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Conserved domains on  [gi|1530902961|gb|RRK11884|]
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homoserine dehydrogenase [Lactiplantibacillus garii]

Protein Classification

homoserine dehydrogenase( domain architecture ID 11482218)

homoserine dehydrogenase catalyzes the conversion from L-homoserine and NAD(P)(+) to L-aspartate 4-semialdehyde and NAD(P)H

EC:  1.1.1.3
Gene Ontology:  GO:0006520|GO:0004412
PubMed:  25945586|3098560|8500624

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-422 0e+00

homoserine dehydrogenase; Provisional


:

Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 598.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   1 METIKIGIVGLGTVGTGVVKMLQAHQEKISEITGRKLELACVVVHNLKKHDQVDLGDVQLTDQIETLIDDPSIQIMVEVM 80
Cdd:PRK06349    1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  81 GSIHPAKEYITRALQAGKHVVTANKDLIAQYGRELVQIARENHRDLFYEASVAGGIPILRTIDNSFAADKIQRVMGIVNG 160
Cdd:PRK06349   81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 161 TTNYIMTQMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGMSLSMDHVQVQGITNISPEDISEAN 240
Cdd:PRK06349  161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 241 QLGYTIKLLGIAEEVDDRIAVSVGPVLVSDQHPLATVQNENNAVMVTGTAVGDTMFYGPGAGELPTANSVLSDITTVAKN 320
Cdd:PRK06349  241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARN 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 321 IALNTTGNTFNSYRQETVLAAPEDVVYPHFIALKMRDVPGMMMKLTAIMTKAEVSFSRIIQNQLSDGNARVVIITHAMND 400
Cdd:PRK06349  321 LVRVPHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSE 400

                         410       420
                  ....*....|....*....|..
gi 1530902961 401 QQLAEITAAIGEQDNMRLLASY 422
Cdd:PRK06349  401 AALRAALAAIEALDVVLGIPSV 422
 
Name Accession Description Interval E-value
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-422 0e+00

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 598.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   1 METIKIGIVGLGTVGTGVVKMLQAHQEKISEITGRKLELACVVVHNLKKHDQVDLGDVQLTDQIETLIDDPSIQIMVEVM 80
Cdd:PRK06349    1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  81 GSIHPAKEYITRALQAGKHVVTANKDLIAQYGRELVQIARENHRDLFYEASVAGGIPILRTIDNSFAADKIQRVMGIVNG 160
Cdd:PRK06349   81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 161 TTNYIMTQMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGMSLSMDHVQVQGITNISPEDISEAN 240
Cdd:PRK06349  161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 241 QLGYTIKLLGIAEEVDDRIAVSVGPVLVSDQHPLATVQNENNAVMVTGTAVGDTMFYGPGAGELPTANSVLSDITTVAKN 320
Cdd:PRK06349  241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARN 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 321 IALNTTGNTFNSYRQETVLAAPEDVVYPHFIALKMRDVPGMMMKLTAIMTKAEVSFSRIIQNQLSDGNARVVIITHAMND 400
Cdd:PRK06349  321 LVRVPHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSE 400

                         410       420
                  ....*....|....*....|..
gi 1530902961 401 QQLAEITAAIGEQDNMRLLASY 422
Cdd:PRK06349  401 AALRAALAAIEALDVVLGIPSV 422
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 23-324 1.01e-150

Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440228 [Multi-domain]  Cd Length: 302  Bit Score: 429.47  E-value: 1.01e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  23 QAHQEKISEITGRKLELACVVVHNLKKHDQVDLGDVQLTDQIETLIDDPSIQIMVEVMGSIHPAKEYITRALQAGKHVVT 102
Cdd:COG0460     1 LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 103 ANKDLIAQYGRELVQIARENHRDLFYEASVAGGIPILRTIDNSFAADKIQRVMGIVNGTTNYIMTQMLTKKWSYEQALSS 182
Cdd:COG0460    81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 183 AQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGMSLSMDHVQVQGITNISPEDISEANQLGYTIKLLGIAEEVDDRIAVS 262
Cdd:COG0460   161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1530902961 263 VGPVLVSDQHPLATVQNENNAVMVTGTAVGDTMFYGPGAGELPTANSVLSDITTVAKNIALN 324
Cdd:COG0460   241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLRAG 302
Homoserine_dh pfam00742
Homoserine dehydrogenase;
137-314 2.07e-89

