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Conserved domains on  [gi|1463310236|emb|SVK39164|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Acinetobacter baumannii]

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]; ...
 2-344 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: 590.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHYDdLQFSVPDAQRLGA-CDVVFFATPHGV 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTD-LVFEPPDPDELAAgCDVVFLALPHGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  81 AHALAGELLDAGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIAVPGCYPTATQLGLI 160
Cdd:COG0002    80 SMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 161 PLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVGLTFVPHLTPMIR 240
Cdd:COG0002   160 PLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 241 GIHATLYAHVADR--SVDLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVVLSVIDNLVKGAS 318
Cdd:COG0002   240 GILATIYARLKDGvtEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAA 319

                         330       340
                  ....*....|....*....|....*.
gi 1463310236 319 GQALQNMNILFGLDERLGLSHAALLP 344
Cdd:COG0002   320 GQAVQNMNLMFGLPETTGLELVPLYP 345
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-344 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: 590.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHYDdLQFSVPDAQRLGA-CDVVFFATPHGV 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTD-LVFEPPDPDELAAgCDVVFLALPHGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  81 AHALAGELLDAGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIAVPGCYPTATQLGLI 160
Cdd:COG0002    80 SMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 161 PLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVGLTFVPHLTPMIR 240
Cdd:COG0002   160 PLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 241 GIHATLYAHVADR--SVDLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVVLSVIDNLVKGAS 318
Cdd:COG0002   240 GILATIYARLKDGvtEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAA 319

                         330       340
                  ....*....|....*....|....*.
gi 1463310236 319 GQALQNMNILFGLDERLGLSHAALLP 344
Cdd:COG0002   320 GQAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-344 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: 529.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVI-TSRSEAGVKVADMYPNLRGHYDDLQFSVPDAQRLGACDVVFFATPHGV 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLvSSRESAGKPVSEVHPHLRGLVDLNLEPIDVEEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  81 AHALAGELLDAGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIAVPGCYPTATQLGLI 160
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 161 PLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVGLTFVPHLTPMIR 240
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 241 GIHATLYAHVAD--RSVDLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVVLSVIDNLVKGAS 318
Cdd:TIGR01850 241 GILATIYAKLKDglTEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|....*.
gi 1463310236 319 GQALQNMNILFGLDERLGLSHAALLP 344
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-344 8.24e-124

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 360.68  E-value: 8.24e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   1 MIKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHYDDLQFSVPDAQrLGACDVVFFATPHGV 80
Cdd:PLN02968   38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDLPNLVAVKDAD-FSDVDAVFCCLPHGT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  81 AHALAGELLDaGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIAVPGCYPTATQLGLI 160
Cdd:PLN02968  117 TQEIIKALPK-DLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLV 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 161 PLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVGLTFVPHLTPMIR 240
Cdd:PLN02968  196 PLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSR 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 241 GIHATLYAHVAD-RSV-DLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVVLSVIDNLVKGAS 318
Cdd:PLN02968  276 GMQSTVYVHYAPgVTAeDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKGAS 355

                         330       340
                  ....*....|....*....|....*.
gi 1463310236 319 GQALQNMNILFGLDERLGLSHAALLP 344
Cdd:PLN02968  356 GQAVQNLNLMMGLPETTGLLQQPLFP 381
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 149-317 9.63e-92

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: 271.27  E-value: 9.63e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 149 GCYPTATQLGLIPLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVG 228
Cdd:cd23934     1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 229 LTFVPHLTPMIRGIHATLYAHVAD--RSVDLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVV 306
Cdd:cd23934    81 VSFTPHLVPMTRGILATIYAKLKDgvTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                         170
                  ....*....|.
gi 1463310236 307 LSVIDNLVKGA 317
Cdd:cd23934   161 VSAIDNLVKGA 171
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 3-142 2.53e-45

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: 150.75  E-value: 2.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   3 KVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSE-AGVKVADMYPNLRGhYDDLQFSVPDAQRLGACDVVFFATPHGVA 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEG-GKDLVVEDVDPEDFKDVDIVFFALPGGVS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1463310236  82 HALAGELLDAGTRVIDLSADFRLAdaeewarwygqphgapallDEAVYGLPEVNREKIRQA 142
Cdd:pfam01118  80 KEIAPKLAEAGAKVIDLSSDFRMD-------------------DDVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 3-142 5.63e-40

