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Conserved domains on  [gi|756973779|ref|WP_042662103|]
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MULTISPECIES: aspartate-semialdehyde dehydrogenase [unclassified Haloferax]

Protein Classification

aspartate-semialdehyde dehydrogenase family protein( domain architecture ID 11483416)

aspartate-semialdehyde dehydrogenase family protein such as aspartate-semialdehyde dehydrogenase and malonyl-CoA reductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-344 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


:

Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 616.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   1 MAVRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEVGSTDPADVPDdIDLL 80
Cdd:PRK08664   2 MKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVRWQLDGPIPEEVADMEVVSTDPEAVDD-VDIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRDERGWDGALVKNPNCSTITMVPTLA 160
Cdd:PRK08664  81 FSALPSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWDGFIVTNPNCSTIGLVLALK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 161 ALDQFGLERVDVTTLQAVSGAGYDGVTSMEIIDNAIPHIGGEEEKMETESRKLLGSFDGAEVALHGAEVNASCNRIPTLD 240
Cdd:PRK08664 161 PLMDFGIERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFPISATCHRVPVID 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 241 GHLESVFADLADDASPEDVAAAMREYPGV----DLPSAPEQLIHVFEDNFRPQPRLDRERGDGMQISAGGIQATEHG-VK 315
Cdd:PRK08664 241 GHTEAVFVKFKEDVDPEEIREALESFKGLpqelGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRLREDGIFdIK 320

                        330       340
                 ....*....|....*....|....*....
gi 756973779 316 YNCLAHNTIRGAAGASVLNGELLAQEGWI 344
Cdd:PRK08664 321 FVVLGHNTVRGAAGASVLNAELLKKKGYL 349
 
Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-344 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 616.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   1 MAVRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEVGSTDPADVPDdIDLL 80
Cdd:PRK08664   2 MKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVRWQLDGPIPEEVADMEVVSTDPEAVDD-VDIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRDERGWDGALVKNPNCSTITMVPTLA 160
Cdd:PRK08664  81 FSALPSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWDGFIVTNPNCSTIGLVLALK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 161 ALDQFGLERVDVTTLQAVSGAGYDGVTSMEIIDNAIPHIGGEEEKMETESRKLLGSFDGAEVALHGAEVNASCNRIPTLD 240
Cdd:PRK08664 161 PLMDFGIERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFPISATCHRVPVID 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 241 GHLESVFADLADDASPEDVAAAMREYPGV----DLPSAPEQLIHVFEDNFRPQPRLDRERGDGMQISAGGIQATEHG-VK 315
Cdd:PRK08664 241 GHTEAVFVKFKEDVDPEEIREALESFKGLpqelGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRLREDGIFdIK 320

                        330       340
                 ....*....|....*....|....*....
gi 756973779 316 YNCLAHNTIRGAAGASVLNGELLAQEGWI 344
Cdd:PRK08664 321 FVVLGHNTVRGAAGASVLNAELLKKKGYL 349
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 3-338 1.10e-149

aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. Separate models are built for the two types in order to exclude the USG-1 protein, found in several species, which is specifically related to the Bacillus subtilis type of aspartate-semialdehyde dehydrogenase. Members of this type are found primarily in organisms that lack peptidoglycan. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273376 [Multi-domain]  Cd Length: 341  Bit Score: 424.94  E-value: 1.10e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779    3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEVGSTDPADVpDDIDLLFS 82
Cdd:TIGR00978   1 MRVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAVKWIEPGDMPEYVRDLPIVEPEPVAS-KDVDIVFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   83 SLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRdERGWDGALVKNPNCSTITMVPTLAAL 162
Cdd:TIGR00978  80 ALPSEVAEEVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQK-ERGWKGFIVTNPNCTTAGLTLALKPL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  163 -DQFGLERVDVTTLQAVSGAGYDGVTSMEIIDNAIPHIGGEEEKMETESRKLLGSFDGAEVALHGAEVNASCNRIPTLDG 241
Cdd:TIGR00978 159 iDAFGIKKVHVTTMQAVSGAGYPGVPSMDILDNIIPHIGGEEEKIERETRKILGKLENGKIEPAPFSVSATTTRVPVLDG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  242 HLESVFADLADDASPEDVAAAMREYPG----VDLPSAPEQLIHVFEDNFRPQPRLDRERGDGMQISAGGIQATEHGVKYN 317
Cdd:TIGR00978 239 HTESVHVEFDKKFDIEEIREALKSFRGlpqkLGLPSAPEKPIIVRDEEDRPQPRLDRDAGGGMAVTVGRLREEGGSLKYV 318

                         330       340
                  ....*....|....*....|.
gi 756973779  318 CLAHNTIRGAAGASVLNGELL 338
Cdd:TIGR00978 319 VLGHNLVRGAAGATLLNAELA 339
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 3-150 2.03e-85

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: 254.72  E-value: 2.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEVGSTDPADvPDDIDLLFS 82
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERSAGKKYGDAVRWKQDTPIPEEVADMVVKECEPEE-FKDCDIVFS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756973779  83 SLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRDERGWDGALVKNPNC 150
Cdd:cd02315   80 ALDSDVAGEIEPAFAKAGIPVFSNASNHRMDPDVPLVIPEVNPDHLDLIEAQRKRRGWKGFIVTNPNN 147
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 3-271 1.22e-59

