|
Name |
Accession |
Description |
Interval |
E-value |
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
7-303 |
3.98e-171 |
|
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: 476.09 E-value: 3.98e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 7 VSELIGKTPIVKLNRIvESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLAMVAAAK 86
Cdd:TIGR01139 1 ISELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 87 GYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATELAKEHG--YFIPQQFQNQSNPEIHRLTTGPEIVEQ 164
Cdd:TIGR01139 80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPnsYFMLQQFENPANPEIHRKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 165 MGDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGGKPGPHKIQGIGAGFIPETLDVKVYDEIIQVKT 244
Cdd:TIGR01139 160 TDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSD 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1266734508 245 EQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVIIPSNGERYLSTPLY 303
Cdd:TIGR01139 240 EEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLSTPLF 298
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
1-300 |
9.34e-171 |
|
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: 474.92 E-value: 9.34e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 1 MRVAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLA 80
Cdd:COG0031 1 MRIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 81 MVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATELAKEH-GYFIPQQFQNQSNPEIHRLTTGP 159
Cdd:COG0031 81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETpGAFWPNQFENPANPEAHYETTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 160 EIVEQMGDQLDAFiagigtggtitgageV---------------LKEAYKDIKIYAVEPADSPVLSGGKPGPHKIQGIGA 224
Cdd:COG0031 161 EIWEQTDGKVDAF---------------VagvgtggtitgvgryLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266734508 225 GFIPETLDVKVYDEIIQVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVIIPSNGERYLST 300
Cdd:COG0031 226 GFVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
7-303 |
6.46e-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: 445.19 E-value: 6.46e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 7 VSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLAMVAAAK 86
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 87 GYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATELAKE-HGYFIPQQFQNQSNPEIHRLTTGPEIVEQM 165
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAEtNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 166 GDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGGKPGPHKIQGIGAGFIPETLDVKVYDEIIQVKTE 245
Cdd:TIGR01136 161 DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1266734508 246 QAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKV-LVIIPSNGERYLSTPLY 303
Cdd:TIGR01136 241 DAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKViVAILPDTGERYLSTGLF 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
12-299 |
5.68e-151 |
|
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: 424.62 E-value: 5.68e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 12 GKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLAMVAAAKGYKAI 91
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 92 LVMPETMSIERRNLLRAYGAELVLTPGPE--GMGGAIRKATELAKEH-GYFIPQQFQNQSNPEIHRLTTGPEIVEQMGDQ 168
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETpNAFWLNQFENPANPEAHYETTAPEIWEQLDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 169 LDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGGKPGPHKIQGIGAGFIPETLDVKVYDEIIQVKTEQAF 248
Cdd:cd01561 161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEAF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1266734508 249 EYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVIIPSNGERYLS 299
Cdd:cd01561 241 AMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
2-304 |
6.19e-114 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 331.89 E-value: 6.19e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 2 RVAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTI-IEPTSGNTGIGLA 80
Cdd:PLN02565 4 SIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 81 MVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATE-LAKEHGYFIPQQFQNQSNPEIHRLTTGP 159
Cdd:PLN02565 84 FMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEiLAKTPNSYILQQFENPANPKIHYETTGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 160 EIVEQMGDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGGKPGPHKIQGIGAGFIPETLDVKVYDEI 239
Cdd:PLN02565 164 EIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266734508 240 IQVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVII-PSNGERYLSTPLYQ 304
Cdd:PLN02565 244 VQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIfPSFGERYLSSVLFE 309
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
1-300 |
