NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20856224|gb|AAM26654|]
View 

At1g14810/F10B6_6 [Arabidopsis thaliana]

Protein Classification

PLN02383 family protein( domain architecture ID 11476727)

PLN02383 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
32-375 0e+00

aspartate semialdehyde dehydrogenase


:

Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 717.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   32 MSLQESAPSLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGS 111
Cdd:PLN02383   1 MALTENGPSVAIVGVTGAVGQEFLSVLTDRDFPYSSLKMLASARSAGKKVTFEGRDYTVEELTEDSFDGVDIALFSAGGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  112 ISKEFGPLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKVGMGKGALIANPNCSTIICLMAVTPLHHHAKVKRM 191
Cdd:PLN02383  81 ISKKFGPIAVDKGAVVVDNSSAFRMEEGVPLVIPEVNPEAMKHIKLGKGKGALIANPNCSTIICLMAVTPLHRHAKVKRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  192 VVSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVT 271
Cdd:PLN02383 161 VVSTYQAASGAGAAAMEELEQQTREVLEGKPPTCNIFAQQYAFNLFSHNAPMQENGYNEEEMKLVKETRKIWNDDDVKVT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  272 ATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDVSQDGNFGLD 351
Cdd:PLN02383 241 ATCIRVPVMRAHAESINLQFEKPLDEATAREILASAPGVKIIDDRANNRFPTPLDASNKDDVAVGRIRQDISQDGNKGLD 320
                        330       340
                 ....*....|....*....|....
gi 20856224  352 IFVCGDQIRKGAALNAVQIAEMLL 375
Cdd:PLN02383 321 IFVCGDQIRKGAALNAVQIAELLL 344
 
Name Accession Description Interval E-value
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
32-375 0e+00

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 717.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   32 MSLQESAPSLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGS 111
Cdd:PLN02383   1 MALTENGPSVAIVGVTGAVGQEFLSVLTDRDFPYSSLKMLASARSAGKKVTFEGRDYTVEELTEDSFDGVDIALFSAGGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  112 ISKEFGPLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKVGMGKGALIANPNCSTIICLMAVTPLHHHAKVKRM 191
Cdd:PLN02383  81 ISKKFGPIAVDKGAVVVDNSSAFRMEEGVPLVIPEVNPEAMKHIKLGKGKGALIANPNCSTIICLMAVTPLHRHAKVKRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  192 VVSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVT 271
Cdd:PLN02383 161 VVSTYQAASGAGAAAMEELEQQTREVLEGKPPTCNIFAQQYAFNLFSHNAPMQENGYNEEEMKLVKETRKIWNDDDVKVT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  272 ATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDVSQDGNFGLD 351
Cdd:PLN02383 241 ATCIRVPVMRAHAESINLQFEKPLDEATAREILASAPGVKIIDDRANNRFPTPLDASNKDDVAVGRIRQDISQDGNKGLD 320
                        330       340
                 ....*....|....*....|....
gi 20856224  352 IFVCGDQIRKGAALNAVQIAEMLL 375
Cdd:PLN02383 321 IFVCGDQIRKGAALNAVQIAELLL 344
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
39-375 4.71e-180

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: 502.64  E-value: 4.71e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  39 PSLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGP 118
Cdd:COG0136   1 YNVAVVGATGAVGRVLLELLEERDFPVGELRLLASSRSAGKTVSFGGKELTVEDATDFDFSGVDIALFSAGGSVSKEYAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 119 LAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAmkgIKVGMGKGaLIANPNCSTIICLMAVTPLHHHAKVKRMVVSTYQA 198
Cdd:COG0136  81 KAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEA---LADHLPKG-IIANPNCSTIQMLVALKPLHDAAGIKRVVVSTYQA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 199 ASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVTATCIRVP 278
Cdd:COG0136 157 VSGAGAAAMDELAEQTAALLNGEEIEPEVFPHPIAFNLIPQIDVFLENGYTKEEMKMVNETRKILGDPDIPVSATCVRVP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 279 VMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDVSQDGnfGLDIFVCGDQ 358
Cdd:COG0136 237 VFRGHSEAVNIEFERPVSLEEARELLAAAPGVKVVDDPAENDYPTPLDASGTDEVFVGRIRKDLSVPN--GLNLWVVADN 314
                       330
                ....*....|....*..
gi 20856224 359 IRKGAALNAVQIAEMLL 375
Cdd:COG0136 315 LRKGAALNAVQIAELLI 331
asd_B TIGR01296
aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families ...
40-374 2.53e-134

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: 387.24  E-value: 2.53e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224    40 SLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGPL 119
Cdd:TIGR01296   1 NVAIVGATGAVGQEMLKLLEERNFPIDKLVLLASARSAGRKLTFKGKELEVEEAETESFEGIDIALFSAGGSVSKEFAPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   120 AAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKvgmgKGALIANPNCSTIICLMAVTPLHHHAKVKRMVVSTYQAA 199
Cdd:TIGR01296  81 AAKAGVIVIDNTSAFRMDPDVPLVVPEVNFEDLKEFN----PKGIIANPNCSTIQMVVVLKPLHDEAKIKRVVVSTYQAV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   200 SGAGAAAMEELVQQTREVLEG--KPPTC----NIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVTAT 273
Cdd:TIGR01296 157 SGAGNAGVEELYNQTKAVLEGaeQLPYIqpkaNKFPYQIAFNAIPHIDSFVDDGYTKEEQKMLFETRKIMGIPDLKVSAT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   274 CIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDVSqDGNfGLDIF 353
Cdd:TIGR01296 237 CVRVPVFTGHSESINIEFEKEISPEDARELLKNAPGVQLIDDPSGNLYPTPLAAVGVDEVFVGRIRKDLP-DGN-GLHLW 314
                         330       340
                  ....*....|....*....|.
gi 20856224   354 VCGDQIRKGAALNAVQIAEML 374
Cdd:TIGR01296 315 VVADNLRKGAALNSVQIAELL 335
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
170-359 8.77e-106

