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Conserved domains on  [gi|2124883267|ref|WP_227106896|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Chromobacterium rhizoryzae]

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]; ...
 2-342 0e+00

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


:

Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 590.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARL-RDCDVVFFATPNGIA 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPDELaAGCDVVFLALPHGVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVANPGCYPTAVQLGFLP 160
Cdd:COG0002    81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 161 LIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVGLTFVPHLTPMIRG 240
Cdd:COG0002   161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 241 IHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVCRIAAHRPQGGDTVVVLSVIDNLVKGAAG 317
Cdd:COG0002   241 ILATIYARLKDGVteeDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                         330       340
                  ....*....|....*....|....*
gi 2124883267 318 QAVQNMNLMFGQPERAGLDIVPLLP 342
Cdd:COG0002   321 QAVQNMNLMFGLPETTGLELVPLYP 345
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-342 0e+00

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


Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 590.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARL-RDCDVVFFATPNGIA 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPDELaAGCDVVFLALPHGVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVANPGCYPTAVQLGFLP 160
Cdd:COG0002    81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 161 LIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVGLTFVPHLTPMIRG 240
Cdd:COG0002   161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 241 IHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVCRIAAHRPQGGDTVVVLSVIDNLVKGAAG 317
Cdd:COG0002   241 ILATIYARLKDGVteeDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                         330       340
                  ....*....|....*....|....*
gi 2124883267 318 QAVQNMNLMFGQPERAGLDIVPLLP 342
Cdd:COG0002   321 QAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-342 0e+00

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


Pssm-ID: 273832 [Multi-domain]  Cd Length: 346  Bit Score: 506.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVT-VVTSRKEAGMKVADLFPSLRGRIDLAFSTPD-EARLRDCDVVFFATPNGI 79
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITyLVSSRESAGKPVSEVHPHLRGLVDLNLEPIDvEEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  80 AMNEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVANPGCYPTAVQLGFL 159
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 160 PLIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVGLTFVPHLTPMIR 239
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 240 GIHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVCRIAAHRPQGGDTVVVLSVIDNLVKGAA 316
Cdd:TIGR01850 241 GILATIYAKLKDGLteeDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|....*.
gi 2124883267 317 GQAVQNMNLMFGQPERAGLDIVPLLP 342
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-342 3.52e-120

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 351.44  E-value: 3.52e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   1 MIKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARLRDCDVVFFATPNGiA 80
Cdd:PLN02968   38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDLPNLVAVKDADFSDVDAVFCCLPHG-T 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVANPGCYPTAVQLGFLP 160
Cdd:PLN02968  117 TQEIIKALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLVP 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 161 LIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVGLTFVPHLTPMIRG 240
Cdd:PLN02968  197 LVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSRG 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 241 IHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVC--RIAAHRPQGgdTVVVLSVIDNLVKGA 315
Cdd:PLN02968  277 MQSTVYVHYAPGVtaeDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCelNVFADRIPG--RAIIISVIDNLVKGA 354

                         330       340
                  ....*....|....*....|....*..
gi 2124883267 316 AGQAVQNMNLMFGQPERAGLDIVPLLP 342
Cdd:PLN02968  355 SGQAVQNLNLMMGLPETTGLLQQPLFP 381
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 148-315 4.70e-89

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: 264.34  E-value: 4.70e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 148 GCYPTAVQLGFLPLIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVG 227
Cdd:cd23934     1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 228 LTFVPHLTPMIRGIHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVCRIAAHRPQGGDTVVV 304
Cdd:cd23934    81 VSFTPHLVPMTRGILATIYAKLKDGVtaeDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                         170
                  ....*....|.
gi 2124883267 305 LSVIDNLVKGA 315
Cdd:cd23934   161 VSAIDNLVKGA 171
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 3-141 1.23e-44

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


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 148.83  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   3 KVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKE-AGMKVADLFPSLRGRIDLAFSTPDEARLRDCDVVFFATPNGIAM 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEGGKDLVVEDVDPEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  82 NEARELLAAGVRVVDLAADYRIRDvaewekwygmshgspdlvaEAVYGLPEINREAIRGA 141
Cdd:pfam01118  81 EIAPKLAEAGAKVIDLSSDFRMDD-------------------DVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 3-141 2.52e-39

