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Conserved domains on  [gi|446858122|ref|WP_000935378|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Escherichia coli]

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.-
PubMed:  10613839
SCOP:  4000077

Graphical summary

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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 ...
2-334 4.69e-171

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: 478.61  E-value: 4.69e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122    2 LNTLIVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGKLISDLHPQLKGIVDLPLQPMsDISEFSPGVDVVFLATA 81
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRES--AGKPVSEVHPHLRGLVDLNLEPI-DVEEILEDADVVFLALP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   82 HEVSHDLAPQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIAVPGCYPTAAQL 161
Cdd:TIGR01850  78 HGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  162 ALKPLIDADLLDLNQWpVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLG------ADVIFTPHLG 233
Cdd:TIGR01850 158 ALAPLLKEGLIDPTSI-IVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHLV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  234 NFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKG-VPALKNVVGLPFCDIGFAVQGE--HLIIVATEDNLL 310
Cdd:TIGR01850 237 PMTRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGgYPSTKAVIGSNFCDIGFAVDERtgRVVVVSAIDNLV 316
                         330       340
                  ....*....|....*....|....
gi 446858122  311 KGAAAQAVQCANIRFGYAETQSLI 334
Cdd:TIGR01850 317 KGAAGQAVQNMNLMFGFDETTGLP 340
 
Name Accession Description Interval E-value
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
2-334 4.69e-171

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: 478.61  E-value: 4.69e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122    2 LNTLIVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGKLISDLHPQLKGIVDLPLQPMsDISEFSPGVDVVFLATA 81
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRES--AGKPVSEVHPHLRGLVDLNLEPI-DVEEILEDADVVFLALP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   82 HEVSHDLAPQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIAVPGCYPTAAQL 161
Cdd:TIGR01850  78 HGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  162 ALKPLIDADLLDLNQWpVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLG------ADVIFTPHLG 233
Cdd:TIGR01850 158 ALAPLLKEGLIDPTSI-IVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHLV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  234 NFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKG-VPALKNVVGLPFCDIGFAVQGE--HLIIVATEDNLL 310
Cdd:TIGR01850 237 PMTRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGgYPSTKAVIGSNFCDIGFAVDERtgRVVVVSAIDNLV 316
                         330       340
                  ....*....|....*....|....
gi 446858122  311 KGAAAQAVQCANIRFGYAETQSLI 334
Cdd:TIGR01850 317 KGAAGQAVQNMNLMFGFDETTGLP 340
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
2-333 8.79e-163

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: 457.61  E-value: 8.79e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   2 LNTLIVGASGYAGAELVTYVNRHPHMNITALTvsaQSNDAGKLISDLHPQLKGIVDLPLQPMsDISEFSPGVDVVFLATA 81
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT---SRSNAGKPVSEVHPHLRGLTDLVFEPP-DPDELAAGCDVVFLALP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  82 HEVSHDLAPQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIAVPGCYPTAAQL 161
Cdd:COG0002   77 HGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 162 ALKPLIDADLLDLNqWPVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLGA------DVIFTPHLG 233
Cdd:COG0002  157 ALAPLLKAGLIDPD-DIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELSRlagedvKVSFTPHLV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 234 NFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKGV-PALKNVVGLPFCDIGFAVQ--GEHLIIVATEDNLL 310
Cdd:COG0002  236 PMVRGILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRlPETKSVRGSNFCDIGVAVDerTGRLVVVSAIDNLV 315
                        330       340
                 ....*....|....*....|...
gi 446858122 311 KGAAAQAVQCANIRFGYAETQSL 333
Cdd:COG0002  316 KGAAGQAVQNMNLMFGLPETTGL 338
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
6-333 4.62e-72