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: 308.67  E-value: 8.77e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 170 CSTIICLMAVTPLHHHAKVKRMVVSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYN 249
Cdd:cd18131   1 CSTIQMVVALKPLHDAFGLKRVVVSTYQAVSGAGAAAMEELEEQTRGLLNGKEAEPKVFPYQIAFNVIPHIDVFLDNGYT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 250 EEEMKLVKETRKIWNDTEVKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSN 329
Cdd:cd18131  81 KEEMKMVNETRKILGDPDLRVSATCVRVPVFRGHSESVNIEFEKPISVEEAREALAKAPGVVVVDDPANNVYPTPLDAAG 160
                       170       180       190
                ....*....|....*....|....*....|
gi 20856224 330 KDDVAVGRIRRDVSQDgnFGLDIFVCGDQI 359
Cdd:cd18131 161 KDDVFVGRIRKDISVP--NGLNLWVVGDNL 188
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
42-155 9.30e-43

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: 144.97  E-value: 9.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224    42 AVVGVTGAVGQEFLSVLsDRDFPYSSIKMLASKRSAGKRVAF------DGHEYTVEELTADSFNGVDIALFSAGGSISKE 115
Cdd:pfam01118   3 AIVGATGYVGQELLRLL-EEHPPVELVVLFASSRSAGKKLAFvhpileGGKDLVVEDVDPEDFKDVDIVFFALPGGVSKE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 20856224   116 FGPLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGI 155
Cdd:pfam01118  82 IAPKLAEAGAKVIDLSSDFRMDDDVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
42-155 5.62e-34

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: 122.27  E-value: 5.62e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224     42 AVVGVTGAVGQEFLSVLSD-RDFPYSSIkmLASKRSAGKRVAFDGH---EYTVEELTADSFN--GVDIALFSAGGSISKE 115
Cdd:smart00859   3 AIVGATGYVGQELLRLLAEhPDFELTAL--AASSRSAGKKVSEAGPhlkGEVVLELDPPDFEelAVDIVFLALPHGVSKE 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 20856224    116 FGPL---AAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGI 155
Cdd:smart00859  81 SAPLlprAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
32-375 0e+00

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 717.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   32 MSLQESAPSLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGS 111
Cdd:PLN02383   1 MALTENGPSVAIVGVTGAVGQEFLSVLTDRDFPYSSLKMLASARSAGKKVTFEGRDYTVEELTEDSFDGVDIALFSAGGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  112 ISKEFGPLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKVGMGKGALIANPNCSTIICLMAVTPLHHHAKVKRM 191
Cdd:PLN02383  81 ISKKFGPIAVDKGAVVVDNSSAFRMEEGVPLVIPEVNPEAMKHIKLGKGKGALIANPNCSTIICLMAVTPLHRHAKVKRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  192 VVSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVT 271
Cdd:PLN02383 161 VVSTYQAASGAGAAAMEELEQQTREVLEGKPPTCNIFAQQYAFNLFSHNAPMQENGYNEEEMKLVKETRKIWNDDDVKVT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  272 ATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDVSQDGNFGLD 351
Cdd:PLN02383 241 ATCIRVPVMRAHAESINLQFEKPLDEATAREILASAPGVKIIDDRANNRFPTPLDASNKDDVAVGRIRQDISQDGNKGLD 320
                        330       340
                 ....*....|....*....|....
gi 20856224  352 IFVCGDQIRKGAALNAVQIAEMLL 375
Cdd:PLN02383 321 IFVCGDQIRKGAALNAVQIAELLL 344
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
39-375 4.71e-180

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: 502.64  E-value: 4.71e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  39 PSLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGP 118
Cdd:COG0136   1 YNVAVVGATGAVGRVLLELLEERDFPVGELRLLASSRSAGKTVSFGGKELTVEDATDFDFSGVDIALFSAGGSVSKEYAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 119 LAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAmkgIKVGMGKGaLIANPNCSTIICLMAVTPLHHHAKVKRMVVSTYQA 198
Cdd:COG0136  81 KAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEA---LADHLPKG-IIANPNCSTIQMLVALKPLHDAAGIKRVVVSTYQA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 199 ASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVTATCIRVP 278
Cdd:COG0136 157 VSGAGAAAMDELAEQTAALLNGEEIEPEVFPHPIAFNLIPQIDVFLENGYTKEEMKMVNETRKILGDPDIPVSATCVRVP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 279 VMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDVSQDGnfGLDIFVCGDQ 358
Cdd:COG0136 237 VFRGHSEAVNIEFERPVSLEEARELLAAAPGVKVVDDPAENDYPTPLDASGTDEVFVGRIRKDLSVPN--GLNLWVVADN 314
                       330
                ....*....|....*..
gi 20856224 359 IRKGAALNAVQIAEMLL 375
Cdd:COG0136 315 LRKGAALNAVQIAELLI 331
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
42-375 3.32e-165