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: 135.37  E-value: 2.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267    3 KVGIVGGTGYTGVELLRLLAGHPSARVT-VVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARLrDCDVVFFATPNGIAM 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTaLAASSRSAGKKVSEAGPHLKGEVVLELDPPDFEEL-AVDIVFLALPHGVSK 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124883267   82 N---EARELLAAGVRVVDLAADYRIRDvaewekwygmshgspdlvaEAVYGLPEINREAIRGA 141
Cdd:smart00859  80 EsapLLPRAAAAGAVVIDLSSAFRMDD-------------------DVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-342 0e+00

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


Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 590.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARL-RDCDVVFFATPNGIA 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEPPDPDELaAGCDVVFLALPHGVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVANPGCYPTAVQLGFLP 160
Cdd:COG0002    81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 161 LIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVGLTFVPHLTPMIRG 240
Cdd:COG0002   161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 241 IHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVCRIAAHRPQGGDTVVVLSVIDNLVKGAAG 317
Cdd:COG0002   241 ILATIYARLKDGVteeDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                         330       340
                  ....*....|....*....|....*
gi 2124883267 318 QAVQNMNLMFGQPERAGLDIVPLLP 342
Cdd:COG0002   321 QAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-342 0e+00

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


Pssm-ID: 273832 [Multi-domain]  Cd Length: 346  Bit Score: 506.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVT-VVTSRKEAGMKVADLFPSLRGRIDLAFSTPD-EARLRDCDVVFFATPNGI 79
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITyLVSSRESAGKPVSEVHPHLRGLVDLNLEPIDvEEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  80 AMNEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVANPGCYPTAVQLGFL 159
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 160 PLIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVGLTFVPHLTPMIR 239
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 240 GIHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVCRIAAHRPQGGDTVVVLSVIDNLVKGAA 316
Cdd:TIGR01850 241 GILATIYAKLKDGLteeDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|....*.
gi 2124883267 317 GQAVQNMNLMFGQPERAGLDIVPLLP 342
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-342 3.52e-120

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 351.44  E-value: 3.52e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   1 MIKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARLRDCDVVFFATPNGiA 80
Cdd:PLN02968   38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDLPNLVAVKDADFSDVDAVFCCLPHG-T 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVANPGCYPTAVQLGFLP 160
Cdd:PLN02968  117 TQEIIKALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLVP 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 161 LIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVGLTFVPHLTPMIRG 240
Cdd:PLN02968  197 LVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSRG 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 241 IHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVC--RIAAHRPQGgdTVVVLSVIDNLVKGA 315
Cdd:PLN02968  277 MQSTVYVHYAPGVtaeDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCelNVFADRIPG--RAIIISVIDNLVKGA 354

                         330       340
                  ....*....|....*....|....*..
gi 2124883267 316 AGQAVQNMNLMFGQPERAGLDIVPLLP 342
Cdd:PLN02968  355 SGQAVQNLNLMMGLPETTGLLQQPLFP 381
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 148-315 4.70e-89

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: 264.34  E-value: 4.70e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 148 GCYPTAVQLGFLPLIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQTVG 227
Cdd:cd23934     1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 228 LTFVPHLTPMIRGIHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVCRIAAHRPQGGDTVVV 304
Cdd:cd23934    81 VSFTPHLVPMTRGILATIYAKLKDGVtaeDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                         170
                  ....*....|.
gi 2124883267 305 LSVIDNLVKGA 315
Cdd:cd23934   161 VSAIDNLVKGA 171
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 2-147 1.82e-81

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: 245.03  E-value: 1.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPD-EARLRDCDVVFFATPNGIA 80
Cdd:cd17895     1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTDLTFEPDDdEEIAEDADVVFLALPHGVS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVANP 147
Cdd:cd17895    81 MELAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFEHAAPELLKEAVYGLPELNREEIKKARLVANP 147
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 2-145 1.55e-55

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: 178.62  E-value: 1.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEarLRDCDVVFFATPNGIAM 81
Cdd:cd24151     1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNLRGRTLLKFVPPEE--LESCDVLFLALPHGESM 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124883267  82 NEARELLAAGVRVVDLAADYRIRDVAEWEKWYGMSHGSPDLVAEAVYGLPEINREAIRGARLVA 145
Cdd:cd24151    79 KRIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLERFVYGLPELHREELRGARYIA 142
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 3-141 1.23e-44

