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Conserved domains on  [gi|1859508136|ref|WP_175187113|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Prosthecochloris ethylica]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 8-338 1.98e-147

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: 419.09  E-value: 1.98e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPALN--LDMTYRAYEG---VPESDICFLALPHGEAL 82
Cdd:COG0002     2 KVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRglTDLVFEPPDPdelAAGCDVVFLALPHGVSM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  83 KLVPELLDNGKMVIDLSGDFRLKNPAEHLTYYKQEKPADAWM---TYAMPELFHDEISQAKAASNPGCYATSIILGLAPV 159
Cdd:COG0002    82 ELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLgeaVYGLPELNREEIKGARLIANPGCYPTAVLLALAPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 160 crppMSCGTV--TSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATSPsFGFAFTPMIAP 237
Cdd:COG0002   162 ----LKAGLIdpDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGED-VKVSFTPHLVP 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 238 LTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICSN--PPEVLHVAHTNFCDIHVTQSAQDGSLIVITAIDNLVK 315
Cdd:COG0002   237 MVRGILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEgrLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVK 316

                         330       340
                  ....*....|....*....|...
gi 1859508136 316 GAAGQAVQNMNIMLGYDETLGIM 338
Cdd:COG0002   317 GAAGQAVQNMNLMFGLPETTGLE 339
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 8-338 1.98e-147

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: 419.09  E-value: 1.98e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPALN--LDMTYRAYEG---VPESDICFLALPHGEAL 82
Cdd:COG0002     2 KVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRglTDLVFEPPDPdelAAGCDVVFLALPHGVSM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  83 KLVPELLDNGKMVIDLSGDFRLKNPAEHLTYYKQEKPADAWM---TYAMPELFHDEISQAKAASNPGCYATSIILGLAPV 159
Cdd:COG0002    82 ELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLgeaVYGLPELNREEIKGARLIANPGCYPTAVLLALAPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 160 crppMSCGTV--TSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATSPsFGFAFTPMIAP 237
Cdd:COG0002   162 ----LKAGLIdpDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGED-VKVSFTPHLVP 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 238 LTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICSN--PPEVLHVAHTNFCDIHVTQSAQDGSLIVITAIDNLVK 315
Cdd:COG0002   237 MVRGILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEgrLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVK 316

                         330       340
                  ....*....|....*....|...
gi 1859508136 316 GAAGQAVQNMNIMLGYDETLGIM 338
Cdd:COG0002   317 GAAGQAVQNMNLMFGLPETTGLE 339
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 8-337 1.45e-129

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: 373.84  E-value: 1.45e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQ-AGNKVSDIYPAL--NLDMTYRAY---EGVPESDICFLALPHGEA 81
Cdd:TIGR01850   2 KVAIVGASGYTGGELLRLLLNHPEVEITYLVSSREsAGKPVSEVHPHLrgLVDLNLEPIdveEILEDADVVFLALPHGVS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  82 LKLVPELLDNGKMVIDLSGDFRLKNPAEHLTYYKQEKPADAWM---TYAMPELFHDEISQAKAASNPGCYATSIILGLAP 158
Cdd:TIGR01850  82 AELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLqkaVYGLPELHREEIKGARLIANPGCYPTATLLALAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 159 VCRPPMscGTVTSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTsATSPSFGFAFTPMIAPL 238
Cdd:TIGR01850 162 LLKEGL--IDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGR-LAGGKVKVSFTPHLVPM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 239 TRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRIC--SNPPEVLHVAHTNFCDIHVTQSAQDGSLIVITAIDNLVKG 316
Cdd:TIGR01850 239 TRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLpeGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKG 318

                         330       340
                  ....*....|....*....|.
gi 1859508136 317 AAGQAVQNMNIMLGYDETLGI 337
Cdd:TIGR01850 319 AAGQAVQNMNLMFGFDETTGL 339
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-338 6.30e-74