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 228.17  E-value: 4.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQsndAGKLISDLHPQLKgIVDLPLQPMSDISEFSpGVDVVFLATAHEVS 85
Cdd:PLN02968  43 VLGASGYTGAEVRRLLANHPDFEITVMTADRK---AGQSFGSVFPHLI-TQDLPNLVAVKDADFS-DVDAVFCCLPHGTT 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  86 HDLApQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIAVPGCYPTAAQLALKP 165
Cdd:PLN02968 118 QEII-KALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLVP 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 166 LIDADLLDLNQWpVINATSGVSGAGRKAAISNSFCEVS--LQPYGVFTHRHQPEI------ATHLGADVIFTPHLGNFPR 237
Cdd:PLN02968 197 LVKAGLIEPDNI-IIDAKSGVSGAGRGAKEANLYTEIAegIGAYGVTRHRHVPEIeqgladAAGSKVTPSFTPHLMPMSR 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 238 GILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKG-VPALKNVVGLPFCDIG-FA--VQGEhLIIVATEDNLLKGA 313
Cdd:PLN02968 276 GMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGaVPHTDHVRGSNYCELNvFAdrIPGR-AIIISVIDNLVKGA 354
                        330       340
                 ....*....|....*....|
gi 446858122 314 AAQAVQCANIRFGYAETQSL 333
Cdd:PLN02968 355 SGQAVQNLNLMMGLPETTGL 374
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
153-313 3.93e-69

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: 213.49  E-value: 3.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 153 GCYPTAAQLALKPLIDADLLDlNQWPVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLG------A 224
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIE-PDDIIIDAKSGVSGAGRKASETTHFSEVneNLKAYKVGGHRHTPEIEQELSklagedV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 225 DVIFTPHLGNFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKGV-PALKNVVGLPFCDIGFAVQGE--HLI 301
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEGQlPSTKAVRGSNFCDIGVAVDGRtgRLI 159
                        170
                 ....*....|..
gi 446858122 302 IVATEDNLLKGA 313
Cdd:cd23934  160 VVSAIDNLVKGA 171
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
6-146 2.15e-39

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: 135.34  E-value: 2.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122    6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGKLISDLHPQLKGIVDLPLQPMsDISEFSpGVDVVFLATAHEVS 85
Cdd:pfam01118   4 IVGATGYVGQELLRLLEEHPPVELVVLFASSRS--AGKKLAFVHPILEGGKDLVVEDV-DPEDFK-DVDIVFFALPGGVS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446858122   86 HDLAPQFLEAGCVVFDLSGAFRVNDvafyekyygfthqypelleQAAYGLAEWCGNKLKEA 146
Cdd:pfam01118  80 KEIAPKLAEAGAKVIDLSSDFRMDD-------------------DVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
6-146 1.51e-31

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: 114.95  E-value: 1.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122     6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGKLISDLHPQLKGIVDLPLQPMSDISEfspGVDVVFLATAHEVS 85
Cdd:smart00859   4 IVGATGYVGQELLRLLAEHPDFELTALAASSRS--AGKKVSEAGPHLKGEVVLELDPPDFEEL---AVDIVFLALPHGVS 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446858122    86 HD---LAPQFLEAGCVVFDLSGAFRVNDvafyekyygfthqypelleQAAYGLAEWCGNKLKEA 146
Cdd:smart00859  79 KEsapLLPRAAAAGAVVIDLSSAFRMDD-------------------DVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
2-334 4.69e-171

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: 478.61  E-value: 4.69e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122    2 LNTLIVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGKLISDLHPQLKGIVDLPLQPMsDISEFSPGVDVVFLATA 81
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRES--AGKPVSEVHPHLRGLVDLNLEPI-DVEEILEDADVVFLALP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   82 HEVSHDLAPQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIAVPGCYPTAAQL 161
Cdd:TIGR01850  78 HGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  162 ALKPLIDADLLDLNQWpVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLG------ADVIFTPHLG 233
Cdd:TIGR01850 158 ALAPLLKEGLIDPTSI-IVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHLV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  234 NFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKG-VPALKNVVGLPFCDIGFAVQGE--HLIIVATEDNLL 310
Cdd:TIGR01850 237 PMTRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGgYPSTKAVIGSNFCDIGFAVDERtgRVVVVSAIDNLV 316
                         330       340
                  ....*....|....*....|....
gi 446858122  311 KGAAAQAVQCANIRFGYAETQSLI 334
Cdd:TIGR01850 317 KGAAGQAVQNMNLMFGFDETTGLP 340
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
2-333 8.79e-163

