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Conserved domains on  [gi|2053307865|gb|QWR51649|]
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aspartate-semialdehyde dehydrogenase [Clostridioides difficile]

Protein Classification

aspartate-semialdehyde dehydrogenase( domain architecture ID 11487465)

aspartate-semialdehyde dehydrogenase catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 4-325 0e+00

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: 571.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKY 83
Cdd:COG0136     1 YNVAVVGATGAVGRVLLELLEERDFPVGELRLLASSRSAGKTVSFGGKELTVEDATDFDF--SGVDIALFSAGGSVSKEY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  84 APIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAVS 161
Cdd:COG0136    79 APKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALADHlpKGIIANPNCSTIQMLVALKPLHDAAGIKRVVVSTYQAVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 162 GSGVKGVEDLEKGM----NGNP--TGFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTVRVPVK 235
Cdd:COG0136   159 GAGAAAMDELAEQTaallNGEEiePEVFPHPIAFNLIPQIDVFLENGYTKEEMKMVNETRKILGDPDIPVSATCVRVPVF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 236 NGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDNGVNLWVVADNIRKG 315
Cdd:COG0136   239 RGHSEAVNIEFERPVSLEEARELLAAAPGVKVVDDPAENDYPTPLDASGTDEVFVGRIRKDLSVPNGLNLWVVADNLRKG 318

                         330
                  ....*....|
gi 2053307865 316 AATNAIQIAE 325
Cdd:COG0136   319 AALNAVQIAE 328
 
Name Accession Description Interval E-value
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 4-325 0e+00

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: 571.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKY 83
Cdd:COG0136     1 YNVAVVGATGAVGRVLLELLEERDFPVGELRLLASSRSAGKTVSFGGKELTVEDATDFDF--SGVDIALFSAGGSVSKEY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  84 APIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAVS 161
Cdd:COG0136    79 APKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALADHlpKGIIANPNCSTIQMLVALKPLHDAAGIKRVVVSTYQAVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 162 GSGVKGVEDLEKGM----NGNP--TGFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTVRVPVK 235
Cdd:COG0136   159 GAGAAAMDELAEQTaallNGEEiePEVFPHPIAFNLIPQIDVFLENGYTKEEMKMVNETRKILGDPDIPVSATCVRVPVF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 236 NGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDNGVNLWVVADNIRKG 315
Cdd:COG0136   239 RGHSEAVNIEFERPVSLEEARELLAAAPGVKVVDDPAENDYPTPLDASGTDEVFVGRIRKDLSVPNGLNLWVVADNLRKG 318

                         330
                  ....*....|
gi 2053307865 316 AATNAIQIAE 325
Cdd:COG0136   319 AALNAVQIAE 328
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
 3-325 0e+00

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 520.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   3 KVNVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFTdrGIQIALFSAGGSISEK 82
Cdd:PRK14874    1 GYNVAVVGATGAVGREMLNILEERNFPVDKLRLLASARSAGKELSFKGKELKVEDLTTFDFS--GVDIALFSAGGSVSKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  83 YAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAV 160
Cdd:PRK14874   79 YAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALAEHrkKGIIANPNCSTIQMVVALKPLHDAAGIKRVVVSTYQAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 161 SGSGVKGVEDLEKGMNG--------NPTGFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTVRV 232
Cdd:PRK14874  159 SGAGKAGMEELFEQTRAvlnaavdpVEPKKFPKPIAFNVIPHIDVFMDDGYTKEEMKMVNETKKILGDPDLKVSATCVRV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 233 PVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDNGVNLWVVADNI 312
Cdd:PRK14874  239 PVFTGHSESVNIEFEEPISVEEAREILAEAPGVVLVDDPENGGYPTPLEAVGKDATFVGRIRKDLTVENGLHLWVVSDNL 318

                         330
                  ....*....|...
gi 2053307865 313 RKGAATNAIQIAE 325
Cdd:PRK14874  319 RKGAALNAVQIAE 331
asd_B TIGR01296
aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families ...
 5-325 1.48e-155

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: 439.25  E-value: 1.48e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   5 NVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKYA 84
Cdd:TIGR01296   1 NVAIVGATGAVGQEMLKLLEERNFPIDKLVLLASARSAGRKLTFKGKELEVEEAETESF--EGIDIALFSAGGSVSKEFA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  85 PIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAVSG 162
Cdd:TIGR01296  79 PKAAKAGVIVIDNTSAFRMDPDVPLVVPEVNFEDLKEFnpKGIIANPNCSTIQMVVVLKPLHDEAKIKRVVVSTYQAVSG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 163 SGVKGVEDLEK-------GMNGNPT-----GFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTV 230
Cdd:TIGR01296 159 AGNAGVEELYNqtkavleGAEQLPYiqpkaNKFPYQIAFNAIPHIDSFVDDGYTKEEQKMLFETRKIMGIPDLKVSATCV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 231 RVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDNGVNLWVVAD 310
Cdd:TIGR01296 239 RVPVFTGHSESINIEFEKEISPEDARELLKNAPGVQLIDDPSGNLYPTPLAAVGVDEVFVGRIRKDLPDGNGLHLWVVAD 318

                         330
                  ....*....|....*
gi 2053307865 311 NIRKGAATNAIQIAE 325
Cdd:TIGR01296 319 NLRKGAALNSVQIAE 333
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
 131-312 1.13e-104

