|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
5-425 |
0e+00 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 621.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 5 INVGVLGLGTVGSGVVHILKEHYKKIALDTGYEVKVKTVVVRDLEKERDVCIDGIAVTSHADEVLNDSNIDIVVEVMGGI 84
Cdd:PRK06349 4 LKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELMGGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 85 EEAKQHIVKALRNKKHVVTANKDLMAVYGAELLQLANVNDCDLCYEASVAGGIPVLRGLTDGLASDQIEKIMGIVNGTTN 164
Cdd:PRK06349 84 EPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNGTTN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 165 YMLTKMSQNGWSYEEALQEAQKLGFAESDPTADVDGLDAARKVAILANLGFSMNVSLDDVQVRGIRKVAKEDLQMAEKLG 244
Cdd:PRK06349 164 YILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAKELG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 245 FTMKLIGKAEKQGAAIHLSVEPTLLPSRHPLSNVNNEFNAVYVHGQAVGEVMFYGPGAGKLPTGSAVVSDIISIVKNMNQ 324
Cdd:PRK06349 244 YRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARNLVR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 325 VPKNKSALKEPVPYELQGDEEVVSKYFLRISLQDEPGMLQKVTECFVNYSVSLKEVIQLPLNRELAEVVVVTHQTSKYQF 404
Cdd:PRK06349 324 VPHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSEAAL 403
|
410 420
....*....|....*....|...
gi 446474188 405 EKVLGAIEA--VASEINSYYIIE 425
Cdd:PRK06349 404 RAALAAIEAldVVLGIPSVIRVE 426
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
24-323 |
1.27e-157 |
|
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: 446.80 E-value: 1.27e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 24 KEHYKKIALDTGYEVKVKTVVVRDLEKERDVCIDGIAVTSHADEVLNDSNIDIVVEVMGGIEEAKQHIVKALRNKKHVVT 103
Cdd:COG0460 1 LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 104 ANKDLMAVYGAELLQLANVNDCDLCYEASVAGGIPVLRGLTDGLASDQIEKIMGIVNGTTNYMLTKMSQNGWSYEEALQE 183
Cdd:COG0460 81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 184 AQKLGFAESDPTADVDGLDAARKVAILANLGFSMNVSLDDVQVRGIRKVAKEDLQMAEKLGFTMKLIGKAEKQGAAIHLS 263
Cdd:COG0460 161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 264 VEPTLLPSRHPLSNVNNEFNAVYVHGQAVGEVMFYGPGAGKLPTGSAVVSDIISIVKNMN 323
Cdd:COG0460 241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLR 300
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
138-315 |
9.04e-95 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 282.34 E-value: 9.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 138 PVLRGLTDGLASDQIEKIMGIVNGTTNYMLTKMSQNGWSYEEALQEAQKLGFAESDPTADVDGLDAARKVAILANLGFSM 217
Cdd:pfam00742 1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 218 NVSLDDVQVRGIRKVAKEDLQMAEKLGFTMKLIGKAEKQGAAIHLSVEPTLLPSRHPLSNVNNEFNAVYVHGQAVGEVMF 297
Cdd:pfam00742 81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160
|
170
....*....|....*...