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: 457.61  E-value: 8.79e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   2 LNTLIVGASGYAGAELVTYVNRHPHMNITALTvsaQSNDAGKLISDLHPQLKGIVDLPLQPMsDISEFSPGVDVVFLATA 81
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT---SRSNAGKPVSEVHPHLRGLTDLVFEPP-DPDELAAGCDVVFLALP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  82 HEVSHDLAPQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIAVPGCYPTAAQL 161
Cdd:COG0002   77 HGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 162 ALKPLIDADLLDLNqWPVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLGA------DVIFTPHLG 233
Cdd:COG0002  157 ALAPLLKAGLIDPD-DIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELSRlagedvKVSFTPHLV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 234 NFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKGV-PALKNVVGLPFCDIGFAVQ--GEHLIIVATEDNLL 310
Cdd:COG0002  236 PMVRGILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRlPETKSVRGSNFCDIGVAVDerTGRLVVVSAIDNLV 315
                        330       340
                 ....*....|....*....|...
gi 446858122 311 KGAAAQAVQCANIRFGYAETQSL 333
Cdd:COG0002  316 KGAAGQAVQNMNLMFGLPETTGL 338
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
6-333 4.62e-72

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 228.17  E-value: 4.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQsndAGKLISDLHPQLKgIVDLPLQPMSDISEFSpGVDVVFLATAHEVS 85
Cdd:PLN02968  43 VLGASGYTGAEVRRLLANHPDFEITVMTADRK---AGQSFGSVFPHLI-TQDLPNLVAVKDADFS-DVDAVFCCLPHGTT 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  86 HDLApQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIAVPGCYPTAAQLALKP 165
Cdd:PLN02968 118 QEII-KALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLVP 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 166 LIDADLLDLNQWpVINATSGVSGAGRKAAISNSFCEVS--LQPYGVFTHRHQPEI------ATHLGADVIFTPHLGNFPR 237
Cdd:PLN02968 197 LVKAGLIEPDNI-IIDAKSGVSGAGRGAKEANLYTEIAegIGAYGVTRHRHVPEIeqgladAAGSKVTPSFTPHLMPMSR 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 238 GILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKG-VPALKNVVGLPFCDIG-FA--VQGEhLIIVATEDNLLKGA 313
Cdd:PLN02968 276 GMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGaVPHTDHVRGSNYCELNvFAdrIPGR-AIIISVIDNLVKGA 354
                        330       340
                 ....*....|....*....|
gi 446858122 314 AAQAVQCANIRFGYAETQSL 333
Cdd:PLN02968 355 SGQAVQNLNLMMGLPETTGL 374
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
153-313 3.93e-69

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: 213.49  E-value: 3.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 153 GCYPTAAQLALKPLIDADLLDlNQWPVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLG------A 224
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIE-PDDIIIDAKSGVSGAGRKASETTHFSEVneNLKAYKVGGHRHTPEIEQELSklagedV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 225 DVIFTPHLGNFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKGV-PALKNVVGLPFCDIGFAVQGE--HLI 301
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEGQlPSTKAVRGSNFCDIGVAVDGRtgRLI 159
                        170
                 ....*....|..
gi 446858122 302 IVATEDNLLKGA 313
Cdd:cd23934  160 VVSAIDNLVKGA 171
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
6-152 1.30e-68

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: 211.90  E-value: 1.30e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQsndAGKLISDLHPQLKGIVDLPLQPmSDISEFSPGVDVVFLATAHEVS 85
Cdd:cd17895    5 IIGASGYTGAELLRLLLNHPEVEIVALTSRSY---AGKPVSEVFPHLRGLTDLTFEP-DDDEEIAEDADVVFLALPHGVS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446858122  86 HDLAPQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIAVP 152
Cdd:cd17895   81 MELAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFEHAAPELLKEAVYGLPELNREEIKKARLVANP 147
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
6-146 2.15e-39

