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Conserved domains on  [gi|1288424414|ref|WP_100536778|]
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MULTISPECIES: aspartate-semialdehyde dehydrogenase [Paenibacillus]

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
 2-358 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


:

Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 600.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   2 SEKLKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEESVqgRWKLATPIPEQVKGIVVQdASQVEQVAaE 81
Cdd:PRK08664    1 MMKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAV--RWQLDGPIPEEVADMEVV-STDPEAVD-D 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  82 VDFVFCAvdMKKNEIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVIAAQRKRLGTTtGFIAVKPNCSIQ 161
Cdd:PRK08664   77 VDIVFSA--LPSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWD-GFIVTNPNCSTI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 162 SYVPALHALLDYKPTHVVASTYQAISGAGKNFTDWPDMLDNVIPYIGGEEEKSEQEPLRIWGSVVNGEIVKAQSPlITTQ 241
Cdd:PRK08664  154 GLVLALKPLMDFGIERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFP-ISAT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 242 CIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSAPKQFITYFEEENRPQTKLDRDIERGMGVSVGRLR 321
Cdd:PRK08664  233 CHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFKGLPQELGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRLR 312

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1288424414 322 EDSLYDYKFVGLSHNTLRGAAGGAVLIAELLKAEGYI 358
Cdd:PRK08664  313 EDGIFDIKFVVLGHNTVRGAAGASVLNAELLKKKGYL 349
 
Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 2-358 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 600.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   2 SEKLKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEESVqgRWKLATPIPEQVKGIVVQdASQVEQVAaE 81
Cdd:PRK08664    1 MMKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAV--RWQLDGPIPEEVADMEVV-STDPEAVD-D 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  82 VDFVFCAvdMKKNEIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVIAAQRKRLGTTtGFIAVKPNCSIQ 161
Cdd:PRK08664   77 VDIVFSA--LPSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWD-GFIVTNPNCSTI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 162 SYVPALHALLDYKPTHVVASTYQAISGAGKNFTDWPDMLDNVIPYIGGEEEKSEQEPLRIWGSVVNGEIVKAQSPlITTQ 241
Cdd:PRK08664  154 GLVLALKPLMDFGIERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFP-ISAT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 242 CIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSAPKQFITYFEEENRPQTKLDRDIERGMGVSVGRLR 321
Cdd:PRK08664  233 CHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFKGLPQELGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRLR 312

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1288424414 322 EDSLYDYKFVGLSHNTLRGAAGGAVLIAELLKAEGYI 358
Cdd:PRK08664  313 EDGIFDIKFVVLGHNTVRGAAGASVLNAELLKKKGYL 349
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 5-353 4.54e-119

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: 347.90  E-value: 4.54e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEESVQgrWKLATPIPEQVKGIVVqdaSQVEQVAAE-VD 83
Cdd:TIGR00978   1 MRVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAVK--WIEPGDMPEYVRDLPI---VEPEPVASKdVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  84 FVFCAVDMKKNEiqALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVIAAQRKRlgTTTGFIAVKPNCSIQSY 163
Cdd:TIGR00978  76 IVFSALPSEVAE--EVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQKER--GWKGFIVTNPNCTTAGL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 164 VPALHALLD-YKPTHVVASTYQAISGAGKNFTDWPDMLDNVIPYIGGEEEKSEQEPLRIWGSVVNGEIVKAQSPLITTqC 242
Cdd:TIGR00978 152 TLALKPLIDaFGIKKVHVTTMQAVSGAGYPGVPSMDILDNIIPHIGGEEEKIERETRKILGKLENGKIEPAPFSVSAT-T 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 243 IRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSAPKQFITYFEEENRPQTKLDRDIERGMGVSVGRLRE 322
Cdd:TIGR00978 231 TRVPVLDGHTESVHVEFDKKFDIEEIREALKSFRGLPQKLGLPSAPEKPIIVRDEEDRPQPRLDRDAGGGMAVTVGRLRE 310

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1288424414 323 DSLyDYKFVGLSHNTLRGAAGGAVLIAELLK 353
Cdd:TIGR00978 311 EGG-SLKYVVLGHNLVRGAAGATLLNAELAY 340
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 158-337 2.22e-74

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: 227.89  E-value: 2.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 158 CSIQSYVPALHALLD-YKPTHVVASTYQAISGAGKNFTDWPDMLDNVIPYIGGEEEKSEQEPLRIWGSVVNGEIVKAqSP 236
Cdd:cd18130     1 CSTAGLALPLKPLHDfFGIEAVIVTTMQAISGAGYPGVPSLDILDNVIPYIGGEEEKIESETKKILGTLNEDKIEPA-DF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 237 LITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSAPKQFITYFEEENRPQTKLDRDIERGMGVS 316
Cdd:cd18130    80 KVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPQVLGPPSAPKPIIVVEDEPRRPQPRLDRDAGDGMAVT 159