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 233.18  E-value: 6.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   2 RGYKKPTVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPAL------NLDMTYRAyeGVPESDICFLA 75
Cdd:PLN02968   34 KSEEKKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLitqdlpNLVAVKDA--DFSDVDAVFCC 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  76 LPHG---EALKLVPELLdngkMVIDLSGDFRLKNPAEHLTYYKQEKPA---DAWMTYAMPELFHDEISQAKAASNPGCYA 149
Cdd:PLN02968  112 LPHGttqEIIKALPKDL----KIVDLSADFRLRDIAEYEEWYGHPHRApelQKEAVYGLTELQREEIKSARLVANPGCYP 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 150 TSIILGLapvcRPPMSCGTV--TSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATSPSf 227
Cdd:PLN02968  188 TGIQLPL----VPLVKAGLIepDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKV- 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 228 GFAFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRIC--SNPPEVLHVAHTNFCDIHVTQSAQDGSLI 305
Cdd:PLN02968  263 TPSFTPHLMPMSRGMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLerGAVPHTDHVRGSNYCELNVFADRIPGRAI 342

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1859508136 306 VITAIDNLVKGAAGQAVQNMNIMLGYDETLGIM 338
Cdd:PLN02968  343 IISVIDNLVKGASGQAVQNLNLMMGLPETTGLL 375
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 146-317 1.66e-66

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: 206.56  E-value: 1.66e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 146 GCYATSIILGLAPVCRPPMscGTVTSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATSP 225
Cdd:cd23934     1 GCYPTAALLALAPLLKAGL--IEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 226 sFGFAFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICSN--PPEVLHVAHTNFCDIHVTQSAQDGS 303
Cdd:cd23934    79 -VEVSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEgqLPSTKAVRGSNFCDIGVAVDGRTGR 157

                         170
                  ....*....|....
gi 1859508136 304 LIVITAIDNLVKGA 317
Cdd:cd23934   158 LIVVSAIDNLVKGA 171
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 8-139 3.14e-30

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: 111.46  E-value: 3.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQ-AGNKVSDIYPALN--LDMTYRAY--EGVPESDICFLALPHGEAL 82
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEggKDLVVEDVdpEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1859508136  83 KLVPELLDNGKMVIDLSGDFRLKNpaehltyykqekpaDAwmTYAMPELFHDEISQA 139
Cdd:pfam01118  81 EIAPKLAEAGAKVIDLSSDFRMDD--------------DV--PYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 8-139 2.38e-26

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: 101.09  E-value: 2.38e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136    8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYS-QAGNKVSDIYPALNlDMTYRAYEGVPES----DICFLALPHGEAL 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSrSAGKKVSEAGPHLK-GEVVLELDPPDFEelavDIVFLALPHGVSK 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   83 KLVPELL---DNGKMVIDLSGDFRLKNPAehltyykqekpadawmTYAMPELFHDEISQA 139
Cdd:smart00859  80 ESAPLLPraaAAGAVVIDLSSAFRMDDDV----------------PYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 8-338 1.98e-147

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: 419.09  E-value: 1.98e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPALN--LDMTYRAYEG---VPESDICFLALPHGEAL 82
Cdd:COG0002     2 KVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRglTDLVFEPPDPdelAAGCDVVFLALPHGVSM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  83 KLVPELLDNGKMVIDLSGDFRLKNPAEHLTYYKQEKPADAWM---TYAMPELFHDEISQAKAASNPGCYATSIILGLAPV 159
Cdd:COG0002    82 ELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLgeaVYGLPELNREEIKGARLIANPGCYPTAVLLALAPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 160 crppMSCGTV--TSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATSPsFGFAFTPMIAP 237
Cdd:COG0002   162 ----LKAGLIdpDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGED-VKVSFTPHLVP 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 238 LTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICSN--PPEVLHVAHTNFCDIHVTQSAQDGSLIVITAIDNLVK 315
Cdd:COG0002   237 MVRGILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEgrLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVK 316

                         330       340
                  ....*....|....*....|...
gi 1859508136 316 GAAGQAVQNMNIMLGYDETLGIM 338
Cdd:COG0002   317 GAAGQAVQNMNLMFGLPETTGLE 339
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 8-337 1.45e-129