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: 136.91  E-value: 5.63e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236    3 KVGIVGGTGYTGVELLRLLAQHPQARV-EVITSRSEAGVKVADMYPNLRGHYDDLqFSVPDAQRLgACDVVFFATPHGVA 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELtALAASSRSAGKKVSEAGPHLKGEVVLE-LDPPDFEEL-AVDIVFLALPHGVS 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1463310236   82 HALAGELL---DAGTRVIDLSADFRLAdaeewarwygqphgapallDEAVYGLPEVNREKIRQA 142
Cdd:smart00859  79 KESAPLLPraaAAGAVVIDLSSAFRMD-------------------DDVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-344 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: 590.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHYDdLQFSVPDAQRLGA-CDVVFFATPHGV 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTD-LVFEPPDPDELAAgCDVVFLALPHGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  81 AHALAGELLDAGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIAVPGCYPTATQLGLI 160
Cdd:COG0002    80 SMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 161 PLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVGLTFVPHLTPMIR 240
Cdd:COG0002   160 PLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 241 GIHATLYAHVADR--SVDLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVVLSVIDNLVKGAS 318
Cdd:COG0002   240 GILATIYARLKDGvtEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAA 319

                         330       340
                  ....*....|....*....|....*.
gi 1463310236 319 GQALQNMNILFGLDERLGLSHAALLP 344
Cdd:COG0002   320 GQAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-344 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: 529.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVI-TSRSEAGVKVADMYPNLRGHYDDLQFSVPDAQRLGACDVVFFATPHGV 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLvSSRESAGKPVSEVHPHLRGLVDLNLEPIDVEEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  81 AHALAGELLDAGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIAVPGCYPTATQLGLI 160
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 161 PLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVGLTFVPHLTPMIR 240
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 241 GIHATLYAHVAD--RSVDLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVVLSVIDNLVKGAS 318
Cdd:TIGR01850 241 GILATIYAKLKDglTEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|....*.
gi 1463310236 319 GQALQNMNILFGLDERLGLSHAALLP 344
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-344 8.24e-124

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 360.68  E-value: 8.24e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   1 MIKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHYDDLQFSVPDAQrLGACDVVFFATPHGV 80
Cdd:PLN02968   38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDLPNLVAVKDAD-FSDVDAVFCCLPHGT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  81 AHALAGELLDaGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIAVPGCYPTATQLGLI 160
Cdd:PLN02968  117 TQEIIKALPK-DLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLV 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 161 PLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVGLTFVPHLTPMIR 240
Cdd:PLN02968  196 PLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSR 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 241 GIHATLYAHVAD-RSV-DLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVVLSVIDNLVKGAS 318
Cdd:PLN02968  276 GMQSTVYVHYAPgVTAeDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKGAS 355

                         330       340
                  ....*....|....*....|....*.
gi 1463310236 319 GQALQNMNILFGLDERLGLSHAALLP 344
Cdd:PLN02968  356 GQAVQNLNLMMGLPETTGLLQQPLFP 381
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 149-317 9.63e-92

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: 271.27  E-value: 9.63e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 149 GCYPTATQLGLIPLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRASGGDVG 228
Cdd:cd23934     1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 229 LTFVPHLTPMIRGIHATLYAHVAD--RSVDLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVV 306
Cdd:cd23934    81 VSFTPHLVPMTRGILATIYAKLKDgvTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                         170
                  ....*....|.
gi 1463310236 307 LSVIDNLVKGA 317
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 ...
 2-148 6.31e-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: 243.87  E-value: 6.31e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHYDDLQFSVPDAQRLGACDVVFFATPHGVA 81
Cdd:cd17895     1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTDLTFEPDDDEEIAEDADVVFLALPHGVS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1463310236  82 HALAGELLDAGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIAVP 148
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 ...
 2-146 6.83e-60

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: 190.18  E-value: 6.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHyDDLQFSVPDAqrLGACDVVFFATPHGVA 81
Cdd:cd24151     1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNLRGR-TLLKFVPPEE--LESCDVLFLALPHGES 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1463310236  82 HALAGELLDAGTRVIDLSADFRLADAEEWARWYGQPHGAPALLDEAVYGLPEVNREKIRQARLIA 146
Cdd:cd24151    78 MKRIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLERFVYGLPELHREELRGARYIA 142
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 3-142 2.53e-45