3.05e-108 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 317.57 E-value: 3.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 1 MRVAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLA 80
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 81 MVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGP------EGMGGAIRKATELAK--EHGYFIPQQFQNQSNPEI 152
Cdd:PRK10717 81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVAsePNGAIWANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 153 HRLTTGPEIVEQMGDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSP----VLSG--GKPGPHKIQGIGAGF 226
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAlysyYKTGelKAEGSSITEGIGQGR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1266734508 227 IPETLDVKVYDEIIQVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVIIPSNGERYLST 300
Cdd:PRK10717 241 ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK 314
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
3-304 |
3.14e-105 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 310.01 E-value: 3.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 3 VAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEG-DTIIEPTSGNTGIGLAM 81
Cdd:PLN00011 7 IKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 82 VAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATE-LAKEHGYFIPQQFQNQSNPEIHRLTTGPE 160
Cdd:PLN00011 87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEiLSKTPGGYIPQQFENPANPEIHYRTTGPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 161 IVEQMGDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGGKPGPHKIQGIGAGFIPETLDVKVYDEII 240
Cdd:PLN00011 167 IWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEII 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1266734508 241 QVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVII-PSNGERYLSTPLYQ 304
Cdd:PLN00011 247 QVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIfPSGGERYLSTKLFE 311
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
2-304 |
2.29e-99 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 296.49 E-value: 2.29e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 2 RVAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDT-IIEPTSGNTGIGLA 80
Cdd:PLN02556 48 KIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 81 MVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATELAKEH-GYFIPQQFQNQSNPEIHRLTTGP 159
Cdd:PLN02556 128 FMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTpDAFMLQQFSNPANTQVHFETTGP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 160 EIVEQMGDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGGKPGPHKIQGIGAGFIPETLDVKVYDEI 239
Cdd:PLN02556 208 EIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKV 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266734508 240 IQVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKG-KKVLVIIPSNGERYLSTPLYQ 304
Cdd:PLN02556 288 LEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKgKLIVTVHPSFGERYLSSVLFQ 353
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
1-304 |
4.78e-95 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 287.83 E-value: 4.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 1 MRVAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTI-IEPTSGNTGIGL 79
Cdd:PLN03013 111 LNIADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 80 AMVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATELAKEH-GYFIPQQFQNQSNPEIHRLTTG 158
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTpDAYMLQQFDNPANPKIHYETTG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 159 PEIVEQMGDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGGKPGPHKIQGIGAGFIPETLDVKVYDE 238
Cdd:PLN03013 271 PEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDE 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1266734508 239 IIQVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVII-PSNGeRYLSTPLYQ 304
Cdd:PLN03013 351 VIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSlFASG-RDIYTPRCS 416
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
6-303 |
3.99e-89 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 267.89 E-value: 3.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 6 SVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLAMVAAA 85
Cdd:PRK11761 5 TLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 86 KGYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATELAKEHGYFIPQQFQNQSNPEIHRLTTGPEIVEQM 165
Cdd:PRK11761 85 KGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEIWRQT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 166 GDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPvlsggkpgphKIQGI---GAGFIPETLDVKVYDEIIQV 242
Cdd:PRK11761 165 EGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGS----------SIPGIrrwPEEYLPKIFDASRVDRVLDV 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1266734508 243 KTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAkKLGKGKKVLVIIPSNGERYLSTPLY 303