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 268.47  E-value: 2.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 137 PILRTIDNSFAADKIQRVMGIVNGTTNYIMTQMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGM 216
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 217 SLSMDHVQVQGITNISPEDISEANQLGYTIKLLGIAEEVDDRIAVSVGPVLVSDQHPLATVQNENNAVMVTGTAVGDTMF 296
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 1530902961 297 YGPGAGELPTANSVLSDI 314
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
ACT_HSDH-Hom cd04881
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ...
 349-422 1.57e-15

ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153153 [Multi-domain]  Cd Length: 79  Bit Score: 71.01  E-value: 1.57e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1530902961 349 HFIALKMRDVPGMMMKLTAIMTKAEVSFSRIIQNQLSDGN-ARVVIITHAMNDQQLAEITAAIGEQDNMRLLASY 422
Cdd:cd04881     1 YYLRLTVKDKPGVLAKITGILAEHGISIESVIQKEADGGEtAPVVIVTHETSEAALNAALAEIEALDAVQGVPSV 75
 
Name Accession Description Interval E-value
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-422 0e+00

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 598.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   1 METIKIGIVGLGTVGTGVVKMLQAHQEKISEITGRKLELACVVVHNLKKHDQVDLGDVQLTDQIETLIDDPSIQIMVEVM 80
Cdd:PRK06349    1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  81 GSIHPAKEYITRALQAGKHVVTANKDLIAQYGRELVQIARENHRDLFYEASVAGGIPILRTIDNSFAADKIQRVMGIVNG 160
Cdd:PRK06349   81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 161 TTNYIMTQMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGMSLSMDHVQVQGITNISPEDISEAN 240
Cdd:PRK06349  161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 241 QLGYTIKLLGIAEEVDDRIAVSVGPVLVSDQHPLATVQNENNAVMVTGTAVGDTMFYGPGAGELPTANSVLSDITTVAKN 320
Cdd:PRK06349  241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARN 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 321 IALNTTGNTFNSYRQETVLAAPEDVVYPHFIALKMRDVPGMMMKLTAIMTKAEVSFSRIIQNQLSDGNARVVIITHAMND 400
Cdd:PRK06349  321 LVRVPHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSE 400

                         410       420
                  ....*....|....*....|..
gi 1530902961 401 QQLAEITAAIGEQDNMRLLASY 422
Cdd:PRK06349  401 AALRAALAAIEALDVVLGIPSV 422
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 23-324 1.01e-150

Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440228 [Multi-domain]  Cd Length: 302  Bit Score: 429.47  E-value: 1.01e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  23 QAHQEKISEITGRKLELACVVVHNLKKHDQVDLGDVQLTDQIETLIDDPSIQIMVEVMGSIHPAKEYITRALQAGKHVVT 102
Cdd:COG0460     1 LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 103 ANKDLIAQYGRELVQIARENHRDLFYEASVAGGIPILRTIDNSFAADKIQRVMGIVNGTTNYIMTQMLTKKWSYEQALSS 182
Cdd:COG0460    81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 183 AQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGMSLSMDHVQVQGITNISPEDISEANQLGYTIKLLGIAEEVDDRIAVS 262
Cdd:COG0460   161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1530902961 263 VGPVLVSDQHPLATVQNENNAVMVTGTAVGDTMFYGPGAGELPTANSVLSDITTVAKNIALN 324
Cdd:COG0460   241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLRAG 302
Homoserine_dh pfam00742
Homoserine dehydrogenase;
137-314 2.07e-89

