|
Name |
Accession |
Description |
Interval |
E-value |
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
7-305 |
7.44e-153 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 431.01 E-value: 7.44e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 7 IGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGvTTLIEPTSGNTGIALAF 86
Cdd:COG0031 3 IYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPG-GTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 87 VAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQTTGPE 166
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 167 IWRQTKGTVDAVVfgvgtggtitgvgRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIYEDVI 246
Cdd:COG0031 162 IWEQTDGKVDAFVagvgtggtitgvgRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLIDEVI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1845980223 247 RIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARpEMAGKLIVTCLPSCGERYM 305
Cdd:COG0031 242 TVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYL 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
16-306 |
2.12e-142 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 404.20 E-value: 2.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 16 GNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGvTTLIEPTSGNTGIALAFVAAAKGYRC 95
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPG-TTIIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 96 IVTMPASMSGERRTLLKAYGSEVVLTDPAK--GMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQTTGPEIWRQTKG 173
Cdd:cd01561 80 IIVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 174 TVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIYEDVIRIHSDEA 253
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1845980223 254 IVMAQRLSYEEGLLGGISSGANVAAALQLAARPEmAGKLIVTCLPSCGERYMT 306
Cdd:cd01561 240 FAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
14-310 |
2.27e-142 |
|
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273463 Cd Length: 299 Bit Score: 404.74 E-value: 2.27e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 14 LIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGvTTLIEPTSGNTGIALAFVAAAKGY 93
Cdd:TIGR01136 4 LIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPG-DTIIEATSGNTGIALAMVAAARGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 94 RCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQTTGPEIWRQTKG 173
Cdd:TIGR01136 83 KLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEIWRDTDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 174 TVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIYEDVIRIHSDEA 253
Cdd:TIGR01136 163 RIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDEDA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1845980223 254 IVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTCLPSCGERYMTSPLY 310
Cdd:TIGR01136 243 IETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
14-310 |
3.61e-142 |
|
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273465 Cd Length: 298 Bit Score: 404.06 E-value: 3.61e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 14 LIGNTPMVYINKLTkGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGvTTLIEPTSGNTGIALAFVAAAKGY 93
Cdd:TIGR01139 4 LIGNTPLVRLNRIE-GCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPG-KTIVEPTSGNTGIALAMVAAARGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 94 RCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGS-IILAQFDNPNNPLVHYQTTGPEIWRQTK 172
Cdd:TIGR01139 82 KLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSyFMLQQFENPANPEIHRKTTGPEIWRDTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 173 GTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIYEDVIRIHSDE 252
Cdd:TIGR01139 162 GKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSDEE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1845980223 253 AIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEmAGKLIVTCLPSCGERYMTSPLY 310
Cdd:TIGR01139 242 AIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
3-323 |
3.86e-136 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 389.67 E-value: 3.86e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 3 DRNSIGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGVTTLIEPTSGNTGI 82
Cdd:PLN02565 1 EKSSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVLIEPTSGNTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 83 ALAFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQT 162
Cdd:PLN02565 81 GLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 163 TGPEIWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIY 242
Cdd:PLN02565 161 TGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 243 EDVIRIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTCLPSCGERYMTSPLYTDIRESAMALAV 322
Cdd:PLN02565 241 DEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKEAENMVF 320
|
.
gi 1845980223 323 E 323
Cdd:PLN02565 321 E 321
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
1-323 |
2.19e-120 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 349.69 E-value: 2.19e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 1 MADRNSIGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGVTTLIEPTSGNT 80
Cdd:PLN00011 1 MEDRCLIKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEATAGNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 81 GIALAFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHY 160
Cdd:PLN00011 81 GIGLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 161 QTTGPEIWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTK 240
Cdd:PLN00011 161 RTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 241 IYEDVIRIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTCLPSCGERYMTSPLYTDIRESAMAL 320
Cdd:PLN00011 241 IVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAENL 320
|
...
gi 1845980223 321 AVE 323
Cdd:PLN00011 321 PIE 323
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
3-323 |
8.64e-120 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 352.16 E-value: 8.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 3 DRNSIGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGVTTLIEPTSGNTGI 82
Cdd:PLN03013 109 DGLNIADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVLVEPTSGNTGI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 83 ALAFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQT 162
Cdd:PLN03013 189 GLAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYET 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 163 TGPEIWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIY 242
Cdd:PLN03013 269 TGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIM 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 243 EDVIRIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTCLPSCGeRYMTSPLYTDIRESAMALAV 322
Cdd:PLN03013 349 DEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRWRKCS 427
|
.
gi 1845980223 323 E 323
Cdd:PLN03013 428 L 428
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
7-320 |
8.65e-119 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 347.33 E-value: 8.65e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 7 IGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGVTTLIEPTSGNTGIALAF 86
Cdd:PLN02556 49 IKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLIEPTSGNMGISLAF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 87 VAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQTTGPE 166
Cdd:PLN02556 129 MAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 167 IWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGRPAGPHKIQGIGAGFAPAVLDTKIYEDVI 246
Cdd:PLN02556 209 IWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVL 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845980223 247 RIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTCLPSCGERYMTSPLYTDIRESAMAL 320
Cdd:PLN02556 289 EVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAENM 362
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
6-310 |
1.72e-104 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 309.48 E-value: 1.72e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 6 SIGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGVTtLIEPTSGNTGIALA 85
Cdd:PRK10717 2 KIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGT-IVEGTAGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 86 FVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLT------DPAKGMKGAIDMANQLKENIP-GSIILAQFDNPNNPLV 158
Cdd:PRK10717 81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVpaapyaNPNNYVKGAGRLAEELVASEPnGAIWANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 159 HYQTTGPEIWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAI----LSG--RPAGPHKIQGIGAGF 232
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGelKAEGSSITEGIGQGR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845980223 233 APAVLDTKIYEDVIRIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARpEMAGKLIVTCLPSCGERYMtSPLY 310
Cdd:PRK10717 241 ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARE-LGPGHTIVTILCDSGERYQ-SKLF 316
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
7-306 |
1.05e-97 |
|
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273464 [Multi-domain] Cd Length: 455 Bit Score: 296.71 E-value: 1.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 7 IGENAAALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGvTTLIEPTSGNTGIALAF 86
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPG-DTIIEPTSGNTGIGLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 87 VAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGM---KGAIDMANQLKENIPGSIILAQFDNPNNPLVHYQTT 163
Cdd:TIGR01137 80 VAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 164 GPEIWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESaILSGRPA------GPHKIQGIGAGFAPAVL 237
Cdd:TIGR01137 160 GPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845980223 238 DTKIYEDVIRIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTCLPSCGERYMT 306
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMT 307
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
14-310 |
4.42e-90 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 271.75 E-value: 4.42e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 14 LIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGvTTLIEPTSGNTGIALAFVAAAKGY 93
Cdd:PRK11761 9 TIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPG-DTLIEATSGNTGIALAMIAAIKGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 94 RCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGsIILAQFDNPNNPLVHYQTTGPEIWRQTKG 173
Cdd:PRK11761 88 RMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEG-KVLDQFANPDNPLAHYETTGPEIWRQTEG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 174 TVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAilsgrpagphKIQGI---GAGFAPAVLDTKIYEDVIRIHS 250
Cdd:PRK11761 167 RITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGS----------SIPGIrrwPEEYLPKIFDASRVDRVLDVSQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 251 DEAIVMAQRLSYEEGLLGGISSGANVAAALQLAARPEMAgkLIVTCLPSCGERYMTSPLY 310
Cdd:PRK11761 237 QEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENPNA--VIVAIICDRGDRYLSTGVF 294
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
12-310 |
2.99e-83 |
|
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 254.07 E-value: 2.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 12 AALIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGvTTLIEPTSGNTGIALAFVAAAK 91
Cdd:TIGR01138 3 EQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPG-DVLIEATSGNTGIALAMIAALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 92 GYRCIVTMPASMSGERRTLLKAYGSEVVLTDPAKGMKGAIDMANQLKENIPGSiILAQFDNPNNPLVHYQTTGPEIWRQT 171
Cdd:TIGR01138 82 GYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPEIWQQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 172 KGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSGrpagphkIQGIGAGFAPAVLDTKIYEDVIRIHSD 251