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: 135.34  E-value: 2.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122    6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGKLISDLHPQLKGIVDLPLQPMsDISEFSpGVDVVFLATAHEVS 85
Cdd:pfam01118   4 IVGATGYVGQELLRLLEEHPPVELVVLFASSRS--AGKKLAFVHPILEGGKDLVVEDV-DPEDFK-DVDIVFFALPGGVS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446858122   86 HDLAPQFLEAGCVVFDLSGAFRVNDvafyekyygfthqypelleQAAYGLAEWCGNKLKEA 146
Cdd:pfam01118  80 KEIAPKLAEAGAKVIDLSSDFRMDD-------------------DVPYGLPEVNREAIKQA 121
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
154-313 1.81e-37

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: 131.85  E-value: 1.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 154 CYPTAAQLALKPLIDADLLDlNQWPVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLGAD--VIFT 229
Cdd:cd18125    1 CYATAALLALYPLLKAGLLK-PTPITVTGVSGTSGAGRAASPASLHPEVagSLRPYALSGHRHTPEIAQNLGGKhnVHFT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 230 PHLGNFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKGV-PALKNVVGLPFCDIGFAVQ--GEHLIIVATE 306
Cdd:cd18125   80 PHVGPWVRGILMTIQCFTQKGWSLRQLHEAYREAYAGEPFVRVMPQGKgPDPKFVQGTNYADIGVELEedTGRLVVMSAI 159

                 ....*..
gi 446858122 307 DNLLKGA 313
Cdd:cd18125  160 DNLVKGA 166
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
6-146 1.51e-31

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: 114.95  E-value: 1.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122     6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGKLISDLHPQLKGIVDLPLQPMSDISEfspGVDVVFLATAHEVS 85
Cdd:smart00859   4 IVGATGYVGQELLRLLAEHPDFELTALAASSRS--AGKKVSEAGPHLKGEVVLELDPPDFEEL---AVDIVFLALPHGVS 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446858122    86 HD---LAPQFLEAGCVVFDLSGAFRVNDvafyekyygfthqypelleQAAYGLAEWCGNKLKEA 146
Cdd:smart00859  79 KEsapLLPRAAAAGAVVIDLSSAFRMDD-------------------DVPYGLPEVNPEAIKKA 123
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
6-150 3.40e-31

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: 115.45  E-value: 3.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTvsAQSNdAGKLISDLHPQLKGIVDLPLQPMSDISEfspgVDVVFLATAHEVS 85
Cdd:cd24151    5 IVGASGYTGGELLRLLLGHPEVEVKQVT--SESL-AGKPVHRVHPNLRGRTLLKFVPPEELES----CDVLFLALPHGES 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446858122  86 HDLAPQFLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQYPELLEQAAYGLAEWCGNKLKEANLIA 150
Cdd:cd24151   78 MKRIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLERFVYGLPELHREELRGARYIA 142
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
153-313 2.52e-28

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: 107.72  E-value: 2.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 153 GCYPTAAQLALKPLIDadllDLNQWPVINATSGVSGAGRKAAISN--SFCEVSLQPYGVFTHRHQPEIATHLGADVIFTP 230
Cdd:cd23936    1 GCYATGAQLALAPLLD----DLDGPPSVFGVSGYSGAGTKPSPKNdpEVLADNLIPYSLVGHIHEREVSRHLGTPVAFMP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 231 HLGNFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDkGVPALKNVVGLPFCDI-GFAVQ--GEHLIIVATED 307
Cdd:cd23936   77 HVAPWFQGITLTISIPLKKSMTADEIRELYQEAYAGEPLIKVTK-EIPLVRDNAGKHGVVVgGFTVHpdGKRVVVVATID 155

                 ....*.
gi 446858122 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 1.11e-27

