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Conserved domains on  [gi|16131307|ref|NP_417891|]
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aspartate-semialdehyde dehydrogenase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

aspartate-semialdehyde dehydrogenase( domain architecture ID 11482335)

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
PRK06598 PRK06598
aspartate-semialdehyde dehydrogenase; Reviewed
1-366 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


:

Pssm-ID: 235839  Cd Length: 369  Bit Score: 823.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307    1 MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNE 80
Cdd:PRK06598   1 MKKVGFVGWRGMVGSVLMQRMVEENDFDLIEPVFFSTSQAGGAAPSFGGKEGTLQDAFDIDALKKLDIIITCQGGDYTNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   81 IYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVAT 160
Cdd:PRK06598  81 VYPKLRAAGWQGYWIDAASTLRMKDDAIIILDPVNRDVIDDALANGVKTFVGGNCTVSLMLMALGGLFKNDLVEWVSVMT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  161 YQAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSR 240
Cdd:PRK06598 161 YQAASGAGARNMRELLTQMGALHGAVADELADPASAILDIDRKVTELMRSGDLPTDNFGVPLAGSLIPWIDKDLGNGQSR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  241 EEWKGQAETNKILN-TSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNPWAKVVPNDREITMRELTPA 319
Cdd:PRK06598 241 EEWKGQAETNKILGlTKNPIPVDGLCVRVGAMRCHSQALTIKLKKDVPLAEIEEILAAHNPWVKVVPNDREATMRELTPA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 16131307  320 AVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQL 366
Cdd:PRK06598 321 AVTGTLTIPVGRLRKLNMGPEYLSAFTVGDQLLWGAAEPLRRMLRIL 367
 
Name Accession Description Interval E-value
PRK06598 PRK06598
aspartate-semialdehyde dehydrogenase; Reviewed
1-366 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 235839  Cd Length: 369  Bit Score: 823.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307    1 MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNE 80
Cdd:PRK06598   1 MKKVGFVGWRGMVGSVLMQRMVEENDFDLIEPVFFSTSQAGGAAPSFGGKEGTLQDAFDIDALKKLDIIITCQGGDYTNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   81 IYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVAT 160
Cdd:PRK06598  81 VYPKLRAAGWQGYWIDAASTLRMKDDAIIILDPVNRDVIDDALANGVKTFVGGNCTVSLMLMALGGLFKNDLVEWVSVMT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  161 YQAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSR 240
Cdd:PRK06598 161 YQAASGAGARNMRELLTQMGALHGAVADELADPASAILDIDRKVTELMRSGDLPTDNFGVPLAGSLIPWIDKDLGNGQSR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  241 EEWKGQAETNKILN-TSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNPWAKVVPNDREITMRELTPA 319
Cdd:PRK06598 241 EEWKGQAETNKILGlTKNPIPVDGLCVRVGAMRCHSQALTIKLKKDVPLAEIEEILAAHNPWVKVVPNDREATMRELTPA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 16131307  320 AVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQL 366
Cdd:PRK06598 321 AVTGTLTIPVGRLRKLNMGPEYLSAFTVGDQLLWGAAEPLRRMLRIL 367
asd_gamma TIGR01745
aspartate-semialdehyde dehydrogenase, gamma-proteobacterial; [Amino acid biosynthesis, ...
2-367 0e+00

aspartate-semialdehyde dehydrogenase, gamma-proteobacterial; [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 130806 [Multi-domain]  Cd Length: 366  Bit Score: 748.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307     2 KNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNEI 81
Cdd:TIGR01745   1 KNVGLVGWRGMVGSVLMQRMQEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDIDALKALDIIITCQGGDYTNEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307    82 YPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATY 161
Cdd:TIGR01745  81 YPKLRESGWQGYWIDAASSLRMKDDAVIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVEWVSVATY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   162 QAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSRE 241
Cdd:TIGR01745 161 QAASGGGARHMRELLTQMGHLYGHVEDELATPSSAILDIERKVTKLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSRE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   242 EWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNPWAKVVPNDREITMRELTPAAV 321
Cdd:TIGR01745 241 EWKGQAETNKILGTSSTIPVDGLCVRIGALRCHSQAFTIKLKKDVSLETIEEIIRAHNPWVKVVPNDREITMRELTPAAV 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 16131307   322 TGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQLA 367
Cdd:TIGR01745 321 TGTLTIPVGRLRKLNMGPEYLSAFTVGDQLLWGAAEPLRRMLRILA 366
ASADH_C_bac_like cd23938
C-terminal catalytic domain of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) and ...
135-351 8.66e-165

