|
Name |
Accession |
Description |
Interval |
E-value |
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
10-304 |
1.35e-169 |
|
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: 471.85 E-value: 1.35e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 10 ELIGNTPVVKLNRlVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAMVAAAKGI 89
Cdd:TIGR01139 3 ELIGNTPLVRLNR-IEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 90 NAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEEHG--YFMPQQFSNEANAEIHRRTTGKEILEQFD 167
Cdd:TIGR01139 82 KLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPnsYFMLQQFENPANPEIHRKTTGPEIWRDTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 168 GELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGIIQVKNED 247
Cdd:TIGR01139 162 GKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSDEE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157679613 248 AFELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKVLAIIPSNGERYLSTPLY 304
Cdd:TIGR01139 242 AIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLSTPLF 298
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
3-301 |
4.17e-168 |
|
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: 468.37 E-value: 4.17e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 3 RIANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAM 82
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 83 VAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEEH-GYFMPQQFSNEANAEIHRRTTGKE 161
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETpGAFWPNQFENPANPEAHYETTGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 162 ILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGII 241
Cdd:COG0031 162 IWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLIDEVI 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 242 QVKNEDAFELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKVLAIIPSNGERYLST 301
Cdd:COG0031 242 TVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
10-304 |
4.50e-159 |
|
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: 445.57 E-value: 4.50e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 10 ELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAMVAAAKGI 89
Cdd:TIGR01136 3 ELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAARGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 90 NAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEE-HGYFMPQQFSNEANAEIHRRTTGKEILEQFDG 168
Cdd:TIGR01136 83 KLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAEtNKYVMLDQFENPANPEAHYKTTGPEIWRDTDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 169 ELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGIIQVKNEDA 248
Cdd:TIGR01136 163 RIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDEDA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157679613 249 FELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKV-LAIIPSNGERYLSTPLY 304
Cdd:TIGR01136 243 IETARRLAREEGILVGISSGAAVAAALKLAKRLENADKViVAILPDTGERYLSTGLF 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
13-300 |
8.27e-149 |
|
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: 419.23 E-value: 8.27e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 13 GNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAMVAAAKGINAI 92
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 93 LVMPDTMSQERRNLLRAYGAELVLTPGAE--GMKGAIKKAEELAEEH-GYFMPQQFSNEANAEIHRRTTGKEILEQFDGE 169
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETpNAFWLNQFENPANPEAHYETTAPEIWEQLDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 170 LDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGIIQVKNEDAF 249
Cdd:cd01561 161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEAF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 157679613 250 ELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKVLAIIPSNGERYLS 300
Cdd:cd01561 241 AMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
3-305 |
5.77e-109 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 319.18 E-value: 5.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 3 RIANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDT-LIEPTSGNTGIGLA 81
Cdd:PLN02565 4 SIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 82 MVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEE-LAEEHGYFMPQQFSNEANAEIHRRTTGK 160
Cdd:PLN02565 84 FMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEiLAKTPNSYILQQFENPANPKIHYETTGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 161 EILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGI 240
Cdd:PLN02565 164 EIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157679613 241 IQVKNEDAFELARKAAKEEGILGGISSGAAIYAALQTAKK-LGKGKKVLAIIPSNGERYLSTPLYQ 305
Cdd:PLN02565 244 VQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRpENAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
3-301 |
8.90e-105 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 308.71 E-value: 8.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 3 RIANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAM 82
Cdd:PRK10717 2 KIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 83 VAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGA------EGMKGAIKKAEELA--EEHGYFMPQQFSNEANAEIH 154
Cdd:PRK10717 82 VAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVasEPNGAIWANQFDNPANREAH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 155 RRTTGKEILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSP----VLSG--GKPGPHKIQGIGAGFI 228