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDIHQR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1845980223 252 EAIVMAQRLSYEEGLLGGISSGANVAAALQLAArpEMAGKLIVTCLPSCGERYMTSPLY 310
Cdd:TIGR01138 234 DAENTMRELAVREGIFCGVSSGGAVAAALRLAR--ELPDAVVVAIICDRGDRYLSTGVF 290
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
14-297 |
2.81e-65 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 207.93 E-value: 2.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 14 LIGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGtvipGVTTLIEPTSGNTGIALAFVAAAKGY 93
Cdd:pfam00291 4 GIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGE----GGKTVVEASSGNHGRALAAAAARLGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 94 RCIVTMPASMSGERRTLLKAYGSEVVLTDPakGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVhYQTTGPEIWRQTKG 173
Cdd:pfam00291 80 KVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEILEQLGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 174 TVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESAILSG---------RPAGPHKIQGIGAGFAPAVLDTKIYED 244
Cdd:pfam00291 157 DPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARslaagrpvpVPVADTIADGLGVGDEPGALALDLLDE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1845980223 245 ----VIRIHSDEAIVMAQRLSYEEGLLGGISSGANVAAALqLAARPEMAGKLIVTCL 297
Cdd:pfam00291 237 yvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALK-LALAGELKGGDRVVVV 292
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
18-298 |
2.14e-64 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 203.90 E-value: 2.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVipGVTTLIEPTSGNTGIALAFVAAAKGYRCIV 97
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL--PKGVIIESTGGNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 98 TMPASMSGERRTLLKAYGSEVVLTDPakGMKGAIDMANQLKENIPGSIILAQFDNPNNPLVHYqTTGPEIWRQTKG-TVD 176
Cdd:cd00640 79 VMPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqKPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 177 AVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEesailsgrpagphkiqgigagfapavldtkiyedVIRIHSDEAIVM 256
Cdd:cd00640 156 AVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------VVTVSDEEALEA 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1845980223 257 AQRLSYEEGLLGGISSGANVAAALQLAARPeMAGKLIVTCLP 298
Cdd:cd00640 202 IRLLAREEGILVEPSSAAALAAALKLAKKL-GKGKTVVVILT 242
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
15-306 |
2.36e-33 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 127.80 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 15 IGNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGvTTLIEPTSGNTGIALAFVAAAKGYR 94
Cdd:PLN02356 51 IGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPG-GVVTEGSAGSTAISLATVAPAYGCK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 95 CIVTMPASMSGERRTLLKAYGSEVVLTDPA-------------------------KGMKGAIDMANQLKEN--------- 140
Cdd:PLN02356 130 CHVVIPDDVAIEKSQILEALGATVERVRPVsithkdhyvniarrraleanelaskRRKGSETDGIHLEKTNgciseeeke 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 141 -------IPGSIILAQFDNPNNPLVHYQTTGPEIWRQTKGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESA 213
Cdd:PLN02356 210 nslfsssCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGSG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 214 ILSG---------------RPAGPHK--IQGIG-----AGFAPAVLDtkiyeDVIRIHSDEAIVMAQRLSYEEGLLGGIS 271
Cdd:PLN02356 290 LFNKvtrgvmytreeaegrRLKNPFDtiTEGIGinrltQNFLMAKLD-----GAFRGTDKEAVEMSRYLLKNDGLFVGSS 364
|
330 340 350
....*....|....*....|....*....|....*
gi 1845980223 272 SGANVAAALQLaARPEMAGKLIVTCLPSCGERYMT 306
Cdd:PLN02356 365 SAMNCVGAVRV-AQSLGPGHTIVTILCDSGMRHLS 398
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
6-301 |
2.33e-15 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 75.71 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 6 SIGEnaaaliGNTPMVYINKLTKGLPG-TVAVKIEYMNPAGSVKDRiGAAMLAAAEKDGtvipGVTTLIEPTSGNTGIAL 84
Cdd:cd01563 17 SLGE------GNTPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDR-GMTVAVSKAKEL----GVKAVACASTGNTSASL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 85 AFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTDpaKGMKGAIDMANQLKENIPGSIIlaqfdNPNNPLVH--YQT 162
Cdd:cd01563 86 AAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVE--GNFDDALRLVRELAEENWIYLS-----NSLNPYRLegQKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 163 TGPEIWRQTKGTV-DAVVFGVGTGGTITGVGRYLQE-QNPGV-----RVFAVEPEES-----AILSGRPAG-----PHKI 225
Cdd:cd01563 159 IAFEIAEQLGWEVpDYVVVPVGNGGNITAIWKGFKElKELGLidrlpRMVGVQAEGAapivrAFKEGKDDIepvenPETI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 226 -QGIGAGF---APAVLDTkIYEDVIRIH--SDEAIVMAQR-LSYEEGLLGGISSGANVAAALQLAARPEMAGKLIVTClP 298
Cdd:cd01563 239 aTAIRIGNpasGPKALRA-VRESGGTAVavSDEEILEAQKlLARTEGIFVEPASAASLAGLKKLREEGIIDKGERVVV-V 316
|
...
gi 1845980223 299 SCG 301
Cdd:cd01563 317 LTG 319
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
16-122 |
1.92e-14 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 73.70 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 16 GNTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRiGAAML--AAAEKdgtvipGVTTLIEPTSGNTGIALAFVAAAKGY 93
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDR-AMQVAvsLALER------GAKTIVCASSGNGSAALAAYAARAGI 137
|
90 100 110
....*....|....*....|....*....|
gi 1845980223 94 RCIVTMPAS-MSGERRTLLKAYGSEVVLTD 122
Cdd:COG0498 138 EVFVFVPEGkVSPGQLAQMLTYGAHVIAVD 167
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
18-294 |
3.06e-11 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 63.52 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRiGA--AMLAAAEKDGTVipGVTTliePTSGNTGIALAFVAAAKGYRC 95
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLR-GAynALASLSEEERAR--GVVA---ASAGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 96 IVTMPASMSGERRTLLKAYGSEVVLTDPAkgMKGAIDMANQL-KENipGSIILAQFDNPNnpLVHYQTT-GPEIWRQTkG 173
Cdd:COG1171 99 TIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAELaEEE--GATFVHPFDDPD--VIAGQGTiALEILEQL-P 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 174 TVDAVVfgvgtggtitgvgrYLQEQNPGVRVFAVEPEESA-----ILSGRPAGPHKIQGIGAGFAPAVLDTKIYE----- 243
Cdd:COG1171 172 DLDAVFvpvggggliagvaaALKALSPDIRVIGVEPEGAAamyrsLAAGEPVTLPGVDTIADGLAVGRPGELTFEilrdl 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1845980223 244 --DVIRIhSDEAIVMAQRLSYE-EGLLGGISSGANVAAALQLaaRPEMAGKLIV 294
Cdd:COG1171 252 vdDIVTV-SEDEIAAAMRLLLErTKIVVEPAGAAALAALLAG--KERLKGKRVV 302
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
17-153 |
4.56e-10 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 60.01 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 17 NTPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDR-IGAAMLAAAEKDGTVIPGVttlIEPTSGNTGIALAFVAAAKGYRC 95
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVHV---VCSSGGNAGLAAAYAARKLGVPC 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1845980223 96 IVTMPASMSGERRTLLKAYGSEVVLTDPAKGmKGAIDMANQLKENIPGSIILAQFDNP 153
Cdd:cd06448 78 TIVVPESTKPRVVEKLRDEGATVVVHGKVWW-EADNYLREELAENDPGPVYVHPFDDP 134
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
6-119 |
6.17e-10 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 59.75 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 6 SIGEnaaaliGNTPMVYINKltkglpgtVAVKIEYMNPAGSVKDRiGAAMLAAAEKDgtviPGVTTLIEPTSGNTGIALA 85
Cdd:PRK06450 53 SLGE------GRTPLIKKGN--------IWFKLDFLNPTGSYKDR-GSVTLISYLAE----KGIKQISEDSSGNAGASIA 113
|
90 100 110
....*....|....*....|....*....|....
gi 1845980223 86 FVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVV 119
Cdd:PRK06450 114 AYGAAAGIEVKIFVPETASGGKLKQIESYGAEVV 147
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
6-122 |
1.68e-09 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 58.47 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 6 SIGEnaaaliGNTPMVYINKLTK--GLPgTVAVKIEYMNPAGSVKDRiGAAMLAAAEKDgtviPGVTTLIEPTSGNTGIA 83
Cdd:PRK08197 74 SLGE------GMTPLLPLPRLGKalGIG-RLWVKDEGLNPTGSFKAR-GLAVGVSRAKE----LGVKHLAMPTNGNAGAA 141
|
90 100 110
....*....|....*....|....*....|....*....
gi 1845980223 84 LAFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTD 122
Cdd:PRK08197 142 WAAYAARAGIRATIFMPADAPEITRLECALAGAELYLVD 180
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
16-178 |
1.87e-09 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 58.18 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 16 GNTPMVYINKLTKGLP-GTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGtvIPGVTTliePTSGNTGIALAFVAAAKGYR 94
Cdd:PRK06381 14 GGTPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLG--YSGITV---GTCGNYGASIAYFARLYGLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 95 CIVTMPASMSGERRTLLKAYGSEVVLTD----PAKGMKGAIDMANQLKENIPGSiilaqfDNPNNPLVHYQTTGPEIWRQ 170
Cdd:PRK06381 89 AVIFIPRSYSNSRVKEMEKYGAEIIYVDgkyeEAVERSRKFAKENGIYDANPGS------VNSVVDIEAYSAIAYEIYEA 162
|
....*...
gi 1845980223 171 TKGTVDAV 178
Cdd:PRK06381 163 LGDVPDAV 170
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
16-141 |
8.14e-09 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 56.24 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 16 GNTPMVYINKLTKGLPGT-VAVKIEYMNPAGSVKDRIGAAMLAAAEKDGtvipgVTTLIEPTSGNTGIALAFVAAAKGYR 94
Cdd:TIGR00260 21 GVTPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRGMAVALTKALELG-----NDTVLCASTGNTGAAAAAYAGKAGLK 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1845980223 95 CIVTMPA-SMSGERRTLLKAYGSEVVltdpakGMKGAIDMANQLKENI 141
Cdd:TIGR00260 96 VVVLYPAgKISLGKLAQALGYNAEVV------AIDGNFDDAQRLVKQL 137
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
18-303 |
1.21e-08 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 55.47 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRiGAA----MLAAAEKDGTVIPGvttliepTSGNTGIALAFVAAAKGY 93
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFR-GASnklrLLNEAQRQQGVITA-------SSGNHGQGVALAAKLAGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 94 RCIVTMPASMSGERRTLLKAYGSEVVLTdPAKGMKGAIDMANQLKENipGSIILAQFdnpNNPLV--HYQTTGPEIWRQT 171
Cdd:PRK06815 93 PVTVYAPEQASAIKLDAIRALGAEVRLY-GGDALNAELAARRAAEQQ--GKVYISPY---NDPQViaGQGTIGMELVEQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 172 kGTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESA-----ILSGR----PAGPHKIQGIGAGFAP-------- 234
Cdd:PRK06815 167 -PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPslytsLEAGEivevAEQPTLSDGTAGGVEPgaitfplc 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845980223 235 -AVLDTKIyedvirIHSDEAIVMAQRL--SYEEGLLGGiSSGANVAAALQLAarPEMAGKLIVTCLpsCGER 303
Cdd:PRK06815 246 qQLIDQKV------LVSEEEIKEAMRLiaETDRWLIEG-AAGVALAAALKLA--PRYQGKKVAVVL--CGKN 306
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
18-294 |
1.23e-08 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 55.57 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRiGA-AMLAAAEKDGTvIPGVTTLiepTSGNTGIALAFVAAAKGYRCI 96
Cdd:cd01562 18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIR-GAyNKLLSLSEEER-AKGVVAA---SAGNHAQGVAYAAKLLGIPAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 97 VTMPASMSGERRTLLKAYGSEVVLTDPakGMKGAIDMANQL-KENipGSIILAQFDNPNnpLVHYQ-TTGPEIWRQTkGT 174
Cdd:cd01562 93 IVMPETAPAAKVDATRAYGAEVVLYGE--DFDEAEAKARELaEEE--GLTFIHPFDDPD--VIAGQgTIGLEILEQV-PD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 175 VDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEESA-----ILSGRPAgPHKIQGIGA-GFAPAVLDTKIYE----- 243
Cdd:cd01562 166 LDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPamaqsLAAGKPV-TLPEVDTIAdGLAVKRPGELTFEiirkl 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1845980223 244 --DVIRIhSDEAIVMAQRLSYE------EGllggiSSGANVAAALQLAARPEmaGKLIV 294