gi 446474188 298 YGPGAGKLPTGSAVVSDI 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 ... |
350-425 |
5.76e-18 |
|
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: 77.94 E-value: 5.76e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446474188 350 YFLRISLQDEPGMLQKVTECFVNYSVSLKEVIQLPLN-RELAEVVVVTHQTSKYQFEKVLGAIEAVAS--EINSYYIIE 425
Cdd:cd04881 1 YYLRLTVKDKPGVLAKITGILAEHGISIESVIQKEADgGETAPVVIVTHETSEAALNAALAEIEALDAvqGVPSVIRVE 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
5-425 |
0e+00 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 621.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 5 INVGVLGLGTVGSGVVHILKEHYKKIALDTGYEVKVKTVVVRDLEKERDVCIDGIAVTSHADEVLNDSNIDIVVEVMGGI 84
Cdd:PRK06349 4 LKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELMGGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 85 EEAKQHIVKALRNKKHVVTANKDLMAVYGAELLQLANVNDCDLCYEASVAGGIPVLRGLTDGLASDQIEKIMGIVNGTTN 164
Cdd:PRK06349 84 EPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNGTTN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 165 YMLTKMSQNGWSYEEALQEAQKLGFAESDPTADVDGLDAARKVAILANLGFSMNVSLDDVQVRGIRKVAKEDLQMAEKLG 244
Cdd:PRK06349 164 YILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAKELG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 245 FTMKLIGKAEKQGAAIHLSVEPTLLPSRHPLSNVNNEFNAVYVHGQAVGEVMFYGPGAGKLPTGSAVVSDIISIVKNMNQ 324
Cdd:PRK06349 244 YRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARNLVR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 325 VPKNKSALKEPVPYELQGDEEVVSKYFLRISLQDEPGMLQKVTECFVNYSVSLKEVIQLPLNRELAEVVVVTHQTSKYQF 404
Cdd:PRK06349 324 VPHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQKGAGGEGAEIVIVTHETSEAAL 403
|
410 420
....*....|....*....|...
gi 446474188 405 EKVLGAIEA--VASEINSYYIIE 425
Cdd:PRK06349 404 RAALAAIEAldVVLGIPSVIRVE 426
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
24-323 |
1.27e-157 |
|
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: 446.80 E-value: 1.27e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 24 KEHYKKIALDTGYEVKVKTVVVRDLEKERDVCIDGIAVTSHADEVLNDSNIDIVVEVMGGIEEAKQHIVKALRNKKHVVT 103
Cdd:COG0460 1 LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 104 ANKDLMAVYGAELLQLANVNDCDLCYEASVAGGIPVLRGLTDGLASDQIEKIMGIVNGTTNYMLTKMSQNGWSYEEALQE 183
Cdd:COG0460 81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 184 AQKLGFAESDPTADVDGLDAARKVAILANLGFSMNVSLDDVQVRGIRKVAKEDLQMAEKLGFTMKLIGKAEKQGAAIHLS 263
Cdd:COG0460 161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 264 VEPTLLPSRHPLSNVNNEFNAVYVHGQAVGEVMFYGPGAGKLPTGSAVVSDIISIVKNMN 323
Cdd:COG0460 241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLR 300
|
|
| PRK06270 |
PRK06270 |
homoserine dehydrogenase; Provisional |
3-324 |
5.05e-97 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 294.08 E-value: 5.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 3 NVINVGVLGLGTVGSGVVHILKEHYKKIALDTGYEVKVKTVVVR----------DLE-----KERDVCID---GIAVTSH 64
Cdd:PRK06270 1 MEMKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIADSsgsaidpdglDLElalkvKEETGKLAdypEGGGEIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 65 ADEVLNDSNIDIVVEVM-----GGiEEAKQHIVKALRNKKHVVTANKDLMAVYGAELLQLANVNDCDLCYEASVAGGIPV 139
Cdd:PRK06270 81 GLEVIRSVDADVVVEATptnieTG-EPALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAMPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 140 LRGLTDGLASDQIEKIMGIVNGTTNYMLTKMSQNGWSYEEALQEAQKLGFAESDPTADVDGLDAARKVAILANLGFSMNV 219
Cdd:PRK06270 160 INLAKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 220 SLDDVQVRGIRKVAKEDLQMAEKLGFTMKLIGKAEKQGaaiHLSVEPTLLPSRHPLsNVNNEFNAVYVHGQAVGEVMFYG 299
Cdd:PRK06270 240 TIKDVEVEGITKITPEAIELAAKEGYRIKLIGEVSREK---DLSVSPRLVPLDHPL-AVSGTLNAATFETDLAGDVTVVG 315
|
330 340
....*....|....*....|....*
gi 446474188 300 PGAGKLPTGSAVVSDIISIVKNMNQ 324
Cdd:PRK06270 316 RGAGSIETASAILSDLIAIHDRYGK 340
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
138-315 |
9.04e-95 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 282.34 E-value: 9.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 138 PVLRGLTDGLASDQIEKIMGIVNGTTNYMLTKMSQNGWSYEEALQEAQKLGFAESDPTADVDGLDAARKVAILANLGFSM 217
Cdd:pfam00742 1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 218 NVSLDDVQVRGIRKVAKEDLQMAEKLGFTMKLIGKAEKQGAAIHLSVEPTLLPSRHPLSNVNNEFNAVYVHGQAVGEVMF 297
Cdd:pfam00742 81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160
|
170
....*....|....*...