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: 459.08  E-value: 8.66e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 135 CTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELP 214
Cdd:cd23938   1 CTVSLMLMALGGLFKNDLVEWISSMTYQAASGAGAKNMRELLSQMGALGDAVSDELADPASAILDIDRKVTELQRSGSFP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 215 VDNFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEEL 294
Cdd:cd23938  81 TDNFGVPLAGSLIPWIDKQLENGQSKEEWKGQVETNKILGTSKPIPIDGLCVRVGAMRCHSQALTIKLKKDVPLDEIEEI 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131307 295 LAAHNPWAKVVPNDREITMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQL 351
Cdd:cd23938 161 IAAHNQWVKVVPNDKEATLRELTPAAVTGTLTVPVGRLRKLNMGPEYLSAFTVGDQL 217
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
2-367 4.98e-161

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: 454.10  E-value: 4.98e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   2 KNVGFIGWRGMVGSVLMQRMvEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDlEALKALDIIVTCQGGDYTNEI 81
Cdd:COG0136   1 YNVAVVGATGAVGRVLLELL-EERDFPVGELRLLASSRSAGKTVSFGGKELTVEDATD-FDFSGVDIALFSAGGSVSKEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  82 YPKLRESGwqGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIrtFVGGNCTVSLMLMSLGGLFANDLVDWVSVATY 161
Cdd:COG0136  79 APKAAAAG--AVVIDNSSAFRMDPDVPLVVPEVNPEALADHLPKGI--IANPNCSTIQMLVALKPLHDAAGIKRVVVSTY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 162 QAASGGGARHMRELLTQMGHLYGhvadelatpssaildierkvttltrSGELPVDNFGVPLAGSLIPWIDKQLDNGQSRE 241
Cdd:COG0136 155 QAVSGAGAAAMDELAEQTAALLN-------------------------GEEIEPEVFPHPIAFNLIPQIDVFLENGYTKE 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 242 EWKGQAETNKILNTSSvIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHnPWAKVVPNdrEITMRELTPAAV 321
Cdd:COG0136 210 EMKMVNETRKILGDPD-IPVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAA-PGVKVVDD--PAENDYPTPLDA 285
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 16131307 322 TGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQLA 367
Cdd:COG0136 286 SGTDEVFVGRIRKDLSVPNGLNLWVVADNLRKGAALNAVQIAELLI 331
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
144-353 5.96e-50

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: 165.18  E-value: 5.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   144 LGGLF-ANDLVDWVSVATYQAASGGGArhmrelltqmghlyghvadelatpssaildierkvttltrsgELPVDNFGVPL 222
Cdd:pfam02774   1 LKPLRdALGGLERVIVDTYQAVSGAGK------------------------------------------KAKPGVFGAPI 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   223 AGSLIPWIDKQLDNG--QSREEWKGQAETNKILNTSSviPVDGLCVRVGALRCHSQAFTIKLK-KDVSIPTVEELLAAHn 299
Cdd:pfam02774  39 ADNLIPYIDGEEHNGtpETREELKMVNETKKILGFTP--KVSATCVRVPVFRGHSETVTVKLKlKPIDVEEVYEAFYAA- 115
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16131307   300 PWAKVVPNDreiTMRELTPAAVTG-TLTTPVGRLRKLNMGPEFLSAFTVGDQLLW 353
Cdd:pfam02774 116 PGVFVVVRP---EEDYPTPRAVRGgTNFVYVGRVRKDPDGDRGLKLVSVIDNLRK 167
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
3-119 2.81e-29