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: 373.84  E-value: 1.45e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQ-AGNKVSDIYPAL--NLDMTYRAY---EGVPESDICFLALPHGEA 81
Cdd:TIGR01850   2 KVAIVGASGYTGGELLRLLLNHPEVEITYLVSSREsAGKPVSEVHPHLrgLVDLNLEPIdveEILEDADVVFLALPHGVS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  82 LKLVPELLDNGKMVIDLSGDFRLKNPAEHLTYYKQEKPADAWM---TYAMPELFHDEISQAKAASNPGCYATSIILGLAP 158
Cdd:TIGR01850  82 AELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLqkaVYGLPELHREEIKGARLIANPGCYPTATLLALAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 159 VCRPPMscGTVTSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTsATSPSFGFAFTPMIAPL 238
Cdd:TIGR01850 162 LLKEGL--IDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGR-LAGGKVKVSFTPHLVPM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 239 TRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRIC--SNPPEVLHVAHTNFCDIHVTQSAQDGSLIVITAIDNLVKG 316
Cdd:TIGR01850 239 TRGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLpeGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKG 318

                         330       340
                  ....*....|....*....|.
gi 1859508136 317 AAGQAVQNMNIMLGYDETLGI 337
Cdd:TIGR01850 319 AAGQAVQNMNLMFGFDETTGL 339
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-338 6.30e-74

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 233.18  E-value: 6.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   2 RGYKKPTVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPAL------NLDMTYRAyeGVPESDICFLA 75
Cdd:PLN02968   34 KSEEKKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLitqdlpNLVAVKDA--DFSDVDAVFCC 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  76 LPHG---EALKLVPELLdngkMVIDLSGDFRLKNPAEHLTYYKQEKPA---DAWMTYAMPELFHDEISQAKAASNPGCYA 149
Cdd:PLN02968  112 LPHGttqEIIKALPKDL----KIVDLSADFRLRDIAEYEEWYGHPHRApelQKEAVYGLTELQREEIKSARLVANPGCYP 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 150 TSIILGLapvcRPPMSCGTV--TSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATSPSf 227
Cdd:PLN02968  188 TGIQLPL----VPLVKAGLIepDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKV- 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 228 GFAFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRIC--SNPPEVLHVAHTNFCDIHVTQSAQDGSLI 305
Cdd:PLN02968  263 TPSFTPHLMPMSRGMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLerGAVPHTDHVRGSNYCELNVFADRIPGRAI 342

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1859508136 306 VITAIDNLVKGAAGQAVQNMNIMLGYDETLGIM 338
Cdd:PLN02968  343 IISVIDNLVKGASGQAVQNLNLMMGLPETTGLL 375
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 146-317 1.66e-66

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: 206.56  E-value: 1.66e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 146 GCYATSIILGLAPVCRPPMscGTVTSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATSP 225
Cdd:cd23934     1 GCYPTAALLALAPLLKAGL--IEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 226 sFGFAFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICSN--PPEVLHVAHTNFCDIHVTQSAQDGS 303
Cdd:cd23934    79 -VEVSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEgqLPSTKAVRGSNFCDIGVAVDGRTGR 157

                         170
                  ....*....|....
gi 1859508136 304 LIVITAIDNLVKGA 317
Cdd:cd23934   158 LIVVSAIDNLVKGA 171
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 9-145 5.65e-50

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: 164.14  E-value: 5.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   9 VSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPALNLDMTYR-----AYEGVPESDICFLALPHGEALK 83
Cdd:cd17895     3 VGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTDLTfepddDEEIAEDADVVFLALPHGVSME 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859508136  84 LVPELLDNGKMVIDLSGDFRLKNPAEHLTYYKQEKPADAWM---TYAMPELFHDEISQAKAASNP 145
Cdd:cd17895    83 LAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFEHAAPELLkeaVYGLPELNREEIKKARLVANP 147
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 146-317 8.62e-37