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: 106.17  E-value: 1.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 153 GCYPTAAQLALKPLIDADLLDLNQwPVINATSGVSGAGRKAAISNSFCEVS--LQPYGVFTHRHQPEIATHLGA-----D 225
Cdd:cd23939    1 GCNATASILALYPLVKAGLLDDER-IVVDVKVGSSGAGAEASEASHHPERSgvVRPYKPTGHRHTAEIEQELGLlareiS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 226 VIFTPHLGNFPRGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLY-DKG----VPALKNVVGLPFCDIGFAV--QGE 298
Cdd:cd23939   80 VSFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYRKAYGNEPFVRIVkDRKgiyrYPDPKLVIGSNFCDIGFELdeDNG 159
                        170
                 ....*....|....*
gi 446858122 299 HLIIVATEDNLLKGA 313
Cdd:cd23939  160 RLVVFSAIDNLMKGA 174
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
6-152 5.82e-25

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: 98.90  E-value: 5.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTvsAQSNdAGKLISDLHPQLKGIVDLPLQPMSDisEFSPGVDVVFLATAHEVS 85
Cdd:cd24148    5 VAGASGYAGGELLRLLLGHPEFEIGALT--AHSN-AGQRLGELHPHLPPLADRVLEPTTP--AVLAGHDVVFLALPHGAS 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446858122  86 HDLAPQfLEAGCVVFDLSGAFRVNDVAFYEKYYGFTHQypellEQAAYGLAEWCGNK--LKEANLIAVP 152
Cdd:cd24148   80 AAIAAQ-LPPDVLVVDCGADHRLEDAAAWEKFYGGEHA-----GGWTYGLPELPGAReaLAGARRIAVP 142
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
163-311 1.39e-21

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: 89.68  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  163 LKPLIDAdlLDLNQWPVINATSGVSGAGRKA--AISNSFCEVSLQPY-GVFTHRHQPEIATHLGADVIFTPHLGNFP--- 236
Cdd:pfam02774   1 LKPLRDA--LGGLERVIVDTYQAVSGAGKKAkpGVFGAPIADNLIPYiDGEEHNGTPETREELKMVNETKKILGFTPkvs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  237 ---------RGILETITCRLKPGVSQVQVAQALQQAYAHKPLMRLYDKGVPALKNVVG-LPFCDIG-FAVQGEH---LII 302
Cdd:pfam02774  79 atcvrvpvfRGHSETVTVKLKLKPIDVEEVYEAFYAAPGVFVVVRPEEDYPTPRAVRGgTNFVYVGrVRKDPDGdrgLKL 158

                  ....*....
gi 446858122  303 VATEDNLLK 311
Cdd:pfam02774 159 VSVIDNLRK 167
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
153-313 2.76e-20

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: 86.50  E-value: 2.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 153 GCYPTAAQLALKPLIDADLLDlNQWPV-INATSGVSGAGRKAAISNSFCE----VSLQPYGV-FTHRHQPEIATH--LGA 224
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLP-ADYPLsIHAVSGYSGGGKKMIEQYEAAEaadlPPPRPYGLgLEHKHLPEMQKHagLAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 225 DVIFTPHLGNFPRGILETIT---CRLKPGVSqvqvaqalqQAYAHKPLMRLYDKG----VPALKNVVGLPFCDIG----- 292
Cdd:cd23935   80 PPIFTPAVGNFYQGMLVTVPlhlDLLEKGVS---------AAEVHEALAEHYAGErfvkVMPLDEPDALGFLDPQalngt 150
                        170       180
                 ....*....|....*....|....*...
gi 446858122 293 -------FAVQGEHLIIVATEDNLLKGA 313
Cdd:cd23935  151 nnlelfvFGNDKGQALLVARLDNLGKGA 178
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
6-166 1.66e-17

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: 78.38  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTvSAQSndAGKLISDLHPQLKgivdlplqPMSDISEFSP-----GVDVVFLAT 80
Cdd:cd02280    5 IIGASGYTGLEIVRLLLGHPYLRVLTLS-SRER--AGPKLREYHPSLI--------ISLQIQEFRPcevlnSADILVLAL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  81 AHEVSHDLAPQFLEAGCVVFDLSGAFRVNDVAFYEKYYGfthqyPELLEQAAYGLAEWCG-NKLKEANLIAVPGCYPTAA 159
Cdd:cd02280   74 PHGASAELVAAISNPQVKIIDLSADFRFTDPEVYRRHPR-----PDLEGGWVYGLPELDReQRIANATRIANPNLVKGAA 148