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 465.02  E-value: 3.32e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   42 AVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGPLAA 121
Cdd:PRK14874   5 AVVGATGAVGREMLNILEERNFPVDKLRLLASARSAGKELSFKGKELKVEDLTTFDFSGVDIALFSAGGSVSKKYAPKAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  122 EKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKvgmGKGaLIANPNCSTIICLMAVTPLHHHAKVKRMVVSTYQAASG 201
Cdd:PRK14874  85 AAGAVVIDNSSAFRMDPDVPLVVPEVNPEALAEHR---KKG-IIANPNCSTIQMVVALKPLHDAAGIKRVVVSTYQAVSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  202 AGAAAMEELVQQTREVLEGK--PPTCNIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVTATCIRVPV 279
Cdd:PRK14874 161 AGKAGMEELFEQTRAVLNAAvdPVEPKKFPKPIAFNVIPHIDVFMDDGYTKEEMKMVNETKKILGDPDLKVSATCVRVPV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  280 MRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDVSQDGnfGLDIFVCGDQI 359
Cdd:PRK14874 241 FTGHSESVNIEFEEPISVEEAREILAEAPGVVLVDDPENGGYPTPLEAVGKDATFVGRIRKDLTVEN--GLHLWVVSDNL 318
                        330
                 ....*....|....*.
gi 20856224  360 RKGAALNAVQIAEMLL 375
Cdd:PRK14874 319 RKGAALNAVQIAELLI 334
asd_B TIGR01296
aspartate-semialdehyde dehydrogenase (peptidoglycan organisms); Two closely related families ...
40-374 2.53e-134

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: 387.24  E-value: 2.53e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224    40 SLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGPL 119
Cdd:TIGR01296   1 NVAIVGATGAVGQEMLKLLEERNFPIDKLVLLASARSAGRKLTFKGKELEVEEAETESFEGIDIALFSAGGSVSKEFAPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   120 AAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKvgmgKGALIANPNCSTIICLMAVTPLHHHAKVKRMVVSTYQAA 199
Cdd:TIGR01296  81 AAKAGVIVIDNTSAFRMDPDVPLVVPEVNFEDLKEFN----PKGIIANPNCSTIQMVVVLKPLHDEAKIKRVVVSTYQAV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   200 SGAGAAAMEELVQQTREVLEG--KPPTC----NIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVTAT 273
Cdd:TIGR01296 157 SGAGNAGVEELYNQTKAVLEGaeQLPYIqpkaNKFPYQIAFNAIPHIDSFVDDGYTKEEQKMLFETRKIMGIPDLKVSAT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   274 CIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDVSqDGNfGLDIF 353
Cdd:TIGR01296 237 CVRVPVFTGHSESINIEFEKEISPEDARELLKNAPGVQLIDDPSGNLYPTPLAAVGVDEVFVGRIRKDLP-DGN-GLHLW 314
                         330       340
                  ....*....|....*....|.
gi 20856224   354 VCGDQIRKGAALNAVQIAEML 374
Cdd:TIGR01296 315 VVADNLRKGAALNSVQIAELL 335
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
170-359 8.77e-106

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: 308.67  E-value: 8.77e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 170 CSTIICLMAVTPLHHHAKVKRMVVSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYN 249
Cdd:cd18131   1 CSTIQMVVALKPLHDAFGLKRVVVSTYQAVSGAGAAAMEELEEQTRGLLNGKEAEPKVFPYQIAFNVIPHIDVFLDNGYT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 250 EEEMKLVKETRKIWNDTEVKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSN 329
Cdd:cd18131  81 KEEMKMVNETRKILGDPDLRVSATCVRVPVFRGHSESVNIEFEKPISVEEAREALAKAPGVVVVDDPANNVYPTPLDAAG 160
                       170       180       190
                ....*....|....*....|....*....|
gi 20856224 330 KDDVAVGRIRRDVSQDgnFGLDIFVCGDQI 359
Cdd:cd18131 161 KDDVFVGRIRKDISVP--NGLNLWVVGDNL 188
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
34-375 4.07e-84

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 259.60  E-value: 4.07e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   34 LQESAPSLAVVGVTGAVGQEFLSVL-SDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSI 112
Cdd:PRK06728   1 MSEKGYHVAVVGATGAVGQKIIELLeKETKFNIAEVTLLSSKRSAGKTVQFKGREIIIQEAKINSFEGVDIAFFSAGGEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  113 SKEFGPLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKvgmgkgALIANPNCSTIICLMAVTPLHHHAKVKRMV 192
Cdd:PRK06728  81 SRQFVNQAVSSGAIVIDNTSEYRMAHDVPLVVPEVNAHTLKEHK------GIIAVPNCSALQMVTALQPIRKVFGLERII 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  193 VSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNIF-----GQQY--AFNLFSHNAPILDNGYNEEEMKLVKETRKIWND 265
Cdd:PRK06728 155 VSTYQAVSGSGIHAIQELKEQAKSILAGEEVESTILpakkdKKHYpiAFNVLPQVDIFTDNDFTFEEVKMIQETKKILED 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  266 TEVKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDRASNTFPTPLDVSNKDDVAVGRIRRDvsQD 345
Cdd:PRK06728 235 PNLKMAATCVRVPVISGHSESVYIELEKEATVAEIKEVLFDAPGVILQDNPSEQLYPMPLYAEGKIDTFVGRIRKD--PD 312
                        330       340       350
                 ....*....|....*....|....*....|
gi 20856224  346 GNFGLDIFVCGDQIRKGAALNAVQIAEMLL 375
Cdd:PRK06728 313 TPNGFHLWIVSDNLLKGAAWNSVQIAETMV 342
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
39-169 2.35e-75

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: 229.63  E-value: 2.35e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  39 PSLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGP 118
Cdd:cd02316   1 YNVAIVGATGAVGQEMLKVLEERNFPVSELRLLASARSAGKTLEFKGKELTVEELTEDSFKGVDIALFSAGGSVSKEFAP 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 20856224 119 LAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKgikvgmGKGALIANPN 169
Cdd:cd02316  81 IAAEAGAVVIDNSSAFRMDPDVPLVVPEVNPEALK------NHKGIIANPN 125
PRK05671 PRK05671
aspartate-semialdehyde dehydrogenase; Reviewed
41-375 9.59e-65