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: 130.44  E-value: 8.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 146 GCYATSIILGLAPVCRPPMSCgtVTSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATSP 225
Cdd:cd23939     1 GCNATASILALYPLVKAGLLD--DERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGLLAREI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 226 SFGfaFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICS------NPPEVLHVAHTNFCDIHVTQSA 299
Cdd:cd23939    79 SVS--FTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYRKAYGNEPFVRIVKdrkgiyRYPDPKLVIGSNFCDIGFELDE 156

                         170
                  ....*....|....*...
gi 1859508136 300 QDGSLIVITAIDNLVKGA 317
Cdd:cd23939   157 DNGRLVVFSAIDNLMKGA 174
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 147-317 4.42e-36

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: 128.39  E-value: 4.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 147 CYATSIILGLAPVCRPPMSCGTVTSVScsALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSATsps 226
Cdd:cd18125     1 CYATAALLALYPLLKAGLLKPTPITVT--GVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNLGGKHN--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 227 fgFAFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICSN--PPEVLHVAHTNFCDIHVTQSAQDGSL 304
Cdd:cd18125    76 --VHFTPHVGPWVRGILMTIQCFTQKGWSLRQLHEAYREAYAGEPFVRVMPQgkGPDPKFVQGTNYADIGVELEEDTGRL 153

                         170
                  ....*....|...
gi 1859508136 305 IVITAIDNLVKGA 317
Cdd:cd18125   154 VVMSAIDNLVKGA 166
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 8-156 1.03e-30

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: 114.29  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPalNL----DMTYRAYEGVPESDICFLALPHGEALK 83
Cdd:cd24151     2 TVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHP--NLrgrtLLKFVPPEELESCDVLFLALPHGESMK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  84 LVPELLDNGKMVIDLSGDFRLKNPAEHLTYYKQEKPADAWM---TYAMPELFHDEISQA---------KAASNPGCYATS 151
Cdd:cd24151    80 RIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLerfVYGLPELHREELRGAryiaganlmKGAAGQAVQAMN 159


                  ....*
gi 1859508136 152 IILGL 156
Cdd:cd24151   160 VMLGF 164
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 8-139 3.14e-30

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: 111.46  E-value: 3.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQ-AGNKVSDIYPALN--LDMTYRAY--EGVPESDICFLALPHGEAL 82
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEggKDLVVEDVdpEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1859508136  83 KLVPELLDNGKMVIDLSGDFRLKNpaehltyykqekpaDAwmTYAMPELFHDEISQA 139
Cdd:pfam01118  81 EIAPKLAEAGAKVIDLSSDFRMDD--------------DV--PYGLPEVNREAIKQA 121
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 146-317 3.16e-27

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: 104.64  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 146 GCYATSIILGLAPVcRPPMScgtvTSVSCSALSGLSGAGR--SAKTELSFseMNNNIRAYKVGMHQHTPEILQALGTSAt 223
Cdd:cd23936     1 GCYATGAQLALAPL-LDDLD----GPPSVFGVSGYSGAGTkpSPKNDPEV--LADNLIPYSLVGHIHEREVSRHLGTPV- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 224 spsfgfAFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICSNPPEVLHVAHTNFCDI-HVTQSAQDG 302
Cdd:cd23936    73 ------AFMPHVAPWFQGITLTISIPLKKSMTADEIRELYQEAYAGEPLIKVTKEIPLVRDNAGKHGVVVgGFTVHPDGK 146

                         170
                  ....*....|....*
gi 1859508136 303 SLIVITAIDNLVKGA 317
Cdd:cd23936   147 RVVVVATIDNLLKGA 161
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 8-139 2.38e-26