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: 150.75  E-value: 2.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   3 KVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSE-AGVKVADMYPNLRGhYDDLQFSVPDAQRLGACDVVFFATPHGVA 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEG-GKDLVVEDVDPEDFKDVDIVFFALPGGVS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1463310236  82 HALAGELLDAGTRVIDLSADFRLAdaeewarwygqphgapallDEAVYGLPEVNREKIRQA 142
Cdd:pfam01118  80 KEIAPKLAEAGAKVIDLSSDFRMD-------------------DDVPYGLPEVNREAIKQA 121
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 150-317 5.78e-45

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: 151.50  E-value: 5.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 150 CYPTATQLGLIPLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLrrasGGDVGL 229
Cdd:cd18125     1 CYATAALLALYPLLKAGLLKPTPITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNL----GGKHNV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 230 TFVPHLTPMIRGIHATLYAHVADRSV--DLQALFEKRYADEPFVDVMPAGSHPETRSVRGANVCRIAVHRPQGGDLVVVL 307
Cdd:cd18125    77 HFTPHVGPWVRGILMTIQCFTQKGWSlrQLHEAYREAYAGEPFVRVMPQGKGPDPKFVQGTNYADIGVELEEDTGRLVVM 156

                         170
                  ....*....|
gi 1463310236 308 SVIDNLVKGA 317
Cdd:cd18125   157 SAIDNLVKGA 166
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 3-142 5.63e-40

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: 136.91  E-value: 5.63e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236    3 KVGIVGGTGYTGVELLRLLAQHPQARV-EVITSRSEAGVKVADMYPNLRGHYDDLqFSVPDAQRLgACDVVFFATPHGVA 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELtALAASSRSAGKKVSEAGPHLKGEVVLE-LDPPDFEEL-AVDIVFLALPHGVS 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1463310236   82 HALAGELL---DAGTRVIDLSADFRLAdaeewarwygqphgapallDEAVYGLPEVNREKIRQA 142
Cdd:smart00859  79 KESAPLLPraaAAGAVVIDLSSAFRMD-------------------DDVPYGLPEVNPEAIKKA 123
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 149-317 7.83e-40

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: 138.53  E-value: 7.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 149 GCYPTATQLGLIPLLEAGLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRaSGGDVG 228
Cdd:cd23939     1 GCNATASILALYPLVKAGLLDDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGL-LAREIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 229 LTFVPHLTPMIRGIHATLYAHVADR--SVDLQALFEKRYADEPFVDVMPA--GSH--PETRSVRGANVCRIAVHRPQGGD 302
Cdd:cd23939    80 VSFTAHSVDMVRGILATAHVFLKEGvtEKDLWKAYRKAYGNEPFVRIVKDrkGIYryPDPKLVIGSNFCDIGFELDEDNG 159

                         170
                  ....*....|....*
gi 1463310236 303 LVVVLSVIDNLVKGA 317
Cdd:cd23939   160 RLVVFSAIDNLMKGA 174
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 2-148 1.06e-38

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: 135.11  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLrGHYDDLQFSVPDAQRLGACDVVFFATPHGVA 81
Cdd:cd24148     1 IRVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHL-PPLADRVLEPTTPAVLAGHDVVFLALPHGAS 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1463310236  82 HALAGElLDAGTRVIDLSADFRLADAEEWARWYGQPH--GAPalldeavYGLPEV--NREKIRQARLIAVP 148
Cdd:cd24148    80 AAIAAQ-LPPDVLVVDCGADHRLEDAAAWEKFYGGEHagGWT-------YGLPELpgAREALAGARRIAVP 142
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 2-148 1.13e-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: 124.60  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHYDDLQFSVPDAqrLGACDVVFFATPHGVA 81
Cdd:cd02280     1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIISLQIQEFRPCEV--LNSADILVLALPHGAS 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1463310236  82 HALAGELLDAGTRVIDLSADFRLADAEEWARWYGqphgaPALLDEAVYGLPEVNRE-KIRQARLIAVP 148
Cdd:cd02280    79 AELVAAISNPQVKIIDLSADFRFTDPEVYRRHPR-----PDLEGGWVYGLPELDREqRIANATRIANP 141
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 2-149 2.48e-32

