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Conserved domains on  [gi|488940559|ref|WP_002851634|]
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MULTISPECIES: N-acetyl-gamma-glutamyl-phosphate reductase [Campylobacter]

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]; ...
 3-340 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: 552.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPN--TPLNLCFENKNLDELELDLLF--LATPHKFS 78
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHlrGLTDLVFEPPDPDELAAGCDVvfLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  79 AKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILSLYP 158
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 159 LFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKITLQFTPHLVPMQRG 238
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 239 ILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKGAAG 318
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|..
gi 488940559 319 QAVQNMNLMFDFDEDEGLKFFA 340
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVP 342
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 3-340 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: 552.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPN--TPLNLCFENKNLDELELDLLF--LATPHKFS 78
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHlrGLTDLVFEPPDPDELAAGCDVvfLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  79 AKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILSLYP 158
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 159 LFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKITLQFTPHLVPMQRG 238
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 239 ILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKGAAG 318
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|..
gi 488940559 319 QAVQNMNLMFDFDEDEGLKFFA 340
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVP 342
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 3-338 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: 532.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559    3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSS-SVGQNYQDLYPNTP----LNLCFENKNLDELELDLLFLATPHKF 77
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSReSAGKPVSEVHPHLRglvdLNLEPIDVEEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   78 SAKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILSLY 157
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  158 PLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKITLQFTPHLVPMQR 237
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  238 GILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKGAA 317
Cdd:TIGR01850 241 GILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|.
gi 488940559  318 GQAVQNMNLMFDFDEDEGLKF 338
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPF 341
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-336 4.67e-110

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 325.63  E-value: 4.67e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   2 KIKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPN---TPLNLCFENKNLDELELDLLFLATPH--- 75
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHlitQDLPNLVAVKDADFSDVDAVFCCLPHgtt 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  76 KFSAKLLNENLlkkmKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILS 155
Cdd:PLN02968 118 QEIIKALPKDL----KIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLP 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 156 LYPLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKITLQFTPHLVPM 235
Cdd:PLN02968 194 LVPLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPM 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 236 QRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKG 315
Cdd:PLN02968 274 SRGMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKG 353

                        330       340
                 ....*....|....*....|.
gi 488940559 316 AAGQAVQNMNLMFDFDEDEGL 336
Cdd:PLN02968 354 ASGQAVQNLNLMMGLPETTGL 374
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 146-316 1.91e-100

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: 293.23  E-value: 1.91e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 146 GCYTTCSILSLYPLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKIT 225
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 226 LQFTPHLVPMQRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIV 305
Cdd:cd23934   81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                        170
                 ....*....|.
gi 488940559 306 LGAIDNLIKGA 316
Cdd:cd23934  161 VSAIDNLVKGA 171
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 156-314 5.85e-30

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: 112.41  E-value: 5.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  156 LYPLFKeKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLA-LHRHTPEIEEHLSYAAKEKITLQFTP---- 230
Cdd:pfam02774   1 LKPLRD-ALGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGeEHNGTPETREELKMVNETKKILGFTPkvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  231 --HLVPMQRGILISAYANLKedLQEQDIRDIYTKYYQ-NNKFIRLLPPQSLPQTRWVKS-SNFADI-NFSVDQRTKRVIV 305
Cdd:pfam02774  80 tcVRVPVFRGHSETVTVKLK--LKPIDVEEVYEAFYAaPGVFVVVRPEEDYPTPRAVRGgTNFVYVgRVRKDPDGDRGLK 157

                         170
                  ....*....|
gi 488940559  306 L-GAIDNLIK 314
Cdd:pfam02774 158 LvSVIDNLRK 167
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-139 2.54e-28