Cdd:PRK10717 162 YETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAlysyYKTGelKAEGSSITEGIGQGRI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157679613 229 PSILNTEVYDGIIQVKNEDAFELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKVLAIIPSNGERYLST 301
Cdd:PRK10717 242 TANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK 314
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
4-305 |
1.17e-98 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 293.06 E-value: 1.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 4 IANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAG-DTLIEPTSGNTGIGLAM 82
Cdd:PLN00011 7 IKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 83 VAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEE-LAEEHGYFMPQQFSNEANAEIHRRTTGKE 161
Cdd:PLN00011 87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEiLSKTPGGYIPQQFENPANPEIHYRTTGPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 162 ILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGII 241
Cdd:PLN00011 167 IWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEII 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157679613 242 QVKNEDAFELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKVLAII-PSNGERYLSTPLYQ 305
Cdd:PLN00011 247 QVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIfPSGGERYLSTKLFE 311
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
3-305 |
9.26e-94 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 282.23 E-value: 9.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 3 RIANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDT-LIEPTSGNTGIGLA 81
Cdd:PLN02556 48 KIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 82 MVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEEH-GYFMPQQFSNEANAEIHRRTTGK 160
Cdd:PLN02556 128 FMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTpDAFMLQQFSNPANTQVHFETTGP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 161 EILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGI 240
Cdd:PLN02556 208 EIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKV 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157679613 241 IQVKNEDAFELARKAAKEEGILGGISSGAAIYAALQTAKKLGKG-KKVLAIIPSNGERYLSTPLYQ 305
Cdd:PLN02556 288 LEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKgKLIVTVHPSFGERYLSSVLFQ 353
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
6-304 |
3.25e-93 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 278.30 E-value: 3.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 6 NSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAMVAA 85
Cdd:PRK11761 4 PTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 86 AKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEEHGYFMPQQFSNEANAEIHRRTTGKEILEQ 165
Cdd:PRK11761 84 IKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEIWRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 166 FDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPvlsggkpgphKIQGI---GAGFIPSILNTEVYDGIIQ 242
Cdd:PRK11761 164 TEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGS----------SIPGIrrwPEEYLPKIFDASRVDRVLD 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157679613 243 VKNEDAFELARKAAKEEGILGGISSGAAIYAALQTAkKLGKGKKVLAIIPSNGERYLSTPLY 304
Cdd:PRK11761 234 VSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIA-RENPNAVIVAIICDRGDRYLSTGVF 294
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
4-305 |
8.25e-91 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 276.66 E-value: 8.25e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 4 IANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDT-LIEPTSGNTGIGLAM 82
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSvLVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 83 VAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEE-LAEEHGYFMPQQFSNEANAEIHRRTTGKE 161
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEiLKNTPDAYMLQQFDNPANPKIHYETTGPE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 162 ILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGII 241
Cdd:PLN03013 273 IWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVI 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157679613 242 QVKNEDAFELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKVLAII-PSNGeRYLSTPLYQ 305
Cdd:PLN03013 353 AISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSlFASG-RDIYTPRCS 416
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
4-300 |
4.22e-85 |
|
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: 262.81 E-value: 4.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 4 IANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAMV 83
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 84 AAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGA------EGMKGAIKKAEElaEEHGYFMPQQFSNEANAEIHRRT 157
Cdd:TIGR01137 81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAaafdspESHIGVAKRLVR--EIPGAHILDQYRNPSNPLAHYDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 158 TGKEILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSpVLSGGKP------GPHKIQGIGAGFIPSI 231
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTV 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 232 LNTEVYDGIIQVKNEDAFELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKV-LAIIPSNGERYLS 300
Cdd:TIGR01137 238 LDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRcVVLLPDSIRNYMT 307
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
7-304 |
4.95e-80 |
|
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: 244.44 E-value: 4.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 7 SVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAMVAAA 86
