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Conserved domains on  [gi|1207624890|ref|WP_087989691|]
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homoserine dehydrogenase [Anaerotignum lactatifermentans]

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
 7-426 0e+00

homoserine dehydrogenase; Provisional


:

Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 625.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890   7 KIALLGMGTVGGGVYEILAKQKPNMPAKIGSTLEVAKVLVRNKAKYAD-KVPADQLTDQWSDIIDDDSISIVVEVMGGIE 85
Cdd:PRK06349    5 KVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGvDLPGILLTTDPEELVNDPDIDIVVELMGGIE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  86 PARTYIREALSKGKHVVTANKDLMATHGHELLEIAREHQCDLLFEAAVAGGIPIIRPMKQCLLGNDITEVMGIINGTTNF 165
Cdd:PRK06349   85 PARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNGTTNY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 166 ILTKMAEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAFHSSVTFDDVYTEGISKITAKDIRYAHELGY 245
Cdd:PRK06349  165 ILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAKELGY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 246 EIKLLGLAKLTPEGIEVKVHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDAMFYGRGAGALPTGSAVVGDIMDIARNVQYH 325
Cdd:PRK06349  245 RIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARNLVRV 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 326 CTGRIGCSCYQSLPVKKMSETRSSYYIRMKLEDRAGTLAALAGLFGSNNVSISMLLQKAKEGNSAEVVIVTYDVMEKQFM 405
Cdd:PRK06349  325 PHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSEAALR 404

                         410       420
                  ....*....|....*....|.
gi 1207624890 406 DSITVIKTMSMVKEISSIIRV 426
Cdd:PRK06349  405 AALAAIEALDVVLGIPSVIRV 425
 
Name Accession Description Interval E-value
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 7-426 0e+00

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 625.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890   7 KIALLGMGTVGGGVYEILAKQKPNMPAKIGSTLEVAKVLVRNKAKYAD-KVPADQLTDQWSDIIDDDSISIVVEVMGGIE 85
Cdd:PRK06349    5 KVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGvDLPGILLTTDPEELVNDPDIDIVVELMGGIE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  86 PARTYIREALSKGKHVVTANKDLMATHGHELLEIAREHQCDLLFEAAVAGGIPIIRPMKQCLLGNDITEVMGIINGTTNF 165
Cdd:PRK06349   85 PARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNGTTNY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 166 ILTKMAEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAFHSSVTFDDVYTEGISKITAKDIRYAHELGY 245
Cdd:PRK06349  165 ILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAKELGY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 246 EIKLLGLAKLTPEGIEVKVHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDAMFYGRGAGALPTGSAVVGDIMDIARNVQYH 325
Cdd:PRK06349  245 RIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARNLVRV 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 326 CTGRIGCSCYQSLPVKKMSETRSSYYIRMKLEDRAGTLAALAGLFGSNNVSISMLLQKAKEGNSAEVVIVTYDVMEKQFM 405
Cdd:PRK06349  325 PHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSEAALR 404

                         410       420
                  ....*....|....*....|.
gi 1207624890 406 DSITVIKTMSMVKEISSIIRV 426
Cdd:PRK06349  405 AALAAIEALDVVLGIPSVIRV 425
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 25-325 1.44e-160

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: 454.50  E-value: 1.44e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  25 AKQKPNMPAKIGSTLEVAKVLVRNKAKYAD-KVPADQLTDQWSDIIDDDSISIVVEVMGGIEPARTYIREALSKGKHVVT 103
Cdd:COG0460     1 LENAEELARRLGLDLRVVGVAVRDGMKPRGiDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 104 ANKDLMATHGHELLEIAREHQCDLLFEAAVAGGIPIIRPMKQCLLGNDITEVMGIINGTTNFILTKMAEDGMEFDDALKL 183
Cdd:COG0460    81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 184 ATDLGYAEADPTADIEGYDAGRKLAIMASIAFHSSVTFDDVYTEGISKITAKDIRYAHELGYEIKLLGLAKLTPEGIEVK 263
Cdd:COG0460   161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207624890 264 VHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDAMFYGRGAGALPTGSAVVGDIMDIARNVQYH 325
Cdd:COG0460   241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLRAG 302
Homoserine_dh pfam00742
Homoserine dehydrogenase;
138-315 8.65e-100

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 295.05  E-value: 8.65e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 138 PIIRPMKQCLLGNDITEVMGIINGTTNFILTKMAEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAFHS 217
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 218 SVTFDDVYTEGISKITAKDIRYAHELGYEIKLLGLAKLTPEGIEVKVHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDAMF 297
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 1207624890 298 YGRGAGALPTGSAVVGDI 315
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 ...
 350-426 2.89e-20