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 268.47  E-value: 2.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 137 PILRTIDNSFAADKIQRVMGIVNGTTNYIMTQMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGM 216
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 217 SLSMDHVQVQGITNISPEDISEANQLGYTIKLLGIAEEVDDRIAVSVGPVLVSDQHPLATVQNENNAVMVTGTAVGDTMF 296
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 1530902961 297 YGPGAGELPTANSVLSDI 314
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 3-324 1.08e-85

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 265.19  E-value: 1.08e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   3 TIKIGIVGLGTVGTGVVKMLQAHQEKISEITGRKLELACV------VVHNlkkhDQVDLGDV----QLTDQIETLIDDPS 72
Cdd:PRK06270    2 EMKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIadssgsAIDP----DGLDLELAlkvkEETGKLADYPEGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  73 IQIMVEVMGSIH----------------PAKEYITRALQAGKHVVTANKDLIAQYGRELVQIARENHRDLFYEASVAGGI 136
Cdd:PRK06270   78 EISGLEVIRSVDadvvveatptnietgePALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 137 PILRTIDNSFAADKIQRVMGIVNGTTNYIMTQMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGM 216
Cdd:PRK06270  158 PIINLAKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 217 SLSMDHVQVQGITNISPEDISEANQLGYTIKLlgIAEEVDDRIAvSVGPVLVSDQHPLAtVQNENNAVMVTGTAVGDTMF 296
Cdd:PRK06270  238 DLTIKDVEVEGITKITPEAIELAAKEGYRIKL--IGEVSREKDL-SVSPRLVPLDHPLA-VSGTLNAATFETDLAGDVTV 313

                         330       340
                  ....*....|....*....|....*...
gi 1530902961 297 YGPGAGELPTANSVLSDITTVAKNIALN 324
Cdd:PRK06270  314 VGRGAGSIETASAILSDLIAIHDRYGKA 341
PRK08374 PRK08374
homoserine dehydrogenase; Provisional
 4-318 1.03e-48

homoserine dehydrogenase; Provisional


Pssm-ID: 169409 [Multi-domain]  Cd Length: 336  Bit Score: 168.83  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   4 IKIGIVGLGTVGTGVVKMLQAHQEKISEITGRKLElacvVVHNLKKHDQV-DLGDVQLTDQIET---------------- 66
Cdd:PRK08374    3 VKVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELK----VVSITDTSGTIwLPEDIDLREAKEVkenfgklsnwgndyev 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  67 -------LIDDPSIQIMVEVMgSIHPAKEYITRALQAGKHVVTANKDLIAQYGRELVQIARENHRDLFYEASVAGGIPIL 139
Cdd:PRK08374   79 ynfspeeIVEEIDADIVVDVT-NDKNAHEWHLEALKEGKSVVTSNKPPIAFHYDELLDLANERNLPYLFEATVMAGTPII 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 140 RTIDNSFAADKIQRVMGIVNGTTNYIMTQMLTKKwSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFgMSLS 219
Cdd:PRK08374  158 GLLRENLLGDTVKRIEAVVNATTTFILTRMEQGK-TFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAF-PPIT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 220 MDHVQVQGITNISPEDISEANQLGYTIKLLGIAEEVDdriaVSVGPVLVSDQHPLATVQNENNAVMVTGTaVGDTMFYGP 299
Cdd:PRK08374  236 FEEVGIRGIKDVTEGEIERAKAKGRNVRLVATVEEGR----ISVKPKKLPENSPLAVEGVENAAVIKTDL-LGELVLKGP 310