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: 304.44  E-value: 1.13e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 131 CSTIQAMVPLKALDDKYKIKRVVYSTYQAVSGSGVKGVEDLEKGM----NGNPT--GFYPHQISYNCLPHIDSFTENGYT 204
Cdd:cd18131     1 CSTIQMVVALKPLHDAFGLKRVVVSTYQAVSGAGAAAMEELEEQTrgllNGKEAepKVFPYQIAFNVIPHIDVFLDNGYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 205 KEEMKMVNETMKILDNYDLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDD 284
Cdd:cd18131    81 KEEMKMVNETRKILGDPDLRVSATCVRVPVFRGHSESVNIEFEKPISVEEAREALAKAPGVVVVDDPANNVYPTPLDAAG 160

                         170       180
                  ....*....|....*....|....*...
gi 2053307865 285 RDEVFVGRIRRDFSVDNGVNLWVVADNI 312
Cdd:cd18131   161 KDDVFVGRIRKDISVPNGLNLWVVGDNL 188
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 140-314 1.05e-45

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: 153.24  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 140 LKALDDKY-KIKRVVYSTYQAVSGSGVKGvedlekgmngnPTGFYPHQISYNCLPHIDSFTENG--YTKEEMKMVNETMK 216
Cdd:pfam02774   1 LKPLRDALgGLERVIVDTYQAVSGAGKKA-----------KPGVFGAPIADNLIPYIDGEEHNGtpETREELKMVNETKK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 217 ILDNYDlKITATTVRVPVKNGHSESINVEFNN-PFELDDLVKTLEEAPGVVVVDNPaKNEYPTAVefDDR---DEVFVGR 292
Cdd:pfam02774  70 ILGFTP-KVSATCVRVPVFRGHSETVTVKLKLkPIDVEEVYEAFYAAPGVFVVVRP-EEDYPTPR--AVRggtNFVYVGR 145

                         170       180
                  ....*....|....*....|..
gi 2053307865 293 IRRDFSVDNGVNLWVVADNIRK 314
Cdd:pfam02774 146 VRKDPDGDRGLKLVSVIDNLRK 167
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 5-122 2.06e-40

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


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 137.68  E-value: 2.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865    5 NVAIVGATGMVGRTFLKVLEE-RNFPIEnlFLFSSSKSAGSKVMFCG---KEYIVEELKETSFTDRGIQIALFSAGGSIS 80
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEhPDFELT--ALAASSRSAGKKVSEAGphlKGEVVLELDPPDFEELAVDIVFLALPHGVS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2053307865   81 E---KYAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH 122
Cdd:smart00859  79 KesaPLLPRAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 4-325 0e+00

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: 571.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKY 83
Cdd:COG0136     1 YNVAVVGATGAVGRVLLELLEERDFPVGELRLLASSRSAGKTVSFGGKELTVEDATDFDF--SGVDIALFSAGGSVSKEY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  84 APIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAVS 161
Cdd:COG0136    79 APKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALADHlpKGIIANPNCSTIQMLVALKPLHDAAGIKRVVVSTYQAVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 162 GSGVKGVEDLEKGM----NGNP--TGFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTVRVPVK 235
Cdd:COG0136   159 GAGAAAMDELAEQTaallNGEEiePEVFPHPIAFNLIPQIDVFLENGYTKEEMKMVNETRKILGDPDIPVSATCVRVPVF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 236 NGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDNGVNLWVVADNIRKG 315
Cdd:COG0136   239 RGHSEAVNIEFERPVSLEEARELLAAAPGVKVVDDPAENDYPTPLDASGTDEVFVGRIRKDLSVPNGLNLWVVADNLRKG 318

                         330
                  ....*....|
gi 2053307865 316 AATNAIQIAE 325
Cdd:COG0136   319 AALNAVQIAE 328
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
 3-325 0e+00

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 520.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   3 KVNVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFTdrGIQIALFSAGGSISEK 82
Cdd:PRK14874    1 GYNVAVVGATGAVGREMLNILEERNFPVDKLRLLASARSAGKELSFKGKELKVEDLTTFDFS--GVDIALFSAGGSVSKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  83 YAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAV 160
Cdd:PRK14874   79 YAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALAEHrkKGIIANPNCSTIQMVVALKPLHDAAGIKRVVVSTYQAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 161 SGSGVKGVEDLEKGMNG--------NPTGFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTVRV 232
Cdd:PRK14874  159 SGAGKAGMEELFEQTRAvlnaavdpVEPKKFPKPIAFNVIPHIDVFMDDGYTKEEMKMVNETKKILGDPDLKVSATCVRV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 233 PVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDNGVNLWVVADNI 312
Cdd:PRK14874  239 PVFTGHSESVNIEFEEPISVEEAREILAEAPGVVLVDDPENGGYPTPLEAVGKDATFVGRIRKDLTVENGLHLWVVSDNL 318

                         330
                  ....*....|...
gi 2053307865 313 RKGAATNAIQIAE 325
Cdd:PRK14874  319 RKGAALNAVQIAE 331
asd_B TIGR01296
aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families ...
 5-325 1.48e-155

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: 439.25  E-value: 1.48e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   5 NVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKYA 84
Cdd:TIGR01296   1 NVAIVGATGAVGQEMLKLLEERNFPIDKLVLLASARSAGRKLTFKGKELEVEEAETESF--EGIDIALFSAGGSVSKEFA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  85 PIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAVSG 162
Cdd:TIGR01296  79 PKAAKAGVIVIDNTSAFRMDPDVPLVVPEVNFEDLKEFnpKGIIANPNCSTIQMVVVLKPLHDEAKIKRVVVSTYQAVSG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 163 SGVKGVEDLEK-------GMNGNPT-----GFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTV 230
Cdd:TIGR01296 159 AGNAGVEELYNqtkavleGAEQLPYiqpkaNKFPYQIAFNAIPHIDSFVDDGYTKEEQKMLFETRKIMGIPDLKVSATCV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 231 RVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDNGVNLWVVAD 310
Cdd:TIGR01296 239 RVPVFTGHSESINIEFEKEISPEDARELLKNAPGVQLIDDPSGNLYPTPLAAVGVDEVFVGRIRKDLPDGNGLHLWVVAD 318

                         330
                  ....*....|....*
gi 2053307865 311 NIRKGAATNAIQIAE 325
Cdd:TIGR01296 319 NLRKGAALNSVQIAE 333
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 5-328 6.86e-147

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 417.63  E-value: 6.86e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   5 NVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKYA 84
Cdd:PLN02383    9 SVAIVGVTGAVGQEFLSVLTDRDFPYSSLKMLASARSAGKKVTFEGRDYTVEELTEDSF--DGVDIALFSAGGSISKKFG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  85 PIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNHK------GIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQ 158
Cdd:PLN02383   87 PIAVDKGAVVVDNSSAFRMEEGVPLVIPEVNPEAMKHIKlgkgkgALIANPNCSTIICLMAVTPLHRHAKVKRMVVSTYQ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 159 AVSGSGVKGVEDLEKG----MNGNPT--GFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTVRV 232
Cdd:PLN02383  167 AASGAGAAAMEELEQQtrevLEGKPPtcNIFAQQYAFNLFSHNAPMQENGYNEEEMKLVKETRKIWNDDDVKVTATCIRV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 233 PVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDN--GVNLWVVAD 310
Cdd:PLN02383  247 PVMRAHAESINLQFEKPLDEATAREILASAPGVKIIDDRANNRFPTPLDASNKDDVAVGRIRQDISQDGnkGLDIFVCGD 326

                         330
                  ....*....|....*...
gi 2053307865 311 NIRKGAATNAIQIAEMAL 328
Cdd:PLN02383  327 QIRKGAALNAVQIAELLL 344
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
 131-312 1.13e-104

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: 304.44  E-value: 1.13e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 131 CSTIQAMVPLKALDDKYKIKRVVYSTYQAVSGSGVKGVEDLEKGM----NGNPT--GFYPHQISYNCLPHIDSFTENGYT 204
Cdd:cd18131     1 CSTIQMVVALKPLHDAFGLKRVVVSTYQAVSGAGAAAMEELEEQTrgllNGKEAepKVFPYQIAFNVIPHIDVFLDNGYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 205 KEEMKMVNETMKILDNYDLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDD 284
Cdd:cd18131    81 KEEMKMVNETRKILGDPDLRVSATCVRVPVFRGHSESVNIEFEKPISVEEAREALAKAPGVVVVDDPANNVYPTPLDAAG 160

                         170       180
                  ....*....|....*....|....*...
gi 2053307865 285 RDEVFVGRIRRDFSVDNGVNLWVVADNI 312
Cdd:cd18131   161 KDDVFVGRIRKDISVPNGLNLWVVGDNL 188
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 2-325 1.86e-104

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 309.67  E-value: 1.86e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   2 KKVNVAIVGATGMVGRTFLKVLE-ERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSIS 80
Cdd:PRK06728    4 KGYHVAVVGATGAVGQKIIELLEkETKFNIAEVTLLSSKRSAGKTVQFKGREIIIQEAKINSF--EGVDIAFFSAGGEVS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  81 EKYAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNHKGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAV 160
Cdd:PRK06728   82 RQFVNQAVSSGAIVIDNTSEYRMAHDVPLVVPEVNAHTLKEHKGIIAVPNCSALQMVTALQPIRKVFGLERIIVSTYQAV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 161 SGSGVKGVEDLEKGMNGNPTG---------------FYPhqISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKI 225
Cdd:PRK06728  162 SGSGIHAIQELKEQAKSILAGeevestilpakkdkkHYP--IAFNVLPQVDIFTDNDFTFEEVKMIQETKKILEDPNLKM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 226 TATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEFDDRDEVFVGRIRRDFSVDNGVNL 305
Cdd:PRK06728  240 AATCVRVPVISGHSESVYIELEKEATVAEIKEVLFDAPGVILQDNPSEQLYPMPLYAEGKIDTFVGRIRKDPDTPNGFHL 319

                         330       340
                  ....*....|....*....|
gi 2053307865 306 WVVADNIRKGAATNAIQIAE 325
Cdd:PRK06728  320 WIVSDNLLKGAAWNSVQIAE 339
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 5-130 6.88e-77

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: 231.94  E-value: 6.88e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   5 NVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKYA 84
Cdd:cd02316     2 NVAIVGATGAVGQEMLKVLEERNFPVSELRLLASARSAGKTLEFKGKELTVEELTEDSF--KGVDIALFSAGGSVSKEFA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2053307865  85 PIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNHKGIIANPN 130
Cdd:cd02316    80 PIAAEAGAVVIDNSSAFRMDPDVPLVVPEVNPEALKNHKGIIANPN 125
PRK05671 PRK05671
aspartate-semialdehyde dehydrogenase; Reviewed
 4-326 7.94e-71

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 168165 [Multi-domain]  Cd Length: 336  Bit Score: 223.45  E-value: 7.94e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFTDrgIQIALFSAGGSISEKY 83
Cdd:PRK05671    5 LDIAVVGATGTVGEALVQILEERDFPVGTLHLLASSESAGHSVPFAGKNLRVREVDSFDFSQ--VQLAFFAAGAAVSRSF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  84 APIAASNGILVVDNSSQWRMNpDVPLVVPEVNPEAIKNHKG--IIANPNCSTIQ---AMVPLKALDDkykIKRVVYSTYQ 158
Cdd:PRK05671   83 AEKARAAGCSVIDLSGALPSA-QAPNVVPEVNAERLASLAApfLVSSPSASAVAlavALAPLKGLLD---IQRVQVTACL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 159 AVSGSGVKGVEDLEKG----MNGNP--TGFYPHQISYNCLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKITATTVRV 232
Cdd:PRK05671  159 AVSSLGREGVSELARQtaelLNARPlePRFFDRQVAFNLLAQVGAPDAQGHTALERRLVAELRQLLGLPELKISVTCIQV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 233 PVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDnpaKNEYPTAVEfdD---RDEVFVGRIRRDFSVDNGVNLWVVA 309
Cdd:PRK05671  239 PVFFGDSLSVALQSAAPVDLAAVNAALEAAPGIELVE---AGDYPTPVG--DavgQDVVYVGRVRAGVDDPCQLNLWLTS 313

                         330
                  ....*....|....*..
gi 2053307865 310 DNIRKGAATNAIQIAEM 326
Cdd:PRK05671  314 DNVRKGAALNAVQVAEL 330
PRK08040 PRK08040
putative semialdehyde dehydrogenase; Provisional
 5-325 1.37e-69

putative semialdehyde dehydrogenase; Provisional


Pssm-ID: 181205 [Multi-domain]  Cd Length: 336  Bit Score: 220.34  E-value: 1.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   5 NVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFTDrgIQIALFSAGGSISEKYA 84
Cdd:PRK08040    6 NIALLGATGAVGEALLELLAERQFPVGELYALASEESAGETLRFGGKSVTVQDAAEFDWSQ--AQLAFFVAGREASAAYA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  85 PIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPNCSTIQAMVPLKALDDKYKIKRVVYSTYQAVSG 162
Cdd:PRK08040   84 EEATNAGCLVIDSSGLFALEPDVPLVVPEVNPFVLADYrnRNIIAVADSLTSQLLTAIKPLIDQAGLSRLHVTNLLSASA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 163 SGVKGVEDL----EKGMNGNPT--GFYPHQISYNCLPHIDSftENGYTKEEMKMVNETMKILDNYDLKITATTVRVPVKN 236
Cdd:PRK08040  164 HGKAAVDALagqsAKLLNGIPIeeGFFGRQLAFNMLPLLPD--SEGSVREERRLVDQVRKILQDEGLPISVSCVQSPVFY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 237 GHSESINVEFNNPFELDDLVKTLEEAPGVVVVDnpaKNEYPTAV-EFDDRDEVFVGRIRRDFSVDNGVNLWVVADNIRKG 315
Cdd:PRK08040  242 GHAQMVHFEALRPLAAEEARDALEQGEDIVLSE---ENDYPTQVgDASGNPHLSIGCVRNDYGMPEQLQFWSVADNVRFG 318

                         330
                  ....*....|
gi 2053307865 316 AATNAIQIAE 325
Cdd:PRK08040  319 GALMAVKTAE 328
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-327 9.77e-68

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 215.84  E-value: 9.77e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   1 MKKVNVAIVGATGMVGRTFLKVLEerNFP-IENLFLFSSSKSAGSK-------VMFCG-----KEYIVEELKETSFTDRG 67
Cdd:PRK08664    1 MMKLKVGILGATGMVGQRFVQLLA--NHPwFEVTALAASERSAGKTygeavrwQLDGPipeevADMEVVSTDPEAVDDVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  68 IqiaLFSA-----GGSISEKYApiaaSNGILVVDNSSQWRMNPDVPLVVPEVNPEAI---------KNHKG-IIANPNCS 132
Cdd:PRK08664   79 I---VFSAlpsdvAGEVEEEFA----KAGKPVFSNASAHRMDPDVPLVIPEVNPEHLelievqrkrRGWDGfIVTNPNCS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 133 TIQAMVPLKALDDkYKIKRVVYSTYQAVSGSGVKGVEDLEkgMNGnptgfyphqisyNCLPHIDsftengytKEEMKMVN 212
Cdd:PRK08664  152 TIGLVLALKPLMD-FGIERVHVTTMQAISGAGYPGVPSMD--IVD------------NVIPYIG--------GEEEKIEK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 213 ETMKIL--------DNYDLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVvvvdnPAKNEYPTAVE--- 281
Cdd:PRK08664  209 ETLKILgkfeggkiVPADFPISATCHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFKGL-----PQELGLPSAPKkpi 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2053307865 282 --FD---------DRD-----EVFVGRIRRDfsVDNGVNLWVVADNIRKGAATNAIQIAEMA 327
Cdd:PRK08664  284 ilFEepdrpqprlDRDagdgmAVSVGRLRED--GIFDIKFVVLGHNTVRGAAGASVLNAELL 343
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 4-328 2.96e-56

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: 186.12  E-value: 2.96e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEER-NFPIENLFlfSSSKSAGSK-------VMFCG-----KEYIVEELKETSFTDRGIqi 70
Cdd:TIGR00978   1 MRVAVLGATGLVGQKFVKLLAKHpYFELAKVV--ASPRSAGKRygeavkwIEPGDmpeyvRDLPIVEPEPVASKDVDI-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  71 aLFSA-GGSISEKYAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAI--------KNHKG-IIANPNCSTIQAMVPL 140
Cdd:TIGR00978  77 -VFSAlPSEVAEEVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLellkvqkeRGWKGfIVTNPNCTTAGLTLAL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 141 KALDDKYKIKRVVYSTYQAVSGSGVKGVEDLEkgmngnptgfyphqISYNCLPHIdsftengyTKEEMKMVNETMKILDN 220
Cdd:TIGR00978 156 KPLIDAFGIKKVHVTTMQAVSGAGYPGVPSMD--------------ILDNIIPHI--------GGEEEKIERETRKILGK 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 221 YD--------LKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVvvvdnPAKNEYPTA-------VEFDDR 285
Cdd:TIGR00978 214 LEngkiepapFSVSATTTRVPVLDGHTESVHVEFDKKFDIEEIREALKSFRGL-----PQKLGLPSApekpiivRDEEDR 288

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2053307865 286 DE------------VFVGRIRRDfsvDNGVNLWVVADNIRKGAATNAIQIAEMAL 328
Cdd:TIGR00978 289 PQprldrdagggmaVTVGRLREE---GGSLKYVVLGHNLVRGAAGATLLNAELAY 340
ASADH_C_USG1_like cd18129
C-terminal domain of USG-1 protein and similar proteins; The family includes Escherichia coli ...
 132-312 3.04e-47

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: 157.74  E-value: 3.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 132 STIQAMVPLKALDDKYKIKRVVYSTYQAVSGSGVKGVEDLEKG----MNGNP--TGFYPHQISYNCLPHIDSFTENGYTK 205
Cdd:cd18129     2 AAIALARVLAPLHDAAGLERVVVTVLQPVSEAGQAGVDELARQtarlLNGQPvePEVFPRQLAFNLLPQVGDFDADGLSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 206 EEMKMVNETMKILDNYDLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEfdDR 285
Cdd:cd18129    82 EERRIAAELRRLLGGPDLPVSVTCVQVPVFYGHSASVHVELAEPVDLEEVRAALAAAPGLELADDAEAPPYPVDAA--GS 159

                         170       180
                  ....*....|....*....|....*..
gi 2053307865 286 DEVFVGRIRRDFSVDNGVNLWVVADNI 312
Cdd:cd18129   160 DDVLVGRVRQDPGNPRGLWLWAVADNL 186
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 140-314 1.05e-45

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: 153.24  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 140 LKALDDKY-KIKRVVYSTYQAVSGSGVKGvedlekgmngnPTGFYPHQISYNCLPHIDSFTENG--YTKEEMKMVNETMK 216
Cdd:pfam02774   1 LKPLRDALgGLERVIVDTYQAVSGAGKKA-----------KPGVFGAPIADNLIPYIDGEEHNGtpETREELKMVNETKK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 217 ILDNYDlKITATTVRVPVKNGHSESINVEFNN-PFELDDLVKTLEEAPGVVVVDNPaKNEYPTAVefDDR---DEVFVGR 292
Cdd:pfam02774  70 ILGFTP-KVSATCVRVPVFRGHSETVTVKLKLkPIDVEEVYEAFYAAPGVFVVVRP-EEDYPTPR--AVRggtNFVYVGR 145

                         170       180
                  ....*....|....*....|..
gi 2053307865 293 IRRDFSVDNGVNLWVVADNIRK 314
Cdd:pfam02774 146 VRKDPDGDRGLKLVSVIDNLRK 167
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 5-122 2.83e-45

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


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 150.37  E-value: 2.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   5 NVAIVGATGMVGRTFLKVLEErNFPIENLFLFSSSKSAGSKVMFC------GKEYIVEELKETSFtdRGIQIALFSAGGS 78
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEE-HPPVELVVLFASSRSAGKKLAFVhpilegGKDLVVEDVDPEDF--KDVDIVFFALPGG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2053307865  79 ISEKYAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH 122
Cdd:pfam01118  78 VSKEIAPKLAEAGAKVIDLSSDFRMDDDVPYGLPEVNREAIKQA 121
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 4-130 8.32e-43

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: 144.79  E-value: 8.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKY 83
Cdd:cd24147     1 LRVGVVGATGAVGSEILQLLAEEPDPLFELRALASEESAGKKAEFAGEAIMVQEADPIDF--LGLDIVFLCAGAGVSAKF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2053307865  84 APIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNHKG--IIANPN 130
Cdd:cd24147    79 APEAARAGVLVIDNAGALRMDPDVPLVVPEVNAEAIGLGEGtpLLVIPN 127
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 5-122 2.06e-40

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


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 137.68  E-value: 2.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865    5 NVAIVGATGMVGRTFLKVLEE-RNFPIEnlFLFSSSKSAGSKVMFCG---KEYIVEELKETSFTDRGIQIALFSAGGSIS 80
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEhPDFELT--ALAASSRSAGKKVSEAGphlKGEVVLELDPPDFEELAVDIVFLALPHGVS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2053307865   81 E---KYAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH 122
Cdd:smart00859  79 KesaPLLPRAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIKKA 123
ASADH_C cd18128
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar ...
 131-312 3.90e-37

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: 130.70  E-value: 3.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 131 CSTIQAMVPLKALDDKYKIKRVVYSTYQAVSGSGVKgvedlekgmngnptgfyphqISYNCLPHIDSFTENGYTKEEMKM 210
Cdd:cd18128     1 CTVSLMLMALGGLFQKFLVEWVSVATYQAVSGAG*P--------------------IAGNLIPWIDVFLDNGQTKEEWKG 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 211 VNETMKILDNYD--LKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAP-GVVVVDNPAKNEYPTAVEFDDRDE 287
Cdd:cd18128    61 QAETNKILGDLDspIPISGTCVRVGVLRCHSQAFTIKLKEDAPIEEVEEAIAAHN*WIKVIPNVDRITPRTPANVTGTLS 140

                         170       180
                  ....*....|....*....|....*
gi 2053307865 288 VFVGRIRRDFSVDNGVNLWVVADNI 312
Cdd:cd18128   141 TPVGRIRKDAMGPFDLQAFTVGDNL 165
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 5-130 3.92e-37

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: 130.18  E-value: 3.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   5 NVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSkSAGSKVMFCGKEY----IVEELKETSFtdRGIQIALFSAGGSIS 80
Cdd:cd02281     2 KVGVVGATGYVGGEFLRLLLEHPFPLFEIVLLAAS-SAGAKKKYFHPKLwgrvLVEFTPEEVL--EQVDIVFTALPGGVS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2053307865  81 EKYAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNHKG--IIANPN 130
Cdd:cd02281    79 AKLAPELSEAGVLVIDNASDFRLDKDVPLVVPEVNREHIGELKGtkIIANPN 130
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 4-130 6.93e-37

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: 129.28  E-value: 6.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEERNFPIENLFLFSSSKSAGSKVMFCGKEYIVEELKETSFtdRGIQIALFSAGGSISEKY 83
Cdd:cd17894     1 YRIAVVGATGLVGKELLELLEERGFPVGRLRLLDSEESAGELVEFGGEPLDVQDLDEFDF--SDVDLVFFAGPAEVARAY 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2053307865  84 APIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKNH--KGIIANPN 130
Cdd:cd17894    79 APRARAAGCLVIDLSGALRSDPDVPLVVPGVNPEALAAAaeRRVVAVPN 127
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 131-311 2.42e-35

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: 126.58  E-value: 2.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 131 CSTIQAMVPLKALDDKYKIKRVVYSTYQAVSGSGVKGVEDLEkgmngnptgfyphqISYNCLPHIdsftengyTKEEMKM 210
Cdd:cd18130     1 CSTAGLALPLKPLHDFFGIEAVIVTTMQAISGAGYPGVPSLD--------------ILDNVIPYI--------GGEEEKI 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 211 VNETMKIL--------DNYDLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNEYPTAVEF 282
Cdd:cd18130    59 ESETKKILgtlnedkiEPADFKVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPQVLGPPSAPKPIIVVE 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2053307865 283 D---------DRDE-----VFVGRIRRDFsvDNGVNLWVVADN 311
Cdd:cd18130   139 DeprrpqprlDRDAgdgmaVTVGRIRKDD--DFDLKFVLLSHN 179
ASADH_C_like cd18124
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 131-312 1.92e-29

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: 111.53  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 131 CSTIQAMVPLKALDDKYKIKRVVYSTYQAVSGSGVKGVEDLEKGMNGN------PTGFYPHQISYNCLPHIDSFTENGYT 204
Cdd:cd18124     1 CTVSLLVMALKPLFAKFLVEWVSVAT*QAVSGAGYENMRELLSQMGELmragplPTGVFS*AIADNLIPWIDKVLDNGQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 205 KEEMKMVNETMKILDNYD--LKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVDNPAKNeyPTAVEF 282
Cdd:cd18124    81 KEEWKIQAEANKILGTLDspIPISVTCNRVPVLDGHSQSFTLKLKEDVPLEEVEEVLDAHKPWVKVIPNDYA--IRPQPR 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2053307865 283 DDRD-----EVFVGRIRRDFSVDNGVNLWVVADNI 312
Cdd:cd18124   159 LDRKvtgglSTPVGRIRKDAMDPFDVNAFAVSDNT 193
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 4-131 1.87e-18

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: 81.00  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEerNFPIENLF-LFSSSKSAGSK----------------VmfcgKEYIVEELKETSFTDr 66
Cdd:cd02315     1 IKVGVLGATGMVGQRFIQLLA--NHPWFELAaLGASERSAGKKygdavrwkqdtpipeeV----ADMVVKECEPEEFKD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  67 gIQIAlFSA-----GGSISEKYApiaaSNGILVVDNSSQWRMNPDVPLVVPEVNPEAIK---------NHKG-IIANPNC 131
Cdd:cd02315    74 -CDIV-FSAldsdvAGEIEPAFA----KAGIPVFSNASNHRMDPDVPLVIPEVNPDHLDlieaqrkrrGWKGfIVTNPNN 147
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 131-311 1.30e-15

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


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 73.32  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 131 CSTIQAMVPLKALDDKYKIKRVVYSTYQAVSGSGVKGVEDLEKGMNGNPtgfyphqisynclphidsftENGYTKEEMKM 210
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSEVRAI--------------------IPNIPKNETKH 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 211 VNETMKILD--NYDLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVV--VVDNPAKNEYPTAVEFDDRD 286
Cdd:cd18122    61 APETGKVLGeiGKPIKVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVqiSAEDGLTYAKVSTRSVGGVY 140

                         170       180
                  ....*....|....*....|....*
gi 2053307865 287 EVFVGRIRRDFSVDNGVNLWVVADN 311
Cdd:cd18122   141 GVPVGRQREFAFDDNKLKVFSAVDN 165
PRK06598 PRK06598
aspartate-semialdehyde dehydrogenase; Reviewed
 1-294 2.39e-15

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 235839  Cd Length: 369  Bit Score: 76.02  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   1 MKKVnvAIVGATGMVGRTFLK-VLEERNFP-IENLFlFSSSKSAGSKVMFCGKE------YIVEELKEtsftdrgIQIAL 72
Cdd:PRK06598    1 MKKV--GFVGWRGMVGSVLMQrMVEENDFDlIEPVF-FSTSQAGGAAPSFGGKEgtlqdaFDIDALKK-------LDIII 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  73 FSAGGSISEK-YAPIAAS--NGILVvDNSSQWRMNPDVPLVVPEVNPEAIKN--HKGI---IANpNCsTIQAMvpLKALD 144
Cdd:PRK06598   71 TCQGGDYTNEvYPKLRAAgwQGYWI-DAASTLRMKDDAIIILDPVNRDVIDDalANGVktfVGG-NC-TVSLM--LMALG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 145 DKYK---IKRVVYSTYQAVSGSGVKGVEDLEKGMN----------GNP----------------TGFYPHQ-----ISYN 190
Cdd:PRK06598  146 GLFKndlVEWVSVMTYQAASGAGARNMRELLTQMGalhgavadelADPasaildidrkvtelmrSGDLPTDnfgvpLAGS 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 191 CLPHIDSFTENGYTKEEMKMVNETMKILDNYDLKIT--ATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEA-PGVVV 267
Cdd:PRK06598  226 LIPWIDKDLGNGQSREEWKGQAETNKILGLTKNPIPvdGLCVRVGAMRCHSQALTIKLKKDVPLAEIEEILAAHnPWVKV 305

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2053307865 268 VDN----PAKNEYPTAVEfdDRDEVFVGRIR 294
Cdd:PRK06598  306 VPNdreaTMRELTPAAVT--GTLTIPVGRLR 334
ASADH_C_bac_like cd23938
C-terminal catalytic domain of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) and ...
 155-295 1.20e-10

C-terminal catalytic domain of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a branch of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes mainly found in proteobacteria, such as Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa and Vibrio cholerae. These proteins have similar overall folds and domain organizations but share less sequence homology with fungal and archaeal ASADHs. 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: 467687  Cd Length: 217  Bit Score: 60.40  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 155 STYQAVSGSGVKGVEDLEKGM-------------------------------NGNPTGFYPHQISYNCLPHIDSFTENGY 203
Cdd:cd23938    25 MTYQAASGAGAKNMRELLSQMgalgdavsdeladpasaildidrkvtelqrsGSFPTDNFGVPLAGSLIPWIDKQLENGQ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 204 TKEEMKMVNETMKILDNYD-LKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEA-PGVVVVDN--PAKNEYPTA 279
Cdd:cd23938   105 SKEEWKGQVETNKILGTSKpIPIDGLCVRVGAMRCHSQALTIKLKKDVPLDEIEEIIAAHnQWVKVVPNdkEATLRELTP 184

                         170
                  ....*....|....*.
gi 2053307865 280 VEFDDRDEVFVGRIRR 295
Cdd:cd23938   185 AAVTGTLTVPVGRLRK 200
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 4-119 2.00e-07

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: 50.02  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEERNFpIENLFLF---SSSKSAGSKVMF-----CGKEYIVEELKETS---FTDRGIqiaL 72
Cdd:cd24150     2 LKAAILGATGLVGIEYVRMLSNHPY-IKPAYLAgkgSVGKPYGEVVRWqtvgqVPKEIADMEIKPTDpklMDDVDI---I 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2053307865  73 FS-----AGGSISEKYAPIaasnGILVVDNSSQWRMNPDVPLVVPEVNPEAI 119
Cdd:cd24150    78 FSplpqgAAGPVEEQFAKE----GFPVISNSPDHRFDPDVPLLVPELNPHTI 125
PRK06901 PRK06901
oxidoreductase;
1-329 3.09e-07

oxidoreductase;


Pssm-ID: 235883 [Multi-domain]  Cd Length: 322  Bit Score: 51.27  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   1 MKKVNVAIVgATGMVGRTFLKVLEERNFPIENL-----FLFSSSKSagskVMFCGK--EYI-VEELKETSFTdrgiqiAL 72
Cdd:PRK06901    1 MATLNIAIA-AEFELSEKLLEALEQSDLEIEQIsiveiEPFGEEQG----IRFNNKavEQIaPEEVEWADFN------YV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865  73 FSAGGSISEKYAPIAASNGILVVDNSSQWRMNPDVPLVVPEVNPEAIKN--HKGIIANPNCSTIQAMVPLKALDDKYKIK 150
Cdd:PRK06901   70 FFAGKMAQAEHLAQAAEAGCIVIDLYGICAALANVPVVVPSVNDEQLAElrQRNIVSLPDPQVSQLALALAPFLQEQPLS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 151 RVVYSTYQAVSGSGVKGVEDL----EKGMNGNPTGFYPHQISYNCLPhidsftengytKEEMKMVNETMKILDNYDlKIT 226
Cdd:PRK06901  150 QIFVTSLLPASYTDAETVKKLagqtARLLNGIPLDEEEQRLAFDVFP-----------ANAQNLELQLQKIFPQLE-NVT 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 227 ATTVRVPVKNGHSESINVEFNNPFELD---------DLVKTLEEApgvvvVDNPAKNEyptavEFDDRDEVFVGRIRRDF 297
Cdd:PRK06901  218 FHSIQVPVFYGLAQMVTALSEYELDIEsqlaewqqnNLLRYHEEK-----LITPVLNG-----ENENGEESVKLHISQLS 287

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2053307865 298 SVDNGVNLWVVADNIRKGAATNAIQIAEMALS 329
Cdd:PRK06901  288 AVENGVQFWSVADEQRFNLAFLAVKLLELIYQ 319
ASADH_C_MCR cd23940
C-terminal catalytic domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar ...
 131-292 1.66e-06

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: 47.82  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 131 CSTIQAMVPLKALDDKYKIKRVVYSTYQAVSGSGVKGVEDLEKGMNGNPTGfyphqisynclphidsfteNGYtkeEMKM 210
Cdd:cd23940     2 CTAQGAAIPLGAIFKDYKMDGAFITTIQSLSGAGYPGIPSLDVVDNILPLG-------------------DGY---DAKT 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865 211 VNETMKILDNY----------DLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGvvvvdNPAKNEYPTAV 280
Cdd:cd23940    60 IKEIFRILSEVkrnvdepkleDVSLAATTHRIATIHGHYEVLYVSFKEETAAEKVKETLENFRG-----EPQDLKLPTAP 134

                         170
                  ....*....|....*....
gi 2053307865 281 EF-------DDRDEVFVGR 292
Cdd:cd23940   135 SKpiivmneDTRPQVYFDR 153
VcASADH1_like_N cd02314
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 5-125 3.19e-06

N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase 1 (ASADH1) and similar proteins; The family corresponds to a branch of bacterial ASADH enzymes mainly found from proteobacteria, such as Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa and Vibrio cholerae. The first isoform of ASADH in Vibrio cholerae is one of the prototypes of this family. They have similar overall folds and domain organizations but sharing less sequence homology with fungal and archaeal ASADHs. 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: 467517  Cd Length: 150  Bit Score: 46.09  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   5 NVAIVGATGMVGRTFLK-VLEERNFPIENLFLFSSSkSAGSKVMFCGKE-------YIVEELKEtsftdrgIQIALFSAG 76
Cdd:cd02314     2 RVGFVGWRGMVGSVLMQrMQEENDFDLIEPVFFSTS-QVGQKGPTFGKDvgplkdaYDIDALKK-------MDIIVTCQG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053307865  77 GSISEK-YAPIAASN--GILvVDNSSQWRMNPDVPLVVPEVNPEAIKN--HKGI 125
Cdd:cd02314    74 GDYTKEvYPKLRKAGwkGYW-IDAASTLRMKDDAVIVLDPVNRDVIDSglASGI 126
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 4-130 6.08e-05

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: 42.80  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053307865   4 VNVAIVGATGMVGRTFLKVLEE-RNFPIENLflfSSSKSAGSKV--MFCGKEYIVEELKETSFTDR---GIQIALFSAGG 77
Cdd:cd17895     1 IKVGIIGASGYTGAELLRLLLNhPEVEIVAL---TSRSYAGKPVseVFPHLRGLTDLTFEPDDDEEiaeDADVVFLALPH 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2053307865  78 SISEKYAPIAASNGILVVDNSSQWRM-NPDV-----------PLVV-------PEVNPEAIKNHKgIIANPN 130
Cdd:cd17895    78 GVSMELAPKLLEAGVKVIDLSADFRLkDPETyekwygfehaaPELLkeavyglPELNREEIKKAR-LVANPN 148
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 222-269 1.51e-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: 38.72  E-value: 1.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053307865 222 DLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVD 269
Cdd:cd18127    65 DLDITTSAVKVPTTLMHLHTINVELKRKVSREEVLEALASNPRIALVD 112
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 216-263 3.51e-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: 37.60  E-value: 3.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053307865 216 KILDNYDLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAP 263
Cdd:cd18123    68 KVLPELNGKLTGMAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAP 115
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
222-269 4.18e-03

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 38.66  E-value: 4.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053307865 222 DLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAPGVVVVD 269
Cdd:PRK04207  204 DLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEALENTPRILLVR 251
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 216-263 8.36e-03

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 36.42  E-value: 8.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053307865 216 KILDNYDLKITATTVRVPVKNGHSESINVEFNNPFELDDLVKTLEEAP 263
Cdd:pfam02800  63 LVLPELKGKLDGMAVRVPTPNVSVVDLVVELEKPVTVEEVNAALKEAA 110
 
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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