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: 101.09  E-value: 2.38e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136    8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYS-QAGNKVSDIYPALNlDMTYRAYEGVPES----DICFLALPHGEAL 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSrSAGKKVSEAGPHLK-GEVVLELDPPDFEelavDIVFLALPHGVSK 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   83 KLVPELL---DNGKMVIDLSGDFRLKNPAehltyykqekpadawmTYAMPELFHDEISQA 139
Cdd:smart00859  80 ESAPLLPraaAAGAVVIDLSSAFRMDDDV----------------PYGLPEVNPEAIKKA 123
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 8-145 2.69e-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: 99.67  E-value: 2.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPALnLDMTYRAYE-----GVPESDICFLALPHGEAL 82
Cdd:cd24148     2 RVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHL-PPLADRVLEpttpaVLAGHDVVFLALPHGASA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859508136  83 KLVPELLDNGKmVIDLSGDFRLKNPAEHLTYYKQEKpADAWmTYAMPEL--FHDEISQAKAASNP 145
Cdd:cd24148    81 AIAAQLPPDVL-VVDCGADHRLEDAAAWEKFYGGEH-AGGW-TYGLPELpgAREALAGARRIAVP 142
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 8-146 5.85e-24

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: 95.64  E-value: 5.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLEnlYAYS--QAGNKVSD------IYPALNLDMTYRAyEGVPESDICFLALPHG 79
Cdd:cd24149     2 RVGLIGARGYVGRELIRLLNRHPNLELA--HVSSreLAGQKVSGytkspiDYLNLSVEDIPEE-VAAREVDAWVLALPNG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859508136  80 EALKLVPEL--LDNGKMVIDLSGDFRLknpaehltyykqekpADAWmTYAMPELFHDEISQAKAASNPG 146
Cdd:cd24149    79 VAKPFVDAIdkANPKSVIVDLSADYRF---------------DDAW-TYGLPELNRRRIAGAKRISNPG 131
argC_other TIGR01851
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ...
 6-330 1.19e-22

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: 96.06  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   6 KPTVSIIGASGYSGAELSGMIARHPSVKLenlyaysqagnkVSdIYPALNLDMTYRAyEGVPESDICFLALPHGEALKLV 85
Cdd:TIGR01851   1 APKVFIDGEAGTTGLQIRERLSGRDDIEL------------LS-IAPDRRKDAAERA-KLLNAADVAILCLPDDAAREAV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  86 pELLDNGKMVI-DLSGDFRLknpaehltyykqekpADAWMtYAMPELF---HDEISQAKAASNPGCYATSIILglapVCR 161
Cdd:TIGR01851  67 -SLVDNPNTCIiDASTAYRT---------------ADDWA-YGFPELApgqREKIRNSKRIANPGCYPTGFIA----LMR 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 162 PPMSCGTVTS---VSCSALSGLSGAGRSAKTELSFSEMNNNIRA----YKVGM-HQHTPEILQALGTsATSPsfgfAFTP 233
Cdd:TIGR01851 126 PLVEAGILPAdfpITINAVSGYSGGGKAMIADYEQGSADNPSLQpfriYGLALtHKHLPEMRVHSGL-ALPP----IFTP 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 234 MIAPLTRGIYTVLNISL-EKQLPVS------EIKEHYR--QFYRSAPFVRICSNPPEVLHVA---HTNFCDIHVTQSAQD 301
Cdd:TIGR01851 201 AVGNFAQGMAVTIPLHLqTLASKVSpadihaALADYYQgeQFVRVAPLDDVETLDNTFLDPQglnGTNRLDLFVFGSDDG 280

                         330       340
                  ....*....|....*....|....*....
gi 1859508136 302 GSLIVITAIDNLVKGAAGQAVQNMNIMLG 330
Cdd:TIGR01851 281 ERALLVARLDNLGKGASGAAVQNLNIMLG 309
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 7-145 3.06e-21

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: 88.78  E-value: 3.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   7 PTVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQAGNKVSDIYPALNLDMT---YRAYEGVPESDICFLALPHGEALK 83
Cdd:cd02280     1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIISLQiqeFRPCEVLNSADILVLALPHGASAE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1859508136  84 LVPELLDNGKMVIDLSGDFRLKNPAEHLTYYKQEKPADaWMtYAMPELF-HDEISQAKAASNP 145
Cdd:cd02280    81 LVAAISNPQVKIIDLSADFRFTDPEVYRRHPRPDLEGG-WV-YGLPELDrEQRIANATRIANP 141
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 167-315 5.36e-18

