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Conserved domains on  [gi|500196241|ref|WP_011869448|]
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homoserine dehydrogenase [Methanococcus maripaludis]

Protein Classification

homoserine dehydrogenase( domain architecture ID 11482168)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 1-337 0e+00

homoserine dehydrogenase; Provisional


:

Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 569.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   1 MKIILVGFGIIGKGVLKTITLKSEHLKKRYGMDLQVAAICDRSGAAIDENGLDLELALKIKEETGKIANYPEKGCEMGIL 80
Cdd:PRK06270   3 MKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIADSSGSAIDPDGLDLELALKVKEETGKLADYPEGGGEISGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  81 EVIESVSADAVVEVSPTNIETGEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGAMPIINL 160
Cdd:PRK06270  83 EVIRSVDADVVVEATPTNIETGEPALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAMPIINL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 161 AKETLAGNDIKLIKGILNGTTNYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGRDVTIK 240
Cdd:PRK06270 163 AKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGADLTIK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 241 DVNLEGITRITPEALAMANKSGHTIKLIGEVTDKK-LEVCPKLIPIDSPLNVKGSLNVAMVNTDLANDIVVVGAGAGDIE 319
Cdd:PRK06270 243 DVEVEGITKITPEAIELAAKEGYRIKLIGEVSREKdLSVSPRLVPLDHPLAVSGTLNAATFETDLAGDVTVVGRGAGSIE 322

                        330
                 ....*....|....*...
gi 500196241 320 TASAILSDLVNIHQTLKN 337
Cdd:PRK06270 323 TASAILSDLIAIHDRYGK 340
 
Name Accession Description Interval E-value
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 1-337 0e+00

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 569.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   1 MKIILVGFGIIGKGVLKTITLKSEHLKKRYGMDLQVAAICDRSGAAIDENGLDLELALKIKEETGKIANYPEKGCEMGIL 80
Cdd:PRK06270   3 MKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIADSSGSAIDPDGLDLELALKVKEETGKLADYPEGGGEISGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  81 EVIESVSADAVVEVSPTNIETGEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGAMPIINL 160
Cdd:PRK06270  83 EVIRSVDADVVVEATPTNIETGEPALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAMPIINL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 161 AKETLAGNDIKLIKGILNGTTNYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGRDVTIK 240
Cdd:PRK06270 163 AKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGADLTIK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 241 DVNLEGITRITPEALAMANKSGHTIKLIGEVTDKK-LEVCPKLIPIDSPLNVKGSLNVAMVNTDLANDIVVVGAGAGDIE 319
Cdd:PRK06270 243 DVEVEGITKITPEAIELAAKEGYRIKLIGEVSREKdLSVSPRLVPLDHPLAVSGTLNAATFETDLAGDVTVVGRGAGSIE 322

                        330
                 ....*....|....*...
gi 500196241 320 TASAILSDLVNIHQTLKN 337
Cdd:PRK06270 323 TASAILSDLIAIHDRYGK 340
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 22-336 6.26e-121

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: 350.11  E-value: 6.26e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  22 KSEHLKKRYGMDLQVAAICDRSGAaiDENGLDLELALKikeetgkianypekgcEMGILEVIESVSADAVVEVSPTniet 101
Cdd:COG0460    3 NAEELARRLGLDLRVVGVAVRDGM--KPRGIDLPRWLL----------------TTDLEELIKDPEIDVVVELTGG---- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 102 GEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGAMPIINLAKETLAGNDIKLIKGILNGTT 181
Cdd:COG0460   61 SEPARELYLAALEAGKHVVTANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 182 NYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGRDVTIKDVNLEGITRITPEALAMANKS 261
Cdd:COG0460  141 NYILTKMEEEGLSFSEALKEAQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKEL 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 262 GHTIKLIGEVTDK----KLEVCPKLIPIDSPL-NVKGSLNVAMVNTDLANDIVVVGAGAGDIETASAILSDLVNIHQTLK 336
Cdd:COG0460  221 GYVIKLLAIAERTgggvEARVHPTLVPADHPLaSVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLR 300
Homoserine_dh pfam00742
Homoserine dehydrogenase;
156-328 6.41e-77

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 233.42  E-value: 6.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  156 PIINLAKETLAGNDIKLIKGILNGTTNYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGR 235
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  236 DVTIKDVNLEGITRITPEALAMANKSGHTIKLIGEV--TDKKLE--VCPKLIPIDSPL-NVKGSLNVAMVNTDLANDIVV 310
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAkrDDGGVEarVGPTLVPKDHPLaSVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 500196241  311 VGAGAGDIETASAILSDL 328
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
 2-72 9.21e-04

NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha -beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133445 [Multi-domain]  Cd Length: 227  Bit Score: 40.21  E-value: 9.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500196241   2 KIILVGFGIIGKGVLKTITlksehlkkRYGMDlqVAAICDRSGAAIDENGLDLELALKIKEETGKIANYPE 72
Cdd:cd01076   33 RVAIQGFGNVGSHAARFLH--------EAGAK--VVAVSDSDGTIYNPDGLDVPALLAYKKEHGSVLGFPG 93
 
Name Accession Description Interval E-value
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 1-337 0e+00

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 569.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   1 MKIILVGFGIIGKGVLKTITLKSEHLKKRYGMDLQVAAICDRSGAAIDENGLDLELALKIKEETGKIANYPEKGCEMGIL 80
Cdd:PRK06270   3 MKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIADSSGSAIDPDGLDLELALKVKEETGKLADYPEGGGEISGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  81 EVIESVSADAVVEVSPTNIETGEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGAMPIINL 160
Cdd:PRK06270  83 EVIRSVDADVVVEATPTNIETGEPALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAMPIINL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 161 AKETLAGNDIKLIKGILNGTTNYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGRDVTIK 240
Cdd:PRK06270 163 AKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGADLTIK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 241 DVNLEGITRITPEALAMANKSGHTIKLIGEVTDKK-LEVCPKLIPIDSPLNVKGSLNVAMVNTDLANDIVVVGAGAGDIE 319
Cdd:PRK06270 243 DVEVEGITKITPEAIELAAKEGYRIKLIGEVSREKdLSVSPRLVPLDHPLAVSGTLNAATFETDLAGDVTVVGRGAGSIE 322

                        330
                 ....*....|....*...
gi 500196241 320 TASAILSDLVNIHQTLKN 337
Cdd:PRK06270 323 TASAILSDLIAIHDRYGK 340
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 22-336 6.26e-121

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: 350.11  E-value: 6.26e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  22 KSEHLKKRYGMDLQVAAICDRSGAaiDENGLDLELALKikeetgkianypekgcEMGILEVIESVSADAVVEVSPTniet 101
Cdd:COG0460    3 NAEELARRLGLDLRVVGVAVRDGM--KPRGIDLPRWLL----------------TTDLEELIKDPEIDVVVELTGG---- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 102 GEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGAMPIINLAKETLAGNDIKLIKGILNGTT 181
Cdd:COG0460   61 SEPARELYLAALEAGKHVVTANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 182 NYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGRDVTIKDVNLEGITRITPEALAMANKS 261
Cdd:COG0460  141 NYILTKMEEEGLSFSEALKEAQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKEL 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 262 GHTIKLIGEVTDK----KLEVCPKLIPIDSPL-NVKGSLNVAMVNTDLANDIVVVGAGAGDIETASAILSDLVNIHQTLK 336
Cdd:COG0460  221 GYVIKLLAIAERTgggvEARVHPTLVPADHPLaSVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLR 300
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-331 6.29e-93

