSAIDNLL 310
Cdd:COG0002  236 PMVRGILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEgRLPETKSVRGSNFCDIGVAVDerTGRLVVVSAIDNLV 315

                        330       340
                 ....*....|....*....|...
gi 515667391 311 KGASSQAMQCLNLRYGFAPLTAL 333
Cdd:COG0002  316 KGAAGQAVQNMNLMFGLPETTGL 338
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 153-313 1.13e-78

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: 237.76  E-value: 1.13e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 153 GCYPTASQLAIKPLVEAKLLDENqWPVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHLG------C 224
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPD-DIIIDAKSGVSGAGRKASETTHFSEVneNLKAYKVGGHRHTPEIEQELSklagedV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 225 DVIFTPHLGNFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGWKVQG--QHII 301
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEgQLPSTKAVRGSNFCDIGVAVDGrtGRLI 159

                        170
                 ....*....|..
gi 515667391 302 VVSAIDNLLKGA 313
Cdd:cd23934  160 VVSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-333 7.08e-74

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 232.79  E-value: 7.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   1 MLKTTIIGASGYTGAELALMINRHPELtlsGLYVSANSVDAGKPIAALHGKLAGLiDMPVQPLTNPEEVAkQSDVIFLAT 80
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDF---EITVMTADRKAGQSFGSVFPHLITQ-DLPNLVAVKDADFS-DVDAVFCCL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  81 AHEVSHDLAPiFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAVAGCYPTASQ 160
Cdd:PLN02968 113 PHGTTQEIIK-ALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQ 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 161 LAIKPLVEAKLLDENQWpVINATSGVTGAGRKATMVNSFCEVS--LQAYGVFNHRHQPEM------AAHLGCDVIFTPHL 232
Cdd:PLN02968 192 LPLVPLVKAGLIEPDNI-IIDAKSGVSGAGRGAKEANLYTEIAegIGAYGVTRHRHVPEIeqgladAAGSKVTPSFTPHL 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 233 GNFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGW---KVQGQHIIvVSAIDN 308
Cdd:PLN02968 271 MPMSRGMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERgAVPHTDHVRGSNYCELNVfadRIPGRAII-ISVIDN 349

                        330       340
                 ....*....|....*....|....*
gi 515667391 309 LLKGASSQAMQCLNLRYGFAPLTAL 333
Cdd:PLN02968 350 LVKGASGQAVQNLNLMMGLPETTGL 374
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-146 3.57e-37

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: 129.57  E-value: 3.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391    6 IIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIAALHGKLAGLIDMPVQPLTnpEEVAKQSDVIFLATAHEVS 85
Cdd:pfam01118   4 IVGATGYVGQELLRLLEEHPPVELVVLFASSRS--AGKKLAFVHPILEGGKDLVVEDVD--PEDFKDVDIVFFALPGGVS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515667391   86 HDLAPIFLENDCQVFDLSGAFRVKgenfyqefygfehqheqwlDKAAYGLAEWNEQEIKEA 146
Cdd:pfam01118  80 KEIAPKLAEAGAKVIDLSSDFRMD-------------------DDVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 6-146 6.13e-32

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: 115.72  E-value: 6.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391     6 IIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIAALHGKLAGLIdmpVQPLTNPEEVAKQSDVIFLATAHEVS 85
Cdd:smart00859   4 IVGATGYVGQELLRLLAEHPDFELTALAASSRS--AGKKVSEAGPHLKGEV---VLELDPPDFEELAVDIVFLALPHGVS 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515667391    86 HD---LAPIFLENDCQVFDLSGAFRVKgenfyqefygfehqheqwlDKAAYGLAEWNEQEIKEA 146
Cdd:smart00859  79 KEsapLLPRAAAAGAVVIDLSSAFRMD-------------------DDVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-333 1.26e-165

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: 465.13  E-value: 1.26e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391    2 LKTTIIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIAALHGKLAGLIDMPVQPLtNPEEVAKQSDVIFLATA 81
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRES--AGKPVSEVHPHLRGLVDLNLEPI-DVEEILEDADVVFLALP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   82 HEVSHDLAPIFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAVAGCYPTASQL 161
Cdd:TIGR01850  78 HGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  162 AIKPLVEAKLLDENQWpVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHLG------CDVIFTPHLG 233
Cdd:TIGR01850 158 ALAPLLKEGLIDPTSI-IVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHLV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  234 NFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGWKVQG--QHIIVVSAIDNLL 310
Cdd:TIGR01850 237 PMTRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEgGYPSTKAVIGSNFCDIGFAVDErtGRVVVVSAIDNLV 316