Cdd:PRK11761 235 SQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIA-RENPNAVIVAIICDRGDRYLSTGVF 294
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
3-299 |
2.28e-87 |
|
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: 268.59 E-value: 2.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 3 VAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLAMV 82
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 83 AAAKGYKAILVMPETMSIERRNLLRAYGAELVLTP---GPEGMGGAIRKATELAKE-HGYFIPQQFQNQSNPEIHRLTTG 158
Cdd:TIGR01137 81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPtaaAFDSPESHIGVAKRLVREiPGAHILDQYRNPSNPLAHYDTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 159 PEIVEQMGDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSpVLSGGKP------GPHKIQGIGAGFIPETLD 232
Cdd:TIGR01137 161 PEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTVLD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1266734508 233 VKVYDEIIQVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVII-PSNGERYLS 299
Cdd:TIGR01137 240 RKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLlPDSIRNYMT 307
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
6-303 |
1.94e-79 |
|
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: 242.90 E-value: 1.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 6 SVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLAMVAAA 85
Cdd:TIGR01138 1 TIEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 86 KGYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIRKATELAKEHGYFIPQQFQNQSNPEIHRLTTGPEIVEQM 165
Cdd:TIGR01138 81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFNNPDNPYAHYTSTGPEIWQQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 166 GDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGgkpgphkIQGIGAGFIPETLDVKVYDEIIQVKTE 245
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDIHQR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1266734508 246 QAFEYARRVAKEEGILVGISSGAVIYAATEVAkKLGKGKKVLVIIPSNGERYLSTPLY 303
Cdd:TIGR01138 234 DAENTMRELAVREGIFCGVSSGGAVAAALRLA-RELPDAVVVAIICDRGDRYLSTGVF 290
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
7-300 |
2.44e-75 |
|
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: 232.86 E-value: 2.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 7 VSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLAMVAAAK 86
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 87 GYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMGG----AIRKATEL-AKEHGYFIPQQFQNQSNPEIHRLTTGPEI 161
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGylgtRIARVRELlASIPDAYWPNQYANPDNPRAHYHGTGREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 162 VEQMgDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSpVLSGGKPGPHKIQGIGAGFIPETLDVKVYDEIIQ 241
Cdd:TIGR03945 161 ARAF-PTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGS-VIFGGPPGRRHIPGLGASVVPELLDESLIDDVVH 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1266734508 242 VKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVAKKLGKGKKVLVIIPSNGERYLST 300
Cdd:TIGR03945 239 VPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDT 297
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
14-277 |
1.09e-69 |
|
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: 216.23 E-value: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 14 TPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKeGDTIIEPTSGNTGIGLAMVAAAKGYKAILV 93
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLP-KGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 94 MPETMSIERRNLLRAYGAELVLTPGpeGMGGAIRKATELAKE-HGYFIPQQFQNQSNPEIHRlTTGPEIVEQMGDQ-LDA 171
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGQkPDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 172 FiagigtggtitgageV---------------LKEAYKDIKIYAVEPadspvlsggkpgphkiqgigagfipetldvkvy 236
Cdd:cd00640 157 V---------------VvpvggggniagiaraLKELLPNVKVIGVEP--------------------------------- 188
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1266734508 237 dEIIQVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVA 277
Cdd:cd00640 189 -EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLA 228
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
7-277 |
7.44e-69 |
|
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: 216.02 E-value: 7.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 7 VSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKgllKEGDTIIEPTSGNTGIGLAMVAAAK 86
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 87 GYKAILVMPETMSIERRNLLRAYGAELVLTPGpeGMGGAIRKATELAKE-HGYFIPQQFQNQSNPEIHRlTTGPEIVEQM 165
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYG-TIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 166 GDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVLSGG---------KPGPHKIQGIGAGFIPETLDVKVY 236