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: 109.56  E-value: 2.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307      3 NVGFIGWRGMVGSVLMQRMVEERDFDaIRPVFFSTSQLGQAAPS-FGGTTGTLQDAFDLEALKAL--DIIVTCQGGDYTN 79
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFE-LTALAASSRSAGKKVSEaGPHLKGEVVLELDPPDFEELavDIVFLALPHGVSK 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 16131307     80 EIYPKLRE-SGWQGYWIDAASSLRMKDDAIIILDPVNQDVI 119
Cdd:smart00859  80 ESAPLLPRaAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAI 120
 
Name Accession Description Interval E-value
PRK06598 PRK06598
aspartate-semialdehyde dehydrogenase; Reviewed
1-366 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 235839  Cd Length: 369  Bit Score: 823.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307    1 MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNE 80
Cdd:PRK06598   1 MKKVGFVGWRGMVGSVLMQRMVEENDFDLIEPVFFSTSQAGGAAPSFGGKEGTLQDAFDIDALKKLDIIITCQGGDYTNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   81 IYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVAT 160
Cdd:PRK06598  81 VYPKLRAAGWQGYWIDAASTLRMKDDAIIILDPVNRDVIDDALANGVKTFVGGNCTVSLMLMALGGLFKNDLVEWVSVMT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  161 YQAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSR 240
Cdd:PRK06598 161 YQAASGAGARNMRELLTQMGALHGAVADELADPASAILDIDRKVTELMRSGDLPTDNFGVPLAGSLIPWIDKDLGNGQSR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  241 EEWKGQAETNKILN-TSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNPWAKVVPNDREITMRELTPA 319
Cdd:PRK06598 241 EEWKGQAETNKILGlTKNPIPVDGLCVRVGAMRCHSQALTIKLKKDVPLAEIEEILAAHNPWVKVVPNDREATMRELTPA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 16131307  320 AVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQL 366
Cdd:PRK06598 321 AVTGTLTIPVGRLRKLNMGPEYLSAFTVGDQLLWGAAEPLRRMLRIL 367
asd_gamma TIGR01745
aspartate-semialdehyde dehydrogenase, gamma-proteobacterial; [Amino acid biosynthesis, ...
2-367 0e+00

aspartate-semialdehyde dehydrogenase, gamma-proteobacterial; [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 130806 [Multi-domain]  Cd Length: 366  Bit Score: 748.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307     2 KNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNEI 81
Cdd:TIGR01745   1 KNVGLVGWRGMVGSVLMQRMQEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDIDALKALDIIITCQGGDYTNEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307    82 YPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATY 161
Cdd:TIGR01745  81 YPKLRESGWQGYWIDAASSLRMKDDAVIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVEWVSVATY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   162 QAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSRE 241
Cdd:TIGR01745 161 QAASGGGARHMRELLTQMGHLYGHVEDELATPSSAILDIERKVTKLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSRE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   242 EWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNPWAKVVPNDREITMRELTPAAV 321
Cdd:TIGR01745 241 EWKGQAETNKILGTSSTIPVDGLCVRIGALRCHSQAFTIKLKKDVSLETIEEIIRAHNPWVKVVPNDREITMRELTPAAV 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 16131307   322 TGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQLA 367
Cdd:TIGR01745 321 TGTLTIPVGRLRKLNMGPEYLSAFTVGDQLLWGAAEPLRRMLRILA 366
ASADH_C_bac_like cd23938
C-terminal catalytic domain of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) and ...
135-351 8.66e-165