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 283.12  E-value: 6.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   1 MKIILVGFGIIGKGVLKTITLKSEHLKKRYGMDLQVAAICDRsgaaidenglDLELALKIKEETGKIANYPEkgcemgil 80
Cdd:PRK06349   4 LKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVR----------DLEKDRGVDLPGILLTTDPE-------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  81 EVIESVSADAVVEVsptnIETGEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGAMPIINL 160
Cdd:PRK06349  66 ELVNDPDIDIVVEL----MGGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 161 AKETLAGNDIKLIKGILNGTTNYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGRDVTIK 240
Cdd:PRK06349 142 LREGLAANRITRVMGIVNGTTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFD 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 241 DVNLEGITRITPEALAMANKSGHTIKLIG--EVTDKKLE--VCPKLIPIDSPL-NVKGSLNVAMVNTDLANDIVVVGAGA 315
Cdd:PRK06349 222 DVYVEGISKITAEDIAYAKELGYRIKLLGiaERTEEGIElrVHPTLIPKSHPLaNVNGVMNAVFVEGDAVGETMFYGPGA 301

                        330
                 ....*....|....*.
gi 500196241 316 GDIETASAILSDLVNI 331
Cdd:PRK06349 302 GGLPTASAVVADLVDI 317
Homoserine_dh pfam00742
Homoserine dehydrogenase;
156-328 6.41e-77

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 233.42  E-value: 6.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  156 PIINLAKETLAGNDIKLIKGILNGTTNYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGR 235
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  236 DVTIKDVNLEGITRITPEALAMANKSGHTIKLIGEV--TDKKLE--VCPKLIPIDSPL-NVKGSLNVAMVNTDLANDIVV 310
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAkrDDGGVEarVGPTLVPKDHPLaSVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 500196241  311 VGAGAGDIETASAILSDL 328
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
PRK08374 PRK08374
homoserine dehydrogenase; Provisional
 1-329 1.17e-73

homoserine dehydrogenase; Provisional


Pssm-ID: 169409 [Multi-domain]  Cd Length: 336  Bit Score: 230.85  E-value: 1.17e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   1 MKIILVGFGIIGKGVLKTITLKSEHLKKRYGMDLQVAAICDRSGAAIDENGLDLELALKIKEETGKIANYPE--KGCEMG 78
Cdd:PRK08374   3 VKVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELKVVSITDTSGTIWLPEDIDLREAKEVKENFGKLSNWGNdyEVYNFS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  79 ILEVIESVSADAVVEVSptnieTGEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGAMPII 158
Cdd:PRK08374  83 PEEIVEEIDADIVVDVT-----NDKNAHEWHLEALKEGKSVVTSNKPPIAFHYDELLDLANERNLPYLFEATVMAGTPII 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 159 NLAKETLAGNDIKLIKGILNGTTNYILTKMEkEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFgRDVT 238
Cdd:PRK08374 158 GLLRENLLGDTVKRIEAVVNATTTFILTRME-QGKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAF-PPIT 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 239 IKDVNLEGITRITPEALAMANKSGHTIKLIGEVTDKKLEVCPKLIPIDSPLNVKGSLNVAMVNTDLANDIVVVGAGAGDI 318
Cdd:PRK08374 236 FEEVGIRGIKDVTEGEIERAKAKGRNVRLVATVEEGRISVKPKKLPENSPLAVEGVENAAVIKTDLLGELVLKGPGAGGK 315

                        330
                 ....*....|.
gi 500196241 319 ETASAILSDLV 329
Cdd:PRK08374 316 ETASGVVTDII 326
PRK06813 PRK06813
homoserine dehydrogenase; Validated
 1-333 1.02e-63

homoserine dehydrogenase; Validated


Pssm-ID: 168683 [Multi-domain]  Cd Length: 346  Bit Score: 205.48  E-value: 1.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   1 MKIILVGFGIIGKGVLKTITLKSEHLKKRYGMDLQVAAICDRSGAAIDENGLDLELALKIKEETGKIANYPEKGCEMgil 80
Cdd:PRK06813   3 IKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNVAIHNEDGLSIHHLLRYGGGSCAIEKYIEHHPEE--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  81 EVIESVSADAVVEVSPTNIETGEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGAMPIINL 160
Cdd:PRK06813  80 RATDNISGTVLVESTVTNLKDGNPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIANVRIRYSGATAAALPTLDI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 161 AKETLAGNDIKLIKGILNGTTNYILTKMEKEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFGRDVTIK 240
Cdd:PRK06813 160 GQFSLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLTNSLMGTENKLT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 241 DVNLEGITRITPEALAMANKSGHTIKLIGEV-----TDKKLEVCPKLIPIDSPL-NVKGSLNVAMVNTDLANDIVVVGAG 314
Cdd:PRK06813 240 DIHIKGIEHVTKQQIRNAKEQNKIIKLIASAykdneGNVNLNVEPYKIEKNHPLaNVNGTEKGITFFTDTMGQVTTIGGA 319

                        330
                 ....*....|....*....
gi 500196241 315 AGDIETASAILSDLVNIHQ 333
Cdd:PRK06813 320 SNPRGAAAAALKDIINLYR 338
PRK06392 PRK06392
homoserine dehydrogenase; Provisional
 1-329 8.33e-45

homoserine dehydrogenase; Provisional


Pssm-ID: 102354 [Multi-domain]  Cd Length: 326  Bit Score: 155.80  E-value: 8.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   1 MKIILVGFGIIGKGVLKTItlKSEHLKKRYGMDLQVAAICDRSGAAIDENGLDLelalkikeetGKIANYPEKGC----- 75
Cdd:PRK06392   1 IRISIIGLGNVGLNVLRII--KSRNDDRRNNNGISVVSVSDSKLSYYNERGLDI----------GKIISYKEKGRleeid 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  76 -EMGILEVIESVSADAVVEVSPTNIEtGEPAKSYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENKVCFRYEASVGGA 154
Cdd:PRK06392  69 yEKIKFDEIFEIKPDVIVDVTPASKD-GIREKNLYINAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRYEATVAGG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 155 MPIINLAKETLAGNDIKLIKGILNGTTNYILTKMEKEQlDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSIFG 234
Cdd:PRK06392 148 VPLFSLRDYSTLPSRIKNFRGIVSSTINYVIRQEANGR-GFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLFG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 235 RDVTIKDVNLEGITRItpEALAMANKsghtiKLIGEV--TDKKLEVCPKLIPIDSP--LNVKGSLNVA-MVNTDLANDIV 309
Cdd:PRK06392 227 KDYTLRDVTYDGIENI--DRSSMDNE-----RLVTEVamINGGPHAESRIRSLSRNdfLGMIGPLSLGyQMETDINGTIN 299

                        330       340
                 ....*....|....*....|
gi 500196241 310 VVGAGAGDIETASAILSDLV 329
Cdd:PRK06392 300 VSDNYDGPYETAGAVVNDVM 319
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 5-331 1.14e-31

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 125.27  E-value: 1.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   5 LVGFGIIGKGVLKTITLKSEHLKKRyGMDLQVAAICDRSGAAIDENGLDLEL---ALKIKEETGKIANYPEKGCEMGILE 81
Cdd:PRK09436 470 VIGVGGVGGALLEQIKRQQPWLKKK-NIDLRVCGIANSRKMLLDEHGIDLDNwreELAEAGEPFDLDRLIRLVKEYHLLN 548

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  82 -VIESVSADAVVevsptnietgepAKSY--MLKA-FeckkHVVSANK----GPLAVsFKDLVKCAKENKVCFRYEASVGG 153
Cdd:PRK09436 549 pVIVDCTSSQAV------------ADQYadFLAAgF----HVVTPNKkantSSYAY-YHQLREAARKSRRKFLYETNVGA 611

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 154 AMPII-NLAKETLAGNDIKLIKGILNGTTNYILTKMEkEQLDFDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSI 232
Cdd:PRK09436 612 GLPVIeTLQNLLNAGDELLKFEGILSGSLSFIFGKLD-EGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILAREA 690

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 233 fGRDVTIKDVNLEGI---------------TRItPEA-------LAMANKSGHTIKLIGEVTDKKLEVCPKLIPIDSPL- 289
Cdd:PRK09436 691 -GYELELEDIEVESVlpeefdasgsvdefmARL-PELdaefaarVAKARAEGKVLRYVGQIEDGKCRVGIAEVDANHPLy 768

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 500196241 290 NVKGSLNVAMVNTDLANDI--VVVGAGAGDIETASAILSDLVNI 331
Cdd:PRK09436 769 KVKGGENALAFYTRYYQPIplVLRGYGAGNEVTAAGVFADLLRT 812
PLN02700 PLN02700
homoserine dehydrogenase family protein
 3-331 7.65e-26

homoserine dehydrogenase family protein


Pssm-ID: 215377 [Multi-domain]  Cd Length: 377  Bit Score: 106.01  E-value: 7.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   3 IILVGFGIIGKGVLKTItLKSEHLKKRYGMDLQVAAICDRSGAAIDENGLDLEL-------------------ALKIKEE 63
Cdd:PLN02700   6 VLLLGCGGVGRHLLRHI-VSCRSLHAKQGVRIRVVGVCDSKSLVLAEDVLNEELddallsevclakskgsplsALGALAG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  64 TGKIANYPE-KGCEMGILEVIESVSADAVVEVSPTnIETGEpaksYMLKAFECKKHVVSANKGPLAVSFKDLVKCAKENK 142
Cdd:PLN02700  85 GCQVFNNSElSRKVIDIATLLGKSTGLVVVDCSAS-METIG----ALNEAVDLGCCIVLANKKPLTSTLEDYDKLAAHPR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 143 VcFRYEASVGGAMPIINLAKETLA-GNDIKLIKGILNGTTNYILTKMEKEQlDFDTVLKEAQELGIAETNPHQDISGLDT 221
Cdd:PLN02700 160 R-IRHESTVGAGLPVIASLNRILSsGDPVHRIVGSLSGTLGYVMSELEDGK-PFSEVVKQAKSLGYTEPDPRDDLGGMDV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 222 AAKIVILAnSIFGRDVTIKDVNLEGI--TRITPEALAM---------------------ANKSGHTIKLIGEVTDKKLEV 278
Cdd:PLN02700 238 ARKALILA-RLLGKRINMDSIKVESLypEEMGPDLMSTddflhsglveldlpieervkeASLKGCVLRYVCVIEGSSCQV 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500196241 279 CPKLIPIDSPL-NVKGSLNVAMVNTDLAND--IVVVGAGAGDIETASAILSDLVNI 331
Cdd:PLN02700 317 GIRELPKDSALgRLRGSDNVVEIYSRCYSEqpLVIQGAGAGNDTTAAGVLADILDL 372
metL PRK09466
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
 3-335 3.86e-22

bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional


Pssm-ID: 236530 [Multi-domain]  Cd Length: 810  Bit Score: 97.30  E-value: 3.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   3 IILVGFGIIGKGVLKTITLKSEHLKKRYGMDLQVAAICDRSGAAIDENGLDLELALKIKEETGKIANYPEKGCEMGILEV 82
Cdd:PRK09466 461 LVLFGKGNIGSRWLELFAREQSTLSARTGFEFVLVGVVDSRRSLLNYDGLDASRALAFFDDEAVEWDEESLFLWLRAHPY 540

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241  83 IESVsadaVVEVSPTnietgEPAKSYMLKAFECKKHVVSANK----GPLAvSFKDLVKCAKENKVCFRYEASVGGAMPIi 158
Cdd:PRK09466 541 DELV----VLDVTAS-----EQLALQYPDFASHGFHVISANKlagsSPSN-FYRQIKDAFAKTGRHWLYNATVGAGLPI- 609