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: 84.49  E-value: 2.89e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207624890 350 YYIRMKLEDRAGTLAALAGLFGSNNVSISMLLQK-AKEGNSAEVVIVTYDVMEKQFMDSITVIKTMSMVKEISSIIRV 426
Cdd:cd04881     1 YYLRLTVKDKPGVLAKITGILAEHGISIESVIQKeADGGETAPVVIVTHETSEAALNAALAEIEALDAVQGVPSVIRV 78
 
Name Accession Description Interval E-value
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 7-426 0e+00

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 625.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890   7 KIALLGMGTVGGGVYEILAKQKPNMPAKIGSTLEVAKVLVRNKAKYAD-KVPADQLTDQWSDIIDDDSISIVVEVMGGIE 85
Cdd:PRK06349    5 KVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGvDLPGILLTTDPEELVNDPDIDIVVELMGGIE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  86 PARTYIREALSKGKHVVTANKDLMATHGHELLEIAREHQCDLLFEAAVAGGIPIIRPMKQCLLGNDITEVMGIINGTTNF 165
Cdd:PRK06349   85 PARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNGTTNY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 166 ILTKMAEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAFHSSVTFDDVYTEGISKITAKDIRYAHELGY 245
Cdd:PRK06349  165 ILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAKELGY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 246 EIKLLGLAKLTPEGIEVKVHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDAMFYGRGAGALPTGSAVVGDIMDIARNVQYH 325
Cdd:PRK06349  245 RIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARNLVRV 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 326 CTGRIGCSCYQSLPVKKMSETRSSYYIRMKLEDRAGTLAALAGLFGSNNVSISMLLQKAKEGNSAEVVIVTYDVMEKQFM 405
Cdd:PRK06349  325 PHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSEAALR 404

                         410       420
                  ....*....|....*....|.
gi 1207624890 406 DSITVIKTMSMVKEISSIIRV 426
Cdd:PRK06349  405 AALAAIEALDVVLGIPSVIRV 425
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 25-325 1.44e-160

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: 454.50  E-value: 1.44e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  25 AKQKPNMPAKIGSTLEVAKVLVRNKAKYAD-KVPADQLTDQWSDIIDDDSISIVVEVMGGIEPARTYIREALSKGKHVVT 103
Cdd:COG0460     1 LENAEELARRLGLDLRVVGVAVRDGMKPRGiDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 104 ANKDLMATHGHELLEIAREHQCDLLFEAAVAGGIPIIRPMKQCLLGNDITEVMGIINGTTNFILTKMAEDGMEFDDALKL 183
Cdd:COG0460    81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 184 ATDLGYAEADPTADIEGYDAGRKLAIMASIAFHSSVTFDDVYTEGISKITAKDIRYAHELGYEIKLLGLAKLTPEGIEVK 263
Cdd:COG0460   161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207624890 264 VHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDAMFYGRGAGALPTGSAVVGDIMDIARNVQYH 325
Cdd:COG0460   241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLRAG 302
Homoserine_dh pfam00742
Homoserine dehydrogenase;
138-315 8.65e-100

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 295.05  E-value: 8.65e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 138 PIIRPMKQCLLGNDITEVMGIINGTTNFILTKMAEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAFHS 217
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 218 SVTFDDVYTEGISKITAKDIRYAHELGYEIKLLGLAKLTPEGIEVKVHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDAMF 297
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 1207624890 298 YGRGAGALPTGSAVVGDI 315
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 7-321 5.89e-89

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 273.66  E-value: 5.89e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890   7 KIALLGMGTVGGGVYEILAKQKPNMPAKIGSTLEV-----------------AKVLVRNKAK---------YADKVPADQ 60
Cdd:PRK06270    4 KIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVvaiadssgsaidpdgldLELALKVKEEtgkladypeGGGEISGLE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  61 LTDQwsdiiddDSISIVVEV-----MGGiEPARTYIREALSKGKHVVTANKDLMATHGHELLEIAREHQCDLLFEAAVAG 135
Cdd:PRK06270   84 VIRS-------VDADVVVEAtptniETG-EPALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 136 GIPIIRPMKQCLLGNDITEVMGIINGTTNFILTKMAEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAF 215
Cdd:PRK06270  156 AMPIINLAKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSIL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 216 HSSVTFDDVYTEGISKITAKDIRYAHELGYEIKLLGLAKLTPEGievKVHPTMIPLQHPLaAVKDSFNAVFVHGDAVDDA 295
Cdd:PRK06270  236 GADLTIKDVEVEGITKITPEAIELAAKEGYRIKLIGEVSREKDL---SVSPRLVPLDHPL-AVSGTLNAATFETDLAGDV 311