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDLL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1266734508 237 ----DEIIQVKTEQAFEYARRVAKEEGILVGISSGAVIYAATEVA 277
Cdd:pfam00291 235 deyvGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLAL 279
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
9-299 |
3.90e-32 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 123.56 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 9 ELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKEGDTIIEPTSGNTGIGLAMVAAAKGY 88
Cdd:PLN02356 49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 89 KAILVMPETMSIERRNLLRAYGAE------LVLTPGPEGMGGAIRK---ATELAKEH----------------------- 136
Cdd:PLN02356 129 KCHVVIPDDVAIEKSQILEALGATvervrpVSITHKDHYVNIARRRaleANELASKRrkgsetdgihlektngciseeek 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 137 ----------GYFIPQQFQNQSNPEIHRLTTGPEIVEQMGDQLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADS 206
Cdd:PLN02356 209 enslfsssctGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 207 PVLSG-------------GK----PGPHKIQGIGAGFIPETLDVKVYDEIIQVKTEQAFEYARRVAKEEGILVGISSGAV 269
Cdd:PLN02356 289 GLFNKvtrgvmytreeaeGRrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMN 368
|
330 340 350
....*....|....*....|....*....|
gi 1266734508 270 IYAATEVAKKLGKGKKVLVIIPSNGERYLS 299
Cdd:PLN02356 369 CVGAVRVAQSLGPGHTIVTILCDSGMRHLS 398
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
2-273 |
6.41e-19 |
|
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: 85.47 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 2 RVAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMI----EDAEKKGllkegdtIIEPTSGNTGI 77
Cdd:COG1171 13 AAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALaslsEEERARG-------VVAASAGNHAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 78 GLAMVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPG--PEgmggAIRKATELAKEHGY-FIPqqfqnqsnPEIHR 154
Cdd:COG1171 86 GVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDtyDD----AEAAAAELAEEEGAtFVH--------PFDDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 155 L------TTGPEIVEQMGDqLDAfiagigtggtitgageV----------------LKEAYKDIKIYAVEPADSPV---- 208
Cdd:COG1171 154 DviagqgTIALEILEQLPD-LDA----------------VfvpvggggliagvaaaLKALSPDIRVIGVEPEGAAAmyrs 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1266734508 209 LSGGKP----GPHKI-QGIGAGFI-PETLDV--KVYDEIIQVKTEQAFEYARRVAKEEGILVGiSSGAVIYAA 273
Cdd:COG1171 217 LAAGEPvtlpGVDTIaDGLAVGRPgELTFEIlrDLVDDIVTVSEDEIAAAMRLLLERTKIVVE-PAGAAALAA 288
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
12-169 |
5.03e-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: 82.64 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 12 GKTPIVKLNRIVESDSA-DVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLlkegDTIIEPTSGNTGIGLAMVAAAKGYKA 90
Cdd:cd01563 21 GNTPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 91 ILVMPETMSIERRNLLRAYGAELVLTPGpeGMGGAIRKATELAKEHGYFipqqFQNQSNPeiHRL----TTGPEIVEQMG 166
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAVEG--NFDDALRLVRELAEENWIY----LSNSLNP--YRLegqkTIAFEIAEQLG 168
|
...
gi 1266734508 167 DQL 169
Cdd:cd01563 169 WEV 171
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
4-273 |
7.62e-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: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 4 AQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMI----EDAEKKGllkegdtIIEPTSGNTGIGL 79
Cdd:cd01562 8 AARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 80 AMVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTpgPEGMGGAIRKATELAKEHGY-FIPqqfqnqsnPEIHRL--- 155
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEGLtFIH--------PFDDPDvia 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 156 ---TTGPEIVEQMGDqLDAfiagigtggtitgageV----------------LKEAYKDIKIYAVEPADSPVLS----GG 212
Cdd:cd01562 151 gqgTIGLEILEQVPD-LDA----------------VfvpvggggliagiataVKALSPNTKVIGVEPEGAPAMAqslaAG 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1266734508 213 KPGPHKIQGIGAGFI------PETLDV--KVYDEIIQVkTEQAFEYARRVAKEEGILVGISSGAVIYAA 273
Cdd:cd01562 214 KPVTLPEVDTIADGLavkrpgELTFEIirKLVDDVVTV-SEDEIAAAMLLLFEREKLVAEPAGALALAA 281
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
12-172 |
8.73e-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: 82.94 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 12 GKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDR---IALAMiedaekkgLLKEG-DTIIEPTSGNTGIGLAMVAAAKG 87
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRamqVAVSL--------ALERGaKTIVCASSGNGSAALAAYAARAG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 88 YKAILVMPET-MSIERRNLLRAYGAELVLTPGpeGMGGAIRKATELAKEHGYFIpqqfqnqSNPeIH--RL----TTGPE 160
Cdd:COG0498 137 IEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDG--NFDDAQRLVKELAADEGLYA-------VNS-INpaRLegqkTYAFE 206
|
170
....*....|..