                 ....*..
gi 446858122 160 QLALKPL 166
Cdd:cd02280  149 GAAVQNL 155
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
6-193 2.64e-14

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: 72.37  E-value: 2.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELV-TYVNRH-PHMNITALTvSAQSndAGKLISdlhpqLKGiVDLPLQPMSDISeFSpGVDVVFLATAHE 83
Cdd:COG0136    5 VVGATGAVGRVLLeLLEERDfPVGELRLLA-SSRS--AGKTVS-----FGG-KELTVEDATDFD-FS-GVDIALFSAGGS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  84 VSHDLAPQFLEAGCVVFDLSGAFR-----------VNdvafyekyygfthqyPELLEQAayglaewcgnklKEANLIAVP 152
Cdd:COG0136   74 VSKEYAPKAAAAGAVVIDNSSAFRmdpdvplvvpeVN---------------PEALADH------------LPKGIIANP 126
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446858122 153 GCypTAAQL--ALKPLIDADLLdlnQWpvINATS--GVSGAGRKA 193
Cdd:COG0136  127 NC--STIQMlvALKPLHDAAGI---KR--VVVSTyqAVSGAGAAA 164
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
6-114 7.05e-12

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: 62.38  E-value: 7.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMN-ITALTVSAQsndAGKLISDLHPQLKGIVdlpLQPMSDISEFSpGVDVVFLATAHEV 84
Cdd:cd02281    5 VVGATGYVGGEFLRLLLEHPFPLfEIVLLAASS---AGAKKKYFHPKLWGRV---LVEFTPEEVLE-QVDIVFTALPGGV 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 446858122  85 SHDLAPQFLEAGCVVFDLSGAFRVNDVAFY 114
Cdd:cd02281   78 SAKLAPELSEAGVLVIDNASDFRLDKDVPL 107
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
6-153 7.93e-12

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: 62.51  E-value: 7.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITAltVSAQSNdAGKLISDLHPQLKGIVDLpLQPMSDISEFSPGVDVVFLAtaheVS 85
Cdd:cd24149    5 LIGARGYVGRELIRLLNRHPNLELAH--VSSREL-AGQKVSGYTKSPIDYLNL-SVEDIPEEVAAREVDAWVLA----LP 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446858122  86 HDLAPQFLEA------GCVVFDLSGAFRVNDvafyekyygfthqypelleQAAYGLAEWCGNKLKEANLIAVPG 153
Cdd:cd24149   77 NGVAKPFVDAidkanpKSVIVDLSADYRFDD-------------------AWTYGLPELNRRRIAGAKRISNPG 131
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
1-195 6.87e-10

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 59.40  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   1 MLNTLIVGASGYAGAELV-TYVNRH-PHMNITALtvsAQSNDAGKLISdlhpqLKGiVDLPLQpmsDISEFSP-GVDVVF 77
Cdd:PRK14874   1 GYNVAVVGATGAVGREMLnILEERNfPVDKLRLL---ASARSAGKELS-----FKG-KELKVE---DLTTFDFsGVDIAL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  78 LATAHEVSHDLAPQFLEAGCVVFDLSGAFRVND-----VafyekyygfthqyPELLEQAaygLAEWCGNklkeaNLIAVP 152
Cdd:PRK14874  69 FSAGGSVSKKYAPKAAAAGAVVIDNSSAFRMDPdvplvV-------------PEVNPEA---LAEHRKK-----GIIANP 127
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446858122 153 GCYPTAAQLALKPLIDAdlldlnqWP---VINAT-SGVSGAGrKAAI 195
Cdd:PRK14874 128 NCSTIQMVVALKPLHDA-------AGikrVVVSTyQAVSGAG-KAGM 166
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
6-110 1.39e-09