                         330       340
                  ....*....|....*....|....*.
gi 1207624890 296 MFYGRGAGALPTGSAVVGDIMDIARN 321
Cdd:PRK06270  312 TVVGRGAGSIETASAILSDLIAIHDR 337
PRK08374 PRK08374
homoserine dehydrogenase; Provisional
 7-319 6.96e-48

homoserine dehydrogenase; Provisional


Pssm-ID: 169409 [Multi-domain]  Cd Length: 336  Bit Score: 166.91  E-value: 6.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890   7 KIALLGMGTVGGGVYEILAKQKPNMPAKIGSTLEVAKVLVRNKAKYA----DKVPADQLTDQWSDIIDDDSISIV----- 77
Cdd:PRK08374    4 KVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELKVVSITDTSGTIWLpediDLREAKEVKENFGKLSNWGNDYEVynfsp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  78 VEVMGGIEP-----------ARTYIREALSKGKHVVTANKDLMATHGHELLEIAREHQCDLLFEAAVAGGIPIIRPMKQC 146
Cdd:PRK08374   84 EEIVEEIDAdivvdvtndknAHEWHLEALKEGKSVVTSNKPPIAFHYDELLDLANERNLPYLFEATVMAGTPIIGLLREN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 147 LLGNDITEVMGIINGTTNFILTKMaEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAFHsSVTFDDVYT 226
Cdd:PRK08374  164 LLGDTVKRIEAVVNATTTFILTRM-EQGKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAFP-PITFEEVGI 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 227 EGISKITAKDIRYAHELGYEIKLLGlaklTPEGIEVKVHPTMIPLQHPLaAVKDSFNAVFVHGDAVDDAMFYGRGAGALP 306
Cdd:PRK08374  242 RGIKDVTEGEIERAKAKGRNVRLVA----TVEEGRISVKPKKLPENSPL-AVEGVENAAVIKTDLLGELVLKGPGAGGKE 316

                         330
                  ....*....|...
gi 1207624890 307 TGSAVVGDIMDIA 319
Cdd:PRK08374  317 TASGVVTDIIKAA 329
PRK06813 PRK06813
homoserine dehydrogenase; Validated
 6-321 1.62e-32

homoserine dehydrogenase; Validated


Pssm-ID: 168683 [Multi-domain]  Cd Length: 346  Bit Score: 125.75  E-value: 1.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890   6 KKIALLGMGTVGGGVYEILAKQKPNMPAKIGSTLEVAKVLVRNKA-----------------------KYADKVPADQLT 62
Cdd:PRK06813    3 IKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNVAihnedglsihhllrygggscaieKYIEHHPEERAT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  63 DQwsDIIDDDSISIVVEVMGGiEPARTYIREALSKGKHVVTANKDLMATHGHELLEIAREHQCDLLFEAAVAGGIPIIRP 142
Cdd:PRK06813   83 DN--ISGTVLVESTVTNLKDG-NPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIANVRIRYSGATAAALPTLDI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 143 MKQCLLGNDITEVMGIINGTTNFILTKMAEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAFHSSVTFD 222
Cdd:PRK06813  160 GQFSLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLTNSLMGTENKLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 223 DVYTEGISKITAKDIRYAHELGYEIKLLGLAKLTPEG-IEVKVHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDAMFYGRG 301
Cdd:PRK06813  240 DIHIKGIEHVTKQQIRNAKEQNKIIKLIASAYKDNEGnVNLNVEPYKIEKNHPLANVNGTEKGITFFTDTMGQVTTIGGA 319

                         330       340
                  ....*....|....*....|
gi 1207624890 302 AGALPTGSAVVGDIMDIARN 321
Cdd:PRK06813  320 SNPRGAAAAALKDIINLYRK 339
PRK06392 PRK06392
homoserine dehydrogenase; Provisional
 92-232 4.86e-27

homoserine dehydrogenase; Provisional


Pssm-ID: 102354 [Multi-domain]  Cd Length: 326  Bit Score: 110.35  E-value: 4.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  92 REALSKGKHVVTANKDLMATHGHELLEIAREHQCDLLFEAAVAGGIPIIRPMKQCLLGNDITEVMGIINGTTNFILTKMA 171
Cdd:PRK06392  103 INAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRYEATVAGGVPLFSLRDYSTLPSRIKNFRGIVSSTINYVIRQEA 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207624890 172 eDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMASIAFHSSVTFDDVYTEGISKI 232
Cdd:PRK06392  183 -NGRGFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLFGKDYTLRDVTYDGIENI 242
ACT_HSDH-Hom cd04881
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ...
 350-426 2.89e-20

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: 84.49  E-value: 2.89e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207624890 350 YYIRMKLEDRAGTLAALAGLFGSNNVSISMLLQK-AKEGNSAEVVIVTYDVMEKQFMDSITVIKTMSMVKEISSIIRV 426
Cdd:cd04881     1 YYLRLTVKDKPGVLAKITGILAEHGISIESVIQKeADGGETAPVVIVTHETSEAALNAALAEIEALDAVQGVPSVIRV 78
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 85-319 1.71e-19