gi 446474188 298 YGPGAGKLPTGSAVVSDI 315
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
|
|
| PRK08374 |
PRK08374 |
homoserine dehydrogenase; Provisional |
5-316 |
8.75e-50 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 169409 [Multi-domain] Cd Length: 336 Bit Score: 171.91 E-value: 8.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 5 INVGVLGLGTVGSGVVHILKEhyKKIALDTGYEVKVKTVVVRD------LEKERDVcIDGIAVTSH-------------- 64
Cdd:PRK08374 3 VKVSIFGFGNVGRAVAEVLAE--KSRVFKERYGVELKVVSITDtsgtiwLPEDIDL-REAKEVKENfgklsnwgndyevy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 65 ---ADEVLNDSNIDIVVEVMGGIEEAKQHIVkALRNKKHVVTANKDLMAVYGAELLQLANVNDCDLCYEASVAGGIPVLR 141
Cdd:PRK08374 80 nfsPEEIVEEIDADIVVDVTNDKNAHEWHLE-ALKEGKSVVTSNKPPIAFHYDELLDLANERNLPYLFEATVMAGTPIIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 142 GLTDGLASDQIEKIMGIVNGTTNYMLTKMSQnGWSYEEALQEAQKLGFAESDPTADVDGLDAARKVAILANLGFSmNVSL 221
Cdd:PRK08374 159 LLRENLLGDTVKRIEAVVNATTTFILTRMEQ-GKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAFP-PITF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 222 DDVQVRGIRKVAKEDLQMAEKLGFTMKLIGKAEKQgaaiHLSVEPTLLPSRHPLSNVNNEfNAVYVHGQAVGEVMFYGPG 301
Cdd:PRK08374 237 EEVGIRGIKDVTEGEIERAKAKGRNVRLVATVEEG----RISVKPKKLPENSPLAVEGVE-NAAVIKTDLLGELVLKGPG 311
|
330
....*....|....*
gi 446474188 302 AGKLPTGSAVVSDII 316
Cdd:PRK08374 312 AGGKETASGVVTDII 326
|
|
| PRK06813 |
PRK06813 |
homoserine dehydrogenase; Validated |
5-321 |
2.80e-41 |
|
homoserine dehydrogenase; Validated
Pssm-ID: 168683 [Multi-domain] Cd Length: 346 Bit Score: 149.63 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 5 INVGVLGLGTVGSGVVHILKEHYKKIALDTGYEVKVKTVVVRDLEKERD---------VCIDGIA-----VTSHADEVLN 70
Cdd:PRK06813 3 IKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNVAIHNEdglsihhllRYGGGSCaiekyIEHHPEERAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 71 DS-NIDIVVE-----VMGGiEEAKQHIVKALRNKKHVVTANKDLMAVYGAELLQLANVNDCDLCYEASVAGGIPVLRGLT 144
Cdd:PRK06813 83 DNiSGTVLVEstvtnLKDG-NPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIANVRIRYSGATAAALPTLDIGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 145 DGLASDQIEKIMGIVNGTTNYMLTKMSQNGWSYEEALQEAQKLGFAESDPTADVDGLDAARKVAILANLGFSMNVSLDDV 224
Cdd:PRK06813 162 FSLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLTNSLMGTENKLTDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 225 QVRGIRKVAKEDLQMAEKLGFTMKLIGKAEK-QGAAIHLSVEPTLLPSRHPLSNVNNEFNAVYVHGQAVGEVMFYGPGAG 303
Cdd:PRK06813 242 HIKGIEHVTKQQIRNAKEQNKIIKLIASAYKdNEGNVNLNVEPYKIEKNHPLANVNGTEKGITFFTDTMGQVTTIGGASN 321
|
330
....*....|....*...