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


Pssm-ID: 467520 [Multi-domain]  Cd Length: 144  Bit Score: 55.71  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRH--PHMNITALtvsAQSNDAGKLISDlhpqlkGIVDLPLQpmsDISEFSP-GVDVVFLATAH 82
Cdd:cd17894    5 VVGATGLVGKELLELLEERgfPVGRLRLL---DSEESAGELVEF------GGEPLDVQ---DLDEFDFsDVDLVFFAGPA 72
                         90       100
                 ....*....|....*....|....*...
gi 446858122  83 EVSHDLAPQFLEAGCVVFDLSGAFRVND 110
Cdd:cd17894   73 EVARAYAPRARAAGCLVIDLSGALRSDP 100
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
6-107 2.80e-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: 55.19  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGK---------LISDLHPQLKgivDLPLQPMSDisEFSPGVDVV 76
Cdd:cd02315    5 VLGATGMVGQRFIQLLANHPWFELAALGASERS--AGKkygdavrwkQDTPIPEEVA---DMVVKECEP--EEFKDCDIV 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446858122  77 FLATAHEVSHDLAPQFLEAGCVVFDLSGAFR 107
Cdd:cd02315   78 FSALDSDVAGEIEPAFAKAGIPVFSNASNHR 108
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
2-132 5.48e-09

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: 53.88  E-value: 5.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   2 LNTLIVGASGYAGAELVTYVNRHPH--MNITALTvSAQSndAGKLISDlhpqlkGIVDLPLQPMSDIsEFSpGVDVVFLA 79
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEPDplFELRALA-SEES--AGKKAEF------AGEAIMVQEADPI-DFL-GLDIVFLC 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446858122  80 TAHEVSHDLAPQFLEAGCVVFDLSGAFR-----------VNDVAFYEKYYGFTHQYPELLEQAA 132
Cdd:cd24147   70 AGAGVSAKFAPEAARAGVLVIDNAGALRmdpdvplvvpeVNAEAIGLGEGTPLLVIPNLLRGAA 133
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
6-110 5.95e-09

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: 53.98  E-value: 5.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYV--NRHPhmnITALTVSAQSNDAGKLISdlhpqLKGiVDLPLQPMSDISeFSpGVDVVFLATAHE 83
Cdd:cd02316    5 IVGATGAVGQEMLKVLeeRNFP---VSELRLLASARSAGKTLE-----FKG-KELTVEELTEDS-FK-GVDIALFSAGGS 73
                         90       100
                 ....*....|....*....|....*..
gi 446858122  84 VSHDLAPQFLEAGCVVFDLSGAFRVND 110
Cdd:cd02316   74 VSKEFAPIAAEAGAVVIDNSSAFRMDP 100
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
1-190 1.47e-08

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 55.60  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   1 MLNTLIVGASGYAGAELVTYVNRHPHMNITALTVSAQSndAGK---------LISDLHPQLKGIVDLPLQPmsdisEFSP 71
Cdd:PRK08664   3 KLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERS--AGKtygeavrwqLDGPIPEEVADMEVVSTDP-----EAVD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  72 GVDVVFLATAHEVSHDLAPQFLEAGCVVFDLSGAFR-----------VNdvafyekyygfthqyPELLEqaaygLAE--- 137
Cdd:PRK08664  76 DVDIVFSALPSDVAGEVEEEFAKAGKPVFSNASAHRmdpdvplvipeVN---------------PEHLE-----LIEvqr 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446858122 138 ----WCGnklkeaNLIAVPGCYPTAAQLALKPLIDADLLDlnqwpvINATS--GVSGAG 190
Cdd:PRK08664 136 krrgWDG------FIVTNPNCSTIGLVLALKPLMDFGIER------VHVTTmqAISGAG 182
PRK05671 PRK05671
aspartate-semialdehyde dehydrogenase; Reviewed
2-193 6.73e-08