                         330       340
                  ....*....|....*....|...
gi 515667391  311 KGASSQAMQCLNLRYGFAPLTAL 333
Cdd:TIGR01850 317 KGAAGQAVQNMNLMFGFDETTGL 339
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-333 8.22e-165

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: 463.00  E-value: 8.22e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   2 LKTTIIGASGYTGAELALMINRHPELTLSglYVSANSvDAGKPIAALHGKLAGLIDMPVQPLTnPEEVAKQSDVIFLATA 81
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIV--ALTSRS-NAGKPVSEVHPHLRGLTDLVFEPPD-PDELAAGCDVVFLALP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  82 HEVSHDLAPIFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAVAGCYPTASQL 161
Cdd:COG0002   77 HGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 162 AIKPLVEAKLLDENqWPVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHL------GCDVIFTPHLG 233
Cdd:COG0002  157 ALAPLLKAGLIDPD-DIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELsrlageDVKVSFTPHLV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 234 NFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGWKVQ--GQHIIVVSAIDNLL 310
Cdd:COG0002  236 PMVRGILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEgRLPETKSVRGSNFCDIGVAVDerTGRLVVVSAIDNLV 315

                        330       340
                 ....*....|....*....|...
gi 515667391 311 KGASSQAMQCLNLRYGFAPLTAL 333
Cdd:COG0002  316 KGAAGQAVQNMNLMFGLPETTGL 338
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 153-313 1.13e-78

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: 237.76  E-value: 1.13e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 153 GCYPTASQLAIKPLVEAKLLDENqWPVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHLG------C 224
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPD-DIIIDAKSGVSGAGRKASETTHFSEVneNLKAYKVGGHRHTPEIEQELSklagedV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 225 DVIFTPHLGNFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGWKVQG--QHII 301
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEgQLPSTKAVRGSNFCDIGVAVDGrtGRLI 159

                        170
                 ....*....|..
gi 515667391 302 VVSAIDNLLKGA 313
Cdd:cd23934  160 VVSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-333 7.08e-74

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 232.79  E-value: 7.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   1 MLKTTIIGASGYTGAELALMINRHPELtlsGLYVSANSVDAGKPIAALHGKLAGLiDMPVQPLTNPEEVAkQSDVIFLAT 80
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDF---EITVMTADRKAGQSFGSVFPHLITQ-DLPNLVAVKDADFS-DVDAVFCCL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  81 AHEVSHDLAPiFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAVAGCYPTASQ 160
Cdd:PLN02968 113 PHGTTQEIIK-ALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQ 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 161 LAIKPLVEAKLLDENQWpVINATSGVTGAGRKATMVNSFCEVS--LQAYGVFNHRHQPEM------AAHLGCDVIFTPHL 232
Cdd:PLN02968 192 LPLVPLVKAGLIEPDNI-IIDAKSGVSGAGRGAKEANLYTEIAegIGAYGVTRHRHVPEIeqgladAAGSKVTPSFTPHL 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 233 GNFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEE-TLPRIQDVEQTPFCDLGW---KVQGQHIIvVSAIDN 308
Cdd:PLN02968 271 MPMSRGMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERgAVPHTDHVRGSNYCELNVfadRIPGRAII-ISVIDN 349

                        330       340
                 ....*....|....*....|....*
gi 515667391 309 LLKGASSQAMQCLNLRYGFAPLTAL 333
Cdd:PLN02968 350 LVKGASGQAVQNLNLMMGLPETTGL 374
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 2-151 9.33e-62

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: 194.57  E-value: 9.33e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   2 LKTTIIGASGYTGAELALMINRHPELTLSGLYVSANsvdAGKPIAALHGKLAGLIDMPVQPLtNPEEVAKQSDVIFLATA 81
Cdd:cd17895    1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSY---AGKPVSEVFPHLRGLTDLTFEPD-DDEEIAEDADVVFLALP 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  82 HEVSHDLAPIFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAV 151
Cdd:cd17895   77 HGVSMELAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFEHAAPELLKEAVYGLPELNREEIKKARLVAN 146
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 154-313 2.54e-46