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: 106.48  E-value: 2.54e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559     4 KVGILGASGYAGNELVRILLNHPKVEISYL-GSSSSVGQNYQDLYPNTP--LNLCFENKNLDELELDLLFLATPHKFS-- 78
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALaASSRSAGKKVSEAGPHLKgeVVLELDPPDFEELAVDIVFLALPHGVSke 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488940559    79 -AKLLNENLLKKMKIIDLSADFRLKNPkdyelwykfthpnqellqnAVYGLCELYKEEIKKA 139
Cdd:smart00859  81 sAPLLPRAAAAGAVVIDLSSAFRMDDD-------------------VPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 3-340 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: 552.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPN--TPLNLCFENKNLDELELDLLF--LATPHKFS 78
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHlrGLTDLVFEPPDPDELAAGCDVvfLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  79 AKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILSLYP 158
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 159 LFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKITLQFTPHLVPMQRG 238
Cdd:COG0002  161 LLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGEDVKVSFTPHLVPMVRG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 239 ILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKGAAG 318
Cdd:COG0002  241 ILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEGRLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLVKGAAG 320

                        330       340
                 ....*....|....*....|..
gi 488940559 319 QAVQNMNLMFDFDEDEGLKFFA 340
Cdd:COG0002  321 QAVQNMNLMFGLPETTGLELVP 342
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 3-338 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: 532.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559    3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSS-SVGQNYQDLYPNTP----LNLCFENKNLDELELDLLFLATPHKF 77
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSReSAGKPVSEVHPHLRglvdLNLEPIDVEEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   78 SAKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILSLY 157
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  158 PLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKITLQFTPHLVPMQR 237
Cdd:TIGR01850 161 PLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGGKVKVSFTPHLVPMTR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  238 GILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKGAA 317
Cdd:TIGR01850 241 GILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEGGYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNLVKGAA 320

                         330       340
                  ....*....|....*....|.
gi 488940559  318 GQAVQNMNLMFDFDEDEGLKF 338
Cdd:TIGR01850 321 GQAVQNMNLMFGFDETTGLPF 341
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-336 4.67e-110

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 325.63  E-value: 4.67e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   2 KIKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPN---TPLNLCFENKNLDELELDLLFLATPH--- 75
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHlitQDLPNLVAVKDADFSDVDAVFCCLPHgtt 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  76 KFSAKLLNENLlkkmKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILS 155
Cdd:PLN02968 118 QEIIKALPKDL----KIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLP 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 156 LYPLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKITLQFTPHLVPM 235
Cdd:PLN02968 194 LVPLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLADAAGSKVTPSFTPHLMPM 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 236 QRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKG 315
Cdd:PLN02968 274 SRGMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGAVPHTDHVRGSNYCELNVFADRIPGRAIIISVIDNLVKG 353

                        330       340
                 ....*....|....*....|.
gi 488940559 316 AAGQAVQNMNLMFDFDEDEGL 336
Cdd:PLN02968 354 ASGQAVQNLNLMMGLPETTGL 374
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 146-316 1.91e-100

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: 293.23  E-value: 1.91e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 146 GCYTTCSILSLYPLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEKIT 225
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGEDVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 226 LQFTPHLVPMQRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIV 305
Cdd:cd23934   81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEGQLPSTKAVRGSNFCDIGVAVDGRTGRLIV 160

                        170
                 ....*....|.
gi 488940559 306 LGAIDNLIKGA 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 ...
 3-145 2.60e-63

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: 198.81  E-value: 2.60e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPN----TPLNLCFENKNLDELELDLLFLATPHKFS 78
Cdd:cd17895    1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHlrglTDLTFEPDDDEEIAEDADVVFLALPHGVS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488940559  79 AKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANP 145
Cdd:cd17895   81 MELAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFEHAAPELLKEAVYGLPELNREEIKKARLVANP 147
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 146-316 1.65e-62

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: 196.69  E-value: 1.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 146 GCYTTCSILSLYPLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKEkIT 225
Cdd:cd23939    1 GCNATASILALYPLVKAGLLDDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGLLARE-IS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 226 LQFTPHLVPMQRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLP----PQSLPQTRWVKSSNFADINFSVDQRTK 301
Cdd:cd23939   80 VSFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYRKAYGNEPFVRIVKdrkgIYRYPDPKLVIGSNFCDIGFELDEDNG 159