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: 459.08  E-value: 8.66e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 135 CTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELP 214
Cdd:cd23938   1 CTVSLMLMALGGLFKNDLVEWISSMTYQAASGAGAKNMRELLSQMGALGDAVSDELADPASAILDIDRKVTELQRSGSFP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 215 VDNFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEEL 294
Cdd:cd23938  81 TDNFGVPLAGSLIPWIDKQLENGQSKEEWKGQVETNKILGTSKPIPIDGLCVRVGAMRCHSQALTIKLKKDVPLDEIEEI 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131307 295 LAAHNPWAKVVPNDREITMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQL 351
Cdd:cd23938 161 IAAHNQWVKVVPNDKEATLRELTPAAVTGTLTVPVGRLRKLNMGPEYLSAFTVGDQL 217
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
2-367 4.98e-161

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: 454.10  E-value: 4.98e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   2 KNVGFIGWRGMVGSVLMQRMvEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDlEALKALDIIVTCQGGDYTNEI 81
Cdd:COG0136   1 YNVAVVGATGAVGRVLLELL-EERDFPVGELRLLASSRSAGKTVSFGGKELTVEDATD-FDFSGVDIALFSAGGSVSKEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  82 YPKLRESGwqGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIrtFVGGNCTVSLMLMSLGGLFANDLVDWVSVATY 161
Cdd:COG0136  79 APKAAAAG--AVVIDNSSAFRMDPDVPLVVPEVNPEALADHLPKGI--IANPNCSTIQMLVALKPLHDAAGIKRVVVSTY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 162 QAASGGGARHMRELLTQMGHLYGhvadelatpssaildierkvttltrSGELPVDNFGVPLAGSLIPWIDKQLDNGQSRE 241
Cdd:COG0136 155 QAVSGAGAAAMDELAEQTAALLN-------------------------GEEIEPEVFPHPIAFNLIPQIDVFLENGYTKE 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 242 EWKGQAETNKILNTSSvIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHnPWAKVVPNdrEITMRELTPAAV 321
Cdd:COG0136 210 EMKMVNETRKILGDPD-IPVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAA-PGVKVVDD--PAENDYPTPLDA 285
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 16131307 322 TGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQLA 367
Cdd:COG0136 286 SGTDEVFVGRIRKDLSVPNGLNLWVVADNLRKGAALNAVQIAELLI 331
ASADH_C_like cd18124
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
135-351 3.14e-101

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: 297.19  E-value: 3.14e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 135 CTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMGhlyghvadelatpssaildierkvtTLTRSGELP 214
Cdd:cd18124   1 CTVSLLVMALKPLFAKFLVEWVSVAT*QAVSGAGYENMRELLSQMG-------------------------ELMRAGPLP 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 215 VDNFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTS-SVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEE 293
Cdd:cd18124  56 TGVFS*AIADNLIPWIDKVLDNGQSKEEWKIQAEANKILGTLdSPIPISVTCNRVPVLDGHSQSFTLKLKEDVPLEEVEE 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131307 294 LLAAHNPWAKVVPNDREITMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQL 351
Cdd:cd18124 136 VLDAHKPWVKVIPNDYAIRPQPRLDRKVTGGLSTPVGRIRKDAMDPFDVNAFAVSDNT 193
VcASADH1_like_N cd02314
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
2-134 1.92e-95

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: 280.68  E-value: 1.92e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   2 KNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNEI 81
Cdd:cd02314   1 KRVGFVGWRGMVGSVLMQRMQEENDFDLIEPVFFSTSQVGQKGPTFGKDVGPLKDAYDIDALKKMDIIVTCQGGDYTKEV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16131307  82 YPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGN 134
Cdd:cd02314  81 YPKLRKAGWKGYWIDAASTLRMKDDAVIVLDPVNRDVIDSGLASGIKTFVGGN 133
ASADH_C cd18128
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar ...
135-351 1.71e-82

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: 248.57  E-value: 1.71e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 135 CTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGArhmrelltqmghlyghvadelatpssaildierkvttltrsgelp 214
Cdd:cd18128   1 CTVSLMLMALGGLFQKFLVEWVSVATYQAVSGAG*--------------------------------------------- 35
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 215 vdnfgvPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTS-SVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEE 293
Cdd:cd18128  36 ------PIAGNLIPWIDVFLDNGQTKEEWKGQAETNKILGDLdSPIPISGTCVRVGVLRCHSQAFTIKLKEDAPIEEVEE 109
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131307 294 LLAAHNPWAKVVPNDREITMRelTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQL 351
Cdd:cd18128 110 AIAAHN*WIKVIPNVDRITPR--TPANVTGTLSTPVGRIRKDAMGPFDLQAFTVGDNL 165
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
144-353 5.96e-50