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: 154.58  E-value: 2.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 154 CYPTASQLAIKPLVEAKLLDENQwPVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHLGCD--VIFT 229
Cdd:cd18125    1 CYATAALLALYPLLKAGLLKPTP-ITVTGVSGTSGAGRAASPASLHPEVagSLRPYALSGHRHTPEIAQNLGGKhnVHFT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 230 PHLGNFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLL-EETLPRIQDVEQTPFCDLGWKVQ--GQHIIVVSAI 306
Cdd:cd18125   80 PHVGPWVRGILMTIQCFTQKGWSLRQLHEAYREAYAGEPFVRVMpQGKGPDPKFVQGTNYADIGVELEedTGRLVVMSAI 159


                 ....*..
gi 515667391 307 DNLLKGA 313
Cdd:cd18125  160 DNLVKGA 166
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-146 3.57e-37

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: 129.57  E-value: 3.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391    6 IIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIAALHGKLAGLIDMPVQPLTnpEEVAKQSDVIFLATAHEVS 85
Cdd:pfam01118   4 IVGATGYVGQELLRLLEEHPPVELVVLFASSRS--AGKKLAFVHPILEGGKDLVVEDVD--PEDFKDVDIVFFALPGGVS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515667391   86 HDLAPIFLENDCQVFDLSGAFRVKgenfyqefygfehqheqwlDKAAYGLAEWNEQEIKEA 146
Cdd:pfam01118  80 KEIAPKLAEAGAKVIDLSSDFRMD-------------------DDVPYGLPEVNREAIKQA 121
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 153-313 6.83e-34

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: 122.36  E-value: 6.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 153 GCYPTASQLAIKPLVeaKLLDENqwPVINATSGVTGAGRKATMVN--SFCEVSLQAYGVFNHRHQPEMAAHLGCDVIFTP 230
Cdd:cd23936    1 GCYATGAQLALAPLL--DDLDGP--PSVFGVSGYSGAGTKPSPKNdpEVLADNLIPYSLVGHIHEREVSRHLGTPVAFMP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 231 HLGNFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEEtLPRIQDVEQTPFCDL-GWKVQ--GQHIIVVSAID 307
Cdd:cd23936   77 HVAPWFQGITLTISIPLKKSMTADEIRELYQEAYAGEPLIKVTKE-IPLVRDNAGKHGVVVgGFTVHpdGKRVVVVATID 155


                 ....*.
gi 515667391 308 NLLKGA 313
Cdd:cd23936  156 NLLKGA 161
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 153-313 2.92e-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: 120.81  E-value: 2.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 153 GCYPTASQLAIKPLVEAKLLDENQwPVINATSGVTGAGRKATMVNSFCEVS--LQAYGVFNHRHQPEMAAHLGC-----D 225
Cdd:cd23939    1 GCNATASILALYPLVKAGLLDDER-IVVDVKVGSSGAGAEASEASHHPERSgvVRPYKPTGHRHTAEIEQELGLlareiS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 226 VIFTPHLGNFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEET-----LPRIQDVEQTPFCDLGWKV--QGQ 298
Cdd:cd23939   80 VSFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYRKAYGNEPFVRIVKDRkgiyrYPDPKLVIGSNFCDIGFELdeDNG 159

                        170
                 ....*....|....*
gi 515667391 299 HIIVVSAIDNLLKGA 313
Cdd:cd23939  160 RLVVFSAIDNLMKGA 174
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 6-146 6.13e-32

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: 115.72  E-value: 6.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391     6 IIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIAALHGKLAGLIdmpVQPLTNPEEVAKQSDVIFLATAHEVS 85
Cdd:smart00859   4 IVGATGYVGQELLRLLAEHPDFELTALAASSRS--AGKKVSEAGPHLKGEV---VLELDPPDFEELAVDIVFLALPHGVS 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515667391    86 HD---LAPIFLENDCQVFDLSGAFRVKgenfyqefygfehqheqwlDKAAYGLAEWNEQEIKEA 146
Cdd:smart00859  79 KEsapLLPRAAAAGAVVIDLSSAFRMD-------------------DDVPYGLPEVNPEAIKKA 123
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 153-313 1.53e-30