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


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 148.83  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   3 KVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKE-AGMKVADLFPSLRGRIDLAFSTPDEARLRDCDVVFFATPNGIAM 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEGGKDLVVEDVDPEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  82 NEARELLAAGVRVVDLAADYRIRDvaewekwygmshgspdlvaEAVYGLPEINREAIRGA 141
Cdd:pfam01118  81 EIAPKLAEAGAKVIDLSSDFRMDD-------------------DVPYGLPEVNREAIKQA 121
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 149-315 9.61e-40

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: 138.02  E-value: 9.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 149 CYPTAVQLGFLPLIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRaaaqTVGL 228
Cdd:cd18125     1 CYATAALLALYPLLKAGLLKPTPITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNLGG----KHNV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 229 TFVPHLTPMIRGIHATLYARLKADV---DVQALFERRYEGEHFVDVLPAGSHPETRSVRGANVCRIAAHRPQGGDTVVVL 305
Cdd:cd18125    77 HFTPHVGPWVRGILMTIQCFTQKGWslrQLHEAYREAYAGEPFVRVMPQGKGPDPKFVQGTNYADIGVELEEDTGRLVVM 156

                         170
                  ....*....|
gi 2124883267 306 SVIDNLVKGA 315
Cdd:cd18125   157 SAIDNLVKGA 166
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 3-141 2.52e-39

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: 135.37  E-value: 2.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267    3 KVGIVGGTGYTGVELLRLLAGHPSARVT-VVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARLrDCDVVFFATPNGIAM 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTaLAASSRSAGKKVSEAGPHLKGEVVLELDPPDFEEL-AVDIVFLALPHGVSK 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124883267   82 N---EARELLAAGVRVVDLAADYRIRDvaewekwygmshgspdlvaEAVYGLPEINREAIRGA 141
Cdd:smart00859  80 EsapLLPRAAAAGAVVIDLSSAFRMDD-------------------DVPYGLPEVNPEAIKKA 123
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 148-315 2.27e-38

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: 134.67  E-value: 2.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 148 GCYPTAVQLGFLPLIEAGAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAQtVG 227
Cdd:cd23939     1 GCNATASILALYPLVKAGLLDDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGLLARE-IS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 228 LTFVPHLTPMIRGIHATLYARLKADV---DVQALFERRYEGEHFVDVLPA--GSH--PETRSVRGANVCRIAAHRPQGGD 300
Cdd:cd23939    80 VSFTAHSVDMVRGILATAHVFLKEGVtekDLWKAYRKAYGNEPFVRIVKDrkGIYryPDPKLVIGSNFCDIGFELDEDNG 159

                         170
                  ....*....|....*
gi 2124883267 301 TVVVLSVIDNLVKGA 315
Cdd:cd23939   160 RLVVFSAIDNLMKGA 174
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 2-147 1.81e-37

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: 132.03  E-value: 1.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARLRDCDVVFFATPNGIAM 81
Cdd:cd24148     1 IRVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHLPPLADRVLEPTTPAVLAGHDVVFLALPHGASA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124883267  82 NEARElLAAGVRVVDLAADYRIRDVAEWEKWYGMSHgspdlvAEA-VYGLPEI--NREAIRGARLVANP 147
Cdd:cd24148    81 AIAAQ-LPPDVLVVDCGADHRLEDAAAWEKFYGGEH------AGGwTYGLPELpgAREALAGARRIAVP 142
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 2-147 2.34e-34

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


Pssm-ID: 467515 [Multi-domain]  Cd Length: 160  Bit Score: 123.83  E-value: 2.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEArLRDCDVVFFATPNGIAM 81
Cdd:cd02280     1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIISLQIQEFRPCEV-LNSADILVLALPHGASA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124883267  82 NEARELLAAGVRVVDLAADYRIRDVAEWEKWYGmshgsPDLVAEAVYGLPEINREA-IRGARLVANP 147
Cdd:cd02280    80 ELVAAISNPQVKIIDLSADFRFTDPEVYRRHPR-----PDLEGGWVYGLPELDREQrIANATRIANP 141
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 2-148 1.12e-33

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: 121.45  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDL-AFSTPDEARLRDCDVVFFATPNGIA 80
Cdd:cd24149     1 KRVGLIGARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVSGYTKSPIDYLNLsVEDIPEEVAAREVDAWVLALPNGVA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MN--EARELLAAGVRVVDLAADYRIRDvaEWekwygmshgspdlvaeaVYGLPEINREAIRGARLVANPG 148
Cdd:cd24149    81 KPfvDAIDKANPKSVIVDLSADYRFDD--AW-----------------TYGLPELNRRRIAGAKRISNPG 131
argC_other TIGR01851
N-acetyl-gamma-glutamyl-phosphate reductase, uncommon form; This model represents the less ...
 37-328 6.94e-31

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: 118.79  E-value: 6.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  37 EAGMKVADLFPSLRGRIDLAFSTPDEARLRD----------CDVVFFATPNgIAMNEARELLA-AGVRVVDLAADYRIRD 105
Cdd:TIGR01851   9 EAGTTGLQIRERLSGRDDIELLSIAPDRRKDaaerakllnaADVAILCLPD-DAAREAVSLVDnPNTCIIDASTAYRTAD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 106 vaEWekwygmshgspdlvaeaVYGLPEIN---REAIRGARLVANPGCYPTAVQLGFLPLIEAGAVELSSLI-ADCKSGVS 181
Cdd:TIGR01851  88 --DW-----------------AYGFPELApgqREKIRNSKRIANPGCYPTGFIALMRPLVEAGILPADFPItINAVSGYS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 182 GAGRKAEVGALLAEAGD----SFKAYGVS-GHRHLPEIRqglgraaaQTVGLTFVPHLTPMIR----------GIHATLY 246
Cdd:TIGR01851 149 GGGKAMIADYEQGSADNpslqPFRIYGLAlTHKHLPEMR--------VHSGLALPPIFTPAVGnfaqgmavtiPLHLQTL 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 247 ARLKADVDVQALFERRYEGEHFVDVLPAGSHPETR-------SVRGANVCRIAAHRPQGGDTVVVLSVIDNLVKGAAGQA 319
Cdd:TIGR01851 221 ASKVSPADIHAALADYYQGEQFVRVAPLDDVETLDntfldpqGLNGTNRLDLFVFGSDDGERALLVARLDNLGKGASGAA 300


                  ....*....
gi 2124883267 320 VQNMNLMFG 328
Cdd:TIGR01851 301 VQNLNIMLG 309
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 2-147 5.63e-25

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


Pssm-ID: 467516 [Multi-domain]  Cd Length: 145  Bit Score: 98.20  E-value: 5.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPS-ARVTVVTSRKEAGMKVADLFPSLRGRIDLAFstPDEARLRDCDVVFFATPNGIA 80
Cdd:cd02281     1 KKVGVVGATGYVGGEFLRLLLEHPFpLFEIVLLAASSAGAKKKYFHPKLWGRVLVEF--TPEEVLEQVDIVFTALPGGVS 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRIRDvaewekwygmshgspdlvaEAVYGLPEINREAI---RGARLVANP 147
Cdd:cd02281    79 AKLAPELSEAGVLVIDNASDFRLDK-------------------DVPLVVPEVNREHIgelKGTKIIANP 129
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 160-313 4.42e-23

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: 93.92  E-value: 4.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 160 PLIEAgAVELSSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSG-HRHLPEIRQGLGRAAAQTVGLTFVP------ 232
Cdd:pfam02774   3 PLRDA-LGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGEeHNGTPETREELKMVNETKKILGFTPkvsatc 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 233 HLTPMIRGIHATLYARLKADV----DVQALFERryEGEHFVDVLPAGSHPETRSVRGA-NVCRIAAHR--PQGGDTVVVL 305
Cdd:pfam02774  82 VRVPVFRGHSETVTVKLKLKPidveEVYEAFYA--APGVFVVVRPEEDYPTPRAVRGGtNFVYVGRVRkdPDGDRGLKLV 159


                  ....*...
gi 2124883267 306 SVIDNLVK 313
Cdd:pfam02774 160 SVIDNLRK 167
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 148-315 1.15e-18

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: 82.26  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 148 GCYPTAVQLGFLPLIEAGAVELSS-LIADCKSGVSGAGRKAeVGALLAEAGDSFKAYGVSG----HRHLPEIRQ--GLGR 220
Cdd:cd23935     1 GCYATGAILLLRPLVEAGLLPADYpLSIHAVSGYSGGGKKM-IEQYEAAEAADLPPPRPYGlgleHKHLPEMQKhaGLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 221 AAaqtvglTFVPHLTPMIRGIHATLYARLKADV------DVQALFERRYEGEHFVDVLPAGSHPETRSVR-----GANVC 289
Cdd:cd23935    80 PP------IFTPAVGNFYQGMLVTVPLHLDLLEkgvsaaEVHEALAEHYAGERFVKVMPLDEPDALGFLDpqalnGTNNL 153

                         170       180
                  ....*....|....*....|....*.
gi 2124883267 290 RIAAHrPQGGDTVVVLSVIDNLVKGA 315
Cdd:cd23935   154 ELFVF-GNDKGQALLVARLDNLGKGA 178
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 148-315 3.14e-18

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: 80.37  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 148 GCYPTAVQLGFLPLIEAGAVELSSLIAdckSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRAAAqtvg 227
Cdd:cd23936     1 GCYATGAQLALAPLLDDLDGPPSVFGV---SGYSGAGTKPSPKNDPEVLADNLIPYSLVGHIHEREVSRHLGTPVA---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 228 ltFVPHLTPMIRGIHATLYARLKADV---DVQALFERRYEGEHFVDVLpaGSHPETRSVRGANVCRIAA-HRPQGGDTVV 303
Cdd:cd23936    74 --FMPHVAPWFQGITLTISIPLKKSMtadEIRELYQEAYAGEPLIKVT--KEIPLVRDNAGKHGVVVGGfTVHPDGKRVV 149

                         170
                  ....*....|..
gi 2124883267 304 VLSVIDNLVKGA 315
Cdd:cd23936   150 VVATIDNLLKGA 161
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-327 4.63e-17

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 81.02  E-value: 4.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   1 MIKVGIVGGTGYTGVELLRLLAGHPSARVTVVT-SRKEAGMKVADL--------FP-SLRgriDLAFSTPDEARLRDCDV 70
Cdd:PRK08664    3 KLKVGILGATGMVGQRFVQLLANHPWFEVTALAaSERSAGKTYGEAvrwqldgpIPeEVA---DMEVVSTDPEAVDDVDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  71 VFFATPNGIAMNEARELLAAGVRVVDLAADYRIR-DVaewekwygmshgsPDLVaeavyglPEINREAI---------RG 140
Cdd:PRK08664   80 VFSALPSDVAGEVEEEFAKAGKPVFSNASAHRMDpDV-------------PLVI-------PEVNPEHLelievqrkrRG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 141 AR--LVANPGCYPTAVQLGFLPLIEAG--AVELSSLIAdcksgVSGAGR----------------KAEVGALLAEagdSF 200
Cdd:PRK08664  140 WDgfIVTNPNCSTIGLVLALKPLMDFGieRVHVTTMQA-----ISGAGYpgvpsmdivdnvipyiGGEEEKIEKE---TL 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 201 KaygVSGHRHLPEIRQGLGRAAAQTvgltfvpHLTPMIRGIHATLYARLKADVDVQALFE--RRYEG-----------EH 267
Cdd:PRK08664  212 K---ILGKFEGGKIVPADFPISATC-------HRVPVIDGHTEAVFVKFKEDVDPEEIREalESFKGlpqelglpsapKK 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124883267 268 FVDVLPAGSHPETRSVR------GANVCRIaahRPQGGDTV--VVLSviDNLVKGAAGQAVQNMNLMF 327
Cdd:PRK08664  282 PIILFEEPDRPQPRLDRdagdgmAVSVGRL---REDGIFDIkfVVLG--HNTVRGAAGASVLNAELLK 344
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 2-202 2.07e-12

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: 66.98  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLA--GHPSARVTVVTSRKEAGMKVadlfpSLRGR----IDLafstpDEARLRDCDVVFFAT 75
Cdd:COG0136     1 YNVAVVGATGAVGRVLLELLEerDFPVGELRLLASSRSAGKTV-----SFGGKeltvEDA-----TDFDFSGVDIALFSA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  76 PNGIAMNEARELLAAGVRVVDLAADYRirdvaewekwygMSHGSPdLVaeavygLPEINREAIRGAR---LVANPGCypT 152
Cdd:COG0136    71 GGSVSKEYAPKAAAAGAVVIDNSSAFR------------MDPDVP-LV------VPEVNPEALADHLpkgIIANPNC--S 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2124883267 153 AVQ----LGflPLIEAGAVE---LSSLIAdcksgVSGAGRKAeVGALLAEAGDSFKA 202
Cdd:COG0136   130 TIQmlvaLK--PLHDAAGIKrvvVSTYQA-----VSGAGAAA-MDELAEQTAALLNG 178
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 3-147 2.48e-11