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 168165 [Multi-domain]  Cd Length: 336  Bit Score: 53.19  E-value: 6.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   2 LNTLIVGASGYAGAELVTYVNRHpHMNITALTVSAQSNDAGKLISDLHPQLKgivdlplqpMSDISEFS-PGVDVVFLAT 80
Cdd:PRK05671   5 LDIAVVGATGTVGEALVQILEER-DFPVGTLHLLASSESAGHSVPFAGKNLR---------VREVDSFDfSQVQLAFFAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  81 AHEVSHDLAPQFLEAGCVVFDLSGAFRVNdvafyekyygfthQYPELLEQA-AYGLAewcgnKLKEANLIAVPGCYPTAA 159
Cdd:PRK05671  75 GAAVSRSFAEKARAAGCSVIDLSGALPSA-------------QAPNVVPEVnAERLA-----SLAAPFLVSSPSASAVAL 136
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446858122 160 QLALKPLidADLLDLNQWPViNATSGVSGAGRKA 193
Cdd:PRK05671 137 AVALAPL--KGLLDIQRVQV-TACLAVSSLGREG 167
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
6-193 3.35e-07

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 51.21  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQSNDAGKLIsdlhpQLKGiVDLPLQPmSDISEFSpGVDVVFLATAHEVS 85
Cdd:PRK06728  10 VVGATGAVGQKIIELLEKETKFNIAEVTLLSSKRSAGKTV-----QFKG-REIIIQE-AKINSFE-GVDIAFFSAGGEVS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  86 HDLAPQFLEAGCVVFDLSGAFRVndvafyekyygfTHQYPELL-EQAAYGLAEWCGnklkeanLIAVPGCYPTAAQLALK 164
Cdd:PRK06728  82 RQFVNQAVSSGAIVIDNTSEYRM------------AHDVPLVVpEVNAHTLKEHKG-------IIAVPNCSALQMVTALQ 142
                        170       180
                 ....*....|....*....|....*....
gi 446858122 165 PLIDADLLDLnqwPVINATSGVSGAGRKA 193
Cdd:PRK06728 143 PIRKVFGLER---IIVSTYQAVSGSGIHA 168
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
154-248 2.38e-05

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: 44.05  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122 154 CYPTAAQLALKPLIDADLLdlnQWPVINATSGVSGAGRKAAISNSFCEV--SLQPYGVFTHRHQPEIATHLG-----ADV 226
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGI---EEILVVTVQAVSGAGPKTKGPILKSEVraIIPNIPKNETKHAPETGKVLGeigkpIKV 77
                         90       100
                 ....*....|....*....|..
gi 446858122 227 IFTPHLGNFPRGILETITCRLK 248
Cdd:cd18122   78 DGIAVRVPATLGHLVTVTVKLE 99
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
6-166 3.99e-05

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 44.76  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRH--PHMNITALTvSAQSndAGKlisdlHPQLKGiVDLPLQPMSDISefSPGVDVVFLATAHE 83
Cdd:PLN02383  12 IVGVTGAVGQEFLSVLTDRdfPYSSLKMLA-SARS--AGK-----KVTFEG-RDYTVEELTEDS--FDGVDIALFSAGGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122  84 VSHDLAPQFLEAGCVVFDLSGAFRVNDvafyekyyGFTHQYPELLEQAAYGLaewcgnKL--KEANLIAVPGCYPTAAQL 161
Cdd:PLN02383  81 ISKKFGPIAVDKGAVVVDNSSAFRMEE--------GVPLVIPEVNPEAMKHI------KLgkGKGALIANPNCSTIICLM 146

                 ....*
gi 446858122 162 ALKPL 166
Cdd:PLN02383 147 AVTPL 151
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
308-329 3.98e-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: 40.17  E-value: 3.98e-04
                         10        20
                 ....*....|....*....|..
gi 446858122 308 NLLKGAAAQAVQCANIRFGYAE 329
Cdd:cd24149  132 NLLKGAATQALQNLNLALGLDE 153
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
6-96 2.11e-03

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: 37.92  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446858122   6 IVGASGYAGAELVTYVNRHPHMNITALTVSAQSNDAGKLISDLhpqlkGIVDLPLQPMSDISEFSPGVDVV--FlaTAHE 83
Cdd:cd02274    5 VAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGGL-----AGIGTGVIVSLDLELAAADADVVidF--TTPE 77
                         90
                 ....*....|...
gi 446858122  84 VSHDLAPQFLEAG 96
Cdd:cd02274   78 ATLENLEAAAKAG 90
 
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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