gi 1266734508 161 IVEQMGDQLDAF 172
Cdd:COG0498 207 IAEQLGRVPDWV 218
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
12-139 |
7.52e-13 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 67.81 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 12 GKTPIVKLNRI-VESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLlkegDTIIEPTSGNTGIGLAMVAAAKGYKA 90
Cdd:PRK06381 14 GGTPLLRARKLeEELGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1266734508 91 ILVMPETMSIERRNLLRAYGAELVLTPGPegMGGAIRKATELAKEHGYF 139
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYVDGK--YEEAVERSRKFAKENGIY 136
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
14-209 |
5.40e-12 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 65.10 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 14 TPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIA----LAMIEDAEKKGllkegdtIIEPTSGNTGIGLAMVAAAKGYK 89
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGAsnklRLLNEAQRQQG-------VITASSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 90 AILVMPETMSIERRNLLRAYGAELVLTPGPegMGGAIRKATELAKEHG------YFIPQQFQNQSnpeihrlTTGPEIVE 163
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVRLYGGD--ALNAELAARRAAEQQGkvyispYNDPQVIAGQG-------TIGMELVE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1266734508 164 QMGDqLDAFIAGIGTGGTITGAGEVLKEAYKDIKIYAVEPADSPVL 209
Cdd:PRK06815 165 QQPD-LDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSL 209
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
5-167 |
7.34e-12 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 65.14 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 5 QSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIA---LAMIEDAEK-KGllkegdtIIEPTSGNTGIGLA 80
Cdd:PRK08638 19 QRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKrKG-------VVACSAGNHAQGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 81 MVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTpgPEGMGGAIRKATELAKEHGYFIPQQFqnqSNPEI--HRLTTG 158
Cdd:PRK08638 92 LSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLH--GDNFNDTIAKVEEIVEEEGRTFIPPY---DDPKViaGQGTIG 166
|
....*....
gi 1266734508 159 PEIVEQMGD 167
Cdd:PRK08638 167 LEILEDLWD 175
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
12-166 |
2.79e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 63.22 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 12 GKTPIVKLNrivesdsaDVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLlkegDTIIEPTSGNTGIGLAMVAAAKGYKAI 91
Cdd:PRK06450 57 GRTPLIKKG--------NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVK 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1266734508 92 LVMPETMSIERRNLLRAYGAELVLTpgpEGMGGAIRKATElaKEHGYFIPQQFQNQSNPEIHRLTTgpEIVEQMG 166
Cdd:PRK06450 125 IFVPETASGGKLKQIESYGAEVVRV---RGSREDVAKAAE--NSGYYYASHVLQPQFRDGIRTLAY--EIAKDLD 192
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
12-169 |
1.14e-10 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 61.56 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 12 GKTPIVKLNRIV-ESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKegdtIIEPTSGNTGIGLAMVAAAKGYKA 90
Cdd:PRK08197 78 GMTPLLPLPRLGkALGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARAGIRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 91 ILVMPETMSIERRNLLRAYGAELVLTPGPEGMGGAIrkATELAKEHGYFIPQQFQnqsnpEIHRL----TTGPEIVEQMG 166
Cdd:PRK08197 154 TIFMPADAPEITRLECALAGAELYLVDGLISDAGKI--VAEAVAEYGWFDVSTLK-----EPYRIegkkTMGLELAEQLG 226
|
...
gi 1266734508 167 DQL 169
Cdd:PRK08197 227 WRL 229
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
4-167 |
7.24e-10 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 58.81 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 4 AQSVSELIGKTPIVKLnRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKkgllkEGDTIIEPTSGNTGIGLAMVA 83
Cdd:PRK08246 14 AQRIAPHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 84 AAKGYKAILVMPETMSIERRNLLRAYGAELVLtpGPEGMGGAIRKATELAKE------HGYFIPQQFQNQSnpeihrlTT 157
Cdd:PRK08246 88 AALGVPATVFVPETAPPAKVARLRALGAEVVV--VGAEYADALEAAQAFAAEtgallcHAYDQPEVLAGAG-------TL 158
|
170
....*....|
gi 1266734508 158 GPEIVEQMGD 167
Cdd:PRK08246 159 GLEIEEQAPG 168
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
14-167 |
1.81e-09 |
|
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: 58.22 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 14 TPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLlKEGdtIIEPTSGNTGIGLAMVAAAKGYKAILV 93
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQR-QRG--VVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1266734508 94 MPETMSIERRNLLRAYGAELVLtpgpEG--MGGAIRKATELAKEHGYFIPQQFQnqsNPEI--HRLTTGPEIVEQMGD 167
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVIL----HGddYDEAYAFATSLAEEEGRVFVHPFD---DEFVmaGQGTIGLEIMEDIPD 148
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
5-141 |
3.57e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 57.09 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 5 QSVSELIGKTPIVK---LNRIVesdSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKegDTIIEPTSGNTGIGLAM 81
Cdd:PRK06608 15 NRIKQYLHLTPIVHsesLNEML---GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLP--DKIVAYSTGNHGQAVAY 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1266734508 82 VAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPG-PEgmggAIRKATELAKEHGYFIP 141
Cdd:PRK06608 90 ASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTrQE----AEEKAKEDEEQGFYYIH 146
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
30-206 |
9.84e-09 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 55.96 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 30 VYLKLEFMNPGSSVKDRIA---LAMIEDAEKkgllkeGDTIIEPTSGNTGIGLAMVAAAKGYKAILVMPETMSIERRNLL 106
Cdd:PRK12483 54 VLLKREDLQPVFSFKIRGAynkMARLPAEQL------ARGVITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 107 RAYGAELVLTPgpEGMGGAIRKATELAKEHGY-FIPQQfqnqSNPEI--HRLTTGPEIVEQMGDQLDAFIAGIGTGGTIT 183
Cdd:PRK12483 128 RAHGGEVVLHG--ESFPDALAHALKLAEEEGLtFVPPF----DDPDViaGQGTVAMEILRQHPGPLDAIFVPVGGGGLIA 201
|
170 180
....*....|....*....|...
gi 1266734508 184 GAGEVLKEAYKDIKIYAVEPADS 206
Cdd:PRK12483 202 GIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
13-209 |
1.29e-08 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 55.53 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 13 KTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIALAMI----EDAEKKGllkegdtIIEPTSGNTGIGLAMVAAAKGY 88
Cdd:PRK09224 20 ETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMaqltEEQLARG-------VITASAGNHAQGVALSAARLGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 89 KAILVMPETMSIERRNLLRAYGAELVLTpGpEGMGGAIRKATELAKEHGY-FIPqqfqnqsnPEIHRL------TTGPEI 161
Cdd:PRK09224 93 KAVIVMPVTTPDIKVDAVRAFGGEVVLH-G-DSFDEAYAHAIELAEEEGLtFIH--------PFDDPDviagqgTIAMEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1266734508 162 VEQMGDQLDA-FiagigtggtitgageV--------------LKEAYKDIKIYAVEPADSPVL 209
Cdd:PRK09224 163 LQQHPHPLDAvF---------------VpvggggliagvaayIKQLRPEIKVIGVEPEDSACL 210
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
66-172 |
2.87e-08 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 54.50 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 66 TIIEPTSGNTGIGLAMVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGpeGMGGAIRKATELAKEHGYFIPQQFQ 145
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDG--NYDDSVRLAAQEAQENGWVVVQDTA 195
|
90 100 110
....*....|....*....|....*....|...
gi 1266734508 146 NQSNPEIHRL------TTGPEIVEQMGDQLDAF 172
Cdd:PRK08206 196 WEGYEEIPTWimqgygTMADEAVEQLKEMGVPP 228
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
14-113 |
3.46e-08 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 54.06 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 14 TPIVKlnrivesDSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLlkegDTIIEPTSGNTGIGLAMVAAAKGYKAILV 93
Cdd:PRK08329 65 TPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVF 133
|
90 100
....*....|....*....|
gi 1266734508 94 MPETMSIERRNLLRAYGAEL 113
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAEL 153
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
12-139 |
1.03e-07 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 52.89 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 12 GKTPIVKlNRIVESDSADVYLKLEFMNPGSSVKDRIALAMIEDaekkGLLKEGDTIIEPTSGNTGIGLAMVAAAKGYKAI 91
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSY----GLPYAANGFIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1266734508 92 LVMPETMSIERRNLLRAYGAELVLTpgPEGMGGAIRKATELAKEHGYF 139
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIRY--GESVDEAIEYAEELARLNGLY 185
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
12-168 |
5.51e-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: 50.46 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 12 GKTPIVKLNRIVES-DSADVYLKLEFMNPGSSVKDRIALAMIEDAEKKGLlkegDTIIEPTSGNTGIGLAMVAAAKGYKA 90
Cdd:TIGR00260 21 GVTPLFRAPALAANvGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 91 ILVMPETmSIERRNLLRA--YGAELVltpgpeGMGGAIRKATELAKEHGYFIPQQFQNQSNPEIHRL----TTGPEIVEQ 164
Cdd:TIGR00260 97 VVLYPAG-KISLGKLAQAlgYNAEVV------AIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLegqkTYAFEAVEQ 169
|
....
gi 1266734508 165 MGDQ 168
Cdd:TIGR00260 170 LGWE 173
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
28-141 |
2.47e-06 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 48.07 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 28 ADVYLKLEFMNPGSSVKDRIALAMIEDaekkgLLKEGDT---IIEPTSGNTGIGLAMVAAAKGYKAILVMPETMSIERRN 104
Cdd:PRK06110 36 CEVWVKHENHTPTGAFKVRGGLVYFDR-----LARRGPRvrgVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNA 110
|
90 100 110
....*....|....*....|....*....|....*...
gi 1266734508 105 LLRAYGAELVltPGPEGMGGAIRKATELAKEHGY-FIP 141
Cdd:PRK06110 111 AMRALGAELI--EHGEDFQAAREEAARLAAERGLhMVP 146
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
30-206 |
2.97e-05 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 45.30 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 30 VYLKLEFMNPGSSVKDRIALAMIEDAEKKGLLKegdTIIEPTSGNTGIGLAMVAAAKGYKAILVMPETMSIERRNLLRAY 109
Cdd:PLN02550 126 VLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDK---GVICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 110 GAELVLTPgpEGMGGAIRKATELAKEHG-YFIPQQfqnqSNPEI--HRLTTGPEIVEQMGDQLDAFIAGIGTGGTITGAG 186
Cdd:PLN02550 203 GATVVLVG--DSYDEAQAYAKQRALEEGrTFIPPF----DHPDViaGQGTVGMEIVRQHQGPLHAIFVPVGGGGLIAGIA 276
|
170 180
....*....|....*....|
gi 1266734508 187 EVLKEAYKDIKIYAVEPADS 206
Cdd:PLN02550 277 AYVKRVRPEVKIIGVEPSDA 296
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
48-116 |
6.48e-05 |
|
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: 44.13 E-value: 6.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1266734508 48 ALAMIEDAEKkglLKEGDTIIEpTSGNTGIGLAMV--AAAKGYKAILVMPETMSIER-RNLLRAYGAELVLT 116
Cdd:cd08290 134 AYRLLEDFVK---LQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
2-167 |
2.93e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 41.87 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 2 RVAQSVSELIGKTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDRIA----LAMIEDAEKKGllkegdtIIEPTSGNTGI 77
Cdd:PRK07476 8 RARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGAtnalLSLSAQERARG-------VVTASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 78 GLAMVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGP--EGMGGAIRkateLAKEHGY-FIPqQFQnqsNPEI-- 152
Cdd:PRK07476 81 ALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSqdDAQAEVER----LVREEGLtMVP-PFD---DPRIia 152
|
170
....*....|....*
gi 1266734508 153 HRLTTGPEIVEQMGD 167
Cdd:PRK07476 153 GQGTIGLEILEALPD 167
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
13-115 |
5.56e-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: 41.13 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 13 KTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDR-IALAMIEDAEKKGLLKEGdtIIEPTSGNTGIGLAMVAAAKGYKAI 91
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCT 78
|
90 100
....*....|....*....|....*..