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: 194.87  E-value: 1.22e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLE--DHPTFELAALtASESSAGKRYDeaakWRVNTPipddvaamEVGSTDPADvPDDIDLL 80
Cdd:COG0136    1 YNVAVVGATGAVGRVLLELLEerDFPVGELRLL-ASSRSAGKTVS----FGGKEL--------TVEDATDFD-FSGVDIA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDlievQRDERGwdgaLVKNPNCSTITMVPTLA 160
Cdd:COG0136   67 LFSAGGSVSKEYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALA----DHLPKG----IIANPNCSTIQMLVALK 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 161 AL-DQFGLERVDVTTLQAVSGAGYDGVTSME--------------------IIDNAIPHIGG--------EEEKMETESR 211
Cdd:COG0136  139 PLhDAAGIKRVVVSTYQAVSGAGAAAMDELAeqtaallngeeiepevfphpIAFNLIPQIDVflengytkEEMKMVNETR 218

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 212 KLLGsfdgaevaLHGAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDL 271
Cdd:COG0136  219 KILG--------DPDIPVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAAPGVKV 270
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 4-131 5.48e-45

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


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 149.98  E-value: 5.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779    4 RVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAkwrvntPIPDDVAAMEVGSTDPADVpDDIDLLFSS 83
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSAGKKLAFVH------PILEGGKDLVVEDVDPEDF-KDVDIVFFA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 756973779   84 LPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLI 131
Cdd:pfam01118  74 LPGGVSKEIAPKLAEAGAKVIDLSSDFRMDDDVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-131 2.05e-36

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: 127.66  E-value: 2.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779     4 RVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRvnTPIPDDVAAMEvgstDPADVpdDIDLLFSS 83
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRSAGKKVSEAGPHL--KGEVVLELDPP----DFEEL--AVDIVFLA 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 756973779    84 LPSSVAAEV---EPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLI 131
Cdd:smart00859  73 LPHGVSKESaplLPRAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-344 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 616.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   1 MAVRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEVGSTDPADVPDdIDLL 80
Cdd:PRK08664   2 MKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVRWQLDGPIPEEVADMEVVSTDPEAVDD-VDIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRDERGWDGALVKNPNCSTITMVPTLA 160
Cdd:PRK08664  81 FSALPSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWDGFIVTNPNCSTIGLVLALK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 161 ALDQFGLERVDVTTLQAVSGAGYDGVTSMEIIDNAIPHIGGEEEKMETESRKLLGSFDGAEVALHGAEVNASCNRIPTLD 240
Cdd:PRK08664 161 PLMDFGIERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFPISATCHRVPVID 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 241 GHLESVFADLADDASPEDVAAAMREYPGV----DLPSAPEQLIHVFEDNFRPQPRLDRERGDGMQISAGGIQATEHG-VK 315
Cdd:PRK08664 241 GHTEAVFVKFKEDVDPEEIREALESFKGLpqelGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRLREDGIFdIK 320

                        330       340
                 ....*....|....*....|....*....
gi 756973779 316 YNCLAHNTIRGAAGASVLNGELLAQEGWI 344
Cdd:PRK08664 321 FVVLGHNTVRGAAGASVLNAELLKKKGYL 349
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 3-338 1.10e-149

aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. Separate models are built for the two types in order to exclude the USG-1 protein, found in several species, which is specifically related to the Bacillus subtilis type of aspartate-semialdehyde dehydrogenase. Members of this type are found primarily in organisms that lack peptidoglycan. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273376 [Multi-domain]  Cd Length: 341  Bit Score: 424.94  E-value: 1.10e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779    3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEVGSTDPADVpDDIDLLFS 82
Cdd:TIGR00978   1 MRVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAVKWIEPGDMPEYVRDLPIVEPEPVAS-KDVDIVFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   83 SLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRdERGWDGALVKNPNCSTITMVPTLAAL 162
Cdd:TIGR00978  80 ALPSEVAEEVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQK-ERGWKGFIVTNPNCTTAGLTLALKPL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  163 -DQFGLERVDVTTLQAVSGAGYDGVTSMEIIDNAIPHIGGEEEKMETESRKLLGSFDGAEVALHGAEVNASCNRIPTLDG 241
Cdd:TIGR00978 159 iDAFGIKKVHVTTMQAVSGAGYPGVPSMDILDNIIPHIGGEEEKIERETRKILGKLENGKIEPAPFSVSATTTRVPVLDG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  242 HLESVFADLADDASPEDVAAAMREYPG----VDLPSAPEQLIHVFEDNFRPQPRLDRERGDGMQISAGGIQATEHGVKYN 317
Cdd:TIGR00978 239 HTESVHVEFDKKFDIEEIREALKSFRGlpqkLGLPSAPEKPIIVRDEEDRPQPRLDRDAGGGMAVTVGRLREEGGSLKYV 318

                         330       340
                  ....*....|....*....|.
gi 756973779  318 CLAHNTIRGAAGASVLNGELL 338
Cdd:TIGR00978 319 VLGHNLVRGAAGATLLNAELA 339
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 3-150 2.03e-85

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: 254.72  E-value: 2.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEVGSTDPADvPDDIDLLFS 82
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERSAGKKYGDAVRWKQDTPIPEEVADMVVKECEPEE-FKDCDIVFS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756973779  83 SLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRDERGWDGALVKNPNC 150
Cdd:cd02315   80 ALDSDVAGEIEPAFAKAGIPVFSNASNHRMDPDVPLVIPEVNPDHLDLIEAQRKRRGWKGFIVTNPNN 147
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 150-323 8.54e-83

C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share 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 and are members of the GAPDH superfamily of proteins. This 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: 467680 [Multi-domain]  Cd Length: 180  Bit Score: 248.69  E-value: 8.54e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 150 CSTITMVPTLAALDQ-FGLERVDVTTLQAVSGAGYDGVTSMEIIDNAIPHIGGEEEKMETESRKLLGSFDGAEVALHGAE 228
Cdd:cd18130    1 CSTAGLALPLKPLHDfFGIEAVIVTTMQAISGAGYPGVPSLDILDNVIPYIGGEEEKIESETKKILGTLNEDKIEPADFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 229 VNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVD----LPSAPEQLIHVFEDNFRPQPRLDRERGDGMQISA 304
Cdd:cd18130   81 VSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPqvlgPPSAPKPIIVVEDEPRRPQPRLDRDAGDGMAVTV 160

                        170       180
                 ....*....|....*....|
gi 756973779 305 GGIQAT-EHGVKYNCLAHNT 323
Cdd:cd18130  161 GRIRKDdDFDLKFVLLSHNT 180
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 3-271 1.22e-59

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: 194.87  E-value: 1.22e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLE--DHPTFELAALtASESSAGKRYDeaakWRVNTPipddvaamEVGSTDPADvPDDIDLL 80
Cdd:COG0136    1 YNVAVVGATGAVGRVLLELLEerDFPVGELRLL-ASSRSAGKTVS----FGGKEL--------TVEDATDFD-FSGVDIA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDlievQRDERGwdgaLVKNPNCSTITMVPTLA 160
Cdd:COG0136   67 LFSAGGSVSKEYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALA----DHLPKG----IIANPNCSTIQMLVALK 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 161 AL-DQFGLERVDVTTLQAVSGAGYDGVTSME--------------------IIDNAIPHIGG--------EEEKMETESR 211
Cdd:COG0136  139 PLhDAAGIKRVVVSTYQAVSGAGAAAMDELAeqtaallngeeiepevfphpIAFNLIPQIDVflengytkEEMKMVNETR 218

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 212 KLLGsfdgaevaLHGAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDL 271
Cdd:COG0136  219 KILG--------DPDIPVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAAPGVKV 270
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
 3-339 1.69e-58

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 191.91  E-value: 1.69e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDH--PTFELAALtASESSAGKRYDEAAKwrvntpipddvaAMEVGSTDPADvPDDIDLL 80
Cdd:PRK14874   2 YNVAVVGATGAVGREMLNILEERnfPVDKLRLL-ASARSAGKELSFKGK------------ELKVEDLTTFD-FSGVDIA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDlievQRDERGwdgaLVKNPNCSTITMVPTLA 160
Cdd:PRK14874  68 LFSAGGSVSKKYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALA----EHRKKG----IIANPNCSTIQMVVALK 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 161 ALDQ-FGLERVDVTTLQAVSGAGYDGVTSM-----EIID-----------------NAIPHIG--------GEEEKMETE 209
Cdd:PRK14874 140 PLHDaAGIKRVVVSTYQAVSGAGKAGMEELfeqtrAVLNaavdpvepkkfpkpiafNVIPHIDvfmddgytKEEMKMVNE 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 210 SRKLLGSFDgaevalhgAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVdlpsapeQLIHVFEDNFRPQ 289
Cdd:PRK14874 220 TKKILGDPD--------LKVSATCVRVPVFTGHSESVNIEFEEPISVEEAREILAEAPGV-------VLVDDPENGGYPT 284

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756973779 290 PrldrergdgmqISAGGIQAT-----------EHGVKYNCLAHNTIRGAAGASVLNGELLA 339
Cdd:PRK14874 285 P-----------LEAVGKDATfvgrirkdltvENGLHLWVVSDNLRKGAALNAVQIAELLI 334
asd_B TIGR01296
aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families ...
 4-341 4.76e-52

aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. This model represents a branch more closely related to the USG-1 protein than to the other aspartate-semialdehyde dehydrogenases represented in model TIGR00978. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273543 [Multi-domain]  Cd Length: 338  Bit Score: 175.38  E-value: 4.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779    4 RVGILGATGAVGQRFIQLLEDHpTFELAALT--ASESSAGKRYDEAAKwrvntpipddvaAMEVGSTDPADvPDDIDLLF 81
Cdd:TIGR01296   1 NVAIVGATGAVGQEMLKLLEER-NFPIDKLVllASARSAGRKLTFKGK------------ELEVEEAETES-FEGIDIAL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   82 SSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDlievQRDERGwdgaLVKNPNCSTITMVPTLAA 161
Cdd:TIGR01296  67 FSAGGSVSKEFAPKAAKAGVIVIDNTSAFRMDPDVPLVVPEVNFEDLK----EFNPKG----IIANPNCSTIQMVVVLKP 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  162 L-DQFGLERVDVTTLQAVSGAGYDGVTSM--------------------------EIIDNAIPHIG--------GEEEKM 206
Cdd:TIGR01296 139 LhDEAKIKRVVVSTYQAVSGAGNAGVEELynqtkavlegaeqlpyiqpkankfpyQIAFNAIPHIDsfvddgytKEEQKM 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  207 ETESRKLLGSFDgaevalhgAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDLPSAPEQLIHVF---- 282
Cdd:TIGR01296 219 LFETRKIMGIPD--------LKVSATCVRVPVFTGHSESINIEFEKEISPEDARELLKNAPGVQLIDDPSGNLYPTplaa 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756973779  283 ---EDNFRPQPRLDRERGDGMQISaggiqatehgvkynCLAHNTIRGAAGASVLNGELLAQE 341
Cdd:TIGR01296 291 vgvDEVFVGRIRKDLPDGNGLHLW--------------VVADNLRKGAALNSVQIAELLIKN 338
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 4-131 5.48e-45

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


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 149.98  E-value: 5.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779    4 RVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAkwrvntPIPDDVAAMEVGSTDPADVpDDIDLLFSS 83
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSAGKKLAFVH------PILEGGKDLVVEDVDPEDF-KDVDIVFFA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 756973779   84 LPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLI 131
Cdd:pfam01118  74 LPGGVSKEIAPKLAEAGAKVIDLSSDFRMDDDVPYGLPEVNREAIKQA 121
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 1-278 5.70e-40

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 143.76  E-value: 5.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   1 MAVRVGILGATGAVGQRFIQLLE--DHPTFELAALtASESSAGKRYDEAAKwrvntpipdDVAAMEVGstdpADVPDDID 78
Cdd:PLN02383   6 NGPSVAIVGVTGAVGQEFLSVLTdrDFPYSSLKML-ASARSAGKKVTFEGR---------DYTVEELT----EDSFDGVD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  79 LLFSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRDErgwdGALVKNPNCSTITMVPT 158
Cdd:PLN02383  72 IALFSAGGSISKKFGPIAVDKGAVVVDNSSAFRMEEGVPLVIPEVNPEAMKHIKLGKGK----GALIANPNCSTIICLMA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 159 LAALDQ-FGLERVDVTTLQAVSGAGYDGVTSM-----EIID---------------NAIPHIGG--------EEEKMETE 209
Cdd:PLN02383 148 VTPLHRhAKVKRMVVSTYQAASGAGAAAMEELeqqtrEVLEgkpptcnifaqqyafNLFSHNAPmqengyneEEMKLVKE 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 756973779 210 SRKLLGSFDgaevalhgAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDLPSAPEQL 278
Cdd:PLN02383 228 TRKIWNDDD--------VKVTATCIRVPVMRAHAESINLQFEKPLDEATAREILASAPGVKIIDDRANN 288
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 3-148 1.89e-37

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: 132.07  E-value: 1.89e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALtASESSAGKRYDEAAKWRVNTPIPDDVAAMEVGSTDPaDVPDDIDLLFS 82
Cdd:cd24150    2 LKAAILGATGLVGIEYVRMLSNHPYIKPAYL-AGKGSVGKPYGEVVRWQTVGQVPKEIADMEIKPTDP-KLMDDVDIIFS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 756973779  83 SLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQRDERGWDGALVKNP 148
Cdd:cd24150   80 PLPQGAAGPVEEQFAKEGFPVISNSPDHRFDPDVPLLVPELNPHTISLIDEQRKRREWKGFIVTTP 145
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-131 2.05e-36

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: 127.66  E-value: 2.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779     4 RVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRvnTPIPDDVAAMEvgstDPADVpdDIDLLFSS 83
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRSAGKKVSEAGPHL--KGEVVLELDPP----DFEEL--AVDIVFLA 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 756973779    84 LPSSVAAEV---EPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLI 131
Cdd:smart00859  73 LPHGVSKESaplLPRAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIKKA 123
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 159-325 4.44e-34

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: 123.19  E-value: 4.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  159 LAAL-DQFG-LERVDVTTLQAVSGAGYD---GVTSMEIIDNAIPHIGGEEEKMETESRKLLGSFDGAEVALH-GAEVNAS 232
Cdd:pfam02774   1 LKPLrDALGgLERVIVDTYQAVSGAGKKakpGVFGAPIADNLIPYIDGEEHNGTPETREELKMVNETKKILGfTPKVSAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  233 CNRIPTLDGHLESVFADLadDASPEDVAAAMREypgvdLPSAPEQLIHVFEDNFRPQPRLDreRGDGMQISAGGIQ---A 309
Cdd:pfam02774  81 CVRVPVFRGHSETVTVKL--KLKPIDVEEVYEA-----FYAAPGVFVVVRPEEDYPTPRAV--RGGTNFVYVGRVRkdpD 151

                         170
                  ....*....|....*.
gi 756973779  310 TEHGVKYNCLAHNTIR 325
Cdd:pfam02774 152 GDRGLKLVSVIDNLRK 167
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 5-344 4.94e-34

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 128.25  E-value: 4.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   5 VGILGATGAVGQRFIQLLEDHPTFELAALT--ASESSAGKRYDEAAKwrvntpipdDVAAMEVGSTDPadvpDDIDLLFS 82
Cdd:PRK06728   8 VAVVGATGAVGQKIIELLEKETKFNIAEVTllSSKRSAGKTVQFKGR---------EIIIQEAKINSF----EGVDIAFF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  83 SLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLdlievqRDERGwdgaLVKNPNCSTITMVPTLAAL 162
Cdd:PRK06728  75 SAGGEVSRQFVNQAVSSGAIVIDNTSEYRMAHDVPLVVPEVNAHTL------KEHKG----IIAVPNCSALQMVTALQPI 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 163 DQ-FGLERVDVTTLQAVSGAGYDGVTSME---------------------------IIDNAIPHIG--------GEEEKM 206
Cdd:PRK06728 145 RKvFGLERIIVSTYQAVSGSGIHAIQELKeqaksilageevestilpakkdkkhypIAFNVLPQVDiftdndftFEEVKM 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 207 ETESRKLLGSfdgaevalHGAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDLPSAPEQLIHvfednf 286
Cdd:PRK06728 225 IQETKKILED--------PNLKMAATCVRVPVISGHSESVYIELEKEATVAEIKEVLFDAPGVILQDNPSEQLY------ 290

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756973779 287 rPQPRLDRERGDGMqisAGGIQA---TEHGVKYNCLAHNTIRGAAGASVLNGELLAQEGWI 344
Cdd:PRK06728 291 -PMPLYAEGKIDTF---VGRIRKdpdTPNGFHLWIVSDNLLKGAAWNSVQIAETMVEEGII 347
ASADH_C cd18128
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar ...
 150-323 1.99e-31

C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; Aspartate beta-semialdehyde dehydrogenase (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 and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467678 [Multi-domain]  Cd Length: 165  Bit Score: 116.06  E-value: 1.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 150 CSTITMVPTLAAL-DQFGLERVDVTTLQAVSGAGYDgvtsmeIIDNAIPHI--------GGEEEKMETESRKLLGSFDGA 220
Cdd:cd18128    1 CTVSLMLMALGGLfQKFLVEWVSVATYQAVSGAG*P------IAGNLIPWIdvfldngqTKEEWKGQAETNKILGDLDSP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 221 evalhgAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPgvdlpsapeQLIHVFEDNFRPQPRLDRERGDGM 300
Cdd:cd18128   75 ------IPISGTCVRVGVLRCHSQAFTIKLKEDAPIEEVEEAIAAHN---------*WIKVIPNVDRITPRTPANVTGTL 139

                        170       180
                 ....*....|....*....|....*.
gi 756973779 301 QISAGGIQ---ATEHGVKYNCLAHNT 323
Cdd:cd18128  140 STPVGRIRkdaMGPFDLQAFTVGDNL 165
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 4-149 1.80e-30

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: 112.84  E-value: 1.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   4 RVGILGATGAVGQRFIQLLEDHPT--FELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEvgstdpadvpdDIDLLF 81
Cdd:cd02281    2 KVGVVGATGYVGGEFLRLLLEHPFplFEIVLLAASSAGAKKKYFHPKLWGRVLVEFTPEEVLE-----------QVDIVF 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756973779  82 SSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIevqrdergWDGALVKNPN 149
Cdd:cd02281   71 TALPGGVSAKLAPELSEAGVLVIDNASDFRLDKDVPLVVPEVNREHIGEL--------KGTKIIANPN 130
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
 150-271 7.66e-28

C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share 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 and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467681  Cd Length: 188  Bit Score: 107.21  E-value: 7.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 150 CSTITMVPTLAAL-DQFGLERVDVTTLQAVSGAGYDGVTSME--------------------IIDNAIPHIGG------- 201
Cdd:cd18131    1 CSTIQMVVALKPLhDAFGLKRVVVSTYQAVSGAGAAAMEELEeqtrgllngkeaepkvfpyqIAFNVIPHIDVfldngyt 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756973779 202 -EEEKMETESRKLLGSFDgaevalhgAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDL 271
Cdd:cd18131   81 kEEMKMVNETRKILGDPD--------LRVSATCVRVPVFRGHSESVNIEFEKPISVEEAREALAKAPGVVV 143
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 3-149 8.26e-27

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: 103.19  E-value: 8.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDH--PTFELAALtASESSAGKRYdeaakwrvntpiPDDVAAMEVGSTDPADVpDDIDLL 80
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEpdPLFELRAL-ASEESAGKKA------------EFAGEAIMVQEADPIDF-LGLDIV 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLievqrderGWDGALVKNPN 149
Cdd:cd24147   67 FLCAGAGVSAKFAPEAARAGVLVIDNAGALRMDPDVPLVVPEVNAEAIGL--------GEGTPLLVIPN 127
ASADH_C_like cd18124
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 150-323 3.17e-25

C-terminal catalytic 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. These proteins 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: 467674 [Multi-domain]  Cd Length: 193  Bit Score: 100.36  E-value: 3.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 150 CSTITMVPTLAAL-DQFGLERVDVTTLQAVSGAGYD--------------------GVTSMEIIDNAIPHIG-------- 200
Cdd:cd18124    1 CTVSLLVMALKPLfAKFLVEWVSVAT*QAVSGAGYEnmrellsqmgelmragplptGVFS*AIADNLIPWIDkvldngqs 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 201 GEEEKMETESRKLLGSFDGAevalhgAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDLPSAPEQLIh 280
Cdd:cd18124   81 KEEWKIQAEANKILGTLDSP------IPISVTCNRVPVLDGHSQSFTLKLKEDVPLEEVEEVLDAHKPWVKVIPNDYAI- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 756973779 281 vfednfRPQPRLDRERGDGMQISAGGIQATEHG---VKYNCLAHNT 323
Cdd:cd18124  154 ------RPQPRLDRKVTGGLSTPVGRIRKDAMDpfdVNAFAVSDNT 193
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 4-149 1.93e-24

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: 96.74  E-value: 1.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   4 RVGILGATGAVGQRFIQLLED--HPTFELAALtASESSAGKRYDeaAKWRvntpipdDVAAMEVGStdpaDVPDDIDLLF 81
Cdd:cd02316    2 NVAIVGATGAVGQEMLKVLEErnFPVSELRLL-ASARSAGKTLE--FKGK-------ELTVEELTE----DSFKGVDIAL 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756973779  82 SSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLdlievqRDERGwdgaLVKNPN 149
Cdd:cd02316   68 FSAGGSVSKEFAPIAAEAGAVVIDNSSAFRMDPDVPLVVPEVNPEAL------KNHKG----IIANPN 125
ASADH_C_MCR cd23940
C-terminal catalytic domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar ...
 156-323 4.19e-22

C-terminal catalytic domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar proteins; Archaeal NADP-dependent malonyl-CoA reductase (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 and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467689 [Multi-domain]  Cd Length: 185  Bit Score: 91.73  E-value: 4.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 156 VPTLAALDQFGLERVDVTTLQAVSGAGYDGVTSMEIIDNAIPHIGGEEEKMETESRKLLGSF--DGAEVALHGAEVNASC 233
Cdd:cd23940    9 IPLGAIFKDYKMDGAFITTIQSLSGAGYPGIPSLDVVDNILPLGDGYDAKTIKEIFRILSEVkrNVDEPKLEDVSLAATT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 234 NRIPTLDGHLESVFADLADDASPEDVAAAMREYPG----VDLPSAPEQLIHVFEDNFRPQPRLDRERGD--GMQISAGGI 307
Cdd:cd23940   89 HRIATIHGHYEVLYVSFKEETAAEKVKETLENFRGepqdLKLPTAPSKPIIVMNEDTRPQVYFDRWAGDipGMSVVVGRL 168

                        170
                 ....*....|....*..
gi 756973779 308 -QATEHGVKYNCLAHNT 323
Cdd:cd23940  169 kQVNKRMIRLVSLIHNT 185
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 150-316 3.59e-18

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: 80.64  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 150 CSTITMVPTLAAL-DQFGLERVDVTTLQAVSGAGYDGVTSMEI--IDNAIPHIGGEEEKMETESRKLLGSFDGAevalhg 226
Cdd:cd18122    1 CTTTGLIPAAKALnDKFGIEEILVVTVQAVSGAGPKTKGPILKseVRAIIPNIPKNETKHAPETGKVLGEIGKP------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 227 AEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVdlpsapEQLIHvfEDNFRPQPRLDRERGDGMQISAGG 306
Cdd:cd18122   75 IKVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEE------VQISA--EDGLTYAKVSTRSVGGVYGVPVGR 146

                        170
                 ....*....|
gi 756973779 307 IQATEHGVKY 316
Cdd:cd18122  147 QREFAFDDNK 156
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 3-103 7.59e-15

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: 74.34  E-value: 7.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTaSESSAGKRYDEAakwrvntpIPD--DVAAMEVGSTDPADVPDDIDLL 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT-SRSNAGKPVSEV--------HPHlrGLTDLVFEPPDPDELAAGCDVV 71

                         90       100
                 ....*....|....*....|...
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVV 103
Cdd:COG0002   72 FLALPHGVSMELAPELLEAGVKV 94
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 3-103 4.68e-14

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: 68.99  E-value: 4.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTaSESSAGKRYDEAAkwrvntpiPD--DVAAMEVGSTDPADVPDDIDLL 80
Cdd:cd17895    1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALT-SRSYAGKPVSEVF--------PHlrGLTDLTFEPDDDEEIAEDADVV 71

                         90       100
                 ....*....|....*....|...
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVV 103
Cdd:cd17895   72 FLALPHGVSMELAPKLLEAGVKV 94
ASADH_C_USG1_like cd18129
C-terminal domain of USG-1 protein and similar proteins; The family includes Escherichia coli ...
 151-276 7.96e-13

C-terminal 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 its biological function remains unknown, it is found to be homologous 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: 467679  Cd Length: 186  Bit Score: 66.06  E-value: 7.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 151 STITMVPTLAAL-DQFGLERVDVTTLQAVSGAGYDGVTSME--------------------IIDNAIPHIG--------G 201
Cdd:cd18129    2 AAIALARVLAPLhDAAGLERVVVTVLQPVSEAGQAGVDELArqtarllngqpvepevfprqLAFNLLPQVGdfdadglsD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756973779 202 EEEKMETESRKLLGSFDgaevalhgAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDLPSAPE 276
Cdd:cd18129   82 EERRIAAELRRLLGGPD--------LPVSVTCVQVPVFYGHSASVHVELAEPVDLEEVRAALAAAPGLELADDAE 148
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 3-291 7.79e-10

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 59.45  E-value: 7.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTAsESSAGKRYDEAAKWRVNTPIPDDVAamevgsTDPADVpDDIDLLFS 82
Cdd:PLN02968  39 KRIFVLGASGYTGAEVRRLLANHPDFEITVMTA-DRKAGQSFGSVFPHLITQDLPNLVA------VKDADF-SDVDAVFC 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  83 SLPSSVAAEVePEFLEAGYVVSSNSSNDRMAPDV--------PLTIPEINPEHL-DLIEVQRDERGwDGALVKNPNCSTI 153
Cdd:PLN02968 111 CLPHGTTQEI-IKALPKDLKIVDLSADFRLRDIAeyeewyghPHRAPELQKEAVyGLTELQREEIK-SARLVANPGCYPT 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 154 TMVPTLAALDQFGLERVDVTTLQAVSGAGYDGVTSMEI-----IDNAIPHIGGEEEKMETESRKLLgsfdgAEVALHGAE 228
Cdd:PLN02968 189 GIQLPLVPLVKAGLIEPDNIIIDAKSGVSGAGRGAKEAnlyteIAEGIGAYGVTRHRHVPEIEQGL-----ADAAGSKVT 263

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756973779 229 VNASCNRIPTLDGHLESVFADLADDASPEDVAAAMRE-YPGvdlpsapEQLIHVFEDNFRPQPR 291
Cdd:PLN02968 264 PSFTPHLMPMSRGMQSTVYVHYAPGVTAEDLHQHLKErYEG-------EEFVKVLERGAVPHTD 320
PRK08040 PRK08040
putative semialdehyde dehydrogenase; Provisional
 5-182 2.83e-09

putative semialdehyde dehydrogenase; Provisional


Pssm-ID: 181205 [Multi-domain]  Cd Length: 336  Bit Score: 57.78  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   5 VGILGATGAVGQRFIQLLEDH--PTFELAALtASESSAGKRYdeaakwRVNtpipddvaAMEVGSTDPADVP-DDIDLLF 81
Cdd:PRK08040   7 IALLGATGAVGEALLELLAERqfPVGELYAL-ASEESAGETL------RFG--------GKSVTVQDAAEFDwSQAQLAF 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  82 SSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLdlievqRDERGWDgaLVKNPNCSTITMVPTLAA 161
Cdd:PRK08040  72 FVAGREASAAYAEEATNAGCLVIDSSGLFALEPDVPLVVPEVNPFVL------ADYRNRN--IIAVADSLTSQLLTAIKP 143

                        170       180
                 ....*....|....*....|..
gi 756973779 162 L-DQFGLERVDVTTLQAVSGAG 182
Cdd:PRK08040 144 LiDQAGLSRLHVTNLLSASAHG 165
PRK05671 PRK05671
aspartate-semialdehyde dehydrogenase; Reviewed
 5-271 4.45e-09

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 168165 [Multi-domain]  Cd Length: 336  Bit Score: 57.04  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   5 VGILGATGAVGQRFIQLLE--DHPTFELaALTASESSAGKRYDEAAKwrvntpipdDVAAMEVGSTDPADVpddiDLLFS 82
Cdd:PRK05671   7 IAVVGATGTVGEALVQILEerDFPVGTL-HLLASSESAGHSVPFAGK---------NLRVREVDSFDFSQV----QLAFF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779  83 SLPSSVAAEVEPEFLEAGYVVS--SNSSNDRMAPDVpltIPEINPEHLDLIEvqrdergwDGALVKNPNCSTITMVPTLA 160
Cdd:PRK05671  73 AAGAAVSRSFAEKARAAGCSVIdlSGALPSAQAPNV---VPEVNAERLASLA--------APFLVSSPSASAVALAVALA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 161 AL-DQFGLERVDVTTLQAVSGAGYDGVTSM-----EIID---------------NAIPHIG--------GEEEKMETESR 211
Cdd:PRK05671 142 PLkGLLDIQRVQVTACLAVSSLGREGVSELarqtaELLNarpleprffdrqvafNLLAQVGapdaqghtALERRLVAELR 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 212 KLLGsfdgaevaLHGAEVNASCNRIPTLDGHLESVFADLADDASPEDVAAAMREYPGVDL 271
Cdd:PRK05671 222 QLLG--------LPELKISVTCIQVPVFFGDSLSVALQSAAPVDLAAVNAALEAAPGIEL 273
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 3-92 4.78e-09

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: 54.60  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTAsESSAGKRYDEaakwrVNTPIPdDVAAMEVGSTDPADVPdDIDLLFS 82
Cdd:cd24148    1 IRVAVAGASGYAGGELLRLLLGHPEFEIGALTA-HSNAGQRLGE-----LHPHLP-PLADRVLEPTTPAVLA-GHDVVFL 72

                         90
                 ....*....|
gi 756973779  83 SLPSSVAAEV 92
Cdd:cd24148   73 ALPHGASAAI 82
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 3-135 1.51e-08

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: 53.01  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPtFELAALTA--SESSAGKRydeaakwrvntpIPDDVAAMEVGSTDPADVpDDIDLL 80
Cdd:cd17894    1 YRIAVVGATGLVGKELLELLEERG-FPVGRLRLldSEESAGEL------------VEFGGEPLDVQDLDEFDF-SDVDLV 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 756973779  81 FSSLPSSVAAEVEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLDLIEVQR 135
Cdd:cd17894   67 FFAGPAEVARAYAPRARAAGCLVIDLSGALRSDPDVPLVVPGVNPEALAAAAERR 121
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 4-90 4.17e-08

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: 51.73  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   4 RVGILGATGAVGQRFIQLLEDHPTFELAAltASESS-AGKR---YDEAAKWRVN---TPIPDDVAAMEVgstdpadvpdd 76
Cdd:cd24149    2 RVGLIGARGYVGRELIRLLNRHPNLELAH--VSSRElAGQKvsgYTKSPIDYLNlsvEDIPEEVAAREV----------- 68

                         90
                 ....*....|....
gi 756973779  77 iDLLFSSLPSSVAA 90
Cdd:cd24149   69 -DAWVLALPNGVAK 81
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 4-149 2.14e-06

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: 47.18  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   4 RVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAakwrvntpiPDDVAAMEVGSTDPADVPDDIDLLFSS 83
Cdd:cd02280    2 RVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYH---------PSLIISLQIQEFRPCEVLNSADILVLA 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756973779  84 LPSSVAAEvEPEFLEAGYVVSSNSSNDRMAPDVPLTIPEINPEHLD-----LIEVQRDERGWDGALVKNPN 149
Cdd:cd02280   73 LPHGASAE-LVAAISNPQVKIIDLSADFRFTDPEVYRRHPRPDLEGgwvygLPELDREQRIANATRIANPN 142
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 3-137 7.50e-06

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: 45.73  E-value: 7.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTaSESSAGKRYDEA-AKWRVNTPIpddvaamevgSTDPADVPDDIDLLF 81
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVT-SESLAGKPVHRVhPNLRGRTLL----------KFVPPEELESCDVLF 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756973779  82 SSLPSSVAAEVEPEFLEAGYVVSSNSSNDRmapdvpLTIPEI----------NPEHLD-----LIEVQRDE 137
Cdd:cd24151   70 LALPHGESMKRIDRFAELAPRIIDLSADFR------LKDPAAydrwyggphpRPELLErfvygLPELHREE 134
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 3-93 3.77e-05

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


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 42.60  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779    3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIpddvaamevgSTDPADVPDDIDLL-- 80
Cdd:pfam01113   1 IKIAVAGASGRMGRELIKAVLEAPDLELVAAVDRPGSSLLGSDAGELAPLGVPV----------TDDLEEVLADADVLid 70

                          90
                  ....*....|...
gi 756973779   81 FSSlPSSVAAEVE 93
Cdd:pfam01113  71 FTT-PEATLENLE 82
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 3-73 3.34e-04

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


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 40.24  E-value: 3.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756973779   3 VRVGILGATGAVGQRFIQLLEDHPTFELAALTASESSAGKRYDEAAKWRVNTPIPDDVAAMEVgsTDPADV 73
Cdd:cd02274    1 IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGGLAGIGTGVIVSLDLELA--AADADV 69
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 3-105 7.52e-04

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 39.45  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779   3 VRVGILGaTGAVGQRFIQLLEDHPTFEL-AALTASESSAGKRYDEAAKWR-VNTPIPDDVAAmeVGSTDPADVpddidLL 80
Cdd:cd24146    1 IRVVVWG-LGAMGRGIARYLLEKPGLEIvGAVDRDPAKVGKDLGELGGGApLGVKVTDDLDA--VLAATKPDV-----VV 72

                         90       100
                 ....*....|....*....|....*....
gi 756973779  81 FSslPSSVAAEVEPEF---LEAGY-VVSS 105
Cdd:cd24146   73 HA--TTSFLADVAPQIerlLEAGLnVITT 99
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 150-267 3.34e-03

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467673  Cd Length: 164  Bit Score: 37.98  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756973779 150 CSTITMVPTLAAL-DQFGLERVDVTTLQAVSG--------AGYDGVTSMEIIDNAIPHIGGEEEKMETESRKLLGSFDGA 220
Cdd:cd18123    1 CTTNCLAPLAKAIhDSFGIKKGRMTTVHAATDtqktvdgpSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 756973779 221 EValhgaevnascnRIPTLDGHLESVFADLADDASPEDVAAAMREYP 267
Cdd:cd18123   81 AV------------RVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAP 115
 
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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