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: 165.18  E-value: 5.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   144 LGGLF-ANDLVDWVSVATYQAASGGGArhmrelltqmghlyghvadelatpssaildierkvttltrsgELPVDNFGVPL 222
Cdd:pfam02774   1 LKPLRdALGGLERVIVDTYQAVSGAGK------------------------------------------KAKPGVFGAPI 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   223 AGSLIPWIDKQLDNG--QSREEWKGQAETNKILNTSSviPVDGLCVRVGALRCHSQAFTIKLK-KDVSIPTVEELLAAHn 299
Cdd:pfam02774  39 ADNLIPYIDGEEHNGtpETREELKMVNETKKILGFTP--KVSATCVRVPVFRGHSETVTVKLKlKPIDVEEVYEAFYAA- 115
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16131307   300 PWAKVVPNDreiTMRELTPAAVTG-TLTTPVGRLRKLNMGPEFLSAFTVGDQLLW 353
Cdd:pfam02774 116 PGVFVVVRP---EEDYPTPRAVRGgTNFVYVGRVRKDPDGDRGLKLVSVIDNLRK 167
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
1-356 3.73e-43

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 152.62  E-value: 3.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307    1 MKNVGFIGWRGMVGSVlMQRMVEERDF--DAIRPvFFSTSQLGQAApSFGGTTGTLQDAfDLEALKALDIIVTCQGGDYT 78
Cdd:PRK14874   1 GYNVAVVGATGAVGRE-MLNILEERNFpvDKLRL-LASARSAGKEL-SFKGKELKVEDL-TTFDFSGVDIALFSAGGSVS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   79 NEIYPKLRESGwqGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIrtFVGGNCTVSLMLMSLGGLfaNDL--VDWV 156
Cdd:PRK14874  77 KKYAPKAAAAG--AVVIDNSSAFRMDPDVPLVVPEVNPEALAEHRKKGI--IANPNCSTIQMVVALKPL--HDAagIKRV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  157 SVATYQAASGGGARHMRELLTQMGHLYghvadelatpSSAILDIERKVttltrsgelpvdnFGVPLAGSLIPWIDKQLDN 236
Cdd:PRK14874 151 VVSTYQAVSGAGKAGMEELFEQTRAVL----------NAAVDPVEPKK-------------FPKPIAFNVIPHIDVFMDD 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  237 GQSREEWKGQAETNKILNTSSvIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAA-------HNPWAKVVPndr 309
Cdd:PRK14874 208 GYTKEEMKMVNETKKILGDPD-LKVSATCVRVPVFTGHSESVNIEFEEPISVEEAREILAEapgvvlvDDPENGGYP--- 283
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 16131307  310 eitmrelTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAA 356
Cdd:PRK14874 284 -------TPLEAVGKDATFVGRIRKDLTVENGLHLWVVSDNLRKGAA 323
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
2-134 7.75e-41

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: 140.58  E-value: 7.75e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   2 KNVGFIGWRGMVGSVLMQRMVEERdFDAIRPVFFSTSQLGQAAPSFGGTTG--TLQDAFDLEALKALDIIVTCQGGDYTN 79
Cdd:cd02281   1 KKVGVVGATGYVGGEFLRLLLEHP-FPLFEIVLLAASSAGAKKKYFHPKLWgrVLVEFTPEEVLEQVDIVFTALPGGVSA 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16131307  80 EIYPKLREsgWQGYWIDAASSLRMKDDAIIILDPVNQDVItdGLNNGIRTFVGGN 134
Cdd:cd02281  80 KLAPELSE--AGVLVIDNASDFRLDKDVPLVVPEVNREHI--GELKGTKIIANPN 130
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
2-134 1.95e-35