Cdd:cd01562 245 vdDVVTV-SEDEIAAAMLLLFEreklvaEP-----AGALALAALLSGKLDLK--GKKVV 295
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
31-281 |
2.39e-07 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 51.49 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 31 PGTVAVKIEYMNPAGSVKDRiGA--AMLAAAE-KDGTVIPgvttliepTSGNTGIALAFVAAAKGYRCIVTMPASMSGER 107
Cdd:PRK08246 36 PAPVWLKLEHLQHTGSFKAR-GAfnRLLAAPVpAAGVVAA--------SGGNAGLAVAYAAAALGVPATVFVPETAPPAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 108 RTLLKAYGSEVVLTDP--AKGMKGAIDMANQlkeniPGSIILAQFDNPNNpLVHYQTTGPEIWRQTKGtVDAVVFGVGTG 185
Cdd:PRK08246 107 VARLRALGAEVVVVGAeyADALEAAQAFAAE-----TGALLCHAYDQPEV-LAGAGTLGLEIEEQAPG-VDTVLVAVGGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 186 GTITGVGRYLQeqnPGVRVFAVEPE-----ESAILSGRPA------------GPHKIQGIGAGFAPAVLDTKIyedvirI 248
Cdd:PRK08246 180 GLIAGIAAWFE---GRARVVAVEPEgaptlHAALAAGEPVdvpvsgiaadslGARRVGEIAFALARAHVVTSV------L 250
|
250 260 270
....*....|....*....|....*....|...
gi 1845980223 249 HSDEAIVMAQRLSYEEGLLGGISSGANVAAALQ 281
Cdd:PRK08246 251 VSDEAIIAARRALWEELRLAVEPGAATALAALL 283
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
18-294 |
8.70e-07 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 50.57 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRiGA----AMLAAAEKDGTVIPGvttliepTSGNTGIALAFVAAAKGY 93
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIR-GAynkmARLPAEQLARGVITA-------SAGNHAQGVALAAARLGV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 94 RCIVTMPASMSGERRTLLKAYGSEVVLTDPAkgMKGAIDMANQLKENiPGSIILAQFDNPNnpLVHYQ-TTGPEIWRQTK 172
Cdd:PRK12483 110 KAVIVMPRTTPQLKVDGVRAHGGEVVLHGES--FPDALAHALKLAEE-EGLTFVPPFDDPD--VIAGQgTVAMEILRQHP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 173 GTVDAVVFGVGTGGTITGVGRYLQEQNPGVRVFAVEPEES-----AILSGRPAGPHKIQGIGAGFAPAVLDTKIYE---- 243
Cdd:PRK12483 185 GPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSnclqaALAAGERVVLGQVGLFADGVAVAQIGEHTFElcrh 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1845980223 244 ---DVIRIHSDEaIVMAQRLSYEEGLLGGISSGA-NVAAALQLAARPEMAGKLIV 294
Cdd:PRK12483 265 yvdEVVTVSTDE-LCAAIKDIYDDTRSITEPAGAlAVAGIKKYAEREGIEGQTLV 318
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
30-142 |
2.95e-06 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 48.28 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 30 LPGTVAVKIEYMNPAGSVKDRiGAAMLAAAEKDgtviPGVTTLIEPTSGNTGIALAFVAAAKGYRCIVTMPASMSGERRT 109
Cdd:PRK08329 70 RSIKVYFKLDYLQPTGSFKDR-GTYVTVAKLKE----EGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKIS 144
|
90 100 110
....*....|....*....|....*....|....*
gi 1845980223 110 LLKAYGSEV--VLTDPAKGMKGAIDMANqlKENIP 142
Cdd:PRK08329 145 LLSRLGAELhfVEGDRMEVHEEAVKFSK--RNNIP 177
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
18-122 |
4.80e-05 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 44.76 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIpgvTTLIEPTSGNTGIALAFVAAAKGYRCIV 97
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLP---DKIVAYSTGNHGQAVAYASKLFGIKTRI 100
|
90 100
....*....|....*....|....*
gi 1845980223 98 TMPASMSGERRTLLKAYGSEVVLTD 122
Cdd:PRK06608 101 YLPLNTSKVKQQAALYYGGEVILTN 125
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
18-297 |
1.99e-04 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 42.91 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGT-VAVKIEYMNPAGSVK--DRIGAAMLAAAEkdgtvipGVTTLIEPT-SGNTGIALAFVAAAKGY 93
Cdd:cd06446 35 TPLYRAKRLSEYLGGAkIYLKREDLNHTGAHKinNALGQALLAKRM-------GKKRVIAETgAGQHGVATATACALFGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 94 RCIVTMPASmSGER----RTLLKAYGSEVV-LTDPAKGMKGAIDMA-----NQLKEN--IPGSIIlAQFDNPNNPLVHYQ 161
Cdd:cd06446 108 ECEIYMGAV-DVERqplnVFRMELLGAEVVpVPSGSGTLKDAISEAirdwvTNVEDThyLLGSVV-GPHPYPNMVRDFQS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 162 TTGPEIWRQTK----GTVDAVV---------------FGvgtggtitgvgrylqeQNPGVRVFAVEPEESAILSGRPAG- 221
Cdd:cd06446 186 VIGEEAKKQILekegELPDVVIacvgggsnaaglfypFI----------------NDKDVKLIGVEAGGCGLETGGHAAy 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 222 --------------------------PHKIQGiG---AGFAP--AVL-DTKIYEdVIRIHSDEAIVMAQRLSYEEGLLGG 269
Cdd:cd06446 250 lfggtagvlhglkmytlqdedgqivpPHSISA-GldyPGVGPehAYLkDSGRVE-YVAVTDEEALEAFKLLARTEGIIPA 327
|
330 340
....*....|....*....|....*....
gi 1845980223 270 ISSGANVAAALQLAarPEMA-GKLIVTCL 297
Cdd:cd06446 328 LESSHAIAYAIKLA--KKLGkEKVIVVNL 354
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
1-119 |
2.77e-04 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 42.29 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 1 MADRNSIgENAAALIGN----TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTVIPGVttlIEPT 76
Cdd:PRK06110 2 MFTLAEL-EAAAAVVYAamppTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRGV---ISAT 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1845980223 77 SGNTGIALAFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVV 119
Cdd:PRK06110 78 RGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELI 120
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
16-119 |
4.36e-04 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 41.72 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 16 GNTPMVYiNKLTKGLPGTVAVKIEYMNPAGSVKDRIGAAMLAAAEKDGTvipgvTTLIEPTSGNTGIALAFVAAAKGYRC 95
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAA-----NGFIVASDGNAAASVAAYSARAGKEA 138
|
90 100
....*....|....*....|....
gi 1845980223 96 IVTMPASMSGERRTLLKAYGSEVV 119
Cdd:PRK05638 139 FVVVPRKVDKGKLIQMIAFGAKII 162
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
71-122 |
5.44e-04 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 41.40 E-value: 5.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1845980223 71 TLIEPTSGNTGIALAFVAAAKGYRCIVTMPASMSGERRTLLKAYGSEVVLTD 122
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITD 169
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
18-121 |
7.20e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 40.72 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRiGA----AMLAAAEKDGTVIPGVTtlieptsGNTGIALAFVAAAKGY 93
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLR-GAtnalLSLSAQERARGVVTAST-------GNHGRALAYAARALGI 91
|
90 100
....*....|....*....|....*...
gi 1845980223 94 RCIVTMPASMSGERRTLLKAYGSEVVLT 121
Cdd:PRK07476 92 RATICMSRLVPANKVDAIRALGAEVRIV 119
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
18-120 |
1.59e-03 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 39.72 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845980223 18 TPMVYINKLTKGLPGTVAVKIEYMNPAGSVKDRiGAA----MLAAAEKDGTVIPGvttliepTSGNTGIALAFVAAAKGY 93
Cdd:PRK08638 28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIR-GAFnklsSLTDAEKRKGVVAC-------SAGNHAQGVALSCALLGI 99
|
90 100
....*....|....*....|....*..
gi 1845980223 94 RCIVTMPASMSGERRTLLKAYGSEVVL 120
Cdd:PRK08638 100 DGKVVMPKGAPKSKVAATCGYGAEVVL 126
|
|
|