gi 1266734508 92 LVMPET---MSIERrnlLRAYGAELVL 115
Cdd:cd06448 79 IVVPEStkpRVVEK---LRDEGATVVV 102
|
|
| butanediol_DH_like |
cd08233 |
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ... |
50-131 |
1.29e-03 |
|
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. 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. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.
Pssm-ID: 176195 [Multi-domain] Cd Length: 351 Bit Score: 39.83 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 50 AMIE------DAEKKGLLKEGDTIIEPTSGNtgIGLAMVAAAKGYKAILVMPETMSIERRNLLRAYGAELVLTPGPEGMG 123
Cdd:cd08233 153 ALVEplavawHAVRRSGFKPGDTALVLGAGP--IGLLTILALKAAGASKIIVSEPSEARRELAEELGATIVLDPTEVDVV 230
|
....*...
gi 1266734508 124 GAIRKATE 131
Cdd:cd08233 231 AEVRKLTG 238
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
30-138 |
5.61e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 38.07 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 30 VYLKLEFMNPGSSVKDRIAL-AMIEDAEKkgllkeGDT--IIEPTSGNTGIGLAMVAAAKGYKAILVMPetmsierrnll 106
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALnALLAGLER------GDErpVICASAGNHAQGVAWSAYRLGVQAITVMP----------- 112
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1266734508 107 raYGAELVLTPGPEGMGGAIRK-----------ATELAKEHGY 138
Cdd:PRK08813 113 --HGAPQTKIAGVAHWGATVRQhgnsydeayafARELADQNGY 153
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
55-130 |
8.53e-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: 37.30 E-value: 8.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266734508 55 AEKKGLLKEGDTIIepTSGNTGIGLAMVAAAKGYKAILVMPEtMSIERRNLLRAYGAELVLTPGPEGMGGAIRKAT 130
Cdd:cd05188 126 LRRAGVLKPGDTVL--VLGAGGVGLLAAQLAKAAGARVIVTD-RSDEKLELAKELGADHVIDYKEEDLEEELRLTG 198
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
13-172 |
9.74e-03 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 37.31 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 13 KTPIVKLNRIVESDSADVYLKLEFMNPGSSVKDR---IALAMIEDAEKKGllkegdTIIEPTSGNTGIGLAMVAAAKGYK 89
Cdd:PRK07048 24 RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRgayNALSQFSPEQRRA------GVVTFSSGNHAQAIALSARLLGIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266734508 90 AILVMPETMSIERRNLLRAYGAELVL----TPGPEGMGgairkaTELAKEHG------YFIPQQFQNQSnpeihrlTTGP 159
Cdd:PRK07048 98 ATIVMPQDAPAAKVAATRGYGGEVVTydryTEDREEIG------RRLAEERGltlippYDHPHVIAGQG-------TAAK 164
|
170
....*....|...
gi 1266734508 160 EIVEQMGDqLDAF 172
Cdd:PRK07048 165 ELFEEVGP-LDAL 176
|
|
| |