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: 126.30  E-value: 1.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   2 KNVGFIGWRGMVGSVLMQRMvEERDFDAIRPVFFSTSQ-LGQAAPsFGGTTGTLQDAFDlEALKALDIIVTCQGGDYTNE 80
Cdd:cd24147   1 LRVGVVGATGAVGSEILQLL-AEEPDPLFELRALASEEsAGKKAE-FAGEAIMVQEADP-IDFLGLDIVFLCAGAGVSAK 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 16131307  81 IYPKLRESGwqGYWIDAASSLRMKDDAIIILDPVNQDVItdGLNNGIRTFVGGN 134
Cdd:cd24147  78 FAPEAARAG--VLVIDNAGALRMDPDVPLVVPEVNAEAI--GLGEGTPLLVIPN 127
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
3-356 4.78e-35

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 131.43  E-value: 4.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307    3 NVGFIGWRGMVGSVLMqRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDaFDLEALKALDIIVTCQGGDYTNEIY 82
Cdd:PLN02383   9 SVAIVGVTGAVGQEFL-SVLTDRDFPYSSLKMLASARSAGKKVTFEGRDYTVEE-LTEDSFDGVDIALFSAGGSISKKFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   83 PKLRESGwqGYWIDAASSLRMKDDAIIILDPVNQDVITD-GLNNGIRTFVGG-NCTVSLMLMSLGGLFANDLVDWVSVAT 160
Cdd:PLN02383  87 PIAVDKG--AVVVDNSSAFRMEEGVPLVIPEVNPEAMKHiKLGKGKGALIANpNCSTIICLMAVTPLHRHAKVKRMVVST 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  161 YQAASGGGARHMRELLTQmghlyghvadelatpSSAILDierkvttltrsGELPVDN-FGVPLAGSLIPWIDKQLDNGQS 239
Cdd:PLN02383 165 YQAASGAGAAAMEELEQQ---------------TREVLE-----------GKPPTCNiFAQQYAFNLFSHNAPMQENGYN 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  240 REEWKGQAETNKILNTSSViPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAhNPWAKVVpNDREiTMRELTPA 319
Cdd:PLN02383 219 EEEMKLVKETRKIWNDDDV-KVTATCIRVPVMRAHAESINLQFEKPLDEATAREILAS-APGVKII-DDRA-NNRFPTPL 294
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 16131307  320 AVTGTLTTPVGRLRK--LNMGPEFLSAFTVGDQLLWGAA 356
Cdd:PLN02383 295 DASNKDDVAVGRIRQdiSQDGNKGLDIFVCGDQIRKGAA 333
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
3-119 6.74e-34

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: 121.48  E-value: 6.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307     3 NVGFIGWRGMVGSVLMQRMveERDFDAIRPVFFSTSQL-GQAAPSFGGTTGTLQD----AFDLEALKALDIIVTCQGGDY 77
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLL--EEHPPVELVVLFASSRSaGKKLAFVHPILEGGKDlvveDVDPEDFKDVDIVFFALPGGV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 16131307    78 TNEIYPKLRESGWqgYWIDAASSLRMKDDAIIILDPVNQDVI 119
Cdd:pfam01118  79 SKEIAPKLAEAGA--KVIDLSSDFRMDDDVPYGLPEVNREAI 118
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
135-351 8.30e-34

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: 123.78  E-value: 8.30e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 135 CTVSLMLMSLGGLfaNDL--VDWVSVATYQAASGGGARHMRELLTQMGHLYGhvadelatpssaildierkvttltrSGE 212
Cdd:cd18131   1 CSTIQMVVALKPL--HDAfgLKRVVVSTYQAVSGAGAAAMEELEEQTRGLLN-------------------------GKE 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 213 LPVDNFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTSSvIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVE 292
Cdd:cd18131  54 AEPKVFPYQIAFNVIPHIDVFLDNGYTKEEMKMVNETRKILGDPD-LRVSATCVRVPVFRGHSESVNIEFEKPISVEEAR 132
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131307 293 ELLAA-------HNPWAKVVPndreitmrelTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQL 351
Cdd:cd18131 133 EALAKapgvvvvDDPANNVYP----------TPLDAAGKDDVFVGRIRKDISVPNGLNLWVVGDNL 188
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
135-351 8.59e-34