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: 80.05  E-value: 5.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 167 GTVTSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVG-MHQHTPEILQALGTSATSPSfGFAFTPMI------APLT 239
Cdd:pfam02774   9 GGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGeEHNGTPETREELKMVNETKK-ILGFTPKVsatcvrVPVF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 240 RGIYTVLNISLE-KQLPVSEIKEhyrQFYRSA-PFVRICSNP--PEVLHVAH-TNFCDI-HVTQSAQDG-SLIVITAIDN 312
Cdd:pfam02774  88 RGHSETVTVKLKlKPIDVEEVYE---AFYAAPgVFVVVRPEEdyPTPRAVRGgTNFVYVgRVRKDPDGDrGLKLVSVIDN 164


                  ...
gi 1859508136 313 LVK 315
Cdd:pfam02774 165 LRK 167
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 9-331 9.26e-18

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 82.95  E-value: 9.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   9 VSIIGASGYSGAELSGMIARHPSVKLENLYA--------YSQAGN-KVSDIYPALNLDMTYRA--YEGVPESDICFLALP 77
Cdd:PRK08664    6 VGILGATGMVGQRFVQLLANHPWFEVTALAAsersagktYGEAVRwQLDGPIPEEVADMEVVStdPEAVDDVDIVFSALP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  78 HGEALKLVPELLDNGKMVIDLSGDFRLK----------NPaEHLTYYKQEKPADAWmtyampelfhdeisQAKAASNPGC 147
Cdd:PRK08664   86 SDVAGEVEEEFAKAGKPVFSNASAHRMDpdvplvipevNP-EHLELIEVQRKRRGW--------------DGFIVTNPNC 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 148 YATSIILGLAPVcrppMSCGtVTSVSCSALSGLSGAGrsaKTELSFSEMNNNIRAYKVG----MHQhtpEILQALGTSAT 223
Cdd:PRK08664  151 STIGLVLALKPL----MDFG-IERVHVTTMQAISGAG---YPGVPSMDIVDNVIPYIGGeeekIEK---ETLKILGKFEG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 224 SPSFGFAFtPMIAPLTR-----GIYTVLNISLEKQLPVSEIKEHYRQF--------YRSAP--FVRICSNP--PEV-LHV 285
Cdd:PRK08664  220 GKIVPADF-PISATCHRvpvidGHTEAVFVKFKEDVDPEEIREALESFkglpqelgLPSAPkkPIILFEEPdrPQPrLDR 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1859508136 286 AHTNFCDIHVTQSAQDGSLIV--ITAIDNLVKGAAGQAVQNMNIM--LGY 331
Cdd:PRK08664  299 DAGDGMAVSVGRLREDGIFDIkfVVLGHNTVRGAAGASVLNAELLkkKGY 348
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 146-317 2.27e-17

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: 78.41  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 146 GCYATSIILGLapvcRPPMSCGTV---TSVSCSALSGLSGAGRS--AKTELSFSEMNNNIRAYKVG-MHQHTPEIlQALG 219
Cdd:cd23935     1 GCYATGAILLL----RPLVEAGLLpadYPLSIHAVSGYSGGGKKmiEQYEAAEAADLPPPRPYGLGlEHKHLPEM-QKHA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 220 TSATSPsfgfAFTPMIAPLTRGIytVLNISLEKQL---PVS--EIKEHYRQFYRSAPFVRICS-NPPEVL------HVAH 287
Cdd:cd23935    76 GLARPP----IFTPAVGNFYQGM--LVTVPLHLDLlekGVSaaEVHEALAEHYAGERFVKVMPlDEPDALgfldpqALNG 149

                         170       180       190
                  ....*....|....*....|....*....|
gi 1859508136 288 TNFCDIHVTQSaQDGSLIVITAIDNLVKGA 317
Cdd:cd23935   150 TNNLELFVFGN-DKGQALLVARLDNLGKGA 178
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 8-105 2.38e-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: 63.54  E-value: 2.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLE-NLYAYSQAGNKVSDIYPALNLDMTYRAYEgvPES----DICFLALPHGEAL 82
Cdd:cd02281     2 KVGVVGATGYVGGEFLRLLLEHPFPLFEiVLLAASSAGAKKKYFHPKLWGRVLVEFTP--EEVleqvDIVFTALPGGVSA 79