                         330
                  ....*....|....*....
gi 1530902961 300 GAGELPTANSVLSDITTVA 318
Cdd:PRK08374  311 GAGGKETASGVVTDIIKAA 329
PRK06813 PRK06813
homoserine dehydrogenase; Validated
 4-320 5.39e-36

homoserine dehydrogenase; Validated


Pssm-ID: 168683 [Multi-domain]  Cd Length: 346  Bit Score: 135.38  E-value: 5.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   4 IKIGIVGLGTVGTGVVKMLQAHQEKISEITGRKLELACVVVHNLKKHDQVDL----------GDVQLTDQIETLIDDP-- 71
Cdd:PRK06813    3 IKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNVAIHNEDGLsihhllryggGSCAIEKYIEHHPEERat 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  72 ---SIQIMVEVMGSI----HPAKEYITRALQAGKHVVTANKDLIAQYGRELVQIARENHRDLFYEASVAGGIPILRTIDN 144
Cdd:PRK06813   83 dniSGTVLVESTVTNlkdgNPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIANVRIRYSGATAAALPTLDIGQF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 145 SFAADKIQRVMGIVNGTTNYIMTQMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGMSLSMDHVQ 224
Cdd:PRK06813  163 SLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLTNSLMGTENKLTDIH 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 225 VQGITNISPEDISEANQLGYTIKLLGIA-EEVDDRIAVSVGPVLVSDQHPLATVQNENNAVMVTGTAVGDTMFYGPGAGE 303
Cdd:PRK06813  243 IKGIEHVTKQQIRNAKEQNKIIKLIASAyKDNEGNVNLNVEPYKIEKNHPLANVNGTEKGITFFTDTMGQVTTIGGASNP 322

                         330
                  ....*....|....*..
gi 1530902961 304 LPTANSVLSDITTVAKN 320
Cdd:PRK06813  323 RGAAAAALKDIINLYRK 339
PRK06392 PRK06392
homoserine dehydrogenase; Provisional
 4-231 7.78e-30

homoserine dehydrogenase; Provisional


Pssm-ID: 102354 [Multi-domain]  Cd Length: 326  Bit Score: 118.05  E-value: 7.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   4 IKIGIVGLGTVGTGVVKMLQAHQEKISEITGRKLELACVVVHNLKKHDQVDLGDV-------QLTD-QIETLIDDPSIQI 75
Cdd:PRK06392    1 IRISIIGLGNVGLNVLRIIKSRNDDRRNNNGISVVSVSDSKLSYYNERGLDIGKIisykekgRLEEiDYEKIKFDEIFEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  76 MVEVMGSIHPA-------KEYITRALQAGKHVVTANKDLIAQYGRELVQIARENHRDLFYEASVAGGIPILRTIDNSFAA 148
Cdd:PRK06392   81 KPDVIVDVTPAskdgireKNLYINAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRYEATVAGGVPLFSLRDYSTLP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 149 DKIQRVMGIVNGTTNYIMTQMLTKKwSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAFGMSLSMDHVQVQGI 228
Cdd:PRK06392  161 SRIKNFRGIVSSTINYVIRQEANGR-GFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLFGKDYTLRDVTYDGI 239


                  ...
gi 1530902961 229 TNI 231
Cdd:PRK06392  240 ENI 242
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 3-314 1.16e-27

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 116.02  E-value: 1.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   3 TIKIGIVGLGTVGTGVVKMLQAHQEKISEitgRKLELACVVVHNLKK----HDQVDLGDVQltDQIETLIDDPSIQIMVE 78
Cdd:PRK09436  465 VLDVFVIGVGGVGGALLEQIKRQQPWLKK---KNIDLRVCGIANSRKmlldEHGIDLDNWR--EELAEAGEPFDLDRLIR 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  79 VMGS---IHP-----------AKEYItRALQAGKHVVTANK----DLIAQYgRELVQIARENHRDLFYEASVAGGIPILR 140
Cdd:PRK09436  540 LVKEyhlLNPvivdctssqavADQYA-DFLAAGFHVVTPNKkantSSYAYY-HQLREAARKSRRKFLYETNVGAGLPVIE 617

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 141 TIDNSFAA-DKIQRVMGIVNGTTNYIMTqMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAfGMSLS 219
Cdd:PRK09436  618 TLQNLLNAgDELLKFEGILSGSLSFIFG-KLDEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILAREA-GYELE 695