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 168165 [Multi-domain]  Cd Length: 336  Bit Score: 209.20  E-value: 9.59e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   41 LAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGPLA 120
Cdd:PRK05671   7 IAVVGATGTVGEALVQILEERDFPVGTLHLLASSESAGHSVPFAGKNLRVREVDSFDFSQVQLAFFAAGAAVSRSFAEKA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  121 AEKGTIVVDNSSAFRmVDGVPLVIPEVNPEAMKGIKvgmgKGALIANPNCSTIICLMAVTPLHHHAKVKRMVVSTYQAAS 200
Cdd:PRK05671  87 RAAGCSVIDLSGALP-SAQAPNVVPEVNAERLASLA----APFLVSSPSASAVALAVALAPLKGLLDIQRVQVTACLAVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  201 GAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIWNDTEVKVTATCIRVPVM 280
Cdd:PRK05671 162 SLGREGVSELARQTAELLNARPLEPRFFDRQVAFNLLAQVGAPDAQGHTALERRLVAELRQLLGLPELKISVTCIQVPVF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  281 RAHAESVNLQFENPLDENTAREILKKAPGVYIIDDrasNTFPTPL-DVSNKDDVAVGRIRRDVSQDGNfgLDIFVCGDQI 359
Cdd:PRK05671 242 FGDSLSVALQSAAPVDLAAVNAALEAAPGIELVEA---GDYPTPVgDAVGQDVVYVGRVRAGVDDPCQ--LNLWLTSDNV 316
                        330
                 ....*....|....*.
gi 20856224  360 RKGAALNAVQIAEMLL 375
Cdd:PRK05671 317 RKGAALNAVQVAELLI 332
PRK08040 PRK08040
putative semialdehyde dehydrogenase; Provisional
40-375 1.32e-57

putative semialdehyde dehydrogenase; Provisional


Pssm-ID: 181205 [Multi-domain]  Cd Length: 336  Bit Score: 190.68  E-value: 1.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   40 SLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGPL 119
Cdd:PRK08040   6 NIALLGATGAVGEALLELLAERQFPVGELYALASEESAGETLRFGGKSVTVQDAAEFDWSQAQLAFFVAGREASAAYAEE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  120 AAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKvgmgKGALIANPNCSTIICLMAVTPLHHHAKVKRMVVSTYQAA 199
Cdd:PRK08040  86 ATNAGCLVIDSSGLFALEPDVPLVVPEVNPFVLADYR----NRNIIAVADSLTSQLLTAIKPLIDQAGLSRLHVTNLLSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  200 SGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFshnaPIL--DNGYNEEEMKLVKETRKIWNDTEVKVTATCIRV 277
Cdd:PRK08040 162 SAHGKAAVDALAGQSAKLLNGIPIEEGFFGRQLAFNML----PLLpdSEGSVREERRLVDQVRKILQDEGLPISVSCVQS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  278 PVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDrasNTFPTPL-DVSNKDDVAVGRIRRDvsqdgnFG----LDI 352
Cdd:PRK08040 238 PVFYGHAQMVHFEALRPLAAEEARDALEQGEDIVLSEE---NDYPTQVgDASGNPHLSIGCVRND------YGmpeqLQF 308
                        330       340
                 ....*....|....*....|...
gi 20856224  353 FVCGDQIRKGAALNAVQIAEMLL 375
Cdd:PRK08040 309 WSVADNVRFGGALMAVKTAEKLV 331
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
42-374 3.67e-55

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 184.64  E-value: 3.67e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   42 AVVGVTGAVGQEFLSVLSDrdFPYSSIKML-ASKRSAGKR----------------VAfdghEYTVEELTADSFNGVDIa 104
Cdd:PRK08664   7 GILGATGMVGQRFVQLLAN--HPWFEVTALaASERSAGKTygeavrwqldgpipeeVA----DMEVVSTDPEAVDDVDI- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  105 LFSA-----GGSISKEFgplaAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKV----GMGKGALIANPNCSTIIC 175
Cdd:PRK08664  80 VFSAlpsdvAGEVEEEF----AKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVqrkrRGWDGFIVTNPNCSTIGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  176 LMAVTPLhHHAKVKRMVVSTYQAasgagaaameelvqqtrevlegkpptcnIFGQQYAFnlfshnAP---ILDN----GY 248
Cdd:PRK08664 156 VLALKPL-MDFGIERVHVTTMQA----------------------------ISGAGYPG------VPsmdIVDNvipyIG 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  249 NEEEmKLVKETRKIW---NDTEV-----KVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKK------------AP 308
Cdd:PRK08664 201 GEEE-KIEKETLKILgkfEGGKIvpadfPISATCHRVPVIDGHTEAVFVKFKEDVDPEEIREALESfkglpqelglpsAP 279
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20856224  309 GVYII----DDRasntfPTP-LDVSNKDD--VAVGRIRrdvsQDGNFGLDiFVC-GDQIRKGAALNAVQIAEML 374
Cdd:PRK08664 280 KKPIIlfeePDR-----PQPrLDRDAGDGmaVSVGRLR----EDGIFDIK-FVVlGHNTVRGAAGASVLNAELL 343
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
42-155 9.30e-43

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: 144.97  E-value: 9.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224    42 AVVGVTGAVGQEFLSVLsDRDFPYSSIKMLASKRSAGKRVAF------DGHEYTVEELTADSFNGVDIALFSAGGSISKE 115
Cdd:pfam01118   3 AIVGATGYVGQELLRLL-EEHPPVELVVLFASSRSAGKKLAFvhpileGGKDLVVEDVDPEDFKDVDIVFFALPGGVSKE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 20856224   116 FGPLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGI 155
Cdd:pfam01118  82 IAPKLAEAGAKVIDLSSDFRMDDDVPYGLPEVNREAIKQA 121
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
42-375 5.20e-42