                        170
                 ....*....|....*
gi 488940559 302 RVIVLGAIDNLIKGA 316
Cdd:cd23939  160 RLVVFSAIDNLMKGA 174
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 147-316 1.12e-54

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: 176.54  E-value: 1.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 147 CYTTCSILSLYPLFKEKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLsyaaKEKITL 226
Cdd:cd18125    1 CYATAALLALYPLLKAGLLKPTPITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNL----GGKHNV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 227 QFTPHLVPMQRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVL 306
Cdd:cd18125   77 HFTPHVGPWVRGILMTIQCFTQKGWSLRQLHEAYREAYAGEPFVRVMPQGKGPDPKFVQGTNYADIGVELEEDTGRLVVM 156

                        170
                 ....*....|
gi 488940559 307 GAIDNLIKGA 316
Cdd:cd18125  157 SAIDNLVKGA 166
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 3-143 1.72e-38

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: 134.71  E-value: 1.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPN----TPLNLCFENKnldELELDLLFLATPHKFS 78
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNlrgrTLLKFVPPEE---LESCDVLFLALPHGES 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488940559  79 AKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVA 143
Cdd:cd24151   78 MKRIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLERFVYGLPELHREELRGARYIA 142
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 156-314 5.85e-30

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: 112.41  E-value: 5.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  156 LYPLFKeKIIDFSSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLA-LHRHTPEIEEHLSYAAKEKITLQFTP---- 230
Cdd:pfam02774   1 LKPLRD-ALGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGeEHNGTPETREELKMVNETKKILGFTPkvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  231 --HLVPMQRGILISAYANLKedLQEQDIRDIYTKYYQ-NNKFIRLLPPQSLPQTRWVKS-SNFADI-NFSVDQRTKRVIV 305
Cdd:pfam02774  80 tcVRVPVFRGHSETVTVKLK--LKPIDVEEVYEAFYAaPGVFVVVRPEEDYPTPRAVRGgTNFVYVgRVRKDPDGDRGLK 157

                         170
                  ....*....|
gi 488940559  306 L-GAIDNLIK 314
Cdd:pfam02774 158 LvSVIDNLRK 167
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-139 2.54e-28

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: 106.48  E-value: 2.54e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559     4 KVGILGASGYAGNELVRILLNHPKVEISYL-GSSSSVGQNYQDLYPNTP--LNLCFENKNLDELELDLLFLATPHKFS-- 78
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALaASSRSAGKKVSEAGPHLKgeVVLELDPPDFEELAVDIVFLALPHGVSke 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488940559    79 -AKLLNENLLKKMKIIDLSADFRLKNPkdyelwykfthpnqellqnAVYGLCELYKEEIKKA 139
Cdd:smart00859  81 sAPLLPRAAAAGAVVIDLSSAFRMDDD-------------------VPYGLPEVNPEAIKKA 123
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 3-145 1.15e-27

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: 106.22  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPNTP--LNLCFENKNLDELELD-LLFLATPHKFSA 79
Cdd:cd24148    1 IRVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHLPplADRVLEPTTPAVLAGHdVVFLALPHGASA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488940559  80 KLLNEnLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQellqnAVYGLCEL--YKEEIKKASLVANP 145
Cdd:cd24148   81 AIAAQ-LPPDVLVVDCGADHRLEDAAAWEKFYGGEHAGG-----WTYGLPELpgAREALAGARRIAVP 142
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 4-139 1.75e-27

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: 104.14  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559    4 KVGILGASGYAGNELVRILLNHPKVEISYLGSSS-SVGQNYQDLYPN--TPLNLCFENKNLDELELDLLF-LATPHKFSA 79
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSrSAGKKLAFVHPIleGGKDLVVEDVDPEDFKDVDIVfFALPGGVSK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   80 KLLNENLLKKMKIIDLSADFRLKNpkdyelwykfthpnqellqNAVYGLCELYKEEIKKA 139
Cdd:pfam01118  81 EIAPKLAEAGAKVIDLSSDFRMDD-------------------DVPYGLPEVNREAIKQA 121
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 3-145 1.15e-25