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: 113.85  E-value: 1.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 153 GCYPTASQLAIKPLVEAKLLDENqWPV-INATSGVTGAGRKATMVNSFCE----VSLQAYGV-FNHRHQPEMAAHLGCDV 226
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPAD-YPLsIHAVSGYSGGGKKMIEQYEAAEaadlPPPRPYGLgLEHKHLPEMQKHAGLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 227 --IFTPHLGNFKRGILATITM---KLADGVTEQQIQDAFEQAYQGKPAVRLLE----ETLPRI--QDVEQTPFCDLGwkV 295
Cdd:cd23935   80 ppIFTPAVGNFYQGMLVTVPLhldLLEKGVSAAEVHEALAEHYAGERFVKVMPldepDALGFLdpQALNGTNNLELF--V 157

                        170       180
                 ....*....|....*....|.
gi 515667391 296 QG---QHIIVVSAIDNLLKGA 313
Cdd:cd23935  158 FGndkGQALLVARLDNLGKGA 178
argC_other TIGR01851
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ...
 65-326 2.13e-28

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: 111.86  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   65 NPEEVAK---QSDVIFLATAHEVSHDLAPIFLENDCQVFDLSGAFRVkgenfyqefygfehqHEQWldkaAYGLAEWN-E 140
Cdd:TIGR01851  39 DAAERAKllnAADVAILCLPDDAAREAVSLVDNPNTCIIDASTAYRT---------------ADDW----AYGFPELApG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  141 Q--EIKEAQLVAVAGCYPTASQLAIKPLVEAKLLDENqWPV-INATSGVTGAGRKatMVNSFCEV-----SLQAYGV--- 209
Cdd:TIGR01851 100 QreKIRNSKRIANPGCYPTGFIALMRPLVEAGILPAD-FPItINAVSGYSGGGKA--MIADYEQGsadnpSLQPFRIygl 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  210 -FNHRHQPEMAAH--LGCDVIFTPHLGNFKRGILATITM---KLADGVTEQQIQDAFEQAYQGKPAVR--------LLEE 275
Cdd:TIGR01851 177 aLTHKHLPEMRVHsgLALPPIFTPAVGNFAQGMAVTIPLhlqTLASKVSPADIHAALADYYQGEQFVRvaplddveTLDN 256

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515667391  276 TLPRIQDVEQTPFCDL---GwKVQGQHIIVVSAIDNLLKGASSQAMQCLNLRYG 326
Cdd:TIGR01851 257 TFLDPQGLNGTNRLDLfvfG-SDDGERALLVARLDNLGKGASGAAVQNLNIMLG 309
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 2-152 6.68e-23

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: 93.49  E-value: 6.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   2 LKTTIIGASGYTGAELALMINRHPELTLsglyVSANSVD-AGKPIAALHGKLAGLIDMPVQPLTNPEEVakqsDVIFLAT 80
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEV----KQVTSESlAGKPVHRVHPNLRGRTLLKFVPPEELESC----DVLFLAL 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515667391  81 AHEVSHDLAPIFLENDCQVFDLSGAFRVKGENFYQEFYGFEHQHEQWLDKAAYGLAEWNEQEIKEAQLVAVA 152
Cdd:cd24151   73 PHGESMKRIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLERFVYGLPELHREELRGARYIAGA 144
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 164-311 6.50e-19

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: 82.36  E-value: 6.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  164 KPLVEAklLDENQWPVINATSGVTGAGRKAT--MVNSFCEVSLQAY-GVFNHRHQPEMAAHLGCDVIFTPHLGNFK---- 236
Cdd:pfam02774   2 KPLRDA--LGGLERVIVDTYQAVSGAGKKAKpgVFGAPIADNLIPYiDGEEHNGTPETREELKMVNETKKILGFTPkvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  237 --------RGILATITMKLAdgVTEQQIQDAFEQAYQG-KPAVRLLEETL-PR-IQDVEQTPFCDLGW----KVQGQHII 301
Cdd:pfam02774  80 tcvrvpvfRGHSETVTVKLK--LKPIDVEEVYEAFYAApGVFVVVRPEEDyPTpRAVRGGTNFVYVGRvrkdPDGDRGLK 157

                         170
                  ....*....|
gi 515667391  302 VVSAIDNLLK 311
Cdd:pfam02774 158 LVSVIDNLRK 167
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 6-151 1.73e-17