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 159 NLAKETL--AGNDIKLIKGILNGTTNYILtkmekEQLD----FDTVLKEAQELGIAETNPHQDISGLDTAAKIVILANSI 232
Cdd:PRK09466 610 NHTVRDLrnSGDSILAISGIFSGTLSWLF-----LQFDgsvpFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILAREA 684

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241 233 fGRDVTIKDVNLEG--------------ITRITP------EALAMANKSGHTIKLIGEVT-DKKLEVCPKLIPIDSPL-N 290
Cdd:PRK09466 685 -GYEIEPDDVRVESlvpahledgsldqfFENGDEldeqmlQRLEAAAEQGKVLRYVARFDaNGKARVGVEAVRPDHPLaN 763

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 500196241 291 VKGSLNVAMVNTDL--ANDIVVVGAGAGDIETASAILSDLVNIHQTL 335
Cdd:PRK09466 764 LLPCDNVFAIESRWyrDNPLVIRGPGAGREVTAGAIQSDLNRLAQLL 810
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 7-148 5.08e-06

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: 44.99  E-value: 5.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241    7 GFGIIGKGVLKTitLKSEHLKKrygmDLQVAAICDRSgaaidengldleLALKIKEetgkiANYPEKGCEMGILEVIESV 86
Cdd:pfam03447   1 GCGAIGSGVLEQ--LLRQQSEI----PLELVAVADRD------------LLSKDPL-----ALLPDEPLTLDLDDLIAHP 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500196241   87 SADAVVEVSPTnietgEPAKSYMLKAFECKKHVVSANKGPLA--VSFKDLVKCAKENKVCFRYE 148
Cdd:pfam03447  58 DPDVVVECASS-----EAVAELVLDALKAGKDVVTASKGALAdlALYEELREAAEANGARIYVE 116
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
 36-72 8.14e-06

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440103 [Multi-domain]  Cd Length: 411  Bit Score: 46.98  E-value: 8.14e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 500196241  36 VAAICDRSGAAIDENGLDLELALKIKEETGKIANYPE 72
Cdd:COG0334  234 VVAVSDSSGGIYDPDGIDLDALKEHKEERGSVAGYPG 270
ELFV_dehydrog pfam00208
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;
36-74 1.72e-05

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;


Pssm-ID: 425526 [Multi-domain]  Cd Length: 240  Bit Score: 45.58  E-value: 1.72e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 500196241   36 VAAICDRSGAAIDENGLDLELALKIKEETGKIANYPEKG 74
Cdd:pfam00208  58 VVAVSDSSGAIYDPDGLDIEELLELKEERGSVDEYALSG 96
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-145 3.99e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 41.45  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500196241   1 MKIILVGFGIIGKGVLKTITLKSehlkkrygmDLQVAAICDRsgaaidenglDLELALKIKEETGkIANYPEkgcemgIL 80
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAALP---------GVELVAVADR----------DPERAEAFAEEYG-VRVYTD------YE 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500196241  81 EVIESVSADAVVEVSPTNIetgepAKSYMLKAFECKKHVVSAnKgPLAVSFKD---LVKCAKENKVCF 145
Cdd:COG0673   58 ELLADPDIDAVVIATPNHL-----HAELAIAALEAGKHVLCE-K-PLALTLEEareLVAAAEEAGVVL 118
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
 2-72 9.21e-04

NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha -beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133445 [Multi-domain]  Cd Length: 227  Bit Score: 40.21  E-value: 9.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500196241   2 KIILVGFGIIGKGVLKTITlksehlkkRYGMDlqVAAICDRSGAAIDENGLDLELALKIKEETGKIANYPE 72
Cdd:cd01076   33 RVAIQGFGNVGSHAARFLH--------EAGAK--VVAVSDSDGTIYNPDGLDVPALLAYKKEHGSVLGFPG 93
 
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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