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: 117.98  E-value: 2.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRGHYDDLQFSVPDAQRLGACDVVFFATPHGVA 81
Cdd:cd24149     1 KRVGLIGARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVSGYTKSPIDYLNLSVEDIPEEVAAREVDAWVLALPNGVA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  82 HALAGEL--LDAGTRVIDLSADFRLADaeEWarwygqphgapalldeaVYGLPEVNREKIRQARLIAVPG 149
Cdd:cd24149    81 KPFVDAIdkANPKSVIVDLSADYRFDD--AW-----------------TYGLPELNRRRIAGAKRISNPG 131
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 2-148 4.47e-24

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: 95.89  E-value: 4.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHP-QARVEVITSRSEAGVKVADMYPNLRGHyDDLQFsvPDAQRLGACDVVFFATPHGV 80
Cdd:cd02281     1 KKVGVVGATGYVGGEFLRLLLEHPfPLFEIVLLAASSAGAKKKYFHPKLWGR-VLVEF--TPEEVLEQVDIVFTALPGGV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1463310236  81 AHALAGELLDAGTRVIDLSADFRLAdaeewarwygqphgapallDEAVYGLPEVNREKI---RQARLIAVP 148
Cdd:cd02281    78 SAKLAPELSEAGVLVIDNASDFRLD-------------------KDVPLVVPEVNREHIgelKGTKIIANP 129
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 159-315 1.06e-21

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


Pssm-ID: 397067 [Multi-domain]  Cd Length: 167  Bit Score: 90.07  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 159 LIPLLEAgLADASRLIADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKG-HRHLPEISQGLRRASGGDVGLTFVP---- 233
Cdd:pfam02774   1 LKPLRDA-LGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGEeHNGTPETREELKMVNETKKILGFTPkvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 234 --HLTPMIRGIHATLYAHVADRSVDLQALFEKRY-ADEPFVDVMPAGSHPETRSVRGA-NVCRIAVHR--PQGGDLVVVL 307
Cdd:pfam02774  80 tcVRVPVFRGHSETVTVKLKLKPIDVEEVYEAFYaAPGVFVVVRPEEDYPTPRAVRGGtNFVYVGRVRkdPDGDRGLKLV 159


                  ....*...
gi 1463310236 308 SVIDNLVK 315
Cdd:pfam02774 160 SVIDNLRK 167
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 149-317 6.39e-20

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: 85.38  E-value: 6.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 149 GCYPTATQLGLIPLLE--AGLADASRLiadckSGVSGAGR--GAK--VGSLfceaGESMMAYAVKGHRHLPEISQGLRRA 222
Cdd:cd23936     1 GCYATGAQLALAPLLDdlDGPPSVFGV-----SGYSGAGTkpSPKndPEVL----ADNLIPYSLVGHIHEREVSRHLGTP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 223 sggdvgLTFVPHLTPMIRGIHATLYAHVAD--RSVDLQALFEKRYADEPFVDVMpaGSHPETRSV---RGANVCRIAVHr 297
Cdd:cd23936    72 ------VAFMPHVAPWFQGITLTISIPLKKsmTADEIRELYQEAYAGEPLIKVT--KEIPLVRDNagkHGVVVGGFTVH- 142

                         170       180
                  ....*....|....*....|
gi 1463310236 298 pQGGDLVVVLSVIDNLVKGA 317
Cdd:cd23936   143 -PDGKRVVVVATIDNLLKGA 161
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 149-317 1.06e-19

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: 84.96  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 149 GCYPTATQLGLIPLLEAGLADAS-RLIADCKSGVSGAGRGAkVGSLFCEAGESMMAYAVKG----HRHLPEIsqglRRAS 223
Cdd:cd23935     1 GCYATGAILLLRPLVEAGLLPADyPLSIHAVSGYSGGGKKM-IEQYEAAEAADLPPPRPYGlgleHKHLPEM----QKHA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 224 GGDVGLTFVPHLTPMIRGIHATLYAHVAD-----RSVDLQALFEKRYADEPFVDVMPAGSHPETRSVR-----GANVCRI 293
Cdd:cd23935    76 GLARPPIFTPAVGNFYQGMLVTVPLHLDLlekgvSAAEVHEALAEHYAGERFVKVMPLDEPDALGFLDpqalnGTNNLEL 155

                         170       180
                  ....*....|....*....|....
gi 1463310236 294 AVHRPQGGDLVVVlSVIDNLVKGA 317
Cdd:cd23935   156 FVFGNDKGQALLV-ARLDNLGKGA 178
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 2-188 6.41e-11

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: 62.74  E-value: 6.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQH--PQARVEVITSRSEAG---------VKVADMYPnlrghyDDLQfsvpdaqrlgACD 70
Cdd:COG0136     1 YNVAVVGATGAVGRVLLELLEERdfPVGELRLLASSRSAGktvsfggkeLTVEDATD------FDFS----------GVD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  71 VVFFATPHGVAHALAGELLDAGTRVIDLSADFRLADaeewarwygqphGAPaLLdeavygLPEVNREKIRQAR---LIAV 147
Cdd:COG0136    65 IALFSAGGSVSKEYAPKAAAAGAVVIDNSSAFRMDP------------DVP-LV------VPEVNPEALADHLpkgIIAN 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1463310236 148 PGCypTATQL--GLIPLLEAGLadASRLIAdckS---GVSGAGRGA 188
Cdd:COG0136   126 PNC--STIQMlvALKPLHDAAG--IKRVVV---StyqAVSGAGAAA 164
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 3-188 6.73e-10

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 59.78  E-value: 6.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   3 KVGIVGGTGYTGVELLRLLAQH--PQARVEVITSRSEAGVKVAdmypnlrghYDDLQFSVPD--AQRLGACDVVFFATPH 78
Cdd:PLN02383    9 SVAIVGVTGAVGQEFLSVLTDRdfPYSSLKMLASARSAGKKVT---------FEGRDYTVEEltEDSFDGVDIALFSAGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  79 GVAHALAGELLDAGTRVIDLSADFRLADaeewarwygqphGAPALldeavygLPEVNREKIRQAR-------LIAVPGCY 151
Cdd:PLN02383   80 SISKKFGPIAVDKGAVVVDNSSAFRMEE------------GVPLV-------IPEVNPEAMKHIKlgkgkgaLIANPNCS 140

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1463310236 152 PTATQLGLIPLLEagLADASRLIADCKSGVSGAGRGA 188
Cdd:PLN02383  141 TIICLMAVTPLHR--HAKVKRMVVSTYQAASGAGAAA 175
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 3-149 3.32e-09

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: 54.53  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   3 KVGIVGGTGYTGVELLRLLAQHPQarVEVITSRSEagvKVADmyPNLRghyddlqfsvpdAQRLGACDVVFFATPHGVAH 82
Cdd:cd17896     2 KVFIDGEAGTTGLQIRERLAGRSD--IELLSIPED---KRKD--PAAR------------AELLNAADIAILCLPDDAAR 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  83 ALAGELLDAGTRVIDLSADFRLADAeeWArwygqphgapalldeavYGLPEVN---REKIRQARLIAVPG 149
Cdd:cd17896    63 EAVALVTNPRTRIIDASTAHRTAPG--WA-----------------YGFPELSpeqREKIATSKRVANPG 113
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-185 5.08e-09

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 56.76  E-value: 5.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   1 MIKVGIVGGTGYTGVELLRLLAQHPQARVEVIT-SRSEAGVKVAD-----MYPNLRGHYDDLQFSVPDAQRLGACDVVFF 74
Cdd:PRK08664    3 KLKVGILGATGMVGQRFVQLLANHPWFEVTALAaSERSAGKTYGEavrwqLDGPIPEEVADMEVVSTDPEAVDDVDIVFS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  75 ATPHGVAHALAGELLDAGTRVIDLSADFRladaeewarwygqphgapalLDEAVYGL-PEVNREKI------RQAR---- 143
Cdd:PRK08664   83 ALPSDVAGEVEEEFAKAGKPVFSNASAHR--------------------MDPDVPLViPEVNPEHLelievqRKRRgwdg 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1463310236 144 -LIAVPGCYPTATQLGLIPLLEAGLadaSRLIADCKSGVSGAG 185
Cdd:PRK08664  143 fIVTNPNCSTIGLVLALKPLMDFGI---ERVHVTTMQAISGAG 182
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 3-148 6.47e-09

N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase 2 (ASADH2) and similar proteins; The family corresponds to a new branch of bacterial ASADH enzymes that has a similar overall fold and domain organization but sharing less sequence homology with the other bacterial ASADHs. The second isoform of ASADH in Vibrio cholerae is one of the prototypes of this family. It also includes ASADHs from Streptococcus pneumoniae, Mycobacterium tuberculosis, Thermus thermophilus, as well as from eukaryotes. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain.