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: 78.48  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   6 IIGASGYTGAELALMINRHPELTLSglYVSANSvDAGKPIAALHGKLAGLIDMPVQPlTNPEEVAKQsDVIFLATAHEVS 85
Cdd:cd24148    5 VAGASGYAGGELLRLLLGHPEFEIG--ALTAHS-NAGQRLGELHPHLPPLADRVLEP-TTPAVLAGH-DVVFLALPHGAS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515667391  86 HDLAPIfLENDCQVFDLSGAFRVKGENFYQEFYGFEHQhEQWldkaAYGLAE--WNEQEIKEAQLVAV 151
Cdd:cd24148   80 AAIAAQ-LPPDVLVVDCGADHRLEDAAAWEKFYGGEHA-GGW----TYGLPElpGAREALAGARRIAV 141
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 3-152 2.61e-16

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: 75.30  E-value: 2.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   3 KTTIIGASGYTGAELALMINRHPELTLsgLYVSANSVdAGKPIAALHGKLagLIDMPVQPLTnPEEVAKQSDVIFLATAH 82
Cdd:cd02280    2 RVAIIGASGYTGLEIVRLLLGHPYLRV--LTLSSRER-AGPKLREYHPSL--IISLQIQEFR-PCEVLNSADILVLALPH 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515667391  83 EVSHDLAPIFLENDCQVFDLSGAFRVKGENFYQEFYGFEHqheqwLDKAAYGLAEWN-EQEIKEAQLVAVA 152
Cdd:cd02280   76 GASAELVAAISNPQVKIIDLSADFRFTDPEVYRRHPRPDL-----EGGWVYGLPELDrEQRIANATRIANP 141
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 3-111 2.75e-11

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: 60.84  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   3 KTTIIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIAALHGKLAGLidMPVQPLtnPEEVAKQSDVIFLATAH 82
Cdd:cd02281    2 KVGVVGATGYVGGEFLRLLLEHPFPLFEIVLLAASS--AGAKKKYFHPKLWGR--VLVEFT--PEEVLEQVDIVFTALPG 75

                         90       100
                 ....*....|....*....|....*....
gi 515667391  83 EVSHDLAPIFLENDCQVFDLSGAFRVKGE 111
Cdd:cd02281   76 GVSAKLAPELSEAGVLVIDNASDFRLDKD 104
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 2-107 1.28e-09

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: 56.35  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   2 LKTTIIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKP-IAALHGKLAGLI-----DMPVQPlTNPEEvAKQSDV 75
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERS--AGKKyGDAVRWKQDTPIpeevaDMVVKE-CEPEE-FKDCDI 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515667391  76 IFLATAHEVSHDLAPIFLENDCQVFDLSGAFR 107
Cdd:cd02315   77 VFSALDSDVAGEIEPAFAKAGIPVFSNASNHR 108
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 154-309 2.37e-08

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: 52.91  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 154 CYPTASQLAIKPLVEAKLLdenQWPVINATSGVTGAGRKATMVNSFCEV--SLQAYGVFNHRHQPEMAAHLG-----CDV 226
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGI---EEILVVTVQAVSGAGPKTKGPILKSEVraIIPNIPKNETKHAPETGKVLGeigkpIKV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391 227 IFTPHLGNFKRGILATITMKLADGVTEQQIQDAFEQAYQGKPAVRLLEETLPRIQD--VEQTPFCDLGWKVQ----GQHI 300
Cdd:cd18122   78 DGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTrsVGGVYGVPVGRQREfafdDNKL 157


                 ....*....
gi 515667391 301 IVVSAIDNL 309
Cdd:cd18122  158 KVFSAVDNE 166
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 2-107 2.66e-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: 51.95  E-value: 2.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   2 LKTTIIGASGYTGAELALMINRHPeLTLSGLYVSANSVDAGKPIaalhgKLAGLiDMPVQPLTNPEevAKQSDVIFLATA 81
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEP-DPLFELRALASEESAGKKA-----EFAGE-AIMVQEADPID--FLGLDIVFLCAG 71

                         90       100
                 ....*....|....*....|....*.
gi 515667391  82 HEVSHDLAPIFLENDCQVFDLSGAFR 107
Cdd:cd24147   72 AGVSAKFAPEAARAGVLVIDNAGALR 97
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 6-79 3.69e-08

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: 52.11  E-value: 3.69e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515667391   6 IIGASGYTGAELALMINRHPELTLSglYVSANSVdAGKPIAAlHGKLAgLIDMPVQPLTNPEEVA-KQSDVIFLA 79
Cdd:cd24149    5 LIGARGYVGRELIRLLNRHPNLELA--HVSSREL-AGQKVSG-YTKSP-IDYLNLSVEDIPEEVAaREVDAWVLA 74
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 6-107 9.65e-08