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: 123.01  E-value: 8.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 135 CTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMGhlyghvadelatpssaiLDIERkvttltrsgelp 214
Cdd:cd18122   1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSEV-----------------RAIIP------------ 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 215 vdnfgvplagslipwidkqldnGQSREEWKGQAETNKILNTSSV-IPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEE 293
Cdd:cd18122  52 ----------------------NIPKNETKHAPETGKVLGEIGKpIKVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAE 109
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131307 294 LLAAHNPWAKVVPNDREiTMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQL 351
Cdd:cd18122 110 AVAEAVEEVQISAEDGL-TYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKVFSAVDNE 166
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
3-119 2.81e-29

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: 109.56  E-value: 2.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307      3 NVGFIGWRGMVGSVLMQRMVEERDFDaIRPVFFSTSQLGQAAPS-FGGTTGTLQDAFDLEALKAL--DIIVTCQGGDYTN 79
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFE-LTALAASSRSAGKKVSEaGPHLKGEVVLELDPPDFEELavDIVFLALPHGVSK 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 16131307     80 EIYPKLRE-SGWQGYWIDAASSLRMKDDAIIILDPVNQDVI 119
Cdd:smart00859  80 ESAPLLPRaAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAI 120
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
3-356 2.31e-22

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 96.66  E-value: 2.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307    3 NVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAfDLEALKALDIIVTCQGGDYTNEIY 82
Cdd:PRK06728   7 HVAVVGATGAVGQKIIELLEKETKFNIAEVTLLSSKRSAGKTVQFKGREIIIQEA-KINSFEGVDIAFFSAGGEVSRQFV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   83 PKLRESGwqGYWIDAASSLRMKDDAIIILDPVNqdviTDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATYQ 162
Cdd:PRK06728  86 NQAVSSG--AIVIDNTSEYRMAHDVPLVVPEVN----AHTLKEHKGIIAVPNCSALQMVTALQPIRKVFGLERIIVSTYQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  163 AASGGGArhmrelltqmghlygHVADELATPSSAILDIERKVTTLtrsgeLPV--DNFGVPLAGSLIPWIDKQLDNGQSR 240
Cdd:PRK06728 160 AVSGSGI---------------HAIQELKEQAKSILAGEEVESTI-----LPAkkDKKHYPIAFNVLPQVDIFTDNDFTF 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  241 EEWKGQAETNKILNTSSvIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELL-------AAHNPWAKVVPndreitm 313
Cdd:PRK06728 220 EEVKMIQETKKILEDPN-LKMAATCVRVPVISGHSESVYIELEKEATVAEIKEVLfdapgviLQDNPSEQLYP------- 291
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 16131307  314 relTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAA 356
Cdd:PRK06728 292 ---MPLYAEGKIDTFVGRIRKDPDTPNGFHLWIVSDNLLKGAA 331
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
98-297 1.09e-09

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 59.07  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   98 ASSLRMKDDAIIILDPVNQDVItdGL------NNGIRTF--VGGNCTVSLMLMSLgglfaNDLVDW----VSVATYQAAS 165
Cdd:PRK08664 107 ASAHRMDPDVPLVIPEVNPEHL--ELievqrkRRGWDGFivTNPNCSTIGLVLAL-----KPLMDFgierVHVTTMQAIS 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307  166 GGGarhmrelltqmghlYGHVadelatPSSAIldierkvttltrsgelpVDNfgvplagsLIPWIDKqldngqsrEEWKG 245
Cdd:PRK08664 180 GAG--------------YPGV------PSMDI-----------------VDN--------VIPYIGG--------EEEKI 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16131307  246 QAETNKILNT---SSVIPVDGL----CVRVGALRCHSQAFTIKLKKDvsiPTVEELLAA 297
Cdd:PRK08664 207 EKETLKILGKfegGKIVPADFPisatCHRVPVIDGHTEAVFVKFKED---VDPEEIREA 262
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
135-338 1.11e-09

