|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00011 |
PLN00011 |
cysteine synthase |
1-323 |
0e+00 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 610.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 1 MEDRCLIKNDITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEPTAGNT 80
Cdd:PLN00011 1 MEDRCLIKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEATAGNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 81 GIGLACMGAARGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIHY 160
Cdd:PLN00011 81 GIGLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 161 RTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGGQPGPHLIQGIGSGIVPFNLDLT 240
Cdd:PLN00011 161 RTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 241 IVDEIIQVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVVFPSGGERYLSTKLFDSIRYEAENL 320
Cdd:PLN00011 241 IVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAENL 320
|
...
gi 145334565 321 PIE 323
Cdd:PLN00011 321 PIE 323
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
3-323 |
1.04e-175 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 489.05 E-value: 1.04e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 3 DRCLIKNDITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEPTAGNTGI 82
Cdd:PLN02565 1 EKSSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVLIEPTSGNTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 83 GLACMGAARGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIHYRT 162
Cdd:PLN02565 81 GLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 163 TGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGGQPGPHLIQGIGSGIVPFNLDLTIV 242
Cdd:PLN02565 161 TGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 243 DEIIQVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVVFPSGGERYLSTKLFDSIRYEAENLPI 322
Cdd:PLN02565 241 DEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKEAENMVF 320
|
.
gi 145334565 323 E 323
Cdd:PLN02565 321 E 321
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
7-307 |
1.90e-151 |
|
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: 426.77 E-value: 1.90e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 7 IKNDITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEPTAGNTGIGLAC 86
Cdd:COG0031 3 IYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPG-GTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 87 MGAARGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIHYRTTGPE 166
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 167 IWRDSAGKVDILvagvgtggtatgvgKFLKEQNKDIKVCVVEPVESPVLSGGQPGPHLIQGIGSGIVPFNLDLTIVDEII 246
Cdd:COG0031 162 IWEQTDGKVDAFvagvgtggtitgvgRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLIDEVI 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334565 247 QVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRpENAGKLIVVVFPSGGERYLST 307
Cdd:COG0031 242 TVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
11-310 |
1.70e-150 |
|
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: 424.47 E-value: 1.70e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 11 ITELIGNTPMVYLNNVvDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKsTLIEPTAGNTGIGLACMGAA 90
Cdd:TIGR01139 1 ISELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGK-TIVEPTSGNTGIALAMVAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 91 RGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAILSKTPGGY-IPQQFENPANPEIHYRTTGPEIWR 169
Cdd:TIGR01139 79 RGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 170 DSAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGGQPGPHLIQGIGSGIVPFNLDLTIVDEIIQVA 249
Cdd:TIGR01139 159 DTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVS 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334565 250 GEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPEnAGKLIVVVFPSGGERYLSTKLF 310
Cdd:TIGR01139 239 DEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
11-310 |
5.01e-148 |
|
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: 418.22 E-value: 5.01e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 11 ITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKsTLIEPTAGNTGIGLACMGAA 90
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGD-TIIEATSGNTGIALAMVAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 91 RGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIHYRTTGPEIWRD 170
Cdd:TIGR01136 80 RGYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 171 SAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGGQPGPHLIQGIGSGIVPFNLDLTIVDEIIQVAG 250
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 251 EEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVVFPSGGERYLSTKLF 310
Cdd:TIGR01136 240 EDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
7-323 |
6.88e-142 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 407.63 E-value: 6.88e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 7 IKNDITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEPTAGNTGIGLAC 86
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVLVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 87 MGAARGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIHYRTTGPE 166
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTGPE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 167 IWRDSAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGGQPGPHLIQGIGSGIVPFNLDLTIVDEII 246
Cdd:PLN03013 273 IWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVI 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334565 247 QVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVVFPSGGeRYLSTKLFDSIRYEAENLPIE 323
Cdd:PLN03013 353 AISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRWRKCSL 428
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
16-306 |
3.02e-137 |
|
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: 390.34 E-value: 3.02e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 16 GNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEPTAGNTGIGLACMGAARGYKV 95
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPG-TTIIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 96 ILVMPSTMSLERRIILRALGAELHLSD--QRIGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIHYRTTGPEIWRDSAG 173
Cdd:cd01561 80 IIVMPETMSEEKRKLLRALGAEVILTPeaEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 174 KVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGGQPGPHLIQGIGSGIVPFNLDLTIVDEIIQVAGEEA 253
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 145334565 254 IETAKLLALKEGLLVGISSGAAAAAALKVAKRPEnAGKLIVVVFPSGGERYLS 306
Cdd:cd01561 240 FAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
7-320 |
2.61e-132 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 380.84 E-value: 2.61e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 7 IKNDITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEPTAGNTGIGLAC 86
Cdd:PLN02556 49 IKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLIEPTSGNMGISLAF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 87 MGAARGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIHYRTTGPE 166
Cdd:PLN02556 129 MAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 167 IWRDSAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGGQPGPHLIQGIGSGIVPFNLDLTIVDEII 246
Cdd:PLN02556 209 IWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVL 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334565 247 QVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVVFPSGGERYLSTKLFDSIRYEAENL 320
Cdd:PLN02556 289 EVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAENM 362
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
7-322 |
2.99e-98 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 292.92 E-value: 2.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 7 IKNDITELIGNTPMVYLNNVVD--GCvaRIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKsTLIEPTAGNTGIGL 84
Cdd:PRK10717 3 IFEDVSDTIGNTPLIRLNRASEatGC--EILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGG-TIVEGTAGNTGIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 85 ACMGAARGYKVILVMPSTMSLERRIILRALGAELHL------SDQRIGLKGMLEKTEAILSKTPGGYI-PQQFENPANPE 157
Cdd:PRK10717 80 ALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLvpaapyANPNNYVKGAGRLAEELVASEPNGAIwANQFDNPANRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 158 IHYRTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLS---GGQ---PGPHLIQGIGSG 231
Cdd:PRK10717 160 AHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyykTGElkaEGSSITEGIGQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 232 IVPFNLDLTIVDEIIQVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRpENAGKLIVVVFPSGGERYLStKLFD 311
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARE-LGPGHTIVTILCDSGERYQS-KLFN 317
|
330
....*....|.
gi 145334565 312 SIRYEAENLPI 322
Cdd:PRK10717 318 PDFLREKGLPV 328
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
7-311 |
5.37e-83 |
|
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: 258.19 E-value: 5.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 7 IKNDITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEPTAGNTGIGLAC 86
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPG-DTIIEPTSGNTGIGLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 87 MGAARGYKVILVMPSTMSLERRIILRALGAEL---------HLSDQRIGLKGMLEKteailsKTPGGYIPQQFENPANPE 157
Cdd:TIGR01137 80 VAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIvrtptaaafDSPESHIGVAKRLVR------EIPGAHILDQYRNPSNPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 158 IHYRTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPvESPVLSGGQP------GPHLIQGIGSG 231
Cdd:TIGR01137 154 AHYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADP-EGSILAQPEElnqtgrTPYKVEGIGYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 232 IVPFNLDLTIVDEIIQVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVVFPSGGERYLsTKLFD 311
Cdd:TIGR01137 233 FIPTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYM-TKFLN 311
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
11-312 |
5.89e-82 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 250.18 E-value: 5.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 11 ITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEPTAGNTGIGLACMGAA 90
Cdd:PRK11761 6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPG-DTLIEATSGNTGIALAMIAAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 91 RGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAiLSKTPGGYIPQQFENPANPEIHYRTTGPEIWRD 170
Cdd:PRK11761 85 KGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQ-MQAEGEGKVLDQFANPDNPLAHYETTGPEIWRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 171 SAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVEspvlsGGQpgphlIQGI---GSGIVPFNLDLTIVDEIIQ 247
Cdd:PRK11761 164 TEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEE-----GSS-----IPGIrrwPEEYLPKIFDASRVDRVLD 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334565 248 VAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAgkLIVVVFPSGGERYLSTKLFDS 312
Cdd:PRK11761 234 VSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENPNA--VIVAIICDRGDRYLSTGVFPA 296
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
11-310 |
8.97e-76 |
|
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: 234.42 E-value: 8.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 11 ITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKsTLIEPTAGNTGIGLACMGAA 90
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGD-VLIEATSGNTGIALAMIAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 91 RGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKGMLEKTEAILSKTPGGYIpQQFENPANPEIHYRTTGPEIWRD 170
Cdd:TIGR01138 81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLL-DQFNNPDNPYAHYTSTGPEIWQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 171 SAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGgqpgphlIQGIGSGIVPFNLDLTIVDEIIQVAG 250
Cdd:TIGR01138 160 TGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDIHQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 251 EEAIETAKLLALKEGLLVGISSGAAAAAALKVAKrpENAGKLIVVVFPSGGERYLSTKLF 310
Cdd:TIGR01138 233 RDAENTMRELAVREGIFCGVSSGGAVAAALRLAR--ELPDAVVVAIICDRGDRYLSTGVF 290
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
11-298 |
9.62e-61 |
|
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: 195.61 E-value: 9.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 11 ITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGlitpGKSTLIEPTAGNTGIGLACMGAA 90
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGE----GGKTVVEASSGNHGRALAAAAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 91 RGYKVILVMPSTMSLERRIILRALGAELHLSDQriGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIhYRTTGPEIWRD 170
Cdd:pfam00291 77 LGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEILEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 171 SAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPVLSGG---------QPGPHLIQGIGSGIVPFNLDLTI 241
Cdd:pfam00291 154 LGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334565 242 ----VDEIIQVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVVFP 298
Cdd:pfam00291 234 ldeyVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLT 294
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
18-300 |
4.45e-59 |
|
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: 189.65 E-value: 4.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 18 TPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLItpGKSTLIEPTAGNTGIGLACMGAARGYKVIL 97
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL--PKGVIIESTGGNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 98 VMPSTMSLERRIILRALGAELHLSDQriGLKGMLEKTEAILSKTPGGYIPQQFENPANPEIHYrTTGPEIWRDsagkvdi 177
Cdd:cd00640 79 VMPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQ------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 178 lvagvgtggtatgvgkfLKEQNKDIKVCvvepvesPVLSGGqpgphLIQGIGSGIVPFNLDLTIV---DEIIQVAGEEAI 254
Cdd:cd00640 149 -----------------LGGQKPDAVVV-------PVGGGG-----NIAGIARALKELLPNVKVIgvePEVVTVSDEEAL 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 145334565 255 ETAKLLALKEGLLVGISSGAAAAAALKVAKRPeNAGKLIVVVFPSG 300
Cdd:cd00640 200 EAIRLLAREEGILVEPSSAAALAAALKLAKKL-GKGKTVVVILTGG 244
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
8-312 |
4.27e-35 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 132.04 E-value: 4.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 8 KNDITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEPTAGNTGIGLACM 87
Cdd:PLN02356 44 RNGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPG-GVVTEGSAGSTAISLATV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 88 GAARGYKVILVMPSTMSLERRIILRALGAELH---------------------------LSDQRIGLK---GMLEKTEAI 137
Cdd:PLN02356 123 APAYGCKCHVVIPDDVAIEKSQILEALGATVErvrpvsithkdhyvniarrraleanelASKRRKGSEtdgIHLEKTNGC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 138 LS---KTP--------GGYIPQQFENPANPEIHYRTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCV 206
Cdd:PLN02356 203 ISeeeKENslfsssctGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 207 VEPVESPVLSG-----------------GQPGPHLIQGIGSGIVPFNLDLTIVDEIIQVAGEEAIETAKLLALKEGLLVG 269
Cdd:PLN02356 283 IDPPGSGLFNKvtrgvmytreeaegrrlKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVG 362
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 145334565 270 ISSGAAAAAALKVAKRPeNAGKLIVVVFPSGGERYLStKLFDS 312
Cdd:PLN02356 363 SSSAMNCVGAVRVAQSL-GPGHTIVTILCDSGMRHLS-KFHDP 403
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
18-301 |
8.01e-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: 52.87 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 18 TPMVY---LNNVVDgcvARIAAKLEMMEPCSSVKDRIAYSMI----KDAEDKGLITPgkstliepTAGNTGIGLACMGAA 90
Cdd:cd01562 18 TPLLTsptLSELLG---AEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKGVVAA--------SAGNHAQGVAYAAKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 91 RGYKVILVMPSTMSLERRIILRALGAELHLSDQRIGLKgmLEKTEAILSKTPGGYIPqqfenPANpeiHYR------TTG 164
Cdd:cd01562 87 LGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEA--EAKARELAEEEGLTFIH-----PFD---DPDviagqgTIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 165 PEIWRDsAGKVDILvagvgtggtatgvgkF---------------LKEQNKDIKVCVVEPVESPVLS----GGQP----- 220
Cdd:cd01562 157 LEILEQ-VPDLDAV---------------FvpvggggliagiataVKALSPNTKVIGVEPEGAPAMAqslaAGKPvtlpe 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 221 GPHLIQGIGSGIV---PFNLDLTIVDEIIQVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPEnaGKLIVVVF 297
Cdd:cd01562 221 VDTIADGLAVKRPgelTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLK--GKKVVVVL 298
|
....
gi 145334565 298 pSGG 301
Cdd:cd01562 299 -SGG 301
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
18-269 |
5.29e-07 |
|
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: 50.42 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 18 TPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMI----KDAEDKGLITPgkstliepTAGNTGIGLACMGAARGY 93
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALaslsEEERARGVVAA--------SAGNHAQGVAYAARLLGI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 94 KVILVMPSTMSLERRIILRALGAELHLSDqriglkGMLEKTEAI---LSKTPGG-YIPqqfenPANPE--IH-YRTTGPE 166
Cdd:COG1171 97 PATIVMPETAPAVKVAATRAYGAEVVLHG------DTYDDAEAAaaeLAEEEGAtFVH-----PFDDPdvIAgQGTIALE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 167 IWRDsAGKVDILvagvgtggtatgvgkF---------------LKEQNKDIKVCVVEPVESPV----LSGGQP----GPH 223
Cdd:COG1171 166 ILEQ-LPDLDAV---------------FvpvggggliagvaaaLKALSPDIRVIGVEPEGAAAmyrsLAAGEPvtlpGVD 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 145334565 224 LI-QGIGSGIV---PFNLDLTIVDEIIQVAGEEAIETAKLLALKEGLLVG 269
Cdd:COG1171 230 TIaDGLAVGRPgelTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVE 279
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
37-122 |
3.14e-06 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 48.28 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 37 KLEMMEPCSSVKDRIAYSMIKDAEDKGLitpgkSTLIEPTAGNTGIGLACMGAARGYKVILVMPSTMSLERRIILRALGA 116
Cdd:PRK08329 77 KLDYLQPTGSFKDRGTYVTVAKLKEEGI-----NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGA 151
|
....*.
gi 145334565 117 ELHLSD 122
Cdd:PRK08329 152 ELHFVE 157
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
7-118 |
3.57e-06 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 47.81 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 7 IKNDITELIGNTPMVYLNNVvdgcvariAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLitpgkSTLIEPTAGNTGIGLAC 86
Cdd:PRK06450 48 IKHFISLGEGRTPLIKKGNI--------WFKLDFLNPTGSYKDRGSVTLISYLAEKGI-----KQISEDSSGNAGASIAA 114
|
90 100 110
....*....|....*....|....*....|..
gi 145334565 87 MGAARGYKVILVMPSTMSLERRIILRALGAEL 118
Cdd:PRK06450 115 YGAAAGIEVKIFVPETASGGKLKQIESYGAEV 146
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
16-119 |
4.41e-06 |
|
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: 47.59 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 16 GNTPMVYLNNVVD-GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAedKGLitpGKSTLIEPTAGNTGIGLACMGAARGYK 94
Cdd:cd01563 21 GNTPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKA--KEL---GVKAVACASTGNTSASLAAYAARAGIK 95
|
90 100
....*....|....*....|....*
gi 145334565 95 VILVMPSTMSLERRIILRALGAELH 119
Cdd:cd01563 96 CVVFLPAGKALGKLAQALAYGATVL 120
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
18-315 |
8.50e-06 |
|
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130197 [Multi-domain] Cd Length: 380 Bit Score: 47.05 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 18 TPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGlitpGKSTLIEPTAGNTGIGLACMGAARGYKVIL 97
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQ----RQRGVVAASAGNHAQGVAYAAKKFGIKAVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 98 VMPSTMSLERRIILRALGAELHLS----DQRIGLKGMLEKTEailsktpgGYIpqqFENPAN-PEI--HYRTTGPEIWRD 170
Cdd:TIGR01127 77 VMPESAPPSKVKATKSYGAEVILHgddyDEAYAFATSLAEEE--------GRV---FVHPFDdEFVmaGQGTIGLEIMED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 171 sAGKVDILVAGVGTGGTATGVGKFLKEQNKDIKVCVVEPVESPV----LSGGQP-----GPHLIQGIG---SGIVPFNLD 238
Cdd:TIGR01127 146 -IPDVDTVIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSmyesLREGKIkavesVRTIADGIAvkkPGDLTFNII 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 239 LTIVDEIIQVAgEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVVfpSGG-------ERYLSTKLFD 311
Cdd:TIGR01127 225 KEYVDDVVTVD-EEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVL--SGGnidlnllNKIIEKGLVK 301
|
....