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: 50.51  E-value: 9.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   6 IIGASGYTGAE-LALMINRHpeLTLSGLYVSANSVDAGKPIAaLHGKlagliDMPVQPLTnpEEVAKQSDVIFLATAHEV 84
Cdd:cd02316    5 IVGATGAVGQEmLKVLEERN--FPVSELRLLASARSAGKTLE-FKGK-----ELTVEELT--EDSFKGVDIALFSAGGSV 74

                         90       100
                 ....*....|....*....|...
gi 515667391  85 SHDLAPIFLENDCQVFDLSGAFR 107
Cdd:cd02316   75 SKEFAPIAAEAGAVVIDNSSAFR 97
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-107 2.25e-06

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 48.67  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   1 MLKTTIIGASGYTGAELALMINRHPELTLSGLYVSANSvdAGKPIA-ALHGKLAGLI-----DMPVQPlTNPEEVaKQSD 74
Cdd:PRK08664   3 KLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERS--AGKTYGeAVRWQLDGPIpeevaDMEVVS-TDPEAV-DDVD 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 515667391  75 VIFLATAHEVSHDLAPIFLENDCQVFDLSGAFR 107
Cdd:PRK08664  79 IVFSALPSDVAGEVEEEFAKAGKPVFSNASAHR 111
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 2-95 4.85e-06

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: 45.63  E-value: 4.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   2 LKTTIIGASGYTGAELALMINRHPELTLSGLYVSANSVDAGKPIAALHGklaglIDMPVQPLTNPEEVAKQSDVI--Fla 79
Cdd:cd02274    1 IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGGLAG-----IGTGVIVSLDLELAAADADVVidF-- 73

                         90
                 ....*....|....*.
gi 515667391  80 TAHEVSHDLAPIFLEN 95
Cdd:cd02274   74 TTPEATLENLEAAAKA 89
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 2-95 5.20e-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: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391    2 LKTTIIGASGYTGAELALMINRHPELTLSGLYVSANSVDAGKPIaalhgklAGLIDMPVQPLTNPEEVAKQSDVIFLATA 81
Cdd:pfam01113   1 IKIAVAGASGRMGRELIKAVLEAPDLELVAAVDRPGSSLLGSDA-------GELAPLGVPVTDDLEEVLADADVLIDFTT 73

                          90
                  ....*....|....
gi 515667391   82 HEVSHDLAPIFLEN 95
Cdd:pfam01113  74 PEATLENLEFALKH 87
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 6-193 9.72e-06

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: 46.56  E-value: 9.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   6 IIGASGYTGAE-LALMINRH-P--ELTLsglYVSANSvdAGKPIAaLHGKlagliDMPVQPLTnpEEVAKQSDVIFLATA 81
Cdd:COG0136    5 VVGATGAVGRVlLELLEERDfPvgELRL---LASSRS--AGKTVS-FGGK-----ELTVEDAT--DFDFSGVDIALFSAG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391  82 HEVSHDLAPIFLENDCQVFDLSGAFR-------VkgenfyqefygfehqheqwldkaaygLAEWNEQEIKEAQ---LVAV 151
Cdd:COG0136   72 GSVSKEYAPKAAAAGAVVIDNSSAFRmdpdvplV--------------------------VPEVNPEALADHLpkgIIAN 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515667391 152 AGCypTASQL--AIKPLVEAKLLdenQWpvINATS--GVTGAGRKA 193
Cdd:COG0136  126 PNC--STIQMlvALKPLHDAAGI---KR--VVVSTyqAVSGAGAAA 164
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 308-330 3.17e-04

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: 40.56  E-value: 3.17e-04
                         10        20
                 ....*....|....*....|...
gi 515667391 308 NLLKGASSQAMQCLNLRYGFAPL 330
Cdd:cd24149  132 NLLKGAATQALQNLNLALGLDEL 154
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 6-95 6.51e-04

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: 40.87  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667391   6 IIGASGYTGAELALMINRHPELTLSGLYVSANSvdagkpiaalHGKLAGLIDMPVQPLTNPEEVAKQSDVI--FlaTAHE 83
Cdd:COG0289    5 VAGASGRMGRELIRAVLEAPDLELVAAIDRPGS----------PGQDAGELALGVPVTDDLEEALAKADVVidF--THPE 72

                         90
                 ....*....|..
gi 515667391  84 VSHDLAPIFLEN 95
Cdd:COG0289   73 ATLENLEAALEA 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH