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Conserved domains on  [gi|446521137|ref|WP_000598483|]
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MULTISPECIES: N-acetyl-gamma-glutamyl-phosphate reductase [Staphylococcus]

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]; ...
 2-343 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: 519.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHLQHIM-QHFEALTVD--NNDCDVIFFATPAPVS 78
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTdLVFEPPDPDelAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  79 KTCIPPLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLISNPGCFPTATLLALHP 158
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 159 LISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVSVIFTPHLVPMTRG 238
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 239 ILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAILVSVIDNLVKGASG 318
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|....*
gi 446521137 319 QAIQNLNILYDFEVTTGLNQSPVYP 343
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVPLYP 345
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-343 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: 519.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHLQHIM-QHFEALTVD--NNDCDVIFFATPAPVS 78
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTdLVFEPPDPDelAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  79 KTCIPPLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLISNPGCFPTATLLALHP 158
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 159 LISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVSVIFTPHLVPMTRG 238
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 239 ILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAILVSVIDNLVKGASG 318
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|....*
gi 446521137 319 QAIQNLNILYDFEVTTGLNQSPVYP 343
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-343 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: 515.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137    2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSK-VDEPLKLTFPHLQHIMQH-FEALTVDNN--DCDVIFFATPAPV 77
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSREsAGKPVSEVHPHLRGLVDLnLEPIDVEEIleDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   78 SKTCIPPLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLISNPGCFPTATLLALH 157
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  158 PLISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVSVIFTPHLVPMTR 237
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  238 GILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAILVSVIDNLVKGAS 317
Cdd:TIGR01850 241 GILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|....*.
gi 446521137  318 GQAIQNLNILYDFEVTTGLNQSPVYP 343
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-343 4.65e-109

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 323.32  E-value: 4.65e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   1 MIKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHL--QHIMQHFEALTVDNNDCDVIFFATPAPVS 78
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLitQDLPNLVAVKDADFSDVDAVFCCLPHGTT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  79 KTCIPpLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLISNPGCFPTATLLALHP 158
Cdd:PLN02968 118 QEIIK-ALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLVP 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 159 LISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVSVIFTPHLVPMTRG 238
Cdd:PLN02968 197 LVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSRG 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 239 ILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAILVSVIDNLVKGASG 318
Cdd:PLN02968 277 MQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKGASG 356

                        330       340
                 ....*....|....*....|....*
gi 446521137 319 QAIQNLNILYDFEVTTGLNQSPVYP 343
Cdd:PLN02968 357 QAVQNLNLMMGLPETTGLLQQPLFP 381
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 146-316 7.74e-102

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: 296.70  E-value: 7.74e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 146 GCFPTATLLALHPLISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVS 225
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 226 VIFTPHLVPMTRGILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAIL 305
Cdd:cd23934   81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                        170
                 ....*....|.
gi 446521137 306 VSVIDNLVKGA 316
Cdd:cd23934  161 VSAIDNLVKGA 171
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 156-314 9.09e-33

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: 119.73  E-value: 9.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  156 LHPLIsEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGN-HKHKPEIEQYLSIIAGQDVSVIFTP---- 230
Cdd:pfam02774   1 LKPLR-DALGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGEeHNGTPETREELKMVNETKKILGFTPkvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  231 --HLVPMTRGILSTIYVKLSSeyTTESLHKLMTSYY-ANQPFVRIRDIGTFPTTKEVLG-SNYCDIG-IYVDETTQTAI- 304
Cdd:pfam02774  80 tcVRVPVFRGHSETVTVKLKL--KPIDVEEVYEAFYaAPGVFVVVRPEEDYPTPRAVRGgTNFVYVGrVRKDPDGDRGLk 157

                         170
                  ....*....|
gi 446521137  305 LVSVIDNLVK 314
Cdd:pfam02774 158 LVSVIDNLRK 167
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 3-107 1.04e-26

Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 102.24  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137     3 KVGIVGGSGYGAIELIRLLQTHPHVTIAHIY-SHSKVDEPLKLTFPHLQHIMQH-FEALTVDNNDCDVIFFATPAPVSKT 80
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAaSSRSAGKKVSEAGPHLKGEVVLeLDPPDFEELAVDIVFLALPHGVSKE 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 446521137    81 CIPPL---VEKGIHVIDLSGAFRIKNREIY 107
Cdd:smart00859  81 SAPLLpraAAAGAVVIDLSSAFRMDDDVPY 110
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 2-343 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: 519.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHLQHIM-QHFEALTVD--NNDCDVIFFATPAPVS 78
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTdLVFEPPDPDelAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  79 KTCIPPLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLISNPGCFPTATLLALHP 158
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 159 LISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVSVIFTPHLVPMTRG 238
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 239 ILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAILVSVIDNLVKGASG 318
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|....*
gi 446521137 319 QAIQNLNILYDFEVTTGLNQSPVYP 343
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 2-343 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: 515.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137    2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSK-VDEPLKLTFPHLQHIMQH-FEALTVDNN--DCDVIFFATPAPV 77
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSREsAGKPVSEVHPHLRGLVDLnLEPIDVEEIleDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   78 SKTCIPPLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLISNPGCFPTATLLALH 157
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  158 PLISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVSVIFTPHLVPMTR 237
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  238 GILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAILVSVIDNLVKGAS 317
Cdd:TIGR01850 241 GILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|....*.
gi 446521137  318 GQAIQNLNILYDFEVTTGLNQSPVYP 343
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPFPPLYP 346
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 1-343 4.65e-109

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 323.32  E-value: 4.65e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   1 MIKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHL--QHIMQHFEALTVDNNDCDVIFFATPAPVS 78
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLitQDLPNLVAVKDADFSDVDAVFCCLPHGTT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  79 KTCIPpLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLISNPGCFPTATLLALHP 158
Cdd:PLN02968 118 QEIIK-ALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPLVP 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 159 LISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVSVIFTPHLVPMTRG 238
Cdd:PLN02968 197 LVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPMSRG 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 239 ILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAILVSVIDNLVKGASG 318
Cdd:PLN02968 277 MQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKGASG 356

                        330       340
                 ....*....|....*....|....*
gi 446521137 319 QAIQNLNILYDFEVTTGLNQSPVYP 343
Cdd:PLN02968 357 QAVQNLNLMMGLPETTGLLQQPLFP 381
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 146-316 7.74e-102

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: 296.70  E-value: 7.74e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 146 GCFPTATLLALHPLISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAGQDVS 225
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 226 VIFTPHLVPMTRGILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAIL 305
Cdd:cd23934   81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                        170
                 ....*....|.
gi 446521137 306 VSVIDNLVKGA 316
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 ...
 2-145 5.51e-58

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: 184.94  E-value: 5.51e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHLQHIMQHF---EALTVDNNDCDVIFFATPAPVS 78
Cdd:cd17895    1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTDLTfepDDDEEIAEDADVVFLALPHGVS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446521137  79 KTCIPPLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLISNP 145
Cdd:cd17895   81 MELAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFEHAAPELLKEAVYGLPELNREEIKKARLVANP 147
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 147-316 2.57e-56

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: 180.78  E-value: 2.57e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 147 CFPTATLLALHPLISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLsiiaGQDVSV 226
Cdd:cd18125    1 CYATAALLALYPLLKAGLLKPTPITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNL----GGKHNV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 227 IFTPHLVPMTRGILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIRDIGTFPTTKEVLGSNYCDIGIYVDETTQTAILV 306
Cdd:cd18125   77 HFTPHVGPWVRGILMTIQCFTQKGWSLRQLHEAYREAYAGEPFVRVMPQGKGPDPKFVQGTNYADIGVELEEDTGRLVVM 156

                        170
                 ....*....|
gi 446521137 307 SVIDNLVKGA 316
Cdd:cd18125  157 SAIDNLVKGA 166
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 146-316 1.69e-54

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: 176.28  E-value: 1.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 146 GCFPTATLLALHPLISEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIAgQDVS 225
Cdd:cd23939    1 GCNATASILALYPLVKAGLLDDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGLLA-REIS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 226 VIFTPHLVPMTRGILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIR----DIGTFPTTKEVLGSNYCDIGIYVDETTQ 301
Cdd:cd23939   80 VSFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYRKAYGNEPFVRIVkdrkGIYRYPDPKLVIGSNFCDIGFELDEDNG 159

                        170
                 ....*....|....*
gi 446521137 302 TAILVSVIDNLVKGA 316
Cdd:cd23939  160 RLVVFSAIDNLMKGA 174
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 156-314 9.09e-33

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: 119.73  E-value: 9.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  156 LHPLIsEKIVDLSSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGN-HKHKPEIEQYLSIIAGQDVSVIFTP---- 230
Cdd:pfam02774   1 LKPLR-DALGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGEeHNGTPETREELKMVNETKKILGFTPkvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  231 --HLVPMTRGILSTIYVKLSSeyTTESLHKLMTSYY-ANQPFVRIRDIGTFPTTKEVLG-SNYCDIG-IYVDETTQTAI- 304
Cdd:pfam02774  80 tcVRVPVFRGHSETVTVKLKL--KPIDVEEVYEAFYaAPGVFVVVRPEEDYPTPRAVRGgTNFVYVGrVRKDPDGDRGLk 157

                         170
                  ....*....|
gi 446521137  305 LVSVIDNLVK 314
Cdd:pfam02774 158 LVSVIDNLRK 167
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 3-107 7.66e-31

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: 113.00  E-value: 7.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137    3 KVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDePLKLTFPHlqHIMQHFEALTVDNND------CDVIFFATPAP 76
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSA-GKKLAFVH--PILEGGKDLVVEDVDpedfkdVDIVFFALPGG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 446521137   77 VSKTCIPPLVEKGIHVIDLSGAFRIKNREIY 107
Cdd:pfam01118  78 VSKEIAPKLAEAGAKVIDLSSDFRMDDDVPY 108
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 146-316 8.33e-29

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: 109.61  E-value: 8.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 146 GCFPTATLLALHPLISEKIVDLSS-IIIDAKTGVSGAGRSLSQRVHFSEMNENLS--AYAIG-NHKHKPEIEQYlsiiAG 221
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPADYpLSIHAVSGYSGGGKKMIEQYEAAEAADLPPprPYGLGlEHKHLPEMQKH----AG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 222 QDVSVIFTPHLVPMTRGILSTI---YVKLSSEYTTESLHKLMTSYYANQPFVRIR-----DIGTFPTTKEVLGSNYCDIG 293
Cdd:cd23935   77 LARPPIFTPAVGNFYQGMLVTVplhLDLLEKGVSAAEVHEALAEHYAGERFVKVMpldepDALGFLDPQALNGTNNLELF 156

                        170       180
                 ....*....|....*....|...
gi 446521137 294 IYVDETTQtAILVSVIDNLVKGA 316
Cdd:cd23935  157 VFGNDKGQ-ALLVARLDNLGKGA 178
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 3-107 1.04e-26

Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 102.24  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137     3 KVGIVGGSGYGAIELIRLLQTHPHVTIAHIY-SHSKVDEPLKLTFPHLQHIMQH-FEALTVDNNDCDVIFFATPAPVSKT 80
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAaSSRSAGKKVSEAGPHLKGEVVLeLDPPDFEELAVDIVFLALPHGVSKE 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 446521137    81 CIPPL---VEKGIHVIDLSGAFRIKNREIY 107
Cdd:smart00859  81 SAPLLpraAAAGAVVIDLSSAFRMDDDVPY 110
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 2-143 1.12e-23

N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; LysY (EC 1.2.1.103/EC 1.2.1.106) is involved in both the arginine and lysine biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LysY is the third enzyme in lysine biosynthesis from AAA. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor. Members in this subfamily belong to the type 1 AGPR family. They contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467527 [Multi-domain]  Cd Length: 170  Bit Score: 95.80  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHLQHIMQHFEALTVDNNDCDVIFFATPAPVSKTC 81
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNLRGRTLLKFVPPEELESCDVLFLALPHGESMKR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446521137  82 IPPLVEKGIHVIDLSGAFRIKNREIYEAYYKETAAAQDDLNHAIYSISEWQSFDNNGTKLIS 143
Cdd:cd24151   81 IDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLERFVYGLPELHREELRGARYIA 142
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 146-316 2.07e-21

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: 89.23  E-value: 2.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 146 GCFPTATLLALHPLISekivDLSSI-IIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSiiagqdV 224
Cdd:cd23936    1 GCYATGAQLALAPLLD----DLDGPpSVFGVSGYSGAGTKPSPKNDPEVLADNLIPYSLVGHIHEREVSRHLG------T 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 225 SVIFTPHLVPMTRGILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRIrdIGTFPTTKEVLGSNYCDI-GIYVDETTQTA 303
Cdd:cd23936   71 PVAFMPHVAPWFQGITLTISIPLKKSMTADEIRELYQEAYAGEPLIKV--TKEIPLVRDNAGKHGVVVgGFTVHPDGKRV 148

                        170
                 ....*....|...
gi 446521137 304 ILVSVIDNLVKGA 316
Cdd:cd23936  149 VVVATIDNLLKGA 161
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 2-111 2.30e-17

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


Pssm-ID: 467515 [Multi-domain]  Cd Length: 160  Bit Score: 78.38  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHL--QHIMQHFEALTVDNNdCDVIFFATPAPVSK 79
Cdd:cd02280    1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLiiSLQIQEFRPCEVLNS-ADILVLALPHGASA 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446521137  80 TCIPPLVEKGIHVIDLSGAFRIKNREIYEAYY 111
Cdd:cd02280   80 ELVAAISNPQVKIIDLSADFRFTDPEVYRRHP 111
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 2-116 9.13e-17

N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate reductase (actinobacAGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC). There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The family includes N-acetyl-gamma-glutamyl-phosphate reductases mainly from actinobacteria. They belong to the type 1 AGPR family. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467524 [Multi-domain]  Cd Length: 164  Bit Score: 76.56  E-value: 9.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHLQHIMQH-FEALTVDN-NDCDVIFFATPAPVSK 79
Cdd:cd24148    1 IRVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHLPPLADRvLEPTTPAVlAGHDVVFLALPHGASA 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446521137  80 TCIPPLVEKgIHVIDLSGAFRIKNREIYEAYYKETAA 116
Cdd:cd24148   81 AIAAQLPPD-VLVVDCGADHRLEDAAAWEKFYGGEHA 116
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 147-312 2.04e-15

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: 72.94  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 147 CFPTATLLALHPLISEKIVDlsSIIIDAKTGVSGAGRSLSQRVHFSEMNENLSAYAIGNHKHKPEIEQYLSIIaGQDVSV 226
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIE--EILVVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGEI-GKPIKV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 227 IFTPHLVPMTRGILSTIYVKLSSEYTTESLHKLMTSYYANQPFVRI-RDIGTFPTTKEVLGSNYCDIGIYV--DETTQTA 303
Cdd:cd18122   78 DGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEdGLTYAKVSTRSVGGVYGVPVGRQRefAFDDNKL 157


                 ....*....
gi 446521137 304 ILVSVIDNL 312
Cdd:cd18122  158 KVFSAVDNE 166
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 2-146 9.06e-13

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: 65.21  E-value: 9.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHSKVDEPLK---LTFPHLQHIMQHFEALTVDNNDCDVIFFATPAPVS 78
Cdd:cd24149    1 KRVGLIGARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVSgytKSPIDYLNLSVEDIPEEVAAREVDAWVLALPNGVA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446521137  79 KtcipPLVE------KGIHVIDLSGAFRIknreiyeayyketaaaqDDLNHaiYSISEWQSFDNNGTKLISNPG 146
Cdd:cd24149   81 K----PFVDaidkanPKSVIVDLSADYRF-----------------DDAWT--YGLPELNRRRIAGAKRISNPG 131
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-329 3.34e-12

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 66.39  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   1 MIKVGIVGGSGYGAIELIRLLQTHPHVTIAHIY----SHSK---------VDEPlkltfphlqhIMQHFEALTV------ 61
Cdd:PRK08664   3 KLKVGILGATGMVGQRFVQLLANHPWFEVTALAaserSAGKtygeavrwqLDGP----------IPEEVADMEVvstdpe 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  62 DNNDCDVIFFATPAPVSKTCIPPLVEKGIHVIDLSGAFR------IKNREIyeayyketaaaqddlNHAIYSISEWQSfD 135
Cdd:PRK08664  73 AVDDVDIVFSALPSDVAGEVEEEFAKAGKPVFSNASAHRmdpdvpLVIPEV---------------NPEHLELIEVQR-K 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 136 NNGTK--LISNPGCFPTATLLALHPLISEKIvdlSSIIIDAKTGVSGAGRSlsqRVHFSEMNENLSAYaIGNHKHKPEIE 213
Cdd:PRK08664 137 RRGWDgfIVTNPNCSTIGLVLALKPLMDFGI---ERVHVTTMQAISGAGYP---GVPSMDIVDNVIPY-IGGEEEKIEKE 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 214 --QYLSIIAGQ-------DVSVifTPHLVPMTRGILSTIYVKLSSEYTTESLHKLMTSY----------YANQPFVRIRD 274
Cdd:PRK08664 210 tlKILGKFEGGkivpadfPISA--TCHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFkglpqelglpSAPKKPIILFE 287

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 275 IGTFPTTKevLGSNYCD-IGIYVDETTQTAI----LVSVIDNLVKGASGQAIQNLNILYD 329
Cdd:PRK08664 288 EPDRPQPR--LDRDAGDgMAVSVGRLREDGIfdikFVVLGHNTVRGAAGASVLNAELLKK 345
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 2-107 8.87e-12

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


Pssm-ID: 467516 [Multi-domain]  Cd Length: 145  Bit Score: 62.00  E-value: 8.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPH-VTIAHIYSHSKVDEPLKLTFPHLQHIMQHFEALTVDNNDCDVIFFATPAPVSKT 80
Cdd:cd02281    1 KKVGVVGATGYVGGEFLRLLLEHPFpLFEIVLLAASSAGAKKKYFHPKLWGRVLVEFTPEEVLEQVDIVFTALPGGVSAK 80

                         90       100
                 ....*....|....*....|....*..
gi 446521137  81 CIPPLVEKGIHVIDLSGAFRIKNREIY 107
Cdd:cd02281   81 LAPELSEAGVLVIDNASDFRLDKDVPL 107
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 3-100 4.34e-07

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: 48.59  E-value: 4.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   3 KVGIVGGSGYGAIELIRLLQTHpHVTIAHIY------SHSKvdeplKLTFPHLQHIMqhfEALTVDN-NDCDVIFFATPA 75
Cdd:cd02316    2 NVAIVGATGAVGQEMLKVLEER-NFPVSELRllasarSAGK-----TLEFKGKELTV---EELTEDSfKGVDIALFSAGG 72

                         90       100
                 ....*....|....*....|....*
gi 446521137  76 PVSKTCIPPLVEKGIHVIDLSGAFR 100
Cdd:cd02316   73 SVSKEFAPIAAEAGAVVIDNSSAFR 97
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 65-327 5.92e-07

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: 50.42  E-value: 5.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  65 DCDVIFFATPAPVSKTCIPPLVEKGIHVIDLSGAFRIK----------NREiyeayyketaAAQDDLNHAIysisewqsf 134
Cdd:COG0136   62 GVDIALFSAGGSVSKEYAPKAAAAGAVVIDNSSAFRMDpdvplvvpevNPE----------ALADHLPKGI--------- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 135 dnngtklISNPGCFPTATLLALHPLisEKIVDLSSIIIDAKTGVSGAGRSlsqrvHFSEMNENLSAYAIGNhkhKPEIEQ 214
Cdd:COG0136  123 -------IANPNCSTIQMLVALKPL--HDAAGIKRVVVSTYQAVSGAGAA-----AMDELAEQTAALLNGE---EIEPEV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137 215 YLSIIAGqdvSVIftPHL-VPM--------------TRGILST---------------------IYVKLSSEYTTESLHK 258
Cdd:COG0136  186 FPHPIAF---NLI--PQIdVFLengytkeemkmvneTRKILGDpdipvsatcvrvpvfrghseaVNIEFERPVSLEEARE 260

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446521137 259 LMtsyyANQPFVRIRD---IGTFPTTKEVLGSNYCDIG-IYVDETTQTAI-LVSVIDNLVKGASGQAIQNLNIL 327
Cdd:COG0136  261 LL----AAAPGVKVVDdpaENDYPTPLDASGTDEVFVGrIRKDLSVPNGLnLWVVADNLRKGAALNAVQIAELL 330
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 3-182 8.84e-07