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: 100.72  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPNTPLNLCFEN--KNLDELELDLLFLATPHKFSAK 80
Cdd:cd02280    1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIISLQIQEfrPCEVLNSADILVLALPHGASAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488940559  81 LLNENLLKKMKIIDLSADFRLKNPKDYElwykfTHPNQELLQNAVYGLCELYKE-EIKKASLVANP 145
Cdd:cd02280   81 LVAAISNPQVKIIDLSADFRFTDPEVYR-----RHPRPDLEGGWVYGLPELDREqRIANATRIANP 141
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 146-316 1.67e-22

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: 92.31  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 146 GCYTTCSILSLYPLFKEkiIDFSSVIIDAkSGVSGAGR--SAK--VENLfcevNENIKAYNLALHRHTPEIEEHLSyaak 221
Cdd:cd23936    1 GCYATGAQLALAPLLDD--LDGPPSVFGV-SGYSGAGTkpSPKndPEVL----ADNLIPYSLVGHIHEREVSRHLG---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 222 ekITLQFTPHLVPMQRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLppQSLPQTRWVKSSNFADIN-FSVDQRT 300
Cdd:cd23936   70 --TPVAFMPHVAPWFQGITLTISIPLKKSMTADEIRELYQEAYAGEPLIKVT--KEIPLVRDNAGKHGVVVGgFTVHPDG 145

                        170
                 ....*....|....*.
gi 488940559 301 KRVIVLGAIDNLIKGA 316
Cdd:cd23936  146 KRVVVVATIDNLLKGA 161
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 3-146 1.40e-21

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: 89.48  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPNTPLNLCFENKNLDELELDLLF----LATPHKFS 78
Cdd:cd24149    1 KRVGLIGARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVSGYTKSPIDYLNLSVEDIPEEVAAREVdawvLALPNGVA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  79 AKLLN--ENLLKKMKIIDLSADFRLkNPKdyelWykfthpnqellqnaVYGLCELYKEEIKKASLVANPG 146
Cdd:cd24149   81 KPFVDaiDKANPKSVIVDLSADYRF-DDA----W--------------TYGLPELNRRRIAGAKRISNPG 131
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 146-316 8.18e-18

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


Pssm-ID: 467684  Cd Length: 178  Bit Score: 79.95  E-value: 8.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 146 GCYTTCSILSLYPLFKEKIIDFSS-VIIDAKSGVSGAGRSAkVENLFCEVNENIKA---YNLAL-HRHTPEIEEHlsyaA 220
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPADYpLSIHAVSGYSGGGKKM-IEQYEAAEAADLPPprpYGLGLeHKHLPEMQKH----A 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 221 KEKITLQFTPHLVPMQRGILIS---AYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQS-------LPQTrwVKSSNFA 290
Cdd:cd23935   76 GLARPPIFTPAVGNFYQGMLVTvplHLDLLEKGVSAAEVHEALAEHYAGERFVKVMPLDEpdalgflDPQA--LNGTNNL 153

                        170       180
                 ....*....|....*....|....*.
gi 488940559 291 DINFSVDQRTkRVIVLGAIDNLIKGA 316
Cdd:cd23935  154 ELFVFGNDKG-QALLVARLDNLGKGA 178
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 147-312 1.67e-16

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: 76.02  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 147 CYTTCSILSLYPLFKEKIIDfsSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYNLALHRHTPEIEEHLSYAAKeKITL 226
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIE--EILVVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGEIGK-PIKV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 227 QFTPHLVPMQRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLP-PQSLPQTRWVKSSN--FADINFSVDQRTKRV 303
Cdd:cd18122   78 DGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGlTYAKVSTRSVGGVYgvPVGRQREFAFDDNKL 157


                 ....*....
gi 488940559 304 IVLGAIDNL 312
Cdd:cd18122  158 KVFSAVDNE 166
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-329 1.65e-15

