|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
7-435 |
0e+00 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 577.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 7 PIRVGLLGAGTVGSQTARILVEQKDELGQRIGRPLEISGIACLDPNEVDFPWIDKSLLTSDTMSVVKNA--DIVVELIGG 84
Cdd:PRK06349 3 PLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPdiDIVVELMGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 85 TGVARTFVLEALNNGASVVTANKALLAKYGPELYKAAEDNHADIYFEAAVGGAIPIVRPLRESLVGDQVKSMLGIVNGTT 164
Cdd:PRK06349 83 IEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 165 NYILDEMTTKGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATLGFHTNVGIDDVTVEGITHITADDIAAATAE 244
Cdd:PRK06349 163 NYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAKEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 245 GKVVKLLAVVDHTEDGVSARVYPALIRNEHPLASVHGSFNAVFLHAEYADDLMFYGRGAGGAPTASAVVGDIVTVARHIA 324
Cdd:PRK06349 243 GYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARNLV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 325 SG-CTGPAIRMYNDYPIAPLSSAKASFAVRFLIHDKPGVLLQVAKEFADRGISINGVNQDlkptatepGYDGEIQQLRLV 403
Cdd:PRK06349 323 RVpHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQK--------GAGGEGAEIVIV 394
|
410 420 430
....*....|....*....|....*....|..
gi 490329778 404 THMTDETTLREAVDAVCQLDSVTGDPSIIRVL 435
Cdd:PRK06349 395 THETSEAALRAALAAIEALDVVLGIPSVIRVE 426
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
28-326 |
3.48e-144 |
|
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: 412.90 E-value: 3.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 28 EQKDELGQRIGRPLEISGIACLDPNEVDFPWIDKSLLTSDTMSVVK--NADIVVELIGGTGVARTFVLEALNNGASVVTA 105
Cdd:COG0460 2 ENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKdpEIDVVVELTGGSEPARELYLAALEAGKHVVTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 106 NKALLAKYGPELYKAAEDNHADIYFEAAVGGAIPIVRPLRESLVGDQVKSMLGIVNGTTNYILDEMTTKGLDFDVALKEA 185
Cdd:COG0460 82 NKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 186 QEKGYAEADPTGDIEGYDAANKAAIMATLGFHTNVGIDDVTVEGITHITADDIAAATAEGKVVKLLAVVDHTEDGVSARV 265
Cdd:COG0460 162 QELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEARV 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490329778 266 YPALIRNEHPLASVHGSFNAVFLHAEYADDLMFYGRGAGGAPTASAVVGDIVTVARHIASG 326
Cdd:COG0460 242 HPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLRAG 302
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
139-316 |
9.25e-84 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 254.60 E-value: 9.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 139 PIVRPLRESLVGDQVKSMLGIVNGTTNYILDEMTTKGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATLGFHT 218
Cdd:pfam00742 1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 219 NVGIDDVTVEGITHITADDIAAATAEGKVVKLLAVVDHTEDGVSARVYPALIRNEHPLASVHGSFNAVFLHAEYADDLMF 298
Cdd:pfam00742 81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160
|
170
....*....|....*...
gi 490329778 299 YGRGAGGAPTASAVVGDI 316
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 ... |
350-435 |
1.99e-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: 79.48 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 350 FAVRFLIHDKPGVLLQVAKEFADRGISINGVNQdlkptatEPGYDGEIQQLRLVTHMTDETTLREAVDAVCQLDSVTGDP 429
Cdd:cd04881 1 YYLRLTVKDKPGVLAKITGILAEHGISIESVIQ-------KEADGGETAPVVIVTHETSEAALNAALAEIEALDAVQGVP 73
|
....*.
gi 490329778 430 SIIRVL 435
Cdd:cd04881 74 SVIRVE 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
7-435 |
0e+00 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 577.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 7 PIRVGLLGAGTVGSQTARILVEQKDELGQRIGRPLEISGIACLDPNEVDFPWIDKSLLTSDTMSVVKNA--DIVVELIGG 84
Cdd:PRK06349 3 PLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPdiDIVVELMGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 85 TGVARTFVLEALNNGASVVTANKALLAKYGPELYKAAEDNHADIYFEAAVGGAIPIVRPLRESLVGDQVKSMLGIVNGTT 164
Cdd:PRK06349 83 IEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 165 NYILDEMTTKGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATLGFHTNVGIDDVTVEGITHITADDIAAATAE 244
Cdd:PRK06349 163 NYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAKEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 245 GKVVKLLAVVDHTEDGVSARVYPALIRNEHPLASVHGSFNAVFLHAEYADDLMFYGRGAGGAPTASAVVGDIVTVARHIA 324
Cdd:PRK06349 243 GYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARNLV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 325 SG-CTGPAIRMYNDYPIAPLSSAKASFAVRFLIHDKPGVLLQVAKEFADRGISINGVNQDlkptatepGYDGEIQQLRLV 403
Cdd:PRK06349 323 RVpHLGFQPSALADLPIAPMEEIESKYYLRLLVADKPGVLAKIAAIFAENGISIESILQK--------GAGGEGAEIVIV 394
|
410 420 430
....*....|....*....|....*....|..
gi 490329778 404 THMTDETTLREAVDAVCQLDSVTGDPSIIRVL 435
Cdd:PRK06349 395 THETSEAALRAALAAIEALDVVLGIPSVIRVE 426
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
28-326 |
3.48e-144 |
|
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: 412.90 E-value: 3.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 28 EQKDELGQRIGRPLEISGIACLDPNEVDFPWIDKSLLTSDTMSVVK--NADIVVELIGGTGVARTFVLEALNNGASVVTA 105
Cdd:COG0460 2 ENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKdpEIDVVVELTGGSEPARELYLAALEAGKHVVTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 106 NKALLAKYGPELYKAAEDNHADIYFEAAVGGAIPIVRPLRESLVGDQVKSMLGIVNGTTNYILDEMTTKGLDFDVALKEA 185
Cdd:COG0460 82 NKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 186 QEKGYAEADPTGDIEGYDAANKAAIMATLGFHTNVGIDDVTVEGITHITADDIAAATAEGKVVKLLAVVDHTEDGVSARV 265
Cdd:COG0460 162 QELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEARV 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490329778 266 YPALIRNEHPLASVHGSFNAVFLHAEYADDLMFYGRGAGGAPTASAVVGDIVTVARHIASG 326
Cdd:COG0460 242 HPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIARGLRAG 302
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
139-316 |
9.25e-84 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 254.60 E-value: 9.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 139 PIVRPLRESLVGDQVKSMLGIVNGTTNYILDEMTTKGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATLGFHT 218
Cdd:pfam00742 1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 219 NVGIDDVTVEGITHITADDIAAATAEGKVVKLLAVVDHTEDGVSARVYPALIRNEHPLASVHGSFNAVFLHAEYADDLMF 298
Cdd:pfam00742 81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160
|
170
....*....|....*...
gi 490329778 299 YGRGAGGAPTASAVVGDI 316
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
|
|
| PRK06270 |
PRK06270 |
homoserine dehydrogenase; Provisional |
8-326 |
1.54e-78 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 247.08 E-value: 1.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 8 IRVGLLGAGTVGSQTARILVEQKDELGQRIGRPLEISGIA-----CLDPNEVDFPWIDKSLLTS-------------DTM 69
Cdd:PRK06270 3 MKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIAdssgsAIDPDGLDLELALKVKEETgkladypegggeiSGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 70 SVVKN--ADIVVEL----IGGTGVARTFVLEALNNGASVVTANKALLAKYGPELYKAAEDNHADIYFEAAVGGAIPIVRP 143
Cdd:PRK06270 83 EVIRSvdADVVVEAtptnIETGEPALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAMPIINL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 144 LRESLVGDQVKSMLGIVNGTTNYILDEMTTKGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATLGFHTNVGID 223
Cdd:PRK06270 163 AKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGADLTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 224 DVTVEGITHITADDIAAATAEGKVVKLLAVVDHTEDgvsARVYPALIRNEHPLAsVHGSFNAVFLHAEYADDLMFYGRGA 303
Cdd:PRK06270 243 DVEVEGITKITPEAIELAAKEGYRIKLIGEVSREKD---LSVSPRLVPLDHPLA-VSGTLNAATFETDLAGDVTVVGRGA 318
|
330 340
....*....|....*....|...
gi 490329778 304 GGAPTASAVVGDIVTVARHIASG 326
Cdd:PRK06270 319 GSIETASAILSDLIAIHDRYGKA 341
|
|
| PRK08374 |
PRK08374 |
homoserine dehydrogenase; Provisional |
8-326 |
2.23e-50 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 169409 [Multi-domain] Cd Length: 336 Bit Score: 173.45 E-value: 2.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 8 IRVGLLGAGTVGSQTARILVEQKDELGQRIGRPLEISGIA-----CLDPNEVDF--------------PW-IDKSLLTSD 67
Cdd:PRK08374 3 VKVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELKVVSITdtsgtIWLPEDIDLreakevkenfgklsNWgNDYEVYNFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 68 TMSVVK--NADIVVELIGGTGvARTFVLEALNNGASVVTANKALLAKYGPELYKAAEDNHADIYFEAAVGGAIPIVRPLR 145
Cdd:PRK08374 83 PEEIVEeiDADIVVDVTNDKN-AHEWHLEALKEGKSVVTSNKPPIAFHYDELLDLANERNLPYLFEATVMAGTPIIGLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 146 ESLVGDQVKSMLGIVNGTTNYILDEMTTkGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATLGFHTnVGIDDV 225
Cdd:PRK08374 162 ENLLGDTVKRIEAVVNATTTFILTRMEQ-GKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAFPP-ITFEEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 226 TVEGITHITADDIAAATAEGKVVKLLAVVdhtEDGvSARVYPALIRNEHPLAsVHGSFNAVFLHAEYADDLMFYGRGAGG 305
Cdd:PRK08374 240 GIRGIKDVTEGEIERAKAKGRNVRLVATV---EEG-RISVKPKKLPENSPLA-VEGVENAAVIKTDLLGELVLKGPGAGG 314
|
330 340
....*....|....*....|.
gi 490329778 306 APTASAVVGDIVTVARHIASG 326
Cdd:PRK08374 315 KETASGVVTDIIKAALKFPKY 335
|
|
| PRK06813 |
PRK06813 |
homoserine dehydrogenase; Validated |
8-321 |
2.52e-33 |
|
homoserine dehydrogenase; Validated
Pssm-ID: 168683 [Multi-domain] Cd Length: 346 Bit Score: 128.06 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 8 IRVGLLGAGTVGSQTARILVEQKDELGQRIGRPLEISGI-------------------ACLDPNEVDFPWIDKSLLTSDT 68
Cdd:PRK06813 3 IKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVlgrnvaihnedglsihhllRYGGGSCAIEKYIEHHPEERAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 69 MSVvkNADIVVEL----IGGTGVARTFVLEALNNGASVVTANKALLAKYGPELYKAAEDNHADIYFEAAVGGAIPIVRPL 144
Cdd:PRK06813 83 DNI--SGTVLVEStvtnLKDGNPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIANVRIRYSGATAAALPTLDIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 145 RESLVGDQVKSMLGIVNGTTNYILDEMTTKGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATLGFHTNVGIDD 224
Cdd:PRK06813 161 QFSLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLTNSLMGTENKLTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 225 VTVEGITHITADDIAAATAEGKVVKLLAVVDHTEDG-VSARVYPALIRNEHPLASVHGSFNAVFLHAEYADDLMFYGRGA 303
Cdd:PRK06813 241 IHIKGIEHVTKQQIRNAKEQNKIIKLIASAYKDNEGnVNLNVEPYKIEKNHPLANVNGTEKGITFFTDTMGQVTTIGGAS 320
|
330
....*....|....*...
gi 490329778 304 GGAPTASAVVGDIVTVAR 321
Cdd:PRK06813 321 NPRGAAAAALKDIINLYR 338
|
|
| PRK06392 |
PRK06392 |
homoserine dehydrogenase; Provisional |
8-321 |
1.39e-26 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 102354 [Multi-domain] Cd Length: 326 Bit Score: 109.19 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 8 IRVGLLGAGTVGSQTARILVEQKDElgQRIGRPLEISGIA----------CLDPNEVdFPWIDKSLLTSDTMSVVK---- 73
Cdd:PRK06392 1 IRISIIGLGNVGLNVLRIIKSRNDD--RRNNNGISVVSVSdsklsyynerGLDIGKI-ISYKEKGRLEEIDYEKIKfdei 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 74 ---NADIVVELIGGT--GV-ARTFVLEALNNGASVVTANKALLAKYGPELYKAAEDNHADIYFEAAVGGAIPIVRPLRES 147
Cdd:PRK06392 78 feiKPDVIVDVTPASkdGIrEKNLYINAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRYEATVAGGVPLFSLRDYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 148 LVGDQVKSMLGIVNGTTNYILDEMTTkGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATLGFHTNVGIDDVTV 227
Cdd:PRK06392 158 TLPSRIKNFRGIVSSTINYVIRQEAN-GRGFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLFGKDYTLRDVTY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 228 EGIthitADDIAAATAEGKVVKLLAVVDHTEDGVSARVypALIRNEHPLASVHGSFnAVFLHAEYADDLMFYGRGAGGAP 307
Cdd:PRK06392 237 DGI----ENIDRSSMDNERLVTEVAMINGGPHAESRIR--SLSRNDFLGMIGPLSL-GYQMETDINGTINVSDNYDGPYE 309
|
330
....*....|....
gi 490329778 308 TASAVVGDIVTVAR 321
Cdd:PRK06392 310 TAGAVVNDVMLLSK 323
|
|
| thrA |
PRK09436 |
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional |
8-320 |
8.52e-19 |
|
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
Pssm-ID: 181856 [Multi-domain] Cd Length: 819 Bit Score: 89.06 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 8 IRVGLLGAGTVGSQtariLVEQ----KDELGQRiGRPLEISGIA-----CLDPNEVDF-PWidKSLLTSDT--------M 69
Cdd:PRK09436 466 LDVFVIGVGGVGGA----LLEQikrqQPWLKKK-NIDLRVCGIAnsrkmLLDEHGIDLdNW--REELAEAGepfdldrlI 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 70 SVVKNAD----IVVELIGGTGVARTFVlEALNNGASVVTANK----ALLAKYGpELYKAAEDNHADIYFEAAVGGAIPIV 141
Cdd:PRK09436 539 RLVKEYHllnpVIVDCTSSQAVADQYA-DFLAAGFHVVTPNKkantSSYAYYH-QLREAARKSRRKFLYETNVGAGLPVI 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 142 RPLReSLV--GDQVKSMLGIVNGTTNYI---LDEmttkGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMA-TLG 215
Cdd:PRK09436 617 ETLQ-NLLnaGDELLKFEGILSGSLSFIfgkLDE----GMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILArEAG 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 216 FHtnVGIDDVTVEGITHITADDIA---------------------AATAEGKVVKLLAVVdhtEDGVsARVYPALIRNEH 274
Cdd:PRK09436 692 YE--LELEDIEVESVLPEEFDASGsvdefmarlpeldaefaarvaKARAEGKVLRYVGQI---EDGK-CRVGIAEVDANH 765
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490329778 275 PLASVHGSFNAVFLHAEYADD--LMFYGRGAGGAPTASAVVGDIVTVA 320
Cdd:PRK09436 766 PLYKVKGGENALAFYTRYYQPipLVLRGYGAGNEVTAAGVFADLLRTL 813
|
|
| ACT_HSDH-Hom |
cd04881 |
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ... |
350-435 |
1.99e-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: 79.48 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 350 FAVRFLIHDKPGVLLQVAKEFADRGISINGVNQdlkptatEPGYDGEIQQLRLVTHMTDETTLREAVDAVCQLDSVTGDP 429
Cdd:cd04881 1 YYLRLTVKDKPGVLAKITGILAEHGISIESVIQ-------KEADGGETAPVVIVTHETSEAALNAALAEIEALDAVQGVP 73
|
....*.
gi 490329778 430 SIIRVL 435
Cdd:cd04881 74 SVIRVE 79
|
|
| NAD_binding_3 |
pfam03447 |
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
14-131 |
6.78e-15 |
|
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: 70.80 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 14 GAGTVGSQTARILVEQKDElgqrigRPLEISGIA----CLDPNEVDFPwidKSLLTSDTMSVVKN--ADIVVELiGGTGV 87
Cdd:pfam03447 1 GCGAIGSGVLEQLLRQQSE------IPLELVAVAdrdlLSKDPLALLP---DEPLTLDLDDLIAHpdPDVVVEC-ASSEA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490329778 88 ARTFVLEALNNGASVVTANKALLA--KYGPELYKAAEDNHADIYFE 131
Cdd:pfam03447 71 VAELVLDALKAGKDVVTASKGALAdlALYEELREAAEANGARIYVE 116
|
|
| PLN02700 |
PLN02700 |
homoserine dehydrogenase family protein |
94-317 |
8.96e-14 |
|
homoserine dehydrogenase family protein
Pssm-ID: 215377 [Multi-domain] Cd Length: 377 Bit Score: 72.50 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 94 EALNNGASVVTANKA-LLAKYgpELYKAAEDNHADIYFEAAVGGAIPIVRPLRESLV-GDQVKSMLGIVNGTTNYILDEM 171
Cdd:PLN02700 128 EAVDLGCCIVLANKKpLTSTL--EDYDKLAAHPRRIRHESTVGAGLPVIASLNRILSsGDPVHRIVGSLSGTLGYVMSEL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 172 TtKGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMATL-GFHTNvgIDDVTVEGITHITADDIAAATAE------ 244
Cdd:PLN02700 206 E-DGKPFSEVVKQAKSLGYTEPDPRDDLGGMDVARKALILARLlGKRIN--MDSIKVESLYPEEMGPDLMSTDDflhsgl 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 245 -----------------GKVVKLLAVVDHTEDGVSARVYPalirNEHPLASVHGSFNAVFLHAE-YADD-LMFYGRGAGG 305
Cdd:PLN02700 283 veldlpieervkeaslkGCVLRYVCVIEGSSCQVGIRELP----KDSALGRLRGSDNVVEIYSRcYSEQpLVIQGAGAGN 358
|
250
....*....|..
gi 490329778 306 APTASAVVGDIV 317
Cdd:PLN02700 359 DTTAAGVLADIL 370
|
|
| metL |
PRK09466 |
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional |
5-321 |
6.27e-13 |
|
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
Pssm-ID: 236530 [Multi-domain] Cd Length: 810 Bit Score: 70.72 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 5 NAPIRVG--LLGAGTVGSQTARILVEQKDELGQRIGRPLEISGIAC----------LDPNEV--DF-----PWIDKSLLT 65
Cdd:PRK09466 454 RAEKRIGlvLFGKGNIGSRWLELFAREQSTLSARTGFEFVLVGVVDsrrsllnydgLDASRAlaFFddeavEWDEESLFL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 66 SdtMSVVKNADIVV-ELIGGTGVARTFvLEALNNGASVVTANKalLAKYGP-ELYKAAEDNHADI----YFEAAVGGAIP 139
Cdd:PRK09466 534 W--LRAHPYDELVVlDVTASEQLALQY-PDFASHGFHVISANK--LAGSSPsNFYRQIKDAFAKTgrhwLYNATVGAGLP 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 140 I---VRPLRESlvGDQVKSMLGIVNGTTNYiLDEMTTKGLDFDVALKEAQEKGYAEADPTGDIEGYDAANKAAIMA-TLG 215
Cdd:PRK09466 609 InhtVRDLRNS--GDSILAISGIFSGTLSW-LFLQFDGSVPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILArEAG 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329778 216 FHtnVGIDDVTVEG--------------------ITHITADDIAAATAEGKVVKLLAVVDHteDGvSARVYPALIRNEHP 275
Cdd:PRK09466 686 YE--IEPDDVRVESlvpahledgsldqffengdeLDEQMLQRLEAAAEQGKVLRYVARFDA--NG-KARVGVEAVRPDHP 760
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490329778 276 LASVHGSFNaVFL--HAEYADD-LMFYGRGAGGAPTASAVVGDIVTVAR 321
Cdd:PRK09466 761 LANLLPCDN-VFAieSRWYRDNpLVIRGPGAGREVTAGAIQSDLNRLAQ 808
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
352-422 |
1.94e-05 |
|
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: 42.29 E-value: 1.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490329778 352 VRFLIHDKPGVLLQVAKEFADRGISINGVNQdlkptatepGYDGEIQQLRLVTHMTDETTLREAVDAVCQL 422
Cdd:pfam01842 3 LEVLVPDRPGLLARVLGALADRGINITSIEQ---------GTSEDKGGIVFVVIVVDEEDLEEVLEALKKL 64
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
352-382 |
3.86e-03 |
|
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: 35.73 E-value: 3.86e-03
10 20 30
....*....|....*....|....*....|.
gi 490329778 352 VRFLIHDKPGVLLQVAKEFADRGISINGVNQ 382
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQ 31
|
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