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 50.15  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   3 KVGIVGGSGYGAIELIRLLQTH--PHVTIAHIYSHSKVDEplKLTFphlQHIMQHFEALTVDN-NDCDVIFFATPAPVSK 79
Cdd:PLN02383   9 SVAIVGVTGAVGQEFLSVLTDRdfPYSSLKMLASARSAGK--KVTF---EGRDYTVEELTEDSfDGVDIALFSAGGSISK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137  80 TCIPPLVEKGIHVIDLSGAFRIKNR---EIYEAYYKETAAAQddlnhaiysisewqsFDNNGTKLISNPGCFPTATLLAL 156
Cdd:PLN02383  84 KFGPIAVDKGAVVVDNSSAFRMEEGvplVIPEVNPEAMKHIK---------------LGKGKGALIANPNCSTIICLMAV 148

                        170       180
                 ....*....|....*....|....*.
gi 446521137 157 HPLisEKIVDLSSIIIDAKTGVSGAG 182
Cdd:PLN02383 149 TPL--HRHAKVKRMVVSTYQAASGAG 172
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 2-100 3.84e-05

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: 43.25  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHPHVTIAHIYSHS-------------KVDEPLKLTFPHLqhIMQHFEAltVDNNDCDV 68
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASErsagkkygdavrwKQDTPIPEEVADM--VVKECEP--EEFKDCDI 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446521137  69 IFFATPAPVSKTCIPPLVEKGIHVIDLSGAFR 100
Cdd:cd02315   77 VFSALDSDVAGEIEPAFAKAGIPVFSNASNHR 108
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-93 2.23e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 42.22  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   1 MIKVGIVGGSGYGAiELIRLLQTHPHVTIAHIYSHSKvdeplkltfPHLQHIMQHFEALT-------VDNNDCDVIFFAT 73
Cdd:COG0673    3 KLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDP---------ERAEAFAEEYGVRVytdyeelLADPDIDAVVIAT 72

                         90       100
                 ....*....|....*....|....
gi 446521137  74 P----APVSKTCIpplvEKGIHVI 93
Cdd:COG0673   73 PnhlhAELAIAAL----EAGKHVL 92
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 2-100 2.96e-04

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: 40.40  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVGGSGYGAIELIRLLQTHP-HVTIAHIYSHSK-VDEPLKLtFPhlQHIMQHfEALTVDNNDCDVIFFATPAPVSK 79
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEPdPLFELRALASEEsAGKKAEF-AG--EAIMVQ-EADPIDFLGLDIVFLCAGAGVSA 76

                         90       100
                 ....*....|....*....|.
gi 446521137  80 TCIPPLVEKGIHVIDLSGAFR 100
Cdd:cd24147   77 KFAPEAARAGVLVIDNAGALR 97
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 67-100 4.71e-04

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: 39.91  E-value: 4.71e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446521137  67 DVIFFATPAPVSKTCIPPLVEKGIHVIDLSGAFR 100
Cdd:cd17894   64 DLVFFAGPAEVARAYAPRARAAGCLVIDLSGALR 97
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 298-326 2.02e-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: 37.97  E-value: 2.02e-03
                         10        20
                 ....*....|....*....|....*....
gi 446521137 298 ETTQTAILVSVIDNLVKGASGQAIQNLNI 326
Cdd:cd17896  101 EKIATSKRVANPGNLGKGASGAAVQNMNL 129
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 2-94 2.10e-03

N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467610 [Multi-domain]  Cd Length: 151  Bit Score: 38.32  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521137   2 IKVGIVggsGYGAI--ELIRLLQTHPHVTIAHIYSHSKVDEPLKLTFPHLQHIMQHFEALtvdnNDCDVIFFATPapvSK 79
Cdd:cd02270    1 IRVAIV---GYGNLgrGVEEAIQANPDMELVGVFRRRDPKSTKELTPVVVVSVVEHISEL----DKVDVAILCGG---SA 70

                         90
                 ....*....|....*...
gi 446521137  80 TCIP---PLVEKGIHVID 94
Cdd:cd02270   71 TDLPeqaPEFAQGFNTVD 88
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 311-326 3.54e-03

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: 37.48  E-value: 3.54e-03
                         10
                 ....*....|....*.
gi 446521137 311 NLVKGASGQAIQNLNI 326
Cdd:cd24149  132 NLLKGAATQALQNLNL 147
 
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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