Pssm-ID: 467519 [Multi-domain]  Cd Length: 142  Bit Score: 53.98  E-value: 6.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   3 KVGIVGGTGYTGVELLRLLAQ--HPQARVEVITSRSEAGVKVAdmypnlrghYDDLQFSVPDAQRLGA--CDVVFFATPH 78
Cdd:cd02316     2 NVAIVGATGAVGQEMLKVLEErnFPVSELRLLASARSAGKTLE---------FKGKELTVEELTEDSFkgVDIALFSAGG 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1463310236  79 GVAHALAGELLDAGTRVIDLSADFRladaeewarwygqphgapalLDEAVYG-LPEVNREKIRQ-ARLIAVP 148
Cdd:cd02316    73 SVSKEFAPIAAEAGAVVIDNSSAFR--------------------MDPDVPLvVPEVNPEALKNhKGIIANP 124
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 2-103 8.46e-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: 54.03  E-value: 8.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVIT--SRSeAGVKVAD---------MYPNLRghydDLQFSVPDAQRLGACD 70
Cdd:cd02315     1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGasERS-AGKKYGDavrwkqdtpIPEEVA----DMVVKECEPEEFKDCD 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1463310236  71 VVFFATPHGVAHALAGELLDAGTRVIDLSADFR 103
Cdd:cd02315    76 IVFSALDSDVAGEIEPAFAKAGIPVFSNASNHR 108
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 4-185 2.46e-08

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 54.67  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   4 VGIVGGTGYTGVELLRLLAQHPQARVEVIT---SRSEAGVKVadmypNLRGHydDLQFSVPDAQRLGACDVVFFATPHGV 80
Cdd:PRK06728    8 VAVVGATGAVGQKIIELLEKETKFNIAEVTllsSKRSAGKTV-----QFKGR--EIIIQEAKINSFEGVDIAFFSAGGEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  81 AHALAGELLDAGTRVIDLSADFRLAdaeewarwygqpHGAPALldeavygLPEVNREKIRQ-ARLIAVPGCYPTATQLGL 159
Cdd:PRK06728   81 SRQFVNQAVSSGAIVIDNTSEYRMA------------HDVPLV-------VPEVNAHTLKEhKGIIAVPNCSALQMVTAL 141

                         170       180
                  ....*....|....*....|....*..
gi 1463310236 160 IPLLEA-GLadaSRLIADCKSGVSGAG 185
Cdd:PRK06728  142 QPIRKVfGL---ERIIVSTYQAVSGSG 165
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 150-313 7.76e-08

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


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 51.37  E-value: 7.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 150 CYPTATQLGLIPLLE-AGLADASrliADCKSGVSGAGRGAKVGSLFCEAGESMMAYAVKGHRHLPEISQGLRRaSGGDVG 228
Cdd:cd18122     1 CTTTGLIPAAKALNDkFGIEEIL---VVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGE-IGKPIK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236 229 LTFVPHLTPMIRGIHATLYAHVADRSV--DLQALFEKRYADEPFVDVMPAGSHPE-TRSVRGANVCRIA--VHRPQGGDL 303
Cdd:cd18122    77 VDGIAVRVPATLGHLVTVTVKLEKTATleQIAEAVAEAVEEVQISAEDGLTYAKVsTRSVGGVYGVPVGrqREFAFDDNK 156

                         170
                  ....*....|
gi 1463310236 304 VVVLSVIDNL 313
Cdd:cd18122   157 LKVFSAVDNE 166
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 2-104 1.40e-06

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: 47.33  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQA--RVEVITSRSEAGVKVADmypnlRGhyDDLQFSVPDAQRLGACDVVFFATPHG 79
Cdd:cd24147     1 LRVGVVGATGAVGSEILQLLAEEPDPlfELRALASEESAGKKAEF-----AG--EAIMVQEADPIDFLGLDIVFLCAGAG 73