Cdd:TIGR01138 1 TIEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 87 KGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEEHGYFMPQQFSNEANAEIHRRTTGKEILEQF 166
Cdd:TIGR01138 81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFNNPDNPYAHYTSTGPEIWQQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 167 DGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGgkpgphkIQGIGAGFIPSILNTEVYDGIIQVKNE 246
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDIHQR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 157679613 247 DAFELARKAAKEEGILGGISSGAAIYAALQTAkKLGKGKKVLAIIPSNGERYLSTPLY 304
Cdd:TIGR01138 234 DAENTMRELAVREGIFCGVSSGGAVAAALRLA-RELPDAVVVAIICDRGDRYLSTGVF 290
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
10-301 |
5.79e-77 |
|
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme. [Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274872 [Multi-domain] Cd Length: 304 Bit Score: 237.10 E-value: 5.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 10 ELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGLAMVAAAKGI 89
Cdd:TIGR03945 3 SLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYKGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 90 NAILVM-PDTMSQErRNLLRAYGA--ELVLTPGAEG--MKGAIKKAEEL-AEEHGYFMPQQFSNEANAEIHRRTTGKEIL 163
Cdd:TIGR03945 83 RFICVVdPNISPQN-LKLLRAYGAevEKVTEPDETGgyLGTRIARVRELlASIPDAYWPNQYANPDNPRAHYHGTGREIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 164 EQFDgELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSpVLSGGKPGPHKIQGIGAGFIPSILNTEVYDGIIQV 243
Cdd:TIGR03945 162 RAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGS-VIFGGPPGRRHIPGLGASVVPELLDESLIDDVVHV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 157679613 244 KNEDAFELARKAAKEEGILGGISSGAAIYAALQTAKKLGKGKKVLAIIPSNGERYLST 301
Cdd:TIGR03945 240 PEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDT 297
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
8-275 |
2.29e-67 |
|
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: 212.17 E-value: 2.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 8 VFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKgtlKAGDTLIEPTSGNTGIGLAMVAAAK 87
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 88 GINAILVMPDTMSQERRNLLRAYGAELVLTPGaeGMKGAIKKAEELAEE-HGYFMPQQFSNEANAEIHrRTTGKEILEQF 166
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEgPGAYYINQYDNPLNIEGY-GTIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 167 DGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVLSGG---------KPGPHKIQGIGAGFIPSILNTEVY 237
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDLL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 157679613 238 ----DGIIQVKNEDAFELARKAAKEEGILGGISSGAAIYAAL 275
Cdd:pfam00291 235 deyvGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALK 276
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
15-278 |
3.79e-67 |
|
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: 210.06 E-value: 3.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGdTLIEPTSGNTGIGLAMVAAAKGINAILV 94
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKG-VIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 95 MPDTMSQERRNLLRAYGAELVLTPGaeGMKGAIKKAEELAEE-HGYFMPQQFSNEANAEIHrRTTGKEILEQFDGE-LDA 172
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQ-GTIGLEILEQLGGQkPDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 173 FIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPtdspvlsggkpgphkiqgigagfipsilntevydGIIQVKNEDAFELA 252
Cdd:cd00640 157 VVVPVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------EVVTVSDEEALEAI 202
|
250 260
....*....|....*....|....*.
gi 157679613 253 RKAAKEEGILGGISSGAAIYAALQTA 278
Cdd:cd00640 203 RLLAREEGILVEPSSAAALAAALKLA 228
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
1-300 |
9.05e-31 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 119.71 E-value: 9.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 1 MARIANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIEPTSGNTGIGL 80
Cdd:PLN02356 40 KKKPRNGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 81 AMVAAAKGINAILVMPDTMSQERRNLLRAYGAE------LVLTPGAEGMKGAIKK---AEELAEEH-------------- 137
Cdd:PLN02356 120 ATVAPAYGCKCHVVIPDDVAIEKSQILEALGATvervrpVSITHKDHYVNIARRRaleANELASKRrkgsetdgihlekt 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 138 -------------------GYFMPQQFSNEANAEIHRRTTGKEILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQ 198
Cdd:PLN02356 200 ngciseeekenslfsssctGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 199 LYAVEPTDSPVLSG-------------GK----PGPHKIQGIGAGFIPSILNTEVYDGIIQVKNEDAFELARKAAKEEGI 261
Cdd:PLN02356 280 CFLIDPPGSGLFNKvtrgvmytreeaeGRrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGL 359
|
330 340 350
....*....|....*....|....*....|....*....
gi 157679613 262 LGGISSGAAIYAALQTAKKLGKGKKVLAIIPSNGERYLS 300
Cdd:PLN02356 360 FVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLS 398
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
13-174 |
1.13e-18 |
|
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: 85.25 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 13 GNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRiALAM-IEDAEAKGTlkagDTLIEPTSGNTGIGLAMVAAAKGINA 91
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDR-AMQVaVSLALERGA----KTIVCASSGNGSAALAAYAARAGIEV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 92 ILVMP-DTMSQERRNLLRAYGAELVLTPGAEGmkGAIKKAEELAEEHGyfmpqqFSNEANAEIHRR----TTGKEILEQF 166
Cdd:COG0498 140 FVFVPeGKVSPGQLAQMLTYGAHVIAVDGNFD--DAQRLVKELAADEG------LYAVNSINPARLegqkTYAFEIAEQL 211
|
....*...
gi 157679613 167 DGELDAFI 174
Cdd:COG0498 212 GRVPDWVV 219
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
13-170 |
1.68e-18 |
|
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: 84.18 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 13 GNTPVVKLNRLVDEDSA-DVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTlkagDTLIEPTSGNTGIGLAMVAAAKGINA 91
Cdd:cd01563 21 GNTPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 92 ILVMPDTMSQERRNLLRAYGAELVLTPGaeGMKGAIKKAEELAEEHGYFmpqqFSNEANaeIHR----RTTGKEILEQFD 167
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAVEG--NFDDALRLVRELAEENWIY----LSNSLN--PYRlegqKTIAFEIAEQLG 168
|
...
gi 157679613 168 GEL 170
Cdd:cd01563 169 WEV 171
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
2-275 |
6.32e-18 |
|
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: 82.15 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 2 ARIANSVFElignTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMI----EDAEAKGTLKAgdtliepTSGNTG 77
Cdd:cd01562 9 ARIKPVVRR----TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKGVVAA-------SAGNHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 78 IGLAMVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTpgAEGMKGAIKKAEELAEEHGYFMpqqfsneanaeIH--- 154
Cdd:cd01562 78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEGLTF-----------IHpfd 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 155 -------RRTTGKEILEQfDGELDAFIagvgtggtitgageV--------------LKEAIPSIQLYAVEPTDSPVLS-- 211
Cdd:cd01562 145 dpdviagQGTIGLEILEQ-VPDLDAVF--------------VpvggggliagiataVKALSPNTKVIGVEPEGAPAMAqs 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 212 --GGKPGPHKIQGIGA--------GFIPSILNTEVYDGIIQVKNE-------DAFELARKAAkeEGilggisSGAAIYAA 274
Cdd:cd01562 210 laAGKPVTLPEVDTIAdglavkrpGELTFEIIRKLVDDVVTVSEDeiaaamlLLFEREKLVA--EP------AGALALAA 281
|
.
gi 157679613 275 L 275
Cdd:cd01562 282 L 282
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
15-208 |
1.50e-17 |
|
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: 81.62 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMI----EDAEAKGtlkagdtLIEPTSGNTGIGLAMVAAAKGIN 90
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALaslsEEERARG-------VVAASAGNHAQGVAYAARLLGIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 91 AILVMPDTMSQERRNLLRAYGAELVLTPG--AEgmkgAIKKAEELAEEHGYFMPQQFSneanaeiHRR------TTGKEI 162
Cdd:COG1171 98 ATIVMPETAPAVKVAATRAYGAEVVLHGDtyDD----AEAAAAELAEEEGATFVHPFD-------DPDviagqgTIALEI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 163 LEQFdGELDAFIagvgtggtitgageV--------------LKEAIPSIQLYAVEPTDSP 208
Cdd:COG1171 167 LEQL-PDLDAVF--------------VpvggggliagvaaaLKALSPDIRVIGVEPEGAA 211
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
13-167 |
1.64e-12 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 67.07 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 13 GNTPVVKLNrlvdedsaDVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTlkagDTLIEPTSGNTGIGLAMVAAAKGINAI 92
Cdd:PRK06450 57 GRTPLIKKG--------NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVK 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157679613 93 LVMPDTMSQERRNLLRAYGAELVltpGAEGMKGAIKKAeelAEEHGYFmpqqFSNEANAEIHR---RTTGKEILEQFD 167
Cdd:PRK06450 125 IFVPETASGGKLKQIESYGAEVV---RVRGSREDVAKA---AENSGYY----YASHVLQPQFRdgiRTLAYEIAKDLD 192
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
1-140 |
1.77e-12 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 66.65 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 1 MARIANSVFELIGNTPVVKLNRLVDE-DSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTlkagDTLIEPTSGNTGIG 79
Cdd:PRK06381 2 EEELSSSEEKPPGGTPLLRARKLEEElGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGAS 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157679613 80 LAMVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAegMKGAIKKAEELAEEHGYF 140
Cdd:PRK06381 78 IAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGK--YEEAVERSRKFAKENGIY 136
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
15-165 |
1.09e-11 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 64.37 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIA---LAMIEDAE-AKGTLKAgdtliepTSGNTGIGLAMVAAAKGIN 90
Cdd:PRK08638 28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEkRKGVVAC-------SAGNHAQGVALSCALLGID 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157679613 91 AILVMPDTMSQERRNLLRAYGAELVLTpgAEGMKGAIKKAEELAEEHGYFMPQQFsNEANAEIHRRTTGKEILEQ 165
Cdd:PRK08638 101 GKVVMPKGAPKSKVAATCGYGAEVVLH--GDNFNDTIAKVEEIVEEEGRTFIPPY-DDPKVIAGQGTIGLEILED 172
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
3-207 |
3.78e-11 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 63.66 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 3 RIANS-VFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIA---LAMI-EDAEAKGTLKAgdtliepTSGNTG 77
Cdd:PRK12483 25 KILAArVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAynkMARLpAEQLARGVITA-------SAGNHA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 78 IGLAMVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTpgAEGMKGAIKKAEELAEEHGYFMPQQFsNEANAEIHRRT 157
Cdd:PRK12483 98 QGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEEGLTFVPPF-DDPDVIAGQGT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157679613 158 TGKEILEQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDS 207
Cdd:PRK12483 175 VAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
15-210 |
4.55e-11 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 62.40 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIA----LAMIEDAEAKGTLKAgdtliepTSGNTGIGLAMVAAAKGIN 90
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGAsnklRLLNEAQRQQGVITA-------SSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 91 AILVMPDTMSQERRNLLRAYGAELVLTPGAegMKGAIKKAEELAEEHG--YFMPQqfsNEANAEIHRRTTGKEILEQFDG 168
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVRLYGGD--ALNAELAARRAAEQQGkvYISPY---NDPQVIAGQGTIGMELVEQQPD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157679613 169 eLDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPVL 210
Cdd:PRK06815 169 -LDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSL 209
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
13-170 |
5.31e-11 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 62.71 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 13 GNTPVVKLNRLVDE-DSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKagdtLIEPTSGNTGIGLAMVAAAKGINA 91
Cdd:PRK08197 78 GMTPLLPLPRLGKAlGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARAGIRA 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157679613 92 ILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIkkAEELAEEHGYFMPQQFSNEANAEiHRRTTGKEILEQFDGEL 170
Cdd:PRK08197 154 TIFMPADAPEITRLECALAGAELYLVDGLISDAGKI--VAEAVAEYGWFDVSTLKEPYRIE-GKKTMGLELAEQLGWRL 229
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
15-219 |
1.83e-10 |
|
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: 60.91 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTlKAGdtLIEPTSGNTGIGLAMVAAAKGINAILV 94
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQR-QRG--VVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 95 MPDTMSQERRNLLRAYGAELVLTpGAEgMKGAIKKAEELAEEHGYFMPQQFSNEanaEI--HRRTTGKEILEQFdGELDA 172
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILH-GDD-YDEAYAFATSLAEEEGRVFVHPFDDE---FVmaGQGTIGLEIMEDI-PDVDT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157679613 173 FIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDSPV----LSGGKPGPHK 219
Cdd:TIGR01127 152 VIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSmyesLREGKIKAVE 202
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
13-276 |
3.69e-10 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 60.21 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 13 GNTPVVKlNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDaeakGTLKAGDTLIEPTSGNTGIGLAMVAAAKGINAI 92
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSY----GLPYAANGFIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 93 LVMPDTMSQERRNLLRAYGAELVLTpgAEGMKGAIKKAEELAEEHGYFMPQQFSNEANAEiHRRTTGKEILEQFDGEL-- 170
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIRY--GESVDEAIEYAEELARLNGLYNVTPEYNIIGLE-GQKTIAFELWEEINPTHvi 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 171 -----DAFIAGVGTGGTITGAGEVLKEaIPsiQLYAVEpTD--SPVLS---GGKPGPHKIQGIGAGFIPSILNTEV---- 236
Cdd:PRK05638 217 vptgsGSYLYSIYKGFKELLEIGVIEE-IP--KLIAVQ-TErcNPIASeilGNKTKCNETKALGLYVKNPVMKEYVseai 292
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 157679613 237 --YDGIIQVKNEDAFELARKAAKEEGILGGISSGAAIYAALQ 276
Cdd:PRK05638 293 keSGGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLK 334
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
15-132 |
4.64e-10 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 59.58 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKLnRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAkgtlkAGDTLIEPTSGNTGIGLAMVAAAKGINAILV 94
Cdd:PRK08246 24 TPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 157679613 95 MPDTMSQERRNLLRAYGAELVLTPG--AEGMKGAIKKAEE 132
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAE 137
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
15-172 |
5.10e-10 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 59.40 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVK---LNRLVDEDsadVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKagDTLIEPTSGNTGIGLAMVAAAKGINA 91
Cdd:PRK06608 24 TPIVHsesLNEMLGHE---IFFKVESLQKTGAFKVRGVLNHLLELKEQGKLP--DKIVAYSTGNHGQAVAYASKLFGIKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 92 ILVMPDTMSQERRNLLRAYGAELVLTPG-AEgmkgAIKKAEELAEEHGYFMPQqfSNEANAEIHRRTTGKEILEQFDGEL 170
Cdd:PRK06608 99 RIYLPLNTSKVKQQAALYYGGEVILTNTrQE----AEEKAKEDEEQGFYYIHP--SDSDSTIAGAGTLCYEALQQLGFSP 172
|
..
gi 157679613 171 DA 172
Cdd:PRK06608 173 DA 174
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
7-210 |
1.26e-09 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 58.61 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 7 SVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMI----EDAEAKGTLKAgdtliepTSGNTGIGLAM 82
Cdd:PRK09224 13 RVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMaqltEEQLARGVITA-------SAGNHAQGVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 83 VAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTpgAEGMKGAIKKAEELAEEHGY-FmpqqfsneanaeIH------- 154
Cdd:PRK09224 86 SAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLH--GDSFDEAYAHAIELAEEEGLtF------------IHpfddpdv 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157679613 155 ---RRTTGKEILEQFDGELDA-FIAgvgtggtitgageV------------LKEAIPSIQLYAVEPTDSPVL 210
Cdd:PRK09224 152 iagQGTIAMEILQQHPHPLDAvFVP-------------VggggliagvaayIKQLRPEIKVIGVEPEDSACL 210
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
15-138 |
1.64e-09 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 57.91 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKlnrlvdeDSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTlkagDTLIEPTSGNTGIGLAMVAAAKGINAILV 94
Cdd:PRK08329 65 TPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVF 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 157679613 95 MPDTMSQERRNLLRAYGAELVLTPGAEgMKgAIKKAEELAEEHG 138
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAELHFVEGDR-ME-VHEEAVKFSKRNN 175
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
63-173 |
9.08e-09 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 56.04 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 63 KAGD-TLIEPTSGNTGIGLAMVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGaeGMKGAIKKAEELAEEHGYFM 141
Cdd:PRK08206 113 KLGDiTFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDG--NYDDSVRLAAQEAQENGWVV 190
|
90 100 110
....*....|....*....|....*....|....*...
gi 157679613 142 PQQFSNEANAEIHRR------TTGKEILEQFDGELDAF 173
Cdd:PRK08206 191 VQDTAWEGYEEIPTWimqgygTMADEAVEQLKEMGVPP 228
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
29-141 |
3.77e-08 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 53.84 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 29 ADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGdtLIEPTSGNTGIGLAMVAAAKGINAILVMPDTMSQERRNLLR 108
Cdd:PRK06110 36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMR 113
|
90 100 110
....*....|....*....|....*....|...
gi 157679613 109 AYGAELVltPGAEGMKGAIKKAEELAEEHGYFM 141
Cdd:PRK06110 114 ALGAELI--EHGEDFQAAREEAARLAAERGLHM 144
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
13-169 |
1.96e-07 |
|
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: 51.61 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 13 GNTPVVKLNRLVDE-DSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTlkagDTLIEPTSGNTGIGLAMVAAAKGINA 91
Cdd:TIGR00260 21 GVTPLFRAPALAANvGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 92 ILVMP-DTMSQERRNLLRAYGAELVltpgaeGMKGAIKKAEELAEEHGYFMPQQFSNEANAEIHR----RTTGKEILEQF 166
Cdd:TIGR00260 97 VVLYPaGKISLGKLAQALGYNAEVV------AIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRlegqKTYAFEAVEQL 170
|
...
gi 157679613 167 DGE 169
Cdd:TIGR00260 171 GWE 173
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
2-165 |
7.88e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 49.58 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 2 ARIANSVFElignTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIA----LAMIEDAEAKGTLKAgdtliepTSGNTG 77
Cdd:PRK07476 11 RRIAGRVRR----TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGAtnalLSLSAQERARGVVTA-------STGNHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 78 IGLAMVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEgmKGAIKKAEELAEEHGYFMPQQFSNEANAEiHRRT 157
Cdd:PRK07476 80 RALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQ--DDAQAEVERLVREEGLTMVPPFDDPRIIA-GQGT 156
|
....*...
gi 157679613 158 TGKEILEQ 165
Cdd:PRK07476 157 IGLEILEA 164
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
15-173 |
9.25e-07 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 49.63 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIE--DAEAKgtlKAGdtLIEPTSGNTGIGLAMVAAAKGINAI 92
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSqfSPEQR---RAG--VVTFSSGNHAQAIALSARLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 93 LVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIkkAEELAEEHG------YFMPQQFSNEAnaeihrrTTGKEILEQF 166
Cdd:PRK07048 100 IVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEI--GRRLAEERGltlippYDHPHVIAGQG-------TAAKELFEEV 170
|
....*..
gi 157679613 167 dGELDAF 173
Cdd:PRK07048 171 -GPLDAL 176
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
4-207 |
1.56e-06 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 49.53 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 4 IANSVFELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMIEDAeAKGTLKAGdtLIEPTSGNTGIGLAMV 83
Cdd:PLN02550 99 LSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKL-PKEQLDKG--VICSSAGNHAQGVALS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 84 AAAKGINAILVMPDTMSQERRNLLRAYGAELVLTpgAEGMKGAIKKAEELAEEHGYFMPQQFSNeANAEIHRRTTGKEIL 163
Cdd:PLN02550 176 AQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLV--GDSYDEAQAYAKQRALEEGRTFIPPFDH-PDVIAGQGTVGMEIV 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 157679613 164 EQFDGELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPTDS 207
Cdd:PLN02550 253 RQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDA 296
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
2-176 |
2.72e-05 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 45.27 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 2 ARIANSVFElignTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIAL----AMIEDAEAKGtlkagdtLIEPTSGNTG 77
Cdd:PRK07334 15 ARLAGQVLR----TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALnkllLLTEEERARG-------VIAMSAGNHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 78 IGLAMVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTpgAEGMKGAIKKAEELAEEHGYFMPQQFSNEANAEiHRRT 157
Cdd:PRK07334 84 QGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLH--GETLDEARAHARELAEEEGLTFVHPYDDPAVIA-GQGT 160
|
170
....*....|....*....
gi 157679613 158 TGKEILEQfDGELDAFIAG 176
Cdd:PRK07334 161 VALEMLED-APDLDTLVVP 178
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
10-169 |
6.59e-05 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 44.03 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 10 ELIGNTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIALAMI----EDAEAKGTLKAgdtliepTSGNTGIGLAMVAA 85
Cdd:PRK08639 21 DVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAIsqlsDEELAAGVVCA-------SAGNHAQGVAYACR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 86 AKGINAILVMPDTMSQERRNLLRAYGA---ELVLTpgaegmkG-----AIKKAEELAEEHGYFMPQQFSNEANAEiHRRT 157
Cdd:PRK08639 94 HLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLV-------GdtfddSAAAAQEYAEETGATFIPPFDDPDVIA-GQGT 165
|
170
....*....|..
gi 157679613 158 TGKEILEQFDGE 169
Cdd:PRK08639 166 VAVEILEQLEKE 177
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
49-134 |
1.55e-04 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 42.59 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 49 ALAMIEDAeakGTLKAGDTLIEpTSGNTGIGLAMV--AAAKGINAILVMPDTMSQER-RNLLRAYGAELVLT-------P 118
Cdd:cd08290 134 AYRLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLTeeelrslL 209
|
90
....*....|....*.
gi 157679613 119 GAEGMKGAIKKAEELA 134
Cdd:cd08290 210 ATELLKSAPGGRPKLA 225
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
14-135 |
4.21e-04 |
|
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: 41.52 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 14 NTPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDR-IALAMIEDAEAKGTLKAGdtLIEPTSGNTGIGLAMVAAAKGINAI 92
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 157679613 93 LVMPDTMSQERRNLLRAYGAELVLTpGAEGMKGAIKKAEELAE 135
Cdd:cd06448 79 IVVPESTKPRVVEKLRDEGATVVVH-GKVWWEADNYLREELAE 120
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
7-170 |
7.05e-04 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 40.95 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 7 SVFEliGNTPVVKLNRLVDE--DSADVYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAGDTLIE-PTSGNTGIGLAMV 83
Cdd:PLN02569 128 SLFE--GNSNLFWAERLGKEflGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAKPVVGVGcASTGDTSAALSAY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 84 AAAKGINAILVMP-DTMSQERRNLLRAYGAeLVLTPGAEgMKGAIKKAEELAEEhgyfMPQQFSNEANA-EIH-RRTTGK 160
Cdd:PLN02569 206 CAAAGIPSIVFLPaDKISIAQLVQPIANGA-LVLSIDTD-FDGCMRLIREVTAE----LPIYLANSLNSlRLEgQKTAAI 279
|
170
....*....|
gi 157679613 161 EILEQFDGEL 170
Cdd:PLN02569 280 EILQQFDWEV 289
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
59-131 |
1.02e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 40.00 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157679613 59 KGTLKAGDT-LIEptsGNTGIGLAMVAAAKGINAILVMPDtMSQERRNLLRAYGAELVLTPGAEGMKGAIKKAE 131
Cdd:cd05188 129 AGVLKPGDTvLVL---GAGGVGLLAAQLAKAAGARVIVTD-RSDEKLELAKELGADHVIDYKEEDLEEELRLTG 198
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
31-139 |
1.72e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 39.61 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 31 VYLKLEYMNPGSSVKDRIALAMIEDAEAKGTLKAgdtLIEPTSGNTGIGLAMVAAAKGINAILVMPDTMSQERRNLLRAY 110
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERP---VICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHW 126
|
90 100
....*....|....*....|....*....
gi 157679613 111 GAelVLTPGAEGMKGAIKKAEELAEEHGY 139
Cdd:PRK08813 127 GA--TVRQHGNSYDEAYAFARELADQNGY 153
|
|
| PLN02970 |
PLN02970 |
serine racemase |
15-205 |
2.04e-03 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 39.28 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 15 TPVVKLNRLVDEDSADVYLKLEYMNPGSSVKDRIA----LAMIEDAEAKGTLKAgdtliepTSGNTGIGLAMVAAAKGIN 90
Cdd:PLN02970 28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGAcnaiFSLSDDQAEKGVVTH-------SSGNHAAALALAAKLRGIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 91 AILVMPDTMSQERRNLLRAYGAELVLTPGAEGMKGAIkkAEELAEE------HGYFMPQQFSNEAnaeihrrTTGKEILE 164
Cdd:PLN02970 101 AYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAV--AARVQQEtgavliHPYNDGRVISGQG-------TIALEFLE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157679613 165 QFDgELDAFIAGVGTGGTITGAGEVLKEAIPSIQLYAVEPT 205
Cdd:PLN02970 172 QVP-ELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPK 211
|
|
| quinone_oxidoreductase_like_1 |
cd08243 |
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ... |
62-140 |
4.05e-03 |
|
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.
Pssm-ID: 176205 [Multi-domain] Cd Length: 320 Bit Score: 38.36 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 62 LKAGDT-LIEptSGNTGIGLAMVAAAKGINAIlVMPDTMSQERRNLLRAYGAELVLTPgaegmKGAIkkAEELAEEHGYF 140
Cdd:cd08243 140 LQPGDTlLIR--GGTSSVGLAALKLAKALGAT-VTATTRSPERAALLKELGADEVVID-----DGAI--AEQLRAAPGGF 209
|
|
| Zn_ADH2 |
cd08256 |
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ... |
56-138 |
5.62e-03 |
|
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176218 [Multi-domain] Cd Length: 350 Bit Score: 38.16 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157679613 56 AEAKGTLKAGDTLIepTSGNTGIGLAMVAAAKGINAILVMPDTMSQERRNLLRAYGAELVLTPGAEgmkGAIKKAEELAE 135
Cdd:cd08256 166 AVDRANIKFDDVVV--LAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALARKFGADVVLNPPEV---DVVEKIKELTG 240
|
...
gi 157679613 136 EHG 138
Cdd:cd08256 241 GYG 243
|
|
| |