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: 149.91  E-value: 5.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224    42 AVVGVTGAVGQEFLSVLSDRdfPYSSI-KMLASKRSAGKRVA------FDG------HEYTVEELTADSFNGVDIALFSA 108
Cdd:TIGR00978   4 AVLGATGLVGQKFVKLLAKH--PYFELaKVVASPRSAGKRYGeavkwiEPGdmpeyvRDLPIVEPEPVASKDVDIVFSAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   109 GGSISKEFGPLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKV---GMGKGALIANPNCSTIICLMAVTPLHHH 185
Cdd:TIGR00978  82 PSEVAEEVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVqkeRGWKGFIVTNPNCTTAGLTLALKPLIDA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   186 AKVKRMVVSTYQAASGAgaaameelvqqtrevleGKP--PTCNIFGqqyafNLFSHnapildngYNEEEMKLVKETRKIW 263
Cdd:TIGR00978 162 FGIKKVHVTTMQAVSGA-----------------GYPgvPSMDILD-----NIIPH--------IGGEEEKIERETRKIL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   264 NDTE--------VKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKK------------APGVYII----DDRasn 319
Cdd:TIGR00978 212 GKLEngkiepapFSVSATTTRVPVLDGHTESVHVEFDKKFDIEEIREALKSfrglpqklglpsAPEKPIIvrdeEDR--- 288
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 20856224   320 tfPTP-LDVSNKDD--VAVGRIRRDvsqdgNFGLDIFVCGDQIRKGAALNAVQIAEMLL 375
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 ...
171-357 5.15e-41

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: 142.72  E-value: 5.15e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 171 STIICLMAVTPLHHHAKVKRMVVSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYNE 250
Cdd:cd18129   2 AAIALARVLAPLHDAAGLERVVVTVLQPVSEAGQAGVDELARQTARLLNGQPVEPEVFPRQLAFNLLPQVGDFDADGLSD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 251 EEMKLVKETRKIWNDTEVKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGVYIIDDraSNTFPTPLDVSNK 330
Cdd:cd18129  82 EERRIAAELRRLLGGPDLPVSVTCVQVPVFYGHSASVHVELAEPVDLEEVRAALAAAPGLELADD--AEAPPYPVDAAGS 159
                       170       180
                ....*....|....*....|....*..
gi 20856224 331 DDVAVGRIRRDVSQDGnfGLDIFVCGD 357
Cdd:cd18129 160 DDVLVGRVRQDPGNPR--GLWLWAVAD 184
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
39-169 1.26e-36

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: 129.66  E-value: 1.26e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  39 PSLAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGP 118
Cdd:cd17894   1 YRIAVVGATGLVGKELLELLEERGFPVGRLRLLDSEESAGELVEFGGEPLDVQDLDEFDFSDVDLVFFAGPAEVARAYAP 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 20856224 119 LAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIkvgmGKGALIANPN 169
Cdd:cd17894  81 RARAAGCLVIDLSGALRSDPDVPLVVPGVNPEALAAA----AERRVVAVPN 127
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
41-169 1.61e-34

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: 124.37  E-value: 1.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  41 LAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGHEYTVEELTADSFNGVDIALFSAGGSISKEFGPLA 120
Cdd:cd24147   3 VGVVGATGAVGSEILQLLAEEPDPLFELRALASEESAGKKAEFAGEAIMVQEADPIDFLGLDIVFLCAGAGVSAKFAPEA 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 20856224 121 AEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKvgmgKGALIANPN 169
Cdd:cd24147  83 ARAGVLVIDNAGALRMDPDVPLVVPEVNAEAIGLGE----GTPLLVIPN 127
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
42-155 5.62e-34

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: 122.27  E-value: 5.62e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224     42 AVVGVTGAVGQEFLSVLSD-RDFPYSSIkmLASKRSAGKRVAFDGH---EYTVEELTADSFN--GVDIALFSAGGSISKE 115
Cdd:smart00859   3 AIVGATGYVGQELLRLLAEhPDFELTAL--AASSRSAGKKVSEAGPhlkGEVVLELDPPDFEelAVDIVFLALPHGVSKE 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 20856224    116 FGPL---AAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGI 155
Cdd:smart00859  81 SAPLlprAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIKKA 123
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
41-169 2.43e-30

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


Pssm-ID: 467516 [Multi-domain]  Cd Length: 145  Bit Score: 113.23  E-value: 2.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  41 LAVVGVTGAVGQEFLSVLSDRDFPYSSIKMLASKRSAGKRVAFDGH---EYTVEELTADSFNGVDIALFSAGGSISKEFG 117
Cdd:cd02281   3 VGVVGATGYVGGEFLRLLLEHPFPLFEIVLLAASSAGAKKKYFHPKlwgRVLVEFTPEEVLEQVDIVFTALPGGVSAKLA 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 20856224 118 PLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKvgmgKGALIANPN 169
Cdd:cd02281  83 PELSEAGVLVIDNASDFRLDKDVPLVVPEVNREHIGELK----GTKIIANPN 130
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
181-361 2.55e-29