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 220 MDHVQVQGI------TNISPED---------------ISEANQLGYTIKLLGiaeEVDDRiAVSVGPVLVSDQHPLATVQ 278
Cdd:PRK09436  696 LEDIEVESVlpeefdASGSVDEfmarlpeldaefaarVAKARAEGKVLRYVG---QIEDG-KCRVGIAEVDANHPLYKVK 771

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1530902961 279 NENNAVMVTgtavgdTMFY--------GPGAGELPTANSVLSDI 314
Cdd:PRK09436  772 GGENALAFY------TRYYqpiplvlrGYGAGNEVTAAGVFADL 809
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 10-129 4.34e-24

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 96.22  E-value: 4.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  10 GLGTVGTGVVKMLQAHQEKIseitgrKLELACVVVHNLKKHD-QVDLGDVQLTDQIETLIDDPSIQIMVEVmGSIHPAKE 88
Cdd:pfam03447   1 GCGAIGSGVLEQLLRQQSEI------PLELVAVADRDLLSKDpLALLPDEPLTLDLDDLIAHPDPDVVVEC-ASSEAVAE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1530902961  89 YITRALQAGKHVVTANKDLIAQ--YGRELVQIARENHRDLFYE 129
Cdd:pfam03447  74 LVLDALKAGKDVVTASKGALADlaLYEELREAAEANGARIYVE 116
ACT_HSDH-Hom cd04881
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ...
 349-422 1.57e-15

ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153153 [Multi-domain]  Cd Length: 79  Bit Score: 71.01  E-value: 1.57e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1530902961 349 HFIALKMRDVPGMMMKLTAIMTKAEVSFSRIIQNQLSDGN-ARVVIITHAMNDQQLAEITAAIGEQDNMRLLASY 422
Cdd:cd04881     1 YYLRLTVKDKPGVLAKITGILAEHGISIESVIQKEADGGEtAPVVIVTHETSEAALNAALAEIEALDAVQGVPSV 75
metL PRK09466
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
 6-320 5.06e-14

bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional


Pssm-ID: 236530 [Multi-domain]  Cd Length: 810  Bit Score: 74.19  E-value: 5.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   6 IGIV--GLGTVGTGVVKMLQAHQEKISEITGRKLELACVVVHN--LKKHDQVDLGDV--------------QLTDQIETL 67
Cdd:PRK09466  459 IGLVlfGKGNIGSRWLELFAREQSTLSARTGFEFVLVGVVDSRrsLLNYDGLDASRAlaffddeavewdeeSLFLWLRAH 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961  68 -IDDpsiQIMVEVMGSIHPAKEYITRAlQAGKHVVTANKdlIA-----QYGRELVQIARENHRDLFYEASVAGGIPI--- 138
Cdd:PRK09466  539 pYDE---LVVLDVTASEQLALQYPDFA-SHGFHVISANK--LAgsspsNFYRQIKDAFAKTGRHWLYNATVGAGLPInht 612

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 139 LRTIDNSfaADKIQRVMGIVNGTTNYIMtQMLTKKWSYEQALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFAfGMSL 218
Cdd:PRK09466  613 VRDLRNS--GDSILAISGIFSGTLSWLF-LQFDGSVPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILAREA-GYEI 688

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 219 SMDHVQVQgitNISPEDIseanQLGYTIKLLGIAEEVDDRI------AVSVGPVL------------------VSDQHPL 274
Cdd:PRK09466  689 EPDDVRVE---SLVPAHL----EDGSLDQFFENGDELDEQMlqrleaAAEQGKVLryvarfdangkarvgveaVRPDHPL 761