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: 60.91  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   3 KVGIVGGTGYTGVELLRLLA--GHPSARVTVVTSRKEAGMKVadlfpSLRGRiDLAFSTPDEARLRDCDVVFFATPNGIA 80
Cdd:cd02316     2 NVAIVGATGAVGQEMLKVLEerNFPVSELRLLASARSAGKTL-----EFKGK-ELTVEELTEDSFKGVDIALFSAGGSVS 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRirdvaewekwygMSHGSPdLVaeavygLPEINREAIRG-ARLVANP 147
Cdd:cd02316    76 KEFAPIAAEAGAVVIDNSSAFR------------MDPDVP-LV------VPEVNPEALKNhKGIIANP 124
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 3-187 2.41e-10

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 60.94  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   3 KVGIVGGTGYTGVELLRLLA--GHPSARVTVVTSRKEAGMKVAdlfpsLRGRiDLAFSTPDEARLRDCDVVFFATPNGIA 80
Cdd:PLN02383    9 SVAIVGVTGAVGQEFLSVLTdrDFPYSSLKMLASARSAGKKVT-----FEGR-DYTVEELTEDSFDGVDIALFSAGGSIS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRirdvaewekwygMSHGSPdLVaeavygLPEINREAIRGAR-------LVANPGCYPTA 153
Cdd:PLN02383   83 KKFGPIAVDKGAVVVDNSSAFR------------MEEGVP-LV------IPEVNPEAMKHIKlgkgkgaLIANPNCSTII 143

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2124883267 154 VQLGFLPLIEagAVELSSLIADCKSGVSGAGRKA 187
Cdd:PLN02383  144 CLMAVTPLHR--HAKVKRMVVSTYQAASGAGAAA 175
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 2-102 1.32e-09

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


Pssm-ID: 467518  Cd Length: 162  Bit Score: 56.35  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVT-SRKEAGMKVADLFpslRGRI---------DLAFSTPDEARLRDCDVV 71
Cdd:cd02315     1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGaSERSAGKKYGDAV---RWKQdtpipeevaDMVVKECEPEEFKDCDIV 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124883267  72 FFATPNGIAMNEARELLAAGVRVVDLAADYR 102
Cdd:cd02315    78 FSALDSDVAGEIEPAFAKAGIPVFSNASNHR 108
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 149-311 1.67e-09

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: 55.99  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 149 CYPTAVQLGFLPLIEAGAVElsSLIADCKSGVSGAGRKAEVGALLAEAGDSFKAYGVSGHRHLPEIRQGLGRaAAQTVGL 228
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIE--EILVVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGE-IGKPIKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 229 TFVPHLTPMIRGIHATLYARLKADVD---VQALFERRYEGEHFVDVLPAGSHPE-TRSVRGANVCRIAAHR--PQGGDTV 302
Cdd:cd18122    78 DGIAVRVPATLGHLVTVTVKLEKTATleqIAEAVAEAVEEVQISAEDGLTYAKVsTRSVGGVYGVPVGRQRefAFDDNKL 157


                  ....*....
gi 2124883267 303 VVLSVIDNL 311
Cdd:cd18122   158 KVFSAVDNE 166
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 2-147 1.44e-08

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


Pssm-ID: 467523 [Multi-domain]  Cd Length: 142  Bit Score: 52.72  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSA--RVTVVTSRKEAGMKvADLFPSlrgriDLAFSTPDEARLRDCDVVFFATPNGI 79
Cdd:cd24147     1 LRVGVVGATGAVGSEILQLLAEEPDPlfELRALASEESAGKK-AEFAGE-----AIMVQEADPIDFLGLDIVFLCAGAGV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124883267  80 AMNEARELLAAGVRVVDLAADYRIRDVAEwekwygmshgspdLVaeavygLPEINREAI---RGARLVANP 147
Cdd:cd24147    75 SAKFAPEAARAGVLVIDNAGALRMDPDVP-------------LV------VPEVNAEAIglgEGTPLLVIP 126
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 2-95 1.34e-07