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: 111.25  E-value: 2.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   181 PLH-HHAKVKRMVVSTYQAASGAgaaameelvqqtrevleGKPPTCNIFGQQYAFNLFSHNAPILDNGYNE--EEMKLVK 257
Cdd:pfam02774   3 PLRdALGGLERVIVDTYQAVSGA-----------------GKKAKPGVFGAPIADNLIPYIDGEEHNGTPEtrEELKMVN 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   258 ETRKIWNDTEvKVTATCIRVPVMRAHAESVNLQFEN-PLDENTAREILKKAPGVYIIdDRASNTFPTPLDVSNK-DDVAV 335
Cdd:pfam02774  66 ETKKILGFTP-KVSATCVRVPVFRGHSETVTVKLKLkPIDVEEVYEAFYAAPGVFVV-VRPEEDYPTPRAVRGGtNFVYV 143
                         170       180
                  ....*....|....*....|....*.
gi 20856224   336 GRIRRDVsqDGNFGLDIFVCGDQIRK 361
Cdd:pfam02774 144 GRVRKDP--DGDRGLKLVSVIDNLRK 167
ASADH_C_like cd18124
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
170-359 1.93e-27

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: 106.90  E-value: 1.93e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 170 CSTIICLMAVTPLHHHAKVKRMVVSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNIFGQQYAFNLFSHNAPILDNGYN 249
Cdd:cd18124   1 CTVSLLVMALKPLFAKFLVEWVSVAT*QAVSGAGYENMRELLSQMGELMRAGPLPTGVFS*AIADNLIPWIDKVLDNGQS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 250 EEEMKLVKETRKIWNDTE--VKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKK-APGVYII-DDRASNTFP-TP 324
Cdd:cd18124  81 KEEWKIQAEANKILGTLDspIPISVTCNRVPVLDGHSQSFTLKLKEDVPLEEVEEVLDAhKPWVKVIpNDYAIRPQPrLD 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 20856224 325 LDVSNKDDVAVGRIRRDvsQDGNFGLDIFVCGDQI 359
Cdd:cd18124 161 RKVTGGLSTPVGRIRKD--AMDPFDVNAFAVSDNT 193
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
42-174 2.19e-26

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: 103.34  E-value: 2.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  42 AVVGVTGAVGQEFLSVLSDRdfPYSSIKML-ASKRSAGK--RVAFDGH----------EYTVEELTADSFNGVDIAlFSA 108
Cdd:cd02315   4 GVLGATGMVGQRFIQLLANH--PWFELAALgASERSAGKkyGDAVRWKqdtpipeevaDMVVKECEPEEFKDCDIV-FSA 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20856224 109 -----GGSISKEFgplaAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKV----GMGKGALIANPNCsTII 174
Cdd:cd02315  81 ldsdvAGEIEPAF----AKAGIPVFSNASNHRMDPDVPLVIPEVNPDHLDLIEAqrkrRGWKGFIVTNPNN-TVR 150
ASADH_C cd18128
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar ...
170-359 3.74e-26

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: 102.58  E-value: 3.74e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 170 CSTIICLMAVTPLHHHAKVKRMVVSTYQAASGAgaaameelvqqtrevlegkpptcnifGQQYAFNLFSHNAPILDNGYN 249
Cdd:cd18128   1 CTVSLMLMALGGLFQKFLVEWVSVATYQAVSGA--------------------------G*PIAGNLIPWIDVFLDNGQT 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 250 EEEMKLVKETRKIWNDTE--VKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAP-GVYIIDDRASNTFPTPLD 326
Cdd:cd18128  55 KEEWKGQAETNKILGDLDspIPISGTCVRVGVLRCHSQAFTIKLKEDAPIEEVEEAIAAHN*WIKVIPNVDRITPRTPAN 134
                       170       180       190
                ....*....|....*....|....*....|...
gi 20856224 327 VSNKDDVAVGRIRRDvsQDGNFGLDIFVCGDQI 359
Cdd:cd18128 135 VTGTLSTPVGRIRKD--AMGPFDLQAFTVGDNL 165
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
170-357 2.82e-20

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: 87.29  E-value: 2.82e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 170 CSTIICLMAVTPLHHHAKVKRMVVSTYQAasgagaaameelvqqtrevlegkpptcnIFGQQYAFnLFSHNapILDN--G 247
Cdd:cd18130   1 CSTAGLALPLKPLHDFFGIEAVIVTTMQA----------------------------ISGAGYPG-VPSLD--ILDNviP 49
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 248 Y-NEEEMKLVKETRKIWNDTE--------VKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKK-----------A 307
Cdd:cd18130  50 YiGGEEEKIESETKKILGTLNedkiepadFKVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENyepepqvlgppS 129
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20856224 308 PGVYIIDDRASNTFPTPL---DVSNKDDVAVGRIRrdvsQDGNFGLDIFVCGD 357
Cdd:cd18130 130 APKPIIVVEDEPRRPQPRldrDAGDGMAVTVGRIR----KDDDFDLKFVLLSH 178
PRK06598 PRK06598
aspartate-semialdehyde dehydrogenase; Reviewed
44-364 1.07e-17