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1530902961 275 ATVQNENNaVMVTGTAvgdtmFY--------GPGAGELPTANSVLSDITTVAKN 320
Cdd:PRK09466  762 ANLLPCDN-VFAIESR-----WYrdnplvirGPGAGREVTAGAIQSDLNRLAQL 809
PLN02700 PLN02700
homoserine dehydrogenase family protein
 100-314 1.16e-12

homoserine dehydrogenase family protein


Pssm-ID: 215377 [Multi-domain]  Cd Length: 377  Bit Score: 69.03  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 100 VVTANKDLIAQYGRELVQIARENHRdLFYEASVAGGIPILRTIDNSFAA-DKIQRVMGIVNGTTNYIMTQMLTKKwSYEQ 178
Cdd:PLN02700  136 IVLANKKPLTSTLEDYDKLAAHPRR-IRHESTVGAGLPVIASLNRILSSgDPVHRIVGSLSGTLGYVMSELEDGK-PFSE 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961 179 ALSSAQDLGFAESDPTNDVEGLDAAYKMIILTQFaFGMSLSMDHVQVQGI--TNISPEDISEANQLGYTIKLL--GIAEE 254
Cdd:PLN02700  214 VVKQAKSLGYTEPDPRDDLGGMDVARKALILARL-LGKRINMDSIKVESLypEEMGPDLMSTDDFLHSGLVELdlPIEER 292

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1530902961 255 VDDRIA---------------VSVGPVLVSDQHPLATVQNENNAVMVTGTAVGDT--MFYGPGAGELPTANSVLSDI 314
Cdd:PLN02700  293 VKEASLkgcvlryvcviegssCQVGIRELPKDSALGRLRGSDNVVEIYSRCYSEQplVIQGAGAGNDTTAAGVLADI 369
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-124 1.18e-07

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 53.00  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   1 METIKIGIVGLGTVGTGVVKMLQAHQEkiseitgrkLELACVVVHNLKKHDQV-DLGDVQLTDQIETLIDDPSIQImVEV 79
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALPG---------VELVAVADRDPERAEAFaEEYGVRVYTDYEELLADPDIDA-VVI 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1530902961  80 MGSIHPAKEYITRALQAGKHV-----VTANkdlIAQyGRELVQIARENHR 124
Cdd:COG0673    71 ATPNHLHAELAIAALEAGKHVlcekpLALT---LEE-ARELVAAAEEAGV 116
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 4-122 2.97e-05

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


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 44.07  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   4 IKIGIVGLGTVGTGVVKMLQAHQEkiseitgrkLELACVVVHNLKKHDQvDLG--------DVQLTDQIETLIDDPSIQI 75
Cdd:cd24146     1 IRVVVWGLGAMGRGIARYLLEKPG---------LEIVGAVDRDPAKVGK-DLGelgggaplGVKVTDDLDAVLAATKPDV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1530902961  76 MVEVMGS-IHPAKEYITRALQAGKHVVTANKDLIAQYGR------ELVQIAREN 122
Cdd:cd24146    71 VVHATTSfLADVAPQIERLLEAGLNVITTCEELFYPWARdpelaeELDALAKEN 124
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
 4-121 4.02e-05

Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 45.52  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   4 IKIGIVGLGTVGTGVVkmLQAHQEK------ISEIT-----------GRKLELACVVVHNLKKHDQVDLGDVQLTDQIET 66
Cdd:COG4091    16 IRVGLIGAGQMGRGLL--AQIRRMPgmevvaIADRNperaraalreaGIPEEDIRVVDTAAEADAAIAAGKTVVTDDAEL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1530902961  67 LIDDPSIQIMVEVMGSIHPAKEYITRALQAGKHVVTANKDLIAQYGRELVQIARE 121
Cdd:COG4091    94 LIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRADE 148
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 4-127 5.64e-05

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 42.20  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530902961   4 IKIGIVGLGTVGTGVVKMLQAHQekiseitgRKLELACVVVHNLKKHDQV-DLGDVQLTDQIETLIDDPSIQImVEVMGS 82
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQ--------PGAELVAILDPNSERAEAVaESFGVEVYSDLEELLNDPEIDA-VIVATP 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1530902961  83 IHPAKEYITRALQAGKHV-----VTANkdliAQYGRELVQIARENHRDLF 127
Cdd:pfam01408  72 NGLHYDLAIAALEAGKHVlcekpLATT----VEEAKELVELAKKKGVRVS 117
 
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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