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


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 49.87  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFPSLRGRIDLAFSTPDEARLRDCDVVF-FATPNGiA 80
Cdd:cd02274     1 IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGGLAGIGTGVIVSLDLELAAADADVVIdFTTPEA-T 79

                          90
                  ....*....|....*
gi 2124883267  81 MNEARELLAAGVRVV 95
Cdd:cd02274    80 LENLEAAAKAGVPLV 94
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 4-187 3.08e-07

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 51.59  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   4 VGIVGGTGYTGVELLRLLAGHPS---ARVTVVTSRKEAGMKVadlfpSLRGRiDLAFSTPDEARLRDCDVVFFATPNGIA 80
Cdd:PRK06728    8 VAVVGATGAVGQKIIELLEKETKfniAEVTLLSSKRSAGKTV-----QFKGR-EIIIQEAKINSFEGVDIAFFSAGGEVS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  81 MNEARELLAAGVRVVDLAADYRirdvaewekwygMSHGSPDLVaeavyglPEINREAIRG-ARLVANPGCYPTAVQLGFL 159
Cdd:PRK06728   82 RQFVNQAVSSGAIVIDNTSEYR------------MAHDVPLVV-------PEVNAHTLKEhKGIIAVPNCSALQMVTALQ 142

                         170       180
                  ....*....|....*....|....*...
gi 2124883267 160 PLIEAGAVElsSLIADCKSGVSGAGRKA 187
Cdd:PRK06728  143 PIRKVFGLE--RIIVSTYQAVSGSGIHA 168
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 49-148 1.78e-06

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: 46.83  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  49 LRGRIDLAFSTPDEARLRD----------CDVVFFATPNGIAMNEARELLAAGVRVVDLAADYRIRDvaEWekwygmshg 118
Cdd:cd17896    20 LAGRSDIELLSIPEDKRKDpaaraellnaADIAILCLPDDAAREAVALVTNPRTRIIDASTAHRTAP--GW--------- 88

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2124883267 119 spdlvaeaVYGLPEIN---REAIRGARLVANPG 148
Cdd:cd17896    89 --------AYGFPELSpeqREKIATSKRVANPG 113
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 2-102 9.31e-06

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


Pssm-ID: 467526  Cd Length: 163  Bit Score: 45.40  E-value: 9.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLFP-SLRGRI-----DLAFSTPDEARLRDCDVVFFAT 75
Cdd:cd24150     2 LKAAILGATGLVGIEYVRMLSNHPYIKPAYLAGKGSVGKPYGEVVRwQTVGQVpkeiaDMEIKPTDPKLMDDVDIIFSPL 81

                          90       100
                  ....*....|....*....|....*..
gi 2124883267  76 PNGIAMNEARELLAAGVRVVDLAADYR 102
Cdd:cd24150    82 PQGAAGPVEEQFAKEGFPVISNSPDHR 108
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 2-95 4.72e-05

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


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 42.22  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVTVVTSRKEAGMKVADLfpSLRGRIDLAFSTPDEARLRDCDVVF-FATPNGiA 80
Cdd:pfam01113   1 IKIAVAGASGRMGRELIKAVLEAPDLELVAAVDRPGSSLLGSDA--GELAPLGVPVTDDLEEVLADADVLIdFTTPEA-T 77

                          90
                  ....*....|....*
gi 2124883267  81 MNEARELLAAGVRVV 95
Cdd:pfam01113  78 LENLEFALKHGVPLV 92
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 2-147 6.31e-05

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


Pssm-ID: 467520 [Multi-domain]  Cd Length: 144  Bit Score: 42.61  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLA--GHPSARVTVVTSRKEAGMKVadlfpSLRGRiDLAFSTPDEARLRDCDVVFFATPNGI 79
Cdd:cd17894     1 YRIAVVGATGLVGKELLELLEerGFPVGRLRLLDSEESAGELV-----EFGGE-PLDVQDLDEFDFSDVDLVFFAGPAEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124883267  80 AMNEARELLAAGVRVVDLAADYRirdvaewekwygmshgSPDLVAEAVYGLPEINREAIRGARLVANP 147
Cdd:cd17894    75 ARAYAPRARAAGCLVIDLSGALR----------------SDPDVPLVVPGVNPEALAAAAERRVVAVP 126
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 2-95 3.58e-04