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 76.40  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   1 MKIKVGILGASGYAGNELVRILLNHPKVEISYLG-SSSSVGQNYQDL---YPNTPLNLCFENknldelelDLLFLATPHK 76
Cdd:PRK08664   2 MKLKVGILGATGMVGQRFVQLLANHPWFEVTALAaSERSAGKTYGEAvrwQLDGPIPEEVAD--------MEVVSTDPEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559  77 -------FS------AKLLNENLLKKMK-IIDLSADFR------LKNPkdyELwykfthpNQELLqnavyGLCELYKEEI 136
Cdd:PRK08664  74 vddvdivFSalpsdvAGEVEEEFAKAGKpVFSNASAHRmdpdvpLVIP---EV-------NPEHL-----ELIEVQRKRR 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 137 -KKASLVANPGCYTTCSILSLYPLFKEKIidfSSVIIDAKSGVSGAGRSAkVENLfcEVNEN----IKAYNLALHRHTPE 211
Cdd:PRK08664 139 gWDGFIVTNPNCSTIGLVLALKPLMDFGI---ERVHVTTMQAISGAGYPG-VPSM--DIVDNvipyIGGEEEKIEKETLK 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559 212 IeehLSYAAKEKITLQFTP-----HLVPMQRGILISAYANLKEDLQEQDIRDIYTKY---YQN-------NKFIRLLPPQ 276
Cdd:PRK08664 213 I---LGKFEGGKIVPADFPisatcHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFkglPQElglpsapKKPIILFEEP 289

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488940559 277 SLPQTRW--------------VKSSNFADINFsvdqrtkrvIVLGaiDNLIKGAAGQAVQNMNLMFD 329
Cdd:PRK08664 290 DRPQPRLdrdagdgmavsvgrLREDGIFDIKF---------VVLG--HNTVRGAAGASVLNAELLKK 345
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 3-145 5.40e-10

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: 56.99  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488940559   3 IKVGILGASGYAGNELVRILLNHP-KVEISYLGSSSSVGQNYQDLYPNTPLNLCFENKNLDELELD-LLFLATPHKFSAK 80
Cdd:cd02281    1 KKVGVVGATGYVGGEFLRLLLEHPfPLFEIVLLAASSAGAKKKYFHPKLWGRVLVEFTPEEVLEQVdIVFTALPGGVSAK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488940559  81 LLNENLLKKMKIIDLSADFRLKnpKDyelwykfthpnqellqnAVYGLCELYKE---EIKKASLVANP 145
Cdd:cd02281   81 LAPELSEAGVLVIDNASDFRLD--KD-----------------VPLVVPEVNREhigELKGTKIIANP 129
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 3-45 1.54e-09

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


Pssm-ID: 467518  Cd Length: 162  Bit Score: 55.96  E-value: 1.54e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLG-SSSSVGQNYQD 45
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGaSERSAGKKYGD 44
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 3-46 1.71e-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: 47.32  E-value: 1.71e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDL 46
Cdd:cd24150    2 LKAAILGATGLVGIEYVRMLSNHPYIKPAYLAGKGSVGKPYGEV 45
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 295-327 2.61e-04

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


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 40.28  E-value: 2.61e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 488940559 295 SVDQR-----TKRVIVLGaidNLIKGAAGQAVQNMNLM 327
Cdd:cd17896   96 SPEQRekiatSKRVANPG---NLGKGASGAAVQNMNLM 130
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 4-41 3.27e-04

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: 40.11  E-value: 3.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488940559   4 KVGILGASGYAGNELVRIL--LNHPKVEISYLGSSSSVGQ 41
Cdd:cd02316    2 NVAIVGATGAVGQEMLKVLeeRNFPVSELRLLASARSAGK 41
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 3-45 6.94e-03

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: 36.55  E-value: 6.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488940559   3 IKVGILGASGYAGNELVRILLNHPKV--EISYLGSSSSVGQNYQD 45
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEPDPlfELRALASEESAGKKAEF 45
 
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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