                          90       100
                  ....*....|....*....|....*
gi 1463310236  80 VAHALAGELLDAGTRVIDLSADFRL 104
Cdd:cd24147    74 VSAKFAPEAARAGVLVIDNAGALRM 98
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 2-148 1.44e-06

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: 47.23  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQH--PQARVEVITSRSEAGVKVadmypnlrgHYDDLQFSVPDAQR--LGACDVVFFATP 77
Cdd:cd17894     1 YRIAVVGATGLVGKELLELLEERgfPVGRLRLLDSEESAGELV---------EFGGEPLDVQDLDEfdFSDVDLVFFAGP 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1463310236  78 HGVAHALAGELLDAGTRVIDLSADFRLADaeewarwygqphGAPALldeavygLPEVNREKI---RQARLIAVP 148
Cdd:cd17894    72 AEVARAYAPRARAAGCLVIDLSGALRSDP------------DVPLV-------VPGVNPEALaaaAERRVVAVP 126
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 2-104 2.50e-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: 46.94  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYP-----NLRGHYDDLQFSVPDAQRLGACDVVFFAT 76
Cdd:cd24150     2 LKAAILGATGLVGIEYVRMLSNHPYIKPAYLAGKGSVGKPYGEVVRwqtvgQVPKEIADMEIKPTDPKLMDDVDIIFSPL 81

                          90       100
                  ....*....|....*....|....*...
gi 1463310236  77 PHGVAHALAGELLDAGTRVIDLSADFRL 104
Cdd:cd24150    82 PQGAAGPVEEQFAKEGFPVISNSPDHRF 109
PRK05671 PRK05671
aspartate-semialdehyde dehydrogenase; Reviewed
 2-188 2.12e-05

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 168165 [Multi-domain]  Cd Length: 336  Bit Score: 45.87  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQH--PQARVEVITSRSEAGVKVADMYPNLR-GHYDDLQFSvpdaqrlgACDVVFFATPH 78
Cdd:PRK05671    5 LDIAVVGATGTVGEALVQILEERdfPVGTLHLLASSESAGHSVPFAGKNLRvREVDSFDFS--------QVQLAFFAAGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236  79 GVAHALAGELLDAGTRVIDLSADFRLADaeewarwygqphgAPALldeavygLPEVNRE---KIRQARLIAVPGCYPTAT 155
Cdd:PRK05671   77 AVSRSFAEKARAAGCSVIDLSGALPSAQ-------------APNV-------VPEVNAErlaSLAAPFLVSSPSASAVAL 136

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1463310236 156 QLGLIPLLeaGLADASRLIADCKSGVSGAGRGA 188
Cdd:PRK05671  137 AVALAPLK--GLLDIQRVQVTACLAVSSLGREG 167
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-92 1.96e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 42.60  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   1 MIKVGIVGgTGYTGVELLRLLAQHPQARVEVITSRSEAGVK-VADMYpNLRgHYDDLQfsvpDAQRLGACDVVFFATPHG 79
Cdd:COG0673     3 KLRVGIIG-AGGIGRAHAPALAALPGVELVAVADRDPERAEaFAEEY-GVR-VYTDYE----ELLADPDIDAVVIATPNH 75

                          90
                  ....*....|...
gi 1463310236  80 VAHALAGELLDAG 92
Cdd:COG0673    76 LHAELAIAALEAG 88
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 312-330 8.14e-03

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


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 36.04  E-value: 8.14e-03
                          10
                  ....*....|....*....
gi 1463310236 312 NLVKGASGQALQNMNILFG 330
Cdd:cd17896   114 NLGKGASGAAVQNMNLMLG 132
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 2-96 9.06e-03

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: 35.65  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463310236   2 IKVGIVGGTGYTGVELLRLLAQHPQARVEVITSRSEAGVKVADMYPNLRgHYDDLQfsvpDAQRLGACDVVFFATPHGVA 81
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEAVAESFGVE-VYSDLE----ELLNDPEIDAVIVATPNGLH 75

                          90
                  ....*....|....*
gi 1463310236  82 HALAGELLDAGTRVI 96
Cdd:pfam01408  76 YDLAIAALEAGKHVL 90
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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