gi 446474188 304 KLPTGSAVVSDIISIVKN 321
Cdd:PRK06813 322 PRGAAAAALKDIINLYRK 339
|
|
| PRK06392 |
PRK06392 |
homoserine dehydrogenase; Provisional |
5-229 |
2.23e-27 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 102354 [Multi-domain] Cd Length: 326 Bit Score: 111.12 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 5 INVGVLGLGTVGSGVVHILKEHYKKIALDTGYEVKVKTVVVRDLEKERDV------------CIDGIAVTSHADEVLNDS 72
Cdd:PRK06392 1 IRISIIGLGNVGLNVLRIIKSRNDDRRNNNGISVVSVSDSKLSYYNERGLdigkiisykekgRLEEIDYEKIKFDEIFEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 73 NIDIVVEVM----GGIEEAKQHIvKALRNKKHVVTANKDLMAVYGAELLQLANVNDCDLCYEASVAGGIPVLRGLTDGLA 148
Cdd:PRK06392 81 KPDVIVDVTpaskDGIREKNLYI-NAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRYEATVAGGVPLFSLRDYSTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 149 SDQIEKIMGIVNGTTNYMLTKMSqNGWSYEEALQEAQKLGFAESDPTADVDGLDAARKVAILANLGFSMNVSLDDVQVRG 228
Cdd:PRK06392 160 PSRIKNFRGIVSSTINYVIRQEA-NGRGFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLFGKDYTLRDVTYDG 238
|
.
gi 446474188 229 I 229
Cdd:PRK06392 239 I 239
|
|
| thrA |
PRK09436 |
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional |
4-318 |
8.98e-23 |
|
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
Pssm-ID: 181856 [Multi-domain] Cd Length: 819 Bit Score: 101.00 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 4 VINVGVLGLGTVGSGVVHILKEHYKKIAldtgyevkvktvvvrdlEKERDVCIDGIAVTSHAdeVLNDSNID-------- 75
Cdd:PRK09436 465 VLDVFVIGVGGVGGALLEQIKRQQPWLK-----------------KKNIDLRVCGIANSRKM--LLDEHGIDldnwreel 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 76 ------------------------IVVEVMGGIEEAKQHiVKALRNKKHVVTANK----DLMAVYgAELLQLANVNDCDL 127
Cdd:PRK09436 526 aeagepfdldrlirlvkeyhllnpVIVDCTSSQAVADQY-ADFLAAGFHVVTPNKkantSSYAYY-HQLREAARKSRRKF 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 128 CYEASVAGGIPVLRGLTDGLAS-DQIEKIMGIVNGTTNYMLTKMSQNGwSYEEALQEAQKLGFAESDPTADVDGLDAARK 206
Cdd:PRK09436 604 LYETNVGAGLPVIETLQNLLNAgDELLKFEGILSGSLSFIFGKLDEGM-SFSEATRLAKEKGYTEPDPRDDLSGMDVARK 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 207 VAILA-NLGfsMNVSLDDVQVRGI---------------RKVAKED------LQMAEKLGFTMKLIGKAEKQGAaihlSV 264
Cdd:PRK09436 683 LLILArEAG--YELELEDIEVESVlpeefdasgsvdefmARLPELDaefaarVAKARAEGKVLRYVGQIEDGKC----RV 756
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446474188 265 EPTLLPSRHPLSNVNNEFNAvyvhgqavgeVMFY------------GPGAGKLPTGSAVVSDIISI 318
Cdd:PRK09436 757 GIAEVDANHPLYKVKGGENA----------LAFYtryyqpiplvlrGYGAGNEVTAAGVFADLLRT 812
|
|
| NAD_binding_3 |
pfam03447 |
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
11-130 |
1.46e-18 |
|
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: 80.81 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 11 GLGTVGSGVVHILKEHYKKIaldtgyEVKVKTVVVRDLE-KERDVCIDGIAVTSHADEVLNDSNIDIVVEVmGGIEEAKQ 89
Cdd:pfam03447 1 GCGAIGSGVLEQLLRQQSEI------PLELVAVADRDLLsKDPLALLPDEPLTLDLDDLIAHPDPDVVVEC-ASSEAVAE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446474188 90 HIVKALRNKKHVVTANKDLMA--VYGAELLQLANVNDCDLCYE 130
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 ... |
350-425 |
5.76e-18 |
|
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: 77.94 E-value: 5.76e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446474188 350 YFLRISLQDEPGMLQKVTECFVNYSVSLKEVIQLPLN-RELAEVVVVTHQTSKYQFEKVLGAIEAVAS--EINSYYIIE 425
Cdd:cd04881 1 YYLRLTVKDKPGVLAKITGILAEHGISIESVIQKEADgGETAPVVIVTHETSEAALNAALAEIEALDAvqGVPSVIRVE 79
|
|
| PLN02700 |
PLN02700 |
homoserine dehydrogenase family protein |
129-318 |
1.17e-14 |
|
homoserine dehydrogenase family protein
Pssm-ID: 215377 [Multi-domain] Cd Length: 377 Bit Score: 75.19 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 129 YEASVAGGIPVLRGLTDGLAS-DQIEKIMGIVNGTTNYMLTKMsQNGWSYEEALQEAQKLGFAESDPTADVDGLDAARKV 207
Cdd:PLN02700 163 HESTVGAGLPVIASLNRILSSgDPVHRIVGSLSGTLGYVMSEL-EDGKPFSEVVKQAKSLGYTEPDPRDDLGGMDVARKA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 208 AILANL-GFSMNvsLDDVQVRGI-----------------RKVAKEDLQMAEKL------GFTMKLIGKAEKQGAAIHLs 263
Cdd:PLN02700 242 LILARLlGKRIN--MDSIKVESLypeemgpdlmstddflhSGLVELDLPIEERVkeaslkGCVLRYVCVIEGSSCQVGI- 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446474188 264 VEptlLPSRHPLSNVNNEFNAVYVHGQAVGE--VMFYGPGAGKLPTGSAVVSDIISI 318
Cdd:PLN02700 319 RE---LPKDSALGRLRGSDNVVEIYSRCYSEqpLVIQGAGAGNDTTAAGVLADILDL 372
|
|
| metL |
PRK09466 |
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional |
100-322 |
2.69e-12 |
|
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
Pssm-ID: 236530 [Multi-domain] Cd Length: 810 Bit Score: 68.80 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 100 HVVTANK-----DLmAVYGAELLQLANVNDCDLcYEASVAGGIPVLRGLTDGLAS-DQIEKIMGIVNGTtnymltkMSqn 173
Cdd:PRK09466 567 HVISANKlagssPS-NFYRQIKDAFAKTGRHWL-YNATVGAGLPINHTVRDLRNSgDSILAISGIFSGT-------LS-- 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 174 gWSYE---------EALQEAQKLGFAESDPTADVDGLDAARKVAILA-NLGFsmNVSLDDVQVRGIRKVAKEDL------ 237
Cdd:PRK09466 636 -WLFLqfdgsvpfsELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILArEAGY--EIEPDDVRVESLVPAHLEDGsldqff 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 238 --------QMAEKL------GFTMKLIGKAEKQGAAiHLSVEptLLPSRHPLSNV---NNEFnavyvhgqaVGEVMFY-- 298
Cdd:PRK09466 713 engdeldeQMLQRLeaaaeqGKVLRYVARFDANGKA-RVGVE--AVRPDHPLANLlpcDNVF---------AIESRWYrd 780
|
250 260 270
....*....|....*....|....*....|
gi 446474188 299 ------GPGAGKLPTGSAVVSDIISIVKNM 322
Cdd:PRK09466 781 nplvirGPGAGREVTAGAIQSDLNRLAQLL 810
|
|
| COG4091 |
COG4091 |
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ... |
2-121 |
2.00e-09 |
|
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];
Pssm-ID: 443267 [Multi-domain] Cd Length: 429 Bit Score: 59.01 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 2 HNVINVGVLGLGTVGSGVVHilkehykKIALDTGYEVKVktVVVRDLEKERDVCID------------------------ 57
Cdd:COG4091 13 GRPIRVGLIGAGQMGRGLLA-------QIRRMPGMEVVA--IADRNPERARAALREagipeedirvvdtaaeadaaiaag 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446474188 58 GIAVTSHADEVLNDSNIDIVVEVMGGIEEAKQHIVKALRNKKHVVTANKDLMAVYGAELLQLAN 121
Cdd:COG4091 84 KTVVTDDAELLIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRAD 147
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
5-101 |
3.49e-04 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 42.22 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 5 INVGVLGLGTVGSGVVHILKEHykkialdtgYEVKVKTVVVRDLEKERDVC-IDGIAVTSHADEVLNDSNIDIVVevmgg 83
Cdd:COG0673 4 LRVGIIGAGGIGRAHAPALAAL---------PGVELVAVADRDPERAEAFAeEYGVRVYTDYEELLADPDIDAVV----- 69
|
90 100
....*....|....*....|....
gi 446474188 84 IeeA------KQHIVKALRNKKHV 101
Cdd:COG0673 70 I--AtpnhlhAELAIAALEAGKHV 91
|
|
| nat-AmDH_N_like |
cd24146 |
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ... |
5-103 |
1.13e-03 |
|
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 39.45 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 5 INVGVLGLGTVGSGVVHILKEHYkkialdtgyEVKVKTVVVRDLEK-ERDV------CIDGIAVTSHADEVLNDSNIDIV 77
Cdd:cd24146 1 IRVVVWGLGAMGRGIARYLLEKP---------GLEIVGAVDRDPAKvGKDLgelgggAPLGVKVTDDLDAVLAATKPDVV 71
|
90 100 110
....*....|....*....|....*....|
gi 446474188 78 V----EVMGGIEEAkqhIVKALRNKKHVVT 103
Cdd:cd24146 72 VhattSFLADVAPQ---IERLLEAGLNVIT 98
|
|
| GFO_IDH_MocA |
pfam01408 |
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ... |
5-102 |
2.73e-03 |
|
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Pssm-ID: 426248 [Multi-domain] Cd Length: 120 Bit Score: 37.57 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446474188 5 INVGVLGLGTVGS---GVVHILKEHYKKIAldtgyevkvktVVVRDLEKERDVCID-GIAVTSHADEVLNDSNIDIVVeV 80
Cdd:pfam01408 1 IRVGIIGAGKIGSkhaRALNASQPGAELVA-----------ILDPNSERAEAVAESfGVEVYSDLEELLNDPEIDAVI-V 68
|
90 100
....*....|....*....|..
gi 446474188 81 MGGIEEAKQHIVKALRNKKHVV 102
Cdd:pfam01408 69 ATPNGLHYDLAIAALEAGKHVL 90
|
|
| |