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 90.99  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  85 EPARTYIrEALSKGKHVVTANK----DLMATHgHELLEIAREHQCDLLFEAAVAGGIPIIRPMKQcLL--GNDITEVMGI 158
Cdd:PRK09436  559 AVADQYA-DFLAAGFHVVTPNKkantSSYAYY-HQLREAARKSRRKFLYETNVGAGLPVIETLQN-LLnaGDELLKFEGI 635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 159 INGTTNFILTKMaEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMA----------SIAFHS----------S 218
Cdd:PRK09436  636 LSGSLSFIFGKL-DEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILAreagyeleleDIEVESvlpeefdasgS 714

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 219 V-TF-------DDVYTEGISKITA--KDIRYAHELgyeikllglakltpEGIEVKVHPTMIPLQHPLAAVKDSFNAVfvh 288
Cdd:PRK09436  715 VdEFmarlpelDAEFAARVAKARAegKVLRYVGQI--------------EDGKCRVGIAEVDANHPLYKVKGGENAL--- 777

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1207624890 289 gdavddaMFY------------GRGAGALPTGSAVVGDIMDIA 319
Cdd:PRK09436  778 -------AFYtryyqpiplvlrGYGAGNEVTAAGVFADLLRTL 813
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 12-130 1.14e-16

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: 75.42  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  12 GMGTVGGGVYEILAKQKPNMPakigstLEVAKVLVRNKAKY--ADKVPADQLTDQWSDIIDDDSISIVVEVmGGIEPART 89
Cdd:pfam03447   1 GCGAIGSGVLEQLLRQQSEIP------LELVAVADRDLLSKdpLALLPDEPLTLDLDDLIAHPDPDVVVEC-ASSEAVAE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1207624890  90 YIREALSKGKHVVTANKDLMA--THGHELLEIAREHQCDLLFE 130
Cdd:pfam03447  74 LVLDALKAGKDVVTASKGALAdlALYEELREAAEANGARIYVE 116
PLN02700 PLN02700
homoserine dehydrogenase family protein
 129-318 3.05e-11

homoserine dehydrogenase family protein


Pssm-ID: 215377 [Multi-domain]  Cd Length: 377  Bit Score: 64.41  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 129 FEAAVAGGIPIIRPMKQCLL-GNDITEVMGIINGTTNFILTKMaEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKL 207
Cdd:PLN02700  163 HESTVGAGLPVIASLNRILSsGDPVHRIVGSLSGTLGYVMSEL-EDGKPFSEVVKQAKSLGYTEPDPRDDLGGMDVARKA 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890 208 AIMASIaFHSSVTFDDVYTEGIskitakdirYAHELGYEIKLL------GLAKL----------------------TPEG 259
Cdd:PLN02700  242 LILARL-LGKRINMDSIKVESL---------YPEEMGPDLMSTddflhsGLVELdlpieervkeaslkgcvlryvcVIEG 311

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207624890 260 IEVKVHPTMIPLQHPLAAVKDSFNAVFVHGDAVDDA--MFYGRGAGALPTGSAVVGDIMDI 318
Cdd:PLN02700  312 SSCQVGIRELPKDSALGRLRGSDNVVEIYSRCYSEQplVIQGAGAGNDTTAAGVLADILDL 372
metL PRK09466
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
 8-211 3.25e-09

bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional


Pssm-ID: 236530 [Multi-domain]  Cd Length: 810  Bit Score: 59.17  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890   8 IALLGMGTVGGGVYEILAKQKPNMPAKIGSTLEVAKVLVRNKA--KYaDKVPADQLTDQWSDIIDDDSISIVVEVMGGI- 84
Cdd:PRK09466  461 LVLFGKGNIGSRWLELFAREQSTLSARTGFEFVLVGVVDSRRSllNY-DGLDASRALAFFDDEAVEWDEESLFLWLRAHp 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207624890  85 -------------EPARTYIrEALSKGKHVVTANKdlMATHG-----HELLEIAREHQCDLLFEAAVAGGIPI---IRPM 143
Cdd:PRK09466  540 ydelvvldvtaseQLALQYP-DFASHGFHVISANK--LAGSSpsnfyRQIKDAFAKTGRHWLYNATVGAGLPInhtVRDL 616

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207624890 144 KQCllGNDITEVMGIINGTTNFiLTKMAEDGMEFDDALKLATDLGYAEADPTADIEGYDAGRKLAIMA 211
Cdd:PRK09466  617 RNS--GDSILAISGIFSGTLSW-LFLQFDGSVPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILA 681
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 350-403 1.20e-04

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 39.98  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207624890 350 YYIRMKLEDRAGTLAALAGLFGSNNVSISMLLQKAKEGnSAEVVIVTYDVMEKQ 403
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSED-KGGIVFVVIVVDEED 53
 
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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