                          90       100
                  ....*....|....*....|...
gi 1859508136  83 KLVPELLDNGKMVIDLSGDFRLK 105
Cdd:cd02281    80 KLAPELSEAGVLVIDNASDFRLD 102
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 147-313 1.08e-11

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


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 62.54  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 147 CYATSIILGLAPVCRppmSCGtVTSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYKVGMHQHTPEILQALGTSatSPS 226
Cdd:cd18122     1 CTTTGLIPAAKALND---KFG-IEEILVVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGEI--GKP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 227 FGFAFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEHYRQFYRSAPFVRICSNPPEVLHVAHTNF-CDIHVTQSAQDGS-- 303
Cdd:cd18122    75 IKVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGvYGVPVGRQREFAFdd 154

                         170
                  ....*....|..
gi 1859508136 304 --LIVITAIDNL 313
Cdd:cd18122   155 nkLKVFSAVDNE 166
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 8-109 1.06e-07

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: 50.41  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   8 TVSIIGASGYSGAELSGMIARHPSVKLE-NLYAYSQ-AGNKVSDIYPALNL-DMTYRAYEGVpesDICFLALPHGEALKL 84
Cdd:cd24147     2 RVGVVGATGAVGSEILQLLAEEPDPLFElRALASEEsAGKKAEFAGEAIMVqEADPIDFLGL---DIVFLCAGAGVSAKF 78

                          90       100
                  ....*....|....*....|....*
gi 1859508136  85 VPELLDNGKMVIDLSGDFRLKNPAE 109
Cdd:cd24147    79 APEAARAGVLVIDNAGALRMDPDVP 103
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 7-329 1.25e-07

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 52.47  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   7 PTVSIIGASGYSGAELSGMIARH--PSVKLENLYAYSQAGNKVSDIYPALNL-DMTYRAYEGVpesDICFLALPHGEALK 83
Cdd:PLN02383    8 PSVAIVGVTGAVGQEFLSVLTDRdfPYSSLKMLASARSAGKKVTFEGRDYTVeELTEDSFDGV---DIALFSAGGSISKK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  84 LVPELLDNGKMVIDLSGDFRlknpaehltyYKQEKPadawmtYAMPE-----LFHDEISQAKAA--SNPGCyatSIILGL 156
Cdd:PLN02383   85 FGPIAVDKGAVVVDNSSAFR----------MEEGVP------LVIPEvnpeaMKHIKLGKGKGAliANPNC---STIICL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 157 APVCrPPMSCGTVTSVSCSALSGLSGAGRSAKTELSfsemnnniraykvgmhQHTPEILQalGTSATSPSFG--FAFT-- 232
Cdd:PLN02383  146 MAVT-PLHRHAKVKRMVVSTYQAASGAGAAAMEELE----------------QQTREVLE--GKPPTCNIFAqqYAFNlf 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 233 PMIAPL---------------TRGIYTVLN-------------------ISLEKQLPVSEIKEhyRQFYRSAPFVRICSN 278
Cdd:PLN02383  207 SHNAPMqengyneeemklvkeTRKIWNDDDvkvtatcirvpvmrahaesINLQFEKPLDEATA--REILASAPGVKIIDD 284

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1859508136 279 P-----PEVLHVAHTNfcDIHVTQSAQDGS------LIVITAIDNLVKGAAGQAVQNMNIML 329
Cdd:PLN02383  285 RannrfPTPLDASNKD--DVAVGRIRQDISqdgnkgLDIFVCGDQIRKGAALNAVQIAELLL 344
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 2-323 9.75e-07

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 50.05  E-value: 9.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   2 RGYKkptVSIIGASGYSGAELSGMIARHPSVKLENLYAYSQ---AGNKVSDIYPALNL-DMTYRAYEGVpesDICFLALP 77
Cdd:PRK06728    4 KGYH---VAVVGATGAVGQKIIELLEKETKFNIAEVTLLSSkrsAGKTVQFKGREIIIqEAKINSFEGV---DIAFFSAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  78 HGEALKLVPELLDNGKMVIDLSGDFRLKnpaehltyykQEKPadawmtYAMPELFHDEISQAKAA-SNPGCYATSIILGL 156
Cdd:PRK06728   78 GEVSRQFVNQAVSSGAIVIDNTSEYRMA----------HDVP------LVVPEVNAHTLKEHKGIiAVPNCSALQMVTAL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 157 APVCR----PPMSCGTVTSVSCSALSGLSGAGRSAKTELSFSEMNNNIRAYK---------------------------- 204
Cdd:PRK06728  142 QPIRKvfglERIIVSTYQAVSGSGIHAIQELKEQAKSILAGEEVESTILPAKkdkkhypiafnvlpqvdiftdndftfee 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136 205 VGMHQHTPEILQalgtsatSPSFGFAFTPMIAPLTRGIYTVLNISLEKQLPVSEIKEhyrqFYRSAPFVRICSNPPEVLH 284
Cdd:PRK06728  222 VKMIQETKKILE-------DPNLKMAATCVRVPVISGHSESVYIELEKEATVAEIKE----VLFDAPGVILQDNPSEQLY 290

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1859508136 285 ---VAHTNFCDIHVTQSAQD-----GSLIVITAiDNLVKGAAGQAVQ 323
Cdd:PRK06728  291 pmpLYAEGKIDTFVGRIRKDpdtpnGFHLWIVS-DNLLKGAAWNSVQ 336
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 312-330 1.82e-05

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


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 43.75  E-value: 1.82e-05
                          10
                  ....*....|....*....
gi 1859508136 312 NLVKGAAGQAVQNMNIMLG 330
Cdd:cd17896   114 NLGKGASGAAVQNMNLMLG 132
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 50-146 3.49e-04

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


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 39.89  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136  50 IYPALNLDMTYRAyEGVPESDICFLALPHGEALKLVpELLDNGKM-VIDLSGDFRLknpaehltyykqekpADAWmTYAM 128
Cdd:cd17896    31 IPEDKRKDPAARA-ELLNAADIAILCLPDDAAREAV-ALVTNPRTrIIDASTAHRT---------------APGW-AYGF 92

                          90       100
                  ....*....|....*....|.
gi 1859508136 129 PEL---FHDEISQAKAASNPG 146
Cdd:cd17896    93 PELspeQREKIATSKRVANPG 113
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 7-104 2.34e-03

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: 37.99  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   7 PTVSIIGASGYSGAELSGMIARHPsVKLENLYAYS---QAGNKVS---DIYPALNLDMTyrAYEGVpesDICFLALPHGE 80
Cdd:cd17894     1 YRIAVVGATGLVGKELLELLEERG-FPVGRLRLLDseeSAGELVEfggEPLDVQDLDEF--DFSDV---DLVFFAGPAEV 74

                          90       100
                  ....*....|....*....|....
gi 1859508136  81 ALKLVPELLDNGKMVIDLSGDFRL 104
Cdd:cd17894    75 ARAYAPRARAAGCLVIDLSGALRS 98
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 9-103 4.30e-03

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: 37.47  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859508136   9 VSIIGASGYSGAELSGMIARHPSVKLENLYA--------YSQAGN-KVSDIYPALNLDMTYR--AYEGVPESDICFLALP 77
Cdd:cd02315     3 VGVLGATGMVGQRFIQLLANHPWFELAALGAsersagkkYGDAVRwKQDTPIPEEVADMVVKecEPEEFKDCDIVFSALD 82

                          90       100
                  ....*....|....*....|....*.
gi 1859508136  78 HGEALKLVPELLDNGKMVIDLSGDFR 103
Cdd:cd02315    83 SDVAGEIEPAFAKAGIPVFSNASNHR 108
 
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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