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: 57.24  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 135 CTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGarhmrelltqmghlYGHVadelatPSSAILDierkvttltrsgelp 214
Cdd:cd18130   1 CSTAGLALPLKPLHDFFGIEAVIVTTMQAISGAG--------------YPGV------PSLDILD--------------- 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 215 vdNfgvplagsLIPWIdkqldngqSREEWKGQAETNKILNTSSV-------IPVDGLCVRVGALRCHSQAFTIKLKKDVS 287
Cdd:cd18130  46 --N--------VIPYI--------GGEEEKIESETKKILGTLNEdkiepadFKVSATCNRVPVIDGHTESVSVKFKERPD 107
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131307 288 IPTVEELLAAHNPWAK------------VVPNDREITMRELTPAAVTGTLTTpVGRLRKLNMG 338
Cdd:cd18130 108 PEEVKEALENYEPEPQvlgppsapkpiiVVEDEPRRPQPRLDRDAGDGMAVT-VGRIRKDDDF 169
ASADH_C_USG1_like cd18129
C-terminal domain of USG-1 protein and similar proteins; The family includes Escherichia coli ...
137-351 2.44e-09

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: 56.05  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 137 VSLMLMSLGGLFANDLVDWVSVATYQAASGGGarhmrelltQMGhlyghvADELATPSSAIL---DIERKVttltrsgel 213
Cdd:cd18129   3 AIALARVLAPLHDAAGLERVVVTVLQPVSEAG---------QAG------VDELARQTARLLngqPVEPEV--------- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307 214 pvdnFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTSSViPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEE 293
Cdd:cd18129  59 ----FPRQLAFNLLPQVGDFDADGLSDEERRIAAELRRLLGGPDL-PVSVTCVQVPVFYGHSASVHVELAEPVDLEEVRA 133
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131307 294 LLAAHnPWAKVVPNDREITmrelTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQL 351
Cdd:cd18129 134 ALAAA-PGLELADDAEAPP----YPVDAAGSDDVLVGRVRQDPGNPRGLWLWAVADNL 186
VcASADH1_like_N cd02314
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
345-366 7.35e-07

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: 48.40  E-value: 7.35e-07
                        10        20
                ....*....|....*....|..
gi 16131307 345 FTVGDQLLWGAAEPLRRMLRQL 366
Cdd:cd02314 129 FVGGNQLLWGAAEPLRRMLRIL 150
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
3-127 4.71e-04

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: 39.91  E-value: 4.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   3 NVGFIGWRGMVGSVLMQRMvEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAfDLEALKALDIIVTCQGGDYTNEIY 82
Cdd:cd17894   2 RIAVVGATGLVGKELLELL-EERGFPVGRLRLLDSEESAGELVEFGGEPLDVQDL-DEFDFSDVDLVFFAGPAEVARAYA 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 16131307  83 PKLRESGwqGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGI 127
Cdd:cd17894  80 PRARAAG--CLVIDLSGALRSDPDVPLVVPGVNPEALAAAAERRV 122
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
3-127 1.26e-03

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: 38.57  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131307   3 NVGFIGWRGMVGSVLMqRMVEERDF--DAIRPvFFSTSQLGQAApSFGGTTGTLQDaFDLEALKALDIIVTCQGGDYTNE 80
Cdd:cd02316   2 NVAIVGATGAVGQEML-KVLEERNFpvSELRL-LASARSAGKTL-EFKGKELTVEE-LTEDSFKGVDIALFSAGGSVSKE 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 16131307  81 IYPKLRESGwqGYWIDAASSLRMKDDAIIILDPVNQDVITDglNNGI 127
Cdd:cd02316  78 FAPIAAEAG--AVVIDNSSAFRMDPDVPLVVPEVNPEALKN--HKGI 120
 
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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