gi 145334565 312 SIRY 315
Cdd:TIGR01127 302 SGRK 305
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
16-120 |
1.48e-05 |
|
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: 46.35 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 16 GNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDR---IAYSMIKDAedkglitpGKSTLIEPTAGNTGIGLACMGAARG 92
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRamqVAVSLALER--------GAKTIVCASSGNGSAALAAYAARAG 136
|
90 100
....*....|....*....|....*....
gi 145334565 93 YKVILVMPST-MSLERRIILRALGAELHL 120
Cdd:COG0498 137 IEVFVFVPEGkVSPGQLAQMLTYGAHVIA 165
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
31-126 |
5.20e-04 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 41.52 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 31 VARIAAKLEMMEPCSSVKDR---IAYSMIKDAedkglitpGKSTLIEPTAGNTGIGLACMGAARGYKVILVMPSTMSLER 107
Cdd:PRK08197 94 IGRLWVKDEGLNPTGSFKARglaVGVSRAKEL--------GVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEIT 165
|
90
....*....|....*....
gi 145334565 108 RIILRALGAELHLSDQRIG 126
Cdd:PRK08197 166 RLECALAGAELYLVDGLIS 184
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
32-296 |
6.01e-04 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 40.83 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 32 ARIAAKLEMMEPCSSVKDRIAYSMIK----DAEDKGLITPgkstliepTAGNTGIGLACMGAARGYKVILVMPSTMSLER 107
Cdd:PRK06815 35 CEVYLKCEHLQHTGSFKFRGASNKLRllneAQRQQGVITA--------SSGNHGQGVALAAKLAGIPVTVYAPEQASAIK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 108 RIILRALGAELHLsdqrIGLKGMLEKTEAILSKTPGG--YIPqqfenPAN-PEI--HYRTTGPEIWRdSAGKVDILVAGV 182
Cdd:PRK06815 107 LDAIRALGAEVRL----YGGDALNAELAARRAAEQQGkvYIS-----PYNdPQViaGQGTIGMELVE-QQPDLDAVFVAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 183 GTGGTATGVGKFLKEQNKDIKV--C----------------VVEPVESPVLSGGQPGphliqGIGSGIVPFNLDLTIVDE 244
Cdd:PRK06815 177 GGGGLISGIATYLKTLSPKTEIigCwpanspslytsleageIVEVAEQPTLSDGTAG-----GVEPGAITFPLCQQLIDQ 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 145334565 245 IIQVAGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPEnaGKLIVVV 296
Cdd:PRK06815 252 KVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ--GKKVAVV 301
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
33-118 |
8.78e-04 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 40.46 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 33 RIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLitpgkSTLIEPTAGNTGIGLACMGAARGYKVILVMPSTMSLERRIILR 112
Cdd:PRK06381 32 KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY-----SGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEME 106
|
....*.
gi 145334565 113 ALGAEL 118
Cdd:PRK06381 107 KYGAEI 112
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
67-118 |
1.83e-03 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 39.59 E-value: 1.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 145334565 67 PGKSTLIEPTAGNTGIGLACMGAARGYKVILVMPSTMSLERRIILRALGAEL 118
Cdd:PRK06110 68 PRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAEL 119
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
8-120 |
4.33e-03 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 38.56 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334565 8 KNDITELIGNTPMVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIAY---SMIKDAE-DKGLITPgkstliepTAGNTGIG 83
Cdd:PRK08638 18 KQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFnklSSLTDAEkRKGVVAC--------SAGNHAQG 89
|
90 100 110
....*....|....*....|....*....|....*..
gi 145334565 84 LACMGAARGYKVILVMPSTMSLERRIILRALGAELHL 120
Cdd:PRK08638 90 VALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVL 126
|
|
|