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 39.88  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLAGHPSARVT-VVTSRKEAGMKVADLFpslrgRIDlAFSTPDE-ARLRDCDVVFFATPNGI 79
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVaILDPNSERAEAVAESF-----GVE-VYSDLEElLNDPEIDAVIVATPNGL 74

                          90
                  ....*....|....*.
gi 2124883267  80 AMNEARELLAAGVRVV 95
Cdd:pfam01408  75 HYDLAIAALEAGKHVL 90
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 310-328 8.91e-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: 38.74  E-value: 8.91e-04
                          10
                  ....*....|....*....
gi 2124883267 310 NLVKGAAGQAVQNMNLMFG 328
Cdd:cd17896   114 NLGKGASGAAVQNMNLMLG 132
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 3-100 1.54e-03

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 39.44  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   3 KVGIVGGTGYTGVELLRLL--AGHpsaRVTVVTSRKEagmKVADLFPslrGRIDLA---FSTPD--EARLRDCDVVFFAT 75
Cdd:COG0702     1 KILVTGATGFIGRRVVRALlaRGH---PVRALVRDPE---KAAALAA---AGVEVVqgdLDDPEslAAALAGVDAVFLLV 71

                          90       100
                  ....*....|....*....|....*
gi 2124883267  76 PNGIAMNEARElLAAGVRVVDLAAD 100
Cdd:COG0702    72 PSGPGGDFAVD-VEGARNLADAAKA 95
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-108 5.38e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 37.98  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   1 MIKVGIVGgTGYTGVELLRLLAGHPSARVTVVTSR-KEAGMKVADLFPslrgriDLAFSTPDEA-RLRDCDVVFFATPNG 78
Cdd:COG0673     3 KLRVGIIG-AGGIGRAHAPALAALPGVELVAVADRdPERAEAFAEEYG------VRVYTDYEELlADPDIDAVVIATPNH 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2124883267  79 I--AMneARELLAAGVRV-------VDLAADYRIRDVAE 108
Cdd:COG0673    76 LhaEL--AIAALEAGKHVlcekplaLTLEEARELVAAAE 112
PRK05671 PRK05671
aspartate-semialdehyde dehydrogenase; Reviewed
 2-321 5.54e-03

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 168165 [Multi-domain]  Cd Length: 336  Bit Score: 38.17  E-value: 5.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267   2 IKVGIVGGTGYTGVELLRLLA--GHPSARVTVVTSRKEAGMKVadlfpSLRGRidlafstpdEARLRDCD--------VV 71
Cdd:PRK05671    5 LDIAVVGATGTVGEALVQILEerDFPVGTLHLLASSESAGHSV-----PFAGK---------NLRVREVDsfdfsqvqLA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267  72 FFATPNGIAMNEARELLAAGVRVVDLaadyrirdvaewekwygmSHGSPDLVAEAVygLPEINREAIRG---ARLVANPG 148
Cdd:PRK05671   71 FFAAGAAVSRSFAEKARAAGCSVIDL------------------SGALPSAQAPNV--VPEVNAERLASlaaPFLVSSPS 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 149 CYPTAVQLGFLPLieAGAVELSSLIADCKSGVSGAGRKA--EVGA-----------------------LLAEAGdsfkAY 203
Cdd:PRK05671  131 ASAVALAVALAPL--KGLLDIQRVQVTACLAVSSLGREGvsELARqtaellnarpleprffdrqvafnLLAQVG----AP 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124883267 204 GVSGH-----RHLPEIRQGLGRAAAQtVGLTFVphLTPMIRGIHATLYARLKADVDVQALfERRYEGEHFVDVLPAGSHP 278
Cdd:PRK05671  205 DAQGHtalerRLVAELRQLLGLPELK-ISVTCI--QVPVFFGDSLSVALQSAAPVDLAAV-NAALEAAPGIELVEAGDYP 280

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2124883267 279 E-TRSVRGANVCRIAAHRpQGGDTVVVLS---VIDNLVKGAAGQAVQ 321
Cdd:PRK05671  281 TpVGDAVGQDVVYVGRVR-AGVDDPCQLNlwlTSDNVRKGAALNAVQ 326
 
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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