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 235839  Cd Length: 369  Bit Score: 83.34  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   44 VGVTGAVGqeflSVLSDR-----DFPYSSIKMLASKRSAGKRVAFDGHE------YTVEELTAdsfngVDIALFSAGGSI 112
Cdd:PRK06598   7 VGWRGMVG----SVLMQRmveenDFDLIEPVFFSTSQAGGAAPSFGGKEgtlqdaFDIDALKK-----LDIIITCQGGDY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  113 SKEFGPLAAEKG--TIVVDNSSAFRMVDGVPLVIPEVNpeaMKGIKVGMGKGalIAN---PNCSTIICLMAVTPLHHHAK 187
Cdd:PRK06598  78 TNEVYPKLRAAGwqGYWIDAASTLRMKDDAIIILDPVN---RDVIDDALANG--VKTfvgGNCTVSLMLMALGGLFKNDL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  188 VKRMVVSTYQAASGAGAAAMEELVQQT----------------------REVLE----GKPPTCNiFGQQYAFNLFshna 241
Cdd:PRK06598 153 VEWVSVMTYQAASGAGARNMRELLTQMgalhgavadeladpasaildidRKVTElmrsGDLPTDN-FGVPLAGSLI---- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  242 P----ILDNGYNEEEMKLVKETRKIWNDTE--VKVTATCIRVPVMRAHAES--VNLQFENPLDEntAREILKKA-PGVYI 312
Cdd:PRK06598 228 PwidkDLGNGQSREEWKGQAETNKILGLTKnpIPVDGLCVRVGAMRCHSQAltIKLKKDVPLAE--IEEILAAHnPWVKV 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 20856224  313 I-DDR-ASNTFPTPLDVSNKDDVAVGRIRRdvsqdGNFG---LDIFVCGDQIRKGAA 364
Cdd:PRK06598 306 VpNDReATMRELTPAAVTGTLTIPVGRLRK-----LNMGpeyLSAFTVGDQLLWGAA 357
ASADH_C_bac_like cd23938
C-terminal catalytic domain of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) and ...
170-359 4.01e-14

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: 70.80  E-value: 4.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 170 CSTIICLMAVTPLHHHAKVKRMVVSTYQAASGAGAAAMEELVQQT----------------------REVLE----GKPP 223
Cdd:cd23938   1 CTVSLMLMALGGLFKNDLVEWISSMTYQAASGAGAKNMRELLSQMgalgdavsdeladpasaildidRKVTElqrsGSFP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 224 TCNiFGQQYAFNLFSHNAPILDNGYNEEEMKLVKETRKIW-NDTEVKVTATCIRVPVMRAHAES--VNLQFENPLDEntA 300
Cdd:cd23938  81 TDN-FGVPLAGSLIPWIDKQLENGQSKEEWKGQVETNKILgTSKPIPIDGLCVRVGAMRCHSQAltIKLKKDVPLDE--I 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20856224 301 REILKKA-PGVYIIDDR--ASNTFPTPLDVSNKDDVAVGRIRRdvsqdGNFG---LDIFVCGDQI 359
Cdd:cd23938 158 EEIIAAHnQWVKVVPNDkeATLRELTPAAVTGTLTVPVGRLRK-----LNMGpeyLSAFTVGDQL 217
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
42-170 8.26e-09

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: 56.62  E-value: 8.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  42 AVVGVTGAVGQEFLSVLSDRdfPYSSIKMLASKRSAGKRVA-----FDGH-EYTVEELTADS-FNGVDIALFSAGGSISK 114
Cdd:COG0002   4 GIVGASGYTGGELLRLLLRH--PEVEIVALTSRSNAGKPVSevhphLRGLtDLVFEPPDPDElAAGCDVVFLALPHGVSM 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20856224 115 EFGPLAAEKGTIVVDNSSAFRMVD--------GVP-----LV------IPEVNPEAMKGIKvgmgkgaLIANPNC 170
Cdd:COG0002  82 ELAPELLEAGVKVIDLSADFRLKDpavyekwyGFEhaapeLLgeavygLPELNREEIKGAR-------LIANPGC 149
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
42-169 1.51e-08

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: 53.59  E-value: 1.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  42 AVVGVTGAVGQEFLSVLSDRdfPYSSIKMLASKRSAGKRVA----FDGHEYTVEELTADS---FNGVDIALFSAGGSISK 114
Cdd:cd17895   4 GIIGASGYTGAELLRLLLNH--PEVEIVALTSRSYAGKPVSevfpHLRGLTDLTFEPDDDeeiAEDADVVFLALPHGVSM 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 115 EFGPLAAEKGTIVVDNSSAFRMVD--------GVPLVIPEVNPEAMKGI------KVgmgKGA-LIANPN 169
Cdd:cd17895  82 ELAPKLLEAGVKVIDLSADFRLKDpetyekwyGFEHAAPELLKEAVYGLpelnreEI---KKArLVANPN 148
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
42-155 2.73e-08

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: 52.72  E-value: 2.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  42 AVVGVTGAVGQEFLSVLSDRdfPYSSIKMLASKRSAGK------------RVAFDGHEYTVEELTADSFNGVDIaLFS-- 107
Cdd:cd24150   5 AILGATGLVGIEYVRMLSNH--PYIKPAYLAGKGSVGKpygevvrwqtvgQVPKEIADMEIKPTDPKLMDDVDI-IFSpl 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 20856224 108 ---AGGSISKEFgplaAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGI 155
Cdd:cd24150  82 pqgAAGPVEEQF----AKEGFPVISNSPDHRFDPDVPLLVPELNPHTISLI 128
PRK06901 PRK06901
oxidoreductase;
75-297 2.82e-08

oxidoreductase;


Pssm-ID: 235883 [Multi-domain]  Cd Length: 322  Bit Score: 54.74  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   75 RSAGKRVAfdghEYTVEELTADSFNGVdialFSAGGSISKEFGPLAAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKG 154
Cdd:PRK06901  47 RFNNKAVE----QIAPEEVEWADFNYV----FFAGKMAQAEHLAQAAEAGCIVIDLYGICAALANVPVVVPSVNDEQLAE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  155 IK----VGMgkgaliANPNCSTiiCLMAVTPLHHHAKVKRMVVSTYQAASGAGAAAMEELVQQTREVLEGKPPTCNifGQ 230
Cdd:PRK06901 119 LRqrniVSL------PDPQVSQ--LALALAPFLQEQPLSQIFVTSLLPASYTDAETVKKLAGQTARLLNGIPLDEE--EQ 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20856224  231 QYAFNLFSHNAPILDNgyneeemklvkETRKIWNDTEvKVTATCIRVPVMRAHAESVNLQFENPLDE 297
Cdd:PRK06901 189 RLAFDVFPANAQNLEL-----------QLQKIFPQLE-NVTFHSIQVPVFYGLAQMVTALSEYELDI 243
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
39-169 3.75e-07