                         170       180
                  ....*....|....*....|.
gi 1288424414 317 VGRLREDSLYDYKFVGLSHNT 337
Cdd:cd18130   160 VGRIRKDDDFDLKFVLLSHNT 180
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 6-136 3.47e-39

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


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 135.37  E-value: 3.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414    6 KVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEESVqgrwklatpipEQVKGIVVQDASQVEQVAAEVDFV 85
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRSAGKKVSEAG-----------PHLKGEVVLELDPPDFEELAVDIV 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1288424414   86 FCAVDMKK-NEIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHID 136
Cdd:smart00859  70 FLALPHGVsKESAPLLPRAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIK 121
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-138 1.08e-38

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: 134.19  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   6 KVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEEsvqgrwklATPIPEQVKGIVVQDASqvEQVAAEVDFV 85
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSAGKKLAF--------VHPILEGGKDLVVEDVD--PEDFKDVDIV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1288424414  86 FCAVDmkkNEI-QALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVI 138
Cdd:pfam01118  71 FFALP---GGVsKEIAPKLAEAGAKVIDLSSDFRMDDDVPYGLPEVNREAIKQA 121
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 5-352 1.17e-38

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: 140.55  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLD--GHPWFEVTSIsASRNSAGKTYeeSVQGrwklatpipeqvKGIVVQDASqvEQVAAEV 82
Cdd:COG0136     1 YNVAVVGATGAVGRVLLELLEerDFPVGELRLL-ASSRSAGKTV--SFGG------------KELTVEDAT--DFDFSGV 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  83 DFV-FCA-VDMKKneiqALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPghiDVIAAQRKRlgtttGFIAVkPNCS- 159
Cdd:COG0136    64 DIAlFSAgGSVSK----EYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNP---EALADHLPK-----GIIAN-PNCSt 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 160 IQSyVPALHALLD-YKPTHVVASTYQAISGAGKN--------FTDWPDMLD------------NVIPYIGG--------E 210
Cdd:COG0136   131 IQM-LVALKPLHDaAGIKRVVVSTYQAVSGAGAAamdelaeqTAALLNGEEiepevfphpiafNLIPQIDVflengytkE 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 211 EEKSEQEPLRIWGSvvnGEIvkaqspLITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKG-----RPQELNLP 285
Cdd:COG0136   210 EMKMVNETRKILGD---PDI------PVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAAPGvkvvdDPAENDYP 280

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288424414 286 SApkqfityfeeenrpqtkldRDIERGMGVSVGRLREDSLYDYkfvGL-----SHNTLRGAAGGAVLIAELL 352
Cdd:COG0136   281 TP-------------------LDASGTDEVFVGRIRKDLSVPN---GLnlwvvADNLRKGAALNAVQIAELL 330
 
Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 2-358 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 600.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   2 SEKLKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEESVqgRWKLATPIPEQVKGIVVQdASQVEQVAaE 81
Cdd:PRK08664    1 MMKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAV--RWQLDGPIPEEVADMEVV-STDPEAVD-D 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  82 VDFVFCAvdMKKNEIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVIAAQRKRLGTTtGFIAVKPNCSIQ 161
Cdd:PRK08664   77 VDIVFSA--LPSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWD-GFIVTNPNCSTI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 162 SYVPALHALLDYKPTHVVASTYQAISGAGKNFTDWPDMLDNVIPYIGGEEEKSEQEPLRIWGSVVNGEIVKAQSPlITTQ 241
Cdd:PRK08664  154 GLVLALKPLMDFGIERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFP-ISAT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 242 CIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSAPKQFITYFEEENRPQTKLDRDIERGMGVSVGRLR 321
Cdd:PRK08664  233 CHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFKGLPQELGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRLR 312

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1288424414 322 EDSLYDYKFVGLSHNTLRGAAGGAVLIAELLKAEGYI 358
Cdd:PRK08664  313 EDGIFDIKFVVLGHNTVRGAAGASVLNAELLKKKGYL 349
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 5-353 4.54e-119

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: 347.90  E-value: 4.54e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEESVQgrWKLATPIPEQVKGIVVqdaSQVEQVAAE-VD 83
Cdd:TIGR00978   1 MRVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAVK--WIEPGDMPEYVRDLPI---VEPEPVASKdVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  84 FVFCAVDMKKNEiqALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVIAAQRKRlgTTTGFIAVKPNCSIQSY 163
Cdd:TIGR00978  76 IVFSALPSEVAE--EVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQKER--GWKGFIVTNPNCTTAGL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 164 VPALHALLD-YKPTHVVASTYQAISGAGKNFTDWPDMLDNVIPYIGGEEEKSEQEPLRIWGSVVNGEIVKAQSPLITTqC 242
Cdd:TIGR00978 152 TLALKPLIDaFGIKKVHVTTMQAVSGAGYPGVPSMDILDNIIPHIGGEEEKIERETRKILGKLENGKIEPAPFSVSAT-T 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 243 IRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSAPKQFITYFEEENRPQTKLDRDIERGMGVSVGRLRE 322
Cdd:TIGR00978 231 TRVPVLDGHTESVHVEFDKKFDIEEIREALKSFRGLPQKLGLPSAPEKPIIVRDEEDRPQPRLDRDAGGGMAVTVGRLRE 310

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1288424414 323 DSLyDYKFVGLSHNTLRGAAGGAVLIAELLK 353
Cdd:TIGR00978 311 EGG-SLKYVVLGHNLVRGAAGATLLNAELAY 340
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 158-337 2.22e-74

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: 227.89  E-value: 2.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 158 CSIQSYVPALHALLD-YKPTHVVASTYQAISGAGKNFTDWPDMLDNVIPYIGGEEEKSEQEPLRIWGSVVNGEIVKAqSP 236
Cdd:cd18130     1 CSTAGLALPLKPLHDfFGIEAVIVTTMQAISGAGYPGVPSLDILDNVIPYIGGEEEKIESETKKILGTLNEDKIEPA-DF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 237 LITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSAPKQFITYFEEENRPQTKLDRDIERGMGVS 316
Cdd:cd18130    80 KVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPQVLGPPSAPKPIIVVEDEPRRPQPRLDRDAGDGMAVT 159

                         170       180
                  ....*....|....*....|.
gi 1288424414 317 VGRLREDSLYDYKFVGLSHNT 337
Cdd:cd18130   160 VGRIRKDDDFDLKFVLLSHNT 180
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 5-160 4.75e-74

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: 226.60  E-value: 4.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEESVqgRWKLATPIPEQVKGIVVQDASQVEqvAAEVDF 84
Cdd:cd02315     1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERSAGKKYGDAV--RWKQDTPIPEEVADMVVKECEPEE--FKDCDI 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288424414  85 VFCAVDmkKNEIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVIAAQRKRLGtTTGFIAVKPNCSI 160
Cdd:cd02315    77 VFSALD--SDVAGEIEPAFAKAGIPVFSNASNHRMDPDVPLVIPEVNPDHLDLIEAQRKRRG-WKGFIVTNPNNTV 149
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 6-136 3.47e-39

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


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 135.37  E-value: 3.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414    6 KVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEESVqgrwklatpipEQVKGIVVQDASQVEQVAAEVDFV 85
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRSAGKKVSEAG-----------PHLKGEVVLELDPPDFEELAVDIV 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1288424414   86 FCAVDMKK-NEIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHID 136
Cdd:smart00859  70 FLALPHGVsKESAPLLPRAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIK 121
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-138 1.08e-38

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: 134.19  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   6 KVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNSAGKTYEEsvqgrwklATPIPEQVKGIVVQDASqvEQVAAEVDFV 85
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSAGKKLAF--------VHPILEGGKDLVVEDVD--PEDFKDVDIV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1288424414  86 FCAVDmkkNEI-QALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVI 138
Cdd:pfam01118  71 FFALP---GGVsKEIAPKLAEAGAKVIDLSSDFRMDDDVPYGLPEVNREAIKQA 121
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 5-352 1.17e-38

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: 140.55  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLD--GHPWFEVTSIsASRNSAGKTYeeSVQGrwklatpipeqvKGIVVQDASqvEQVAAEV 82
Cdd:COG0136     1 YNVAVVGATGAVGRVLLELLEerDFPVGELRLL-ASSRSAGKTV--SFGG------------KELTVEDAT--DFDFSGV 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  83 DFV-FCA-VDMKKneiqALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPghiDVIAAQRKRlgtttGFIAVkPNCS- 159
Cdd:COG0136    64 DIAlFSAgGSVSK----EYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNP---EALADHLPK-----GIIAN-PNCSt 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 160 IQSyVPALHALLD-YKPTHVVASTYQAISGAGKN--------FTDWPDMLD------------NVIPYIGG--------E 210
Cdd:COG0136   131 IQM-LVALKPLHDaAGIKRVVVSTYQAVSGAGAAamdelaeqTAALLNGEEiepevfphpiafNLIPQIDVflengytkE 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 211 EEKSEQEPLRIWGSvvnGEIvkaqspLITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKG-----RPQELNLP 285
Cdd:COG0136   210 EMKMVNETRKILGD---PDI------PVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAAPGvkvvdDPAENDYP 280

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288424414 286 SApkqfityfeeenrpqtkldRDIERGMGVSVGRLREDSLYDYkfvGL-----SHNTLRGAAGGAVLIAELL 352
Cdd:COG0136   281 TP-------------------LDASGTDEVFVGRIRKDLSVPN---GLnlwvvADNLRKGAALNAVQIAELL 330
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 6-352 1.15e-35

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 132.97  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   6 KVGIVGGTGMVGQRFMQLLDGHPwFEVTSIS--ASRNSAGKtyeesvqgrwKLATpipeQVKGIVVQDASqvEQVAAEVD 83
Cdd:PLN02383    9 SVAIVGVTGAVGQEFLSVLTDRD-FPYSSLKmlASARSAGK----------KVTF----EGRDYTVEELT--EDSFDGVD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  84 FVFCAVD----MKKNEIQAleeayaKTGTPVISNNSAHRWTPDVPMVIPEINPGhidviAAQRKRLGTTTGFIAVKPNCS 159
Cdd:PLN02383   72 IALFSAGgsisKKFGPIAV------DKGAVVVDNSSAFRMEEGVPLVIPEVNPE-----AMKHIKLGKGKGALIANPNCS 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 160 iqsyvpALHALLDYKPTH-------VVASTYQAISGAGK---------------------NFTDWPDMLdNVIPYIGG-- 209
Cdd:PLN02383  141 ------TIICLMAVTPLHrhakvkrMVVSTYQAASGAGAaameeleqqtrevlegkpptcNIFAQQYAF-NLFSHNAPmq 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 210 ------EEEKSEQEPLRIWGsvvngeivkAQSPLITTQCIRVPVTDGHLATVFASFENKPSKDEILDRwqqfkgrpqeln 283
Cdd:PLN02383  214 engyneEEMKLVKETRKIWN---------DDDVKVTATCIRVPVMRAHAESINLQFEKPLDEATAREI------------ 272

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288424414 284 LPSAPKQFITYFEEENR---PQTKLDRDiergmGVSVGRLREDSLYDYKFvGLS-----HNTLRGAAGGAVLIAELL 352
Cdd:PLN02383  273 LASAPGVKIIDDRANNRfptPLDASNKD-----DVAVGRIRQDISQDGNK-GLDifvcgDQIRKGAALNAVQIAELL 343
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 175-339 3.78e-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: 123.58  E-value: 3.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 175 PTHVVASTYQAISGAGKNFTdwPDM-----LDNVIPYIGGEEEKSEQEPLRIWGSVVNGEIVKAQSPLITTQCIRVPVTD 249
Cdd:pfam02774  11 LERVIVDTYQAVSGAGKKAK--PGVfgapiADNLIPYIDGEEHNGTPETREELKMVNETKKILGFTPKVSATCVRVPVFR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 250 GHLATVFASFenKPSKDEILDRWQQFKGrpqelnlpsAPKQFITYFEEENRPQTKLDRDIerGMGVSVGRLREDSLYDY- 328
Cdd:pfam02774  89 GHSETVTVKL--KLKPIDVEEVYEAFYA---------APGVFVVVRPEEDYPTPRAVRGG--TNFVYVGRVRKDPDGDRg 155

                         170
                  ....*....|..
gi 1288424414 329 -KFVGLSHNTLR 339
Cdd:pfam02774 156 lKLVSVIDNLRK 167
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
 4-352 1.29e-30

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 118.72  E-value: 1.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   4 KLKVGIVGGTGMVGQRFMQLLDGHPwFEVTSIS--ASRNSAGKTyeesvqgrwklatpIPEQVKGIVVQDASqvEQVAAE 81
Cdd:PRK14874    1 GYNVAVVGATGAVGREMLNILEERN-FPVDKLRllASARSAGKE--------------LSFKGKELKVEDLT--TFDFSG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  82 VDFV-FCA-VDMKKneiqALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPghiDVIAAQRKRlgtttGFIAvKPNCS 159
Cdd:PRK14874   64 VDIAlFSAgGSVSK----KYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNP---EALAEHRKK-----GIIA-NPNCS 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 160 -IQSyVPALHALLD-YKPTHVVASTYQAISGAGK--------------NFTDWPDMLD--------NVIPYIG------- 208
Cdd:PRK14874  131 tIQM-VVALKPLHDaAGIKRVVVSTYQAVSGAGKagmeelfeqtravlNAAVDPVEPKkfpkpiafNVIPHIDvfmddgy 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 209 -GEEEKSEQEPLRIWGSvvngeivkaQSPLITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGrpQELNLPSA 287
Cdd:PRK14874  210 tKEEMKMVNETKKILGD---------PDLKVSATCVRVPVFTGHSESVNIEFEEPISVEEAREILAEAPG--VVLVDDPE 278

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288424414 288 PKQFITyfeeenrPQTKLDRDiergmGVSVGRLREDsLYDYKFVGL---SHNTLRGAAGGAVLIAELL 352
Cdd:PRK14874  279 NGGYPT-------PLEAVGKD-----ATFVGRIRKD-LTVENGLHLwvvSDNLRKGAALNAVQIAELL 333
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 5-156 2.46e-26

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: 102.79  E-value: 2.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPWFEVTSIsASRNSAGKTYEESVqgRWKLATPIPEQVKGIVVQDASqvEQVAAEVDF 84
Cdd:cd24150     2 LKAAILGATGLVGIEYVRMLSNHPYIKPAYL-AGKGSVGKPYGEVV--RWQTVGQVPKEIADMEIKPTD--PKLMDDVDI 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288424414  85 VFCAvdMKKNEIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVIAAQRKRLgTTTGFIAVKP 156
Cdd:cd24150    77 IFSP--LPQGAAGPVEEQFAKEGFPVISNSPDHRFDPDVPLLVPELNPHTISLIDEQRKRR-EWKGFIVTTP 145
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 1-358 1.58e-21

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 93.96  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   1 MSEK-LKVGIVGGTGMVGQRFMQLLDGHPWFEVTSIS--ASRNSAGKTYEesVQGRwklatpipeqvkGIVVQDASQVEQ 77
Cdd:PRK06728    1 MSEKgYHVAVVGATGAVGQKIIELLEKETKFNIAEVTllSSKRSAGKTVQ--FKGR------------EIIIQEAKINSF 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  78 VAAEVDFVFCAVDMKKneiQALEEAYAkTGTPVISNNSAHRWTPDVPMVIPEINPghidviaaqrKRLGTTTGFIAVkPN 157
Cdd:PRK06728   67 EGVDIAFFSAGGEVSR---QFVNQAVS-SGAIVIDNTSEYRMAHDVPLVVPEVNA----------HTLKEHKGIIAV-PN 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 158 CSIQSYVPALHALLD-YKPTHVVASTYQAISGAGKNFTDwpDMLDNVIPYIGGEEEKSEQEPLR-------IWGSVV--- 226
Cdd:PRK06728  132 CSALQMVTALQPIRKvFGLERIIVSTYQAVSGSGIHAIQ--ELKEQAKSILAGEEVESTILPAKkdkkhypIAFNVLpqv 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 227 ------------------NGEIVKAQSPLITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNlPSAP 288
Cdd:PRK06728  210 diftdndftfeevkmiqeTKKILEDPNLKMAATCVRVPVISGHSESVYIELEKEATVAEIKEVLFDAPGVILQDN-PSEQ 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1288424414 289 KQFITYFEEenrpqTKLDrdiergmgVSVGRLRE--DSLYDYKFVGLSHNTLRGAAGGAVLIAELLKAEGYI 358
Cdd:PRK06728  289 LYPMPLYAE-----GKID--------TFVGRIRKdpDTPNGFHLWIVSDNLLKGAAWNSVQIAETMVEEGII 347
ASADH_C_MCR cd23940
C-terminal catalytic domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar ...
 158-337 1.91e-20

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: 87.50  E-value: 1.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 158 CSIQ-SYVPALHALLDYKPTHVVASTYQAISGAGKNFTDWPDMLDNVIPYIGGEEEKSEQEPLRIWGSVVNgeivKAQSP 236
Cdd:cd23940     2 CTAQgAAIPLGAIFKDYKMDGAFITTIQSLSGAGYPGIPSLDVVDNILPLGDGYDAKTIKEIFRILSEVKR----NVDEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 237 LITTQCI-----RVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSAPKQFITYFEEENRPQTKLDR--DI 309
Cdd:cd23940    78 KLEDVSLaatthRIATIHGHYEVLYVSFKEETAAEKVKETLENFRGEPQDLKLPTAPSKPIIVMNEDTRPQVYFDRwaGD 157

                         170       180
                  ....*....|....*....|....*...
gi 1288424414 310 ERGMGVSVGRLREDSLYDYKFVGLSHNT 337
Cdd:cd23940   158 IPGMSVVVGRLKQVNKRMIRLVSLIHNT 185
ASADH_C cd18128
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar ...
 158-337 1.24e-19

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: 84.86  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 158 CSIQSYVPALHALLDYKPTH-VVASTYQAISGAGKnftdwpDMLDNVIPYI--------GGEEEKSEQEPLRIWGSvvng 228
Cdd:cd18128     1 CTVSLMLMALGGLFQKFLVEwVSVATYQAVSGAG*------PIAGNLIPWIdvfldngqTKEEWKGQAETNKILGD---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 229 eivkAQSPL-ITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGrpqelnlpsapkqFITYFEEENRPQTKLDR 307
Cdd:cd18128    71 ----LDSPIpISGTCVRVGVLRCHSQAFTIKLKEDAPIEEVEEAIAAHN*-------------WIKVIPNVDRITPRTPA 133

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1288424414 308 DIERGMGVSVGRLREDSL--YDYKFVGLSHNT 337
Cdd:cd18128   134 NVTGTLSTPVGRIRKDAMgpFDLQAFTVGDNL 165
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 5-132 3.89e-19

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: 82.48  E-value: 3.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPwFEVTSIS--ASRNSAGKTYEesVQGrwklatpipeqvKGIVVQDASqvEQVAAEV 82
Cdd:cd02316     1 YNVAIVGATGAVGQEMLKVLEERN-FPVSELRllASARSAGKTLE--FKG------------KELTVEELT--EDSFKGV 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1288424414  83 DFVFCAV--DMKKneiqALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINP 132
Cdd:cd02316    64 DIALFSAggSVSK----EFAPIAAEAGAVVIDNSSAFRMDPDVPLVVPEVNP 111
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 5-135 9.12e-17

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: 76.22  E-value: 9.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPW--FEVTSISASRnSAGKTYEESVQGrwklatpipeqvkgIVVQDASQVEqvAAEV 82
Cdd:cd24147     1 LRVGVVGATGAVGSEILQLLAEEPDplFELRALASEE-SAGKKAEFAGEA--------------IMVQEADPID--FLGL 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1288424414  83 DFVFCAVDMKKneIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHI 135
Cdd:cd24147    64 DIVFLCAGAGV--SAKFAPEAARAGVLVIDNAGALRMDPDVPLVVPEVNAEAI 114
ASADH_C_like cd18124
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 158-337 7.68e-16

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: 74.93  E-value: 7.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 158 CSIQSYVPALHALLDYKPTH-VVASTYQAISGAGKNF------------------TDWPD--MLDNVIPYIG-------- 208
Cdd:cd18124     1 CTVSLLVMALKPLFAKFLVEwVSVAT*QAVSGAGYENmrellsqmgelmragplpTGVFS*aIADNLIPWIDkvldngqs 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 209 GEEEKSEQEPLRIWGSvvngeivkAQSPL-ITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGRPQELNLPSA 287
Cdd:cd18124    81 KEEWKIQAEANKILGT--------LDSPIpISVTCNRVPVLDGHSQSFTLKLKEDVPLEEVEEVLDAHKPWVKVIPNDYA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1288424414 288 PkqfityfeeenRPQTKLDRDIERGMGVSVGRLREDSL--YDYKFVGLSHNT 337
Cdd:cd18124   153 I-----------RPQPRLDRKVTGGLSTPVGRIRKDAMdpFDVNAFAVSDNT 193
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 6-136 1.46e-15

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: 72.78  E-value: 1.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   6 KVGIVGGTGMVGQRFMQLLDGHPW--FEVTSISASRNSAGKTYEESVQGRWKLATPIPEQVKGivvqdasqveqvaaEVD 83
Cdd:cd02281     2 KVGVVGATGYVGGEFLRLLLEHPFplFEIVLLAASSAGAKKKYFHPKLWGRVLVEFTPEEVLE--------------QVD 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1288424414  84 FVFCAVDMKKNEiqALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHID 136
Cdd:cd02281    68 IVFTALPGGVSA--KLAPELSEAGVLVIDNASDFRLDKDVPLVVPEVNREHIG 118
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
 158-323 4.71e-12

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: 64.07  E-value: 4.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 158 CS-IQSyVPALHALLD-YKPTHVVASTYQAISGAGKNFTD-------------------WPDMLD-NVIPYIGG------ 209
Cdd:cd18131     1 CStIQM-VVALKPLHDaFGLKRVVVSTYQAVSGAGAAAMEeleeqtrgllngkeaepkvFPYQIAfNVIPHIDVfldngy 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 210 --EEEKSEQEPLRIWGSvvngeivkaQSPLITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGrpqelnlpsa 287
Cdd:cd18131    80 tkEEMKMVNETRKILGD---------PDLRVSATCVRVPVFRGHSESVNIEFEKPISVEEAREALAKAPG---------- 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1288424414 288 pkqfITYFE--EENRPQTKLD---RDiergmGVSVGRLRED 323
Cdd:cd18131   141 ----VVVVDdpANNVYPTPLDaagKD-----DVFVGRIRKD 172
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 5-346 9.47e-12

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: 65.48  E-value: 9.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISaSRNSAGKTYEE---SVQGRWKLatpipeqvkgiVVQDASqVEQVAAE 81
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT-SRSNAGKPVSEvhpHLRGLTDL-----------VFEPPD-PDELAAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  82 VDFVFCAVD----MKknEIQALEEAyaktGTPVI--SNnsAHR------------WTPDVPMVI-------PEINPghiD 136
Cdd:COG0002    68 CDVVFLALPhgvsME--LAPELLEA----GVKVIdlSA--DFRlkdpavyekwygFEHAAPELLgeavyglPELNR---E 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 137 VIAAQRkrlgtttgFIAVkPNC---SIQ-SYVPALHA-LLDYKPTHVVASTyqAISGAGKN------FtdwPDMLDNVIP 205
Cdd:COG0002   137 EIKGAR--------LIAN-PGCyptAVLlALAPLLKAgLIDPDDIIIDAKS--GVSGAGRKasegthF---SEVNENFRA 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 206 Y-IGG-------EEEkseqepLriwgSVVNGEIVKAQ-SPlittqcIRVPVTDGHLATVFASFENKPSKDEILDRWQQF- 275
Cdd:COG0002   203 YkVGGhrhtpeiEQE------L----SRLAGEDVKVSfTP------HLVPMVRGILATIYARLKDGVTEEDLRAAYEEFy 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 276 KGRPqelnlpsapkqFITYFEEENRPQTK-------------LDRDIERGMGVSVgrlrEDslydykfvglshNTLRGAA 342
Cdd:COG0002   267 ADEP-----------FVRVLPEGRLPETKsvrgsnfcdigvaVDERTGRLVVVSA----ID------------NLVKGAA 319


                  ....
gi 1288424414 343 GGAV 346
Cdd:COG0002   320 GQAV 323
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 158-337 3.32e-11

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: 61.00  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 158 CSIQSYVPALHALLD-YKPTHVVASTYQAISGAGKNfTDWP---DMLDNVIPYIGGEEEKSEQEplriwgsvVNGEIVKA 233
Cdd:cd18122     1 CTTTGLIPAAKALNDkFGIEEILVVTVQAVSGAGPK-TKGPilkSEVRAIIPNIPKNETKHAPE--------TGKVLGEI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 234 QSPL-ITTQCIRVPVTDGHLATVFASFENKPSKDEILDrwqqfkgrpqelNLPSAPKQFITYFEEENRPQTKLDRDIERG 312
Cdd:cd18122    72 GKPIkVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAE------------AVAEAVEEVQISAEDGLTYAKVSTRSVGGV 139

                         170       180
                  ....*....|....*....|....*..
gi 1288424414 313 MGVSVGRLREDSLYDY--KFVGLSHNT 337
Cdd:cd18122   140 YGVPVGRQREFAFDDNklKVFSAVDNE 166
PRK08040 PRK08040
putative semialdehyde dehydrogenase; Provisional
 1-355 7.12e-10

putative semialdehyde dehydrogenase; Provisional


Pssm-ID: 181205 [Multi-domain]  Cd Length: 336  Bit Score: 59.71  E-value: 7.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   1 MSEKLKVGIVGGTGMVGQRFMQLLD--GHPWFEVTSIsASRNSAGKTYEesVQGrwklatpipeqvKGIVVQDASQVEQV 78
Cdd:PRK08040    1 MSEGWNIALLGATGAVGEALLELLAerQFPVGELYAL-ASEESAGETLR--FGG------------KSVTVQDAAEFDWS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  79 AAEVDFvFCAvdMKKNEIQALEEAyAKTGTPVISNNSAHRWTPDVPMVIPEINPghiDVIAAQRKRlgtttGFIAVkPNC 158
Cdd:PRK08040   66 QAQLAF-FVA--GREASAAYAEEA-TNAGCLVIDSSGLFALEPDVPLVVPEVNP---FVLADYRNR-----NIIAV-ADS 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 159 SIQSYVPALHALLDYKP-THVVASTYQAISGAGKNFTD---------------WPDMLD-----NVIPYIgGEEEKSEQE 217
Cdd:PRK08040  133 LTSQLLTAIKPLIDQAGlSRLHVTNLLSASAHGKAAVDalagqsakllngipiEEGFFGrqlafNMLPLL-PDSEGSVRE 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 218 PLRIWGSVvnGEIVKAQSPLITTQCIRVPVTDGHLATVfaSFEN-KP-SKDEILDRWQQFKGrpqelnlpsapkqfITYF 295
Cdd:PRK08040  212 ERRLVDQV--RKILQDEGLPISVSCVQSPVFYGHAQMV--HFEAlRPlAAEEARDALEQGED--------------IVLS 273

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288424414 296 EEENRPqTKLDrDIERGMGVSVGRLREdslyDY------KFVGLSHNTLRGAAGGAVLIAELLKAE 355
Cdd:PRK08040  274 EENDYP-TQVG-DASGNPHLSIGCVRN----DYgmpeqlQFWSVADNVRFGGALMAVKTAEKLVQE 333
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 5-89 1.38e-09

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: 56.67  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISaSRNSAGKTYEESVQgrwklatpipeQVKGIVVQ--DASQVEQVAAEV 82
Cdd:cd17895     1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALT-SRSYAGKPVSEVFP-----------HLRGLTDLtfEPDDDEEIAEDA 68


                  ....*..
gi 1288424414  83 DFVFCAV 89
Cdd:cd17895    69 DVVFLAL 75
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 6-131 2.74e-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: 52.50  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   6 KVGIVGGTGMVGQRFMQLLDGHPWFEVTSISaSRNSAGKtyeesvqgrwKLATPIPEQVKGIVVQDASQVEQVAA-EVDF 84
Cdd:cd24149     2 RVGLIGARGYVGRELIRLLNRHPNLELAHVS-SRELAGQ----------KVSGYTKSPIDYLNLSVEDIPEEVAArEVDA 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1288424414  85 VFCAVDMKKNE--IQALEEAYAKTgtpVISNNSA-HRWTPDVPMVIPEIN 131
Cdd:cd24149    71 WVLALPNGVAKpfVDAIDKANPKS---VIVDLSAdYRFDDAWTYGLPELN 117
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 5-142 2.36e-07

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: 49.54  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPwFEVTSISA--SRNSAGKTyeESVQGRwklatpipeqvkGIVVQDASQVEqvAAEV 82
Cdd:cd17894     1 YRIAVVGATGLVGKELLELLEERG-FPVGRLRLldSEESAGEL--VEFGGE------------PLDVQDLDEFD--FSDV 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  83 DFVFCAVDmkKNEIQALEEAYAKTGTPVISNNSAHRWTPDVPMVIPEINPGHIDVIAAQR 142
Cdd:cd17894    64 DLVFFAGP--AEVARAYAPRARAAGCLVIDLSGALRSDPDVPLVVPGVNPEALAAAAERR 121
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 6-157 7.22e-07

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: 48.44  E-value: 7.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   6 KVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNsAGKTYEE------SVQGRwKLATPIPEQVKGI-VV-------QD 71
Cdd:cd24148     2 RVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSN-AGQRLGElhphlpPLADR-VLEPTTPAVLAGHdVVflalphgAS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414  72 ASQVEQVAAEVDFVFCAVDMKKNEIQALEEAYAKTgtpvisnnSAHRWtpdvPMVIPEInPGHIDVIAAQRKrlgtttgf 151
Cdd:cd24148    80 AAIAAQLPPDVLVVDCGADHRLEDAAAWEKFYGGE--------HAGGW----TYGLPEL-PGAREALAGARR-------- 138


                  ....*.
gi 1288424414 152 IAVkPN 157
Cdd:cd24148   139 IAV-PN 143
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 5-45 3.38e-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: 46.88  E-value: 3.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1288424414   5 LKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISaSRNSAGKT 45
Cdd:cd24151     1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVT-SESLAGKP 40
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 6-120 7.53e-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: 45.64  E-value: 7.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   6 KVGIVGGTGMVGQRFMQLLDGHPWFEVTSISaSRNSAGKTYEE---SVQGRWKLATPIPEQVKGivvqdasqveqvaaEV 82
Cdd:cd02280     2 RVAIIGASGYTGLEIVRLLLGHPYLRVLTLS-SRERAGPKLREyhpSLIISLQIQEFRPCEVLN--------------SA 66

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1288424414  83 DFVFCAVDMKKNEIQAleEAYAKTGTPVISNNSAHRWT 120
Cdd:cd02280    67 DILVLALPHGASAELV--AAISNPQVKIIDLSADFRFT 102
ASADH_C_USG1_like cd18129
C-terminal domain of USG-1 protein and similar proteins; The family includes Escherichia coli ...
 165-324 4.63e-05

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: 43.72  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 165 PALHALLD-YKPTHVVASTYQAISGAGK--------------NFTDWPD------MLDNVIPYIGGEEEKSEQEPLRIWG 223
Cdd:cd18129     8 RVLAPLHDaAGLERVVVTVLQPVSEAGQagvdelarqtarllNGQPVEPevfprqLAFNLLPQVGDFDADGLSDEERRIA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414 224 SVVnGEIVKAQSPLITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQQFKGrpqeLNLPSAPkqfityfEEENRPQT 303
Cdd:cd18129    88 AEL-RRLLGGPDLPVSVTCVQVPVFYGHSASVHVELAEPVDLEEVRAALAAAPG----LELADDA-------EAPPYPVD 155

                         170       180
                  ....*....|....*....|.
gi 1288424414 304 KLDRDiergmGVSVGRLREDS 324
Cdd:cd18129   156 AAGSD-----DVLVGRVRQDP 171
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
6-89 4.54e-04

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 41.00  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   6 KVGIVGGTGMVGQRFMQLL--DGHpwfEVTSIsaSRNSAgktyeesvqgrwKLATPIPeQVKGIV--VQDASQVEQVAAE 81
Cdd:COG2910     1 KIAVIGATGRVGSLIVREAlaRGH---EVTAL--VRNPE------------KLPDEHP-GLTVVVgdVLDPAAVAEALAG 62


                  ....*...
gi 1288424414  82 VDFVFCAV 89
Cdd:COG2910    63 ADAVVSAL 70
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-118 4.85e-04

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 41.74  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288424414   2 SEKLKVGIVGGTGMVGQRFMQLLDGHPWFEVTSISASRNsAGKTYEESVQGRWKLATPipeqvKGIVVQDASqveqvAAE 81
Cdd:PLN02968   36 EEKKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRK-AGQSFGSVFPHLITQDLP-----NLVAVKDAD-----FSD 104

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1288424414  82 VDFVFCAV--DMKKNEIQALEEayaktGTPVISNNSAHR 118
Cdd:PLN02968  105 VDAVFCCLphGTTQEIIKALPK-----DLKIVDLSADFR 138
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 238-273 4.64e-03

C-terminal catalytic domain of type II 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). The family corresponds to type II NADP+ utilizing GAPDHs, mainly from archaea.


Pssm-ID: 467677  Cd Length: 162  Bit Score: 37.57  E-value: 4.64e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1288424414 238 ITTQCIRVPVTDGHLATVFASFENKPSKDEILDRWQ 273
Cdd:cd18127    68 ITTSAVKVPTTLMHLHTINVELKRKVSREEVLEALA 103
 
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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