|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
1-427 |
0e+00 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 664.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 1 MKEIQVGLLGLGTVGSGVVRIITDHQERLIHQVGCPVKVTKVLVQNIEKEREVEVPSTLLTQDAHEILDNPNIDVVIEVM 80
Cdd:PRK06349 1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 81 GGIDDAKAYILQALQSGKHVVTANKDLMALHGAELLAVAKDNKADLFYEASVAGGIPILRSIVEGLSSDLITKVMGIVNG 160
Cdd:PRK06349 81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 161 TTNFILTKMSDEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILATLGFSTNVELGDVKVKGITSITEEDIEYSK 240
Cdd:PRK06349 161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 241 SLGYTIKLIGLAKRDGEKLEVTVEPTLLPNTHPLAAVQNEYNAVYVYGEAVGETMFYGPGAGSLPTATAVVSDLVAVMQN 320
Cdd:PRK06349 241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 321 IRLGVNGNSAVSPQYKKVLKEPDEIVVKKFLRLHVKDEIGVFAKITSLFSERGVSFEKIIQMPLEEkGKAEIVIVTHRAS 400
Cdd:PRK06349 321 LVRVPHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGG-EGAEIVIVTHETS 399
|
410 420
....*....|....*....|....*..
gi 446581749 401 LADYDYILHTLQGYEEIDCVKANYRIE 427
Cdd:PRK06349 400 EAALRAALAAIEALDVVLGIPSVIRVE 426
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
23-324 |
1.49e-162 |
|
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: 459.51 E-value: 1.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 23 TDHQERLIHQVGCPVKVTKVLVQNIEKEREVEVPSTLLTQDAHEILDNPNIDVVIEVMGGIDDAKAYILQALQSGKHVVT 102
Cdd:COG0460 1 LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 103 ANKDLMALHGAELLAVAKDNKADLFYEASVAGGIPILRSIVEGLSSDLITKVMGIVNGTTNFILTKMSDEGRAYNDVLKE 182
Cdd:COG0460 81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 183 AQQLGFAEADPTSDVEGLDAARKMTILATLGFSTNVELGDVKVKGITSITEEDIEYSKSLGYTIKLIGLAKRDGEKLEVT 262
Cdd:COG0460 161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581749 263 VEPTLLPNTHPLAAVQNEYNAVYVYGEAVGETMFYGPGAGSLPTATAVVSDLVAVMQNIRLG 324
Cdd:COG0460 241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLRAG 302
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
137-314 |
2.25e-95 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 283.88 E-value: 2.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 137 PILRSIVEGLSSDLITKVMGIVNGTTNFILTKMSDEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILATLGFST 216
Cdd:pfam00742 1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 217 NVELGDVKVKGITSITEEDIEYSKSLGYTIKLIGLAKRDGEKLEVTVEPTLLPNTHPLAAVQNEYNAVYVYGEAVGETMF 296
Cdd:pfam00742 81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160
|
170
....*....|....*...
gi 446581749 297 YGPGAGSLPTATAVVSDL 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 ... |
350-427 |
6.76e-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: 83.33 E-value: 6.76e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581749 350 FLRLHVKDEIGVFAKITSLFSERGVSFEKIIQMPLEEKGKAEIVIVTHRASLADYDYILHTLQGYEEIDCVKANYRIE 427
Cdd:cd04881 2 YLRLTVKDKPGVLAKITGILAEHGISIESVIQKEADGGETAPVVIVTHETSEAALNAALAEIEALDAVQGVPSVIRVE 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
1-427 |
0e+00 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 664.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 1 MKEIQVGLLGLGTVGSGVVRIITDHQERLIHQVGCPVKVTKVLVQNIEKEREVEVPSTLLTQDAHEILDNPNIDVVIEVM 80
Cdd:PRK06349 1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 81 GGIDDAKAYILQALQSGKHVVTANKDLMALHGAELLAVAKDNKADLFYEASVAGGIPILRSIVEGLSSDLITKVMGIVNG 160
Cdd:PRK06349 81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 161 TTNFILTKMSDEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILATLGFSTNVELGDVKVKGITSITEEDIEYSK 240
Cdd:PRK06349 161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 241 SLGYTIKLIGLAKRDGEKLEVTVEPTLLPNTHPLAAVQNEYNAVYVYGEAVGETMFYGPGAGSLPTATAVVSDLVAVMQN 320
Cdd:PRK06349 241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 321 IRLGVNGNSAVSPQYKKVLKEPDEIVVKKFLRLHVKDEIGVFAKITSLFSERGVSFEKIIQMPLEEkGKAEIVIVTHRAS 400
Cdd:PRK06349 321 LVRVPHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGG-EGAEIVIVTHETS 399
|
410 420
....*....|....*....|....*..
gi 446581749 401 LADYDYILHTLQGYEEIDCVKANYRIE 427
Cdd:PRK06349 400 EAALRAALAAIEALDVVLGIPSVIRVE 426
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
23-324 |
1.49e-162 |
|
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: 459.51 E-value: 1.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 23 TDHQERLIHQVGCPVKVTKVLVQNIEKEREVEVPSTLLTQDAHEILDNPNIDVVIEVMGGIDDAKAYILQALQSGKHVVT 102
Cdd:COG0460 1 LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 103 ANKDLMALHGAELLAVAKDNKADLFYEASVAGGIPILRSIVEGLSSDLITKVMGIVNGTTNFILTKMSDEGRAYNDVLKE 182
Cdd:COG0460 81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 183 AQQLGFAEADPTSDVEGLDAARKMTILATLGFSTNVELGDVKVKGITSITEEDIEYSKSLGYTIKLIGLAKRDGEKLEVT 262
Cdd:COG0460 161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581749 263 VEPTLLPNTHPLAAVQNEYNAVYVYGEAVGETMFYGPGAGSLPTATAVVSDLVAVMQNIRLG 324
Cdd:COG0460 241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLRAG 302
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
137-314 |
2.25e-95 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 283.88 E-value: 2.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 137 PILRSIVEGLSSDLITKVMGIVNGTTNFILTKMSDEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILATLGFST 216
Cdd:pfam00742 1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 217 NVELGDVKVKGITSITEEDIEYSKSLGYTIKLIGLAKRDGEKLEVTVEPTLLPNTHPLAAVQNEYNAVYVYGEAVGETMF 296
Cdd:pfam00742 81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160
|
170
....*....|....*...
gi 446581749 297 YGPGAGSLPTATAVVSDL 314
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
|
|
| PRK06270 |
PRK06270 |
homoserine dehydrogenase; Provisional |
2-322 |
1.97e-93 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 285.22 E-value: 1.97e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 2 KEIQVGLLGLGTVGSGVVRIITDHQERLIHQVGCPVKVTKV--------------LVQNIEKEREV----EVPSTLLTQD 63
Cdd:PRK06270 1 MEMKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIadssgsaidpdgldLELALKVKEETgklaDYPEGGGEIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 64 AHEILDNPNIDVVIEVM-GGIDD---AKAYILQALQSGKHVVTANKDLMALHGAELLAVAKDNKADLFYEASVAGGIPIL 139
Cdd:PRK06270 81 GLEVIRSVDADVVVEATpTNIETgepALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAMPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 140 RSIVEGLSSDLITKVMGIVNGTTNFILTKMSDEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILATLGFSTNVE 219
Cdd:PRK06270 161 NLAKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGADLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 220 LGDVKVKGITSITEEDIEYSKSLGYTIKLIGLAKRDGeklEVTVEPTLLPNTHPLaAVQNEYNAVYVYGEAVGETMFYGP 299
Cdd:PRK06270 241 IKDVEVEGITKITPEAIELAAKEGYRIKLIGEVSREK---DLSVSPRLVPLDHPL-AVSGTLNAATFETDLAGDVTVVGR 316
|
330 340
....*....|....*....|...
gi 446581749 300 GAGSLPTATAVVSDLVAVMQNIR 322
Cdd:PRK06270 317 GAGSIETASAILSDLIAIHDRYG 339
|
|
| PRK08374 |
PRK08374 |
homoserine dehydrogenase; Provisional |
2-315 |
1.60e-51 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 169409 [Multi-domain] Cd Length: 336 Bit Score: 176.54 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 2 KEIQVGLLGLGTVGSGVVRIITDHQERLIHQVGCPVKVTKV--------LVQNIEKEREVEVPSTL-----LTQD----- 63
Cdd:PRK08374 1 MEVKVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELKVVSItdtsgtiwLPEDIDLREAKEVKENFgklsnWGNDyevyn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 64 --AHEILDNPNIDVVIEVMGGiDDAKAYILQALQSGKHVVTANKDLMALHGAELLAVAKDNKADLFYEASVAGGIPILRS 141
Cdd:PRK08374 81 fsPEEIVEEIDADIVVDVTND-KNAHEWHLEALKEGKSVVTSNKPPIAFHYDELLDLANERNLPYLFEATVMAGTPIIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 142 IVEGLSSDLITKVMGIVNGTTNFILTKMSdEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILATLGFSTnVELG 221
Cdd:PRK08374 160 LRENLLGDTVKRIEAVVNATTTFILTRME-QGKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAFPP-ITFE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 222 DVKVKGITSITEEDIEYSKSLGYTIKLIGLAkrdgEKLEVTVEPTLLPNTHPLAAVQNEyNAVYVYGEAVGETMFYGPGA 301
Cdd:PRK08374 238 EVGIRGIKDVTEGEIERAKAKGRNVRLVATV----EEGRISVKPKKLPENSPLAVEGVE-NAAVIKTDLLGELVLKGPGA 312
|
330
....*....|....
gi 446581749 302 GSLPTATAVVSDLV 315
Cdd:PRK08374 313 GGKETASGVVTDII 326
|
|
| PRK06813 |
PRK06813 |
homoserine dehydrogenase; Validated |
3-320 |
5.86e-36 |
|
homoserine dehydrogenase; Validated
Pssm-ID: 168683 [Multi-domain] Cd Length: 346 Bit Score: 135.38 E-value: 5.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 3 EIQVGLLGLGTVGSGVVRIITDHQERLIHQVGCPVKVTKVLVQN--IEKEREVEVPSTLLTQDAHEIL------------ 68
Cdd:PRK06813 2 KIKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNvaIHNEDGLSIHHLLRYGGGSCAIekyiehhpeera 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 69 -DNPNIDVVIE-----VMGGiDDAKAYILQALQSGKHVVTANKDLMALHGAELLAVAKDNKADLFYEASVAGGIPILRSI 142
Cdd:PRK06813 82 tDNISGTVLVEstvtnLKDG-NPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIANVRIRYSGATAAALPTLDIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 143 VEGLSSDLITKVMGIVNGTTNFILTKMSDEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILATLGFSTNVELGD 222
Cdd:PRK06813 161 QFSLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLTNSLMGTENKLTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 223 VKVKGITSITEEDIEYSKSLGYTIKLIGLA-KRDGEKLEVTVEPTLLPNTHPLAAVQNEYNAVYVYGEAVGETMFYGPGA 301
Cdd:PRK06813 241 IHIKGIEHVTKQQIRNAKEQNKIIKLIASAyKDNEGNVNLNVEPYKIEKNHPLANVNGTEKGITFFTDTMGQVTTIGGAS 320
|
330
....*....|....*....
gi 446581749 302 GSLPTATAVVSDLVAVMQN 320
Cdd:PRK06813 321 NPRGAAAAALKDIINLYRK 339
|
|
| PRK06392 |
PRK06392 |
homoserine dehydrogenase; Provisional |
4-241 |
1.41e-28 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 102354 [Multi-domain] Cd Length: 326 Bit Score: 114.58 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 4 IQVGLLGLGTVGSGVVRIITDHQERliHQVGCPVKVTKV-----------------LVQNIEKEREVEVP-STLLTQDAH 65
Cdd:PRK06392 1 IRISIIGLGNVGLNVLRIIKSRNDD--RRNNNGISVVSVsdsklsyynergldigkIISYKEKGRLEEIDyEKIKFDEIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 66 EILDNPNIDVVIEVMGGIDDAKAYIlQALQSGKHVVTANKDLMALHGAELLAVAKDNKADLFYEASVAGGIPILRSIVEG 145
Cdd:PRK06392 79 EIKPDVIVDVTPASKDGIREKNLYI-NAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRYEATVAGGVPLFSLRDYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 146 LSSDLITKVMGIVNGTTNFILTKMSDeGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILATLGFSTNVELGDVKV 225
Cdd:PRK06392 158 TLPSRIKNFRGIVSSTINYVIRQEAN-GRGFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLFGKDYTLRDVTY 236
|
250
....*....|....*.
gi 446581749 226 KGITSIteeDIEYSKS 241
Cdd:PRK06392 237 DGIENI---DRSSMDN 249
|
|
| thrA |
PRK09436 |
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional |
2-325 |
2.65e-23 |
|
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
Pssm-ID: 181856 [Multi-domain] Cd Length: 819 Bit Score: 102.93 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 2 KEIQVGLLGLGTVGSGVVRIITDHQERLiHQVGCPVKV-----TKVLVQNIE-------KER--EVEVPSTL-----LTQ 62
Cdd:PRK09436 464 QVLDVFVIGVGGVGGALLEQIKRQQPWL-KKKNIDLRVcgianSRKMLLDEHgidldnwREElaEAGEPFDLdrlirLVK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 63 DAHeiLDNPnidVVIEVMGGIDDAKAYIlQALQSGKHVVTANK----DLMALHgAELLAVAKDNKADLFYEASVAGGIPI 138
Cdd:PRK09436 543 EYH--LLNP---VIVDCTSSQAVADQYA-DFLAAGFHVVTPNKkantSSYAYY-HQLREAARKSRRKFLYETNVGAGLPV 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 139 LRSIVEGLSS-DLITKVMGIVNGTTNFILTKMsDEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILA-TLGFst 216
Cdd:PRK09436 616 IETLQNLLNAgDELLKFEGILSGSLSFIFGKL-DEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILArEAGY-- 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 217 NVELGDVKVKGI---------------TSITEEDIEYS------KSLGYTIKLIGlaKRDGEKLEVTVEPtlLPNTHPLA 275
Cdd:PRK09436 693 ELELEDIEVESVlpeefdasgsvdefmARLPELDAEFAarvakaRAEGKVLRYVG--QIEDGKCRVGIAE--VDANHPLY 768
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446581749 276 AVQNEYNAVYVYgeavgeTMFY--------GPGAGSLPTATAVVSDLVAVMqNIRLGV 325
Cdd:PRK09436 769 KVKGGENALAFY------TRYYqpiplvlrGYGAGNEVTAAGVFADLLRTL-SWKLGV 819
|
|
| NAD_binding_3 |
pfam03447 |
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
10-129 |
1.68e-20 |
|
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: 86.21 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 10 GLGTVGSGVVRIITDHQERlihqvgCPVKVTKVLVQN-IEKEREVEVPSTLLTQDAHEILDNPNIDVVIEVmGGIDDAKA 88
Cdd:pfam03447 1 GCGAIGSGVLEQLLRQQSE------IPLELVAVADRDlLSKDPLALLPDEPLTLDLDDLIAHPDPDVVVEC-ASSEAVAE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446581749 89 YILQALQSGKHVVTANKDLMAL--HGAELLAVAKDNKADLFYE 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 ... |
350-427 |
6.76e-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: 83.33 E-value: 6.76e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581749 350 FLRLHVKDEIGVFAKITSLFSERGVSFEKIIQMPLEEKGKAEIVIVTHRASLADYDYILHTLQGYEEIDCVKANYRIE 427
Cdd:cd04881 2 YLRLTVKDKPGVLAKITGILAEHGISIESVIQKEADGGETAPVVIVTHETSEAALNAALAEIEALDAVQGVPSVIRVE 79
|
|
| metL |
PRK09466 |
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional |
2-320 |
7.37e-17 |
|
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
Pssm-ID: 236530 [Multi-domain] Cd Length: 810 Bit Score: 83.05 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 2 KEIQVGLLGLGTVGSGVVRIITDHQERLIHQVGCPVKVTKVL----------------VQNIEKEREVEVPST-LLTQda 64
Cdd:PRK09466 457 KRIGLVLFGKGNIGSRWLELFAREQSTLSARTGFEFVLVGVVdsrrsllnydgldasrALAFFDDEAVEWDEEsLFLW-- 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 65 heiLDNPNID--VVIEVMGGIDDAKAYiLQALQSGKHVVTANKdlmaLHGAELLAV---AKDN--KADLF--YEASVAGG 135
Cdd:PRK09466 535 ---LRAHPYDelVVLDVTASEQLALQY-PDFASHGFHVISANK----LAGSSPSNFyrqIKDAfaKTGRHwlYNATVGAG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 136 IPI---LRSIVEglSSDLITKVMGIVNGTTNFiLTKMSDEGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKMTILA-T 211
Cdd:PRK09466 607 LPInhtVRDLRN--SGDSILAISGIFSGTLSW-LFLQFDGSVPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILArE 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 212 LGFstNVELGDVKVKG-----------------ITSITE---EDIEYSKSLGYTIKLIGLAKRDGeKLEVTVEptLLPNT 271
Cdd:PRK09466 684 AGY--EIEPDDVRVESlvpahledgsldqffenGDELDEqmlQRLEAAAEQGKVLRYVARFDANG-KARVGVE--AVRPD 758
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446581749 272 HPLAAVQNEYNaVYVYgeavgETMFY--------GPGAGSLPTATAVVSDLVAVMQN 320
Cdd:PRK09466 759 HPLANLLPCDN-VFAI-----ESRWYrdnplvirGPGAGREVTAGAIQSDLNRLAQL 809
|
|
| PLN02700 |
PLN02700 |
homoserine dehydrogenase family protein |
128-315 |
1.18e-13 |
|
homoserine dehydrogenase family protein
Pssm-ID: 215377 [Multi-domain] Cd Length: 377 Bit Score: 72.11 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 128 YEASVAGGIPILRSIVEGLSS-DLITKVMGIVNGTTNFILTKMSDeGRAYNDVLKEAQQLGFAEADPTSDVEGLDAARKM 206
Cdd:PLN02700 163 HESTVGAGLPVIASLNRILSSgDPVHRIVGSLSGTLGYVMSELED-GKPFSEVVKQAKSLGYTEPDPRDDLGGMDVARKA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 207 TILATL-GFSTNVElgDVKVK--------------------GITSI---TEEDIEYSKSLGYTIKLIglAKRDGEKLEVT 262
Cdd:PLN02700 242 LILARLlGKRINMD--SIKVEslypeemgpdlmstddflhsGLVELdlpIEERVKEASLKGCVLRYV--CVIEGSSCQVG 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446581749 263 VEPtlLPNTHPLAAVQNEYNAVYVYGEAVGET--MFYGPGAGSLPTATAVVSDLV 315
Cdd:PLN02700 318 IRE--LPKDSALGRLRGSDNVVEIYSRCYSEQplVIQGAGAGNDTTAAGVLADIL 370
|
|
| COG4091 |
COG4091 |
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ... |
2-120 |
1.18e-06 |
|
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];
Pssm-ID: 443267 [Multi-domain] Cd Length: 429 Bit Score: 50.53 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 2 KEIQVGLLGLGTVGSGV-----------VRIITD-HQERLIH---QVGCPVKVTKVLVQNIEKEREVEVPSTLLTQDAHE 66
Cdd:COG4091 14 RPIRVGLIGAGQMGRGLlaqirrmpgmeVVAIADrNPERARAalrEAGIPEEDIRVVDTAAEADAAIAAGKTVVTDDAEL 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446581749 67 ILDNPNIDVVIEVMGGIDDAKAYILQALQSGKHVVTANKDLMALHGAELLAVAK 120
Cdd:COG4091 94 LIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRAD 147
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
351-403 |
1.04e-05 |
|
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.
Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 42.66 E-value: 1.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446581749 351 LRLHVKDEIGVFAKITSLFSERGVSFEKIIQMPLEEKGKAEIVIVTHRASLAD 403
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDLE 53
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
351-403 |
1.07e-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: 1.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446581749 351 LRLHVKDEIGVFAKITSLFSERGVSFEKIIQMPLEEKGK-AEIVIVTHRASLAD 403
Cdd:pfam01842 3 LEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGiVFVVIVVDEEDLEE 56
|
|
| ACT_AHAS |
cd04878 |
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid ... |
351-397 |
3.20e-04 |
|
N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS); ACT_AHAS: N-terminal ACT domain of the Escherichia coli IlvH-like regulatory subunit of acetohydroxyacid synthase (AHAS). AHAS catalyses the first common step in the biosynthesis of the three branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. Bacterial AHASs generally consist of regulatory and catalytic subunits. The effector (valine) binding sites are proposed to be located in two symmetrically related positions in the interface between a pair of N-terminal ACT domains with the C-terminal domain of IlvH contacting the catalytic dimer. Plants Arabidopsis and Oryza have tandem IlvH subunits; both the first and second ACT domain sequences are present in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153150 Cd Length: 72 Bit Score: 39.03 E-value: 3.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446581749 351 LRLHVKDEIGVFAKITSLFSERGVSFEKIIQMPLEEKGKAEIVIVTH 397
Cdd:cd04878 3 LSVLVENEPGVLNRISGLFARRGFNIESLTVGPTEDPGISRITIVVE 49
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-123 |
3.88e-04 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 42.22 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581749 1 MKEIQVGLLGLGTVGSGVVRIITDHQErlIHQVGCpVKVTKVLVQNIEKEREVEVpstllTQDAHEILDNPNIDVVIevm 80
Cdd:COG0673 1 MDKLRVGIIGAGGIGRAHAPALAALPG--VELVAV-ADRDPERAEAFAEEYGVRV-----YTDYEELLADPDIDAVV--- 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446581749 81 ggI---DDA-KAYILQALQSGKHV-----VTANKDlmalHGAELLAVAKDNK 123
Cdd:COG0673 70 --IatpNHLhAELAIAALEAGKHVlcekpLALTLE----EARELVAAAEEAG 115
|
|
| |