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: 49.49  E-value: 3.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  39 PSLAVVGVTGAVGQEFLSVLSDRdfPYSSIKMLASKRSAGKRVAFDgHEYTVEELTADSF------NGVDIALFSAGGSI 112
Cdd:cd02280   1 PRVAIIGASGYTGLEIVRLLLGH--PYLRVLTLSSRERAGPKLREY-HPSLIISLQIQEFrpcevlNSADILVLALPHGA 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20856224 113 SKEFGPLAAEKGTIVVDNSSAFRMVD--------------GVPLVIPEVNPEA-MKGIKVgmgkgalIANPN 169
Cdd:cd02280  78 SAELVAAISNPQVKIIDLSADFRFTDpevyrrhprpdlegGWVYGLPELDREQrIANATR-------IANPN 142
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
170-345 3.40e-05

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: 43.66  E-value: 3.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 170 CSTIICLMAVTPLHHHAKVKRMVVSTYQAASGAGAAAMEELvqqtrevlegkpptcnifgqqyafNLFSHNAPIldNGYN 249
Cdd:cd18122   1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI------------------------LKSEVRAII--PNIP 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 250 EEEMKLVKETRKIWN--DTEVKVTATCIRVPVMRAHAESVNLQFENPLDENTAREILKKAPGV--YIIDDRASNTFPTPL 325
Cdd:cd18122  55 KNETKHAPETGKVLGeiGKPIKVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEvqISAEDGLTYAKVSTR 134
                       170       180
                ....*....|....*....|
gi 20856224 326 DVSNKDDVAVGRIRRDVSQD 345
Cdd:cd18122 135 SVGGVYGVPVGRQREFAFDD 154
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
4-170 1.19e-04

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 43.66  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224    4 FTHQTPQTHFLSRLPLRAKPRH-FSARVKMSLQESAPSLAVVGVTGAVGQEFLSVLSDRdfPYSSIKMLASKRSAGKRVA 82
Cdd:PLN02968   3 FADSVGSKGLASRASVTSSPQSvVSSASSSVKSEEKKRIFVLGASGYTGAEVRRLLANH--PDFEITVMTADRKAGQSFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224   83 FD-GHEYT------VEELTADsFNGVDIALFSAGGSISKEFGPlAAEKGTIVVDNSSAFRMVD--------GVPLVIPEV 147
Cdd:PLN02968  81 SVfPHLITqdlpnlVAVKDAD-FSDVDAVFCCLPHGTTQEIIK-ALPKDLKIVDLSADFRLRDiaeyeewyGHPHRAPEL 158
                        170       180
                 ....*....|....*....|....*..
gi 20856224  148 NPEAMKGI----KVGMGKGALIANPNC 170
Cdd:PLN02968 159 QKEAVYGLtelqREEIKSARLVANPGC 185
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
40-169 1.87e-04

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: 41.50  E-value: 1.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  40 SLAVVGVTGAVGQEFLSVLSDRdfPYSSIKMLASKRSAGKRVAfDGH-------EYTVEELTADSFNGVDIaLFSA---G 109
Cdd:cd24148   2 RVAVAGASGYAGGELLRLLLGH--PEFEIGALTAHSNAGQRLG-ELHphlpplaDRVLEPTTPAVLAGHDV-VFLAlphG 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20856224 110 GSiskefGPLAAEKG--TIVVDNSSAFRMVD--------------GVPLVIPEVNP--EAMKGIKvgmgkgaLIANPN 169
Cdd:cd24148  78 AS-----AAIAAQLPpdVLVVDCGADHRLEDaaawekfyggehagGWTYGLPELPGarEALAGAR-------RIAVPN 143
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
40-163 8.68e-04

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: 39.57  E-value: 8.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  40 SLAVVGVTGAVGQEFLSVLSDRdfPYSSIKMLASKRSAGKRV-------------AFDgHEYTVEEltadsfngVDIaLF 106
Cdd:cd24151   2 TVSIVGASGYTGGELLRLLLGH--PEVEVKQVTSESLAGKPVhrvhpnlrgrtllKFV-PPEELES--------CDV-LF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224 107 SA--GGSISKEFGPLAaEKGTIVVDNSSAFRMVD--------GVPLV-----------IPEVNPEAMKGIK----VGMGK 161
Cdd:cd24151  70 LAlpHGESMKRIDRFA-ELAPRIIDLSADFRLKDpaaydrwyGGPHPrpellerfvygLPELHREELRGARyiagANLMK 148

                ..
gi 20856224 162 GA 163
Cdd:cd24151 149 GA 150
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
40-168 1.51e-03

N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. The model corresponds to the AGPR N-terminal NAD(P)-binding domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467525 [Multi-domain]  Cd Length: 154  Bit Score: 38.63  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20856224  40 SLAVVGVTGAVGQEFLSVLSDRdfPYSSIKmLASKRS-AGKRVAfdghEYTVEELTADSFNGVDIALFSAGGSI------ 112
Cdd:cd24149   2 RVGLIGARGYVGRELIRLLNRH--PNLELA-HVSSRElAGQKVS----GYTKSPIDYLNLSVEDIPEEVAAREVdawvla 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20856224 113 -----SKEFGPL--AAEKGTIVVDNSSAFRMVDGVPLVIPEVNPEAMKGIKvgmgkgaLIANP 168
Cdd:cd24149  75 lpngvAKPFVDAidKANPKSVIVDLSADYRFDDAWTYGLPELNRRRIAGAK-------RISNP 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH