|
Name |
Accession |
Description |
Interval |
E-value |
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
3-305 |
7.55e-170 |
|
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: 473.00 E-value: 7.55e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 3 KIYESVTELIGGTPILNAKNFAKqaGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGL 82
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSP--GPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 83 ASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHRATTG 162
Cdd:COG0031 80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 163 PEIWKDTDGKVDIFvagvgtggtvtgigEYLKEQNPDIKVVAVEPATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYDE 242
Cdd:COG0031 160 PEIWEQTDGKVDAFvagvgtggtitgvgRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLIDE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547292877 243 VLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRpENAGKNIVVLLPDTGDRYLST 305
Cdd:COG0031 240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
8-308 |
1.70e-159 |
|
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: 446.43 E-value: 1.70e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 8 VTELIGGTPILNAKNfakQAGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGLASIAA 87
Cdd:TIGR01139 1 ISELIGNTPLVRLNR---IEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 88 AKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEI-EGAFIPSQFENPANPAAHRATTGPEIW 166
Cdd:TIGR01139 78 ARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTpNSYFMLQQFENPANPEIHRKTTGPEIW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 167 KDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYDEVLPI 246
Cdd:TIGR01139 158 RDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547292877 247 ENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPEnAGKNIVVLLPDTGDRYLSTALF 308
Cdd:TIGR01139 238 SDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
8-308 |
2.35e-156 |
|
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: 438.64 E-value: 2.35e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 8 VTELIGGTPILNAKNFAKqaGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGLASIAA 87
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAP--GCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 88 AKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHRATTGPEIWK 167
Cdd:TIGR01136 79 ARGYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEIWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 168 DTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYDEVLPIE 247
Cdd:TIGR01136 159 DTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVS 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547292877 248 NEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAGKNIVVLLPDTGDRYLSTALF 308
Cdd:TIGR01136 239 DEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
13-304 |
4.06e-150 |
|
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: 422.69 E-value: 4.06e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 13 GGTPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGLASIAAAKGYR 92
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAE--IYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 93 IILTMPETMSVERRNLLKAYGAELVLTEGAK--GMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHRATTGPEIWKDTD 170
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 171 GKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYDEVLPIENED 250
Cdd:cd01561 159 GKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 547292877 251 AFAAGRAFAKAEGVLVGISSGAALHAATILANRPEnAGKNIVVLLPDTGDRYLS 304
Cdd:cd01561 239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
4-308 |
7.51e-121 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 349.61 E-value: 7.51e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 4 IYESVTELIGGTPILNAKNFAKqaGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEG-SVIIEPTSGNTGIGL 82
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVD--GCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGeSVLIEPTSGNTGIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 83 ASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHRATTG 162
Cdd:PLN02565 83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 163 PEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYDE 242
Cdd:PLN02565 163 PEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDE 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547292877 243 VLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAGKNIVVLLPDTGDRYLSTALF 308
Cdd:PLN02565 243 VVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLF 308
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
4-308 |
1.26e-110 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 323.88 E-value: 1.26e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 4 IYESVTELIGGTPILNAKNFAKqaGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEG-SVIIEPTSGNTGIGL 82
Cdd:PLN00011 7 IKNDVTELIGNTPMVYLNNIVD--GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 83 ASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHRATTG 162
Cdd:PLN00011 85 ACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 163 PEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYDE 242
Cdd:PLN00011 165 PEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547292877 243 VLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAGKNIVVLLPDTGDRYLSTALF 308
Cdd:PLN00011 245 IIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLF 310
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
3-310 |
1.35e-109 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 321.43 E-value: 1.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 3 KIYESVTELIGGTPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGL 82
Cdd:PRK10717 2 KIFEDVSDTIGNTPLIRLNRASEATGCE--ILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 83 ASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGA------KGMKGAIAKAEELAK-EIEGAFIPSQFENPANPA 155
Cdd:PRK10717 80 ALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVAsEPNGAIWANQFDNPANRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 156 AHRATTGPEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLS---KGEA---GPHKIQGIGAG 229
Cdd:PRK10717 160 AHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyykTGELkaeGSSITEGIGQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 230 FVPDTLNTKIYDEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILAnRPENAGKNIVVLLPDTGDRYLSTALFA 309
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLA-RELGPGHTIVTILCDSGERYQSKLFNP 318
|
.
gi 547292877 310 D 310
Cdd:PRK10717 319 D 319
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
4-308 |
1.43e-106 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 317.10 E-value: 1.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 4 IYESVTELIGGTPILNAKNFAKqaGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEG-SVIIEPTSGNTGIGL 82
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAK--GCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGkSVLVEPTSGNTGIGL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 83 ASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHRATTG 162
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 163 PEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYDE 242
Cdd:PLN03013 271 PEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDE 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547292877 243 VLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAGKNIVVLLPDTGdRYLSTALF 308
Cdd:PLN03013 351 VIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRC 415
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
3-310 |
2.23e-101 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 301.88 E-value: 2.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 3 KIYESVTELIGGTPILNAKNFAKqaGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEG-SVIIEPTSGNTGIG 81
Cdd:PLN02556 48 KIKTDASQLIGKTPLVYLNKVTE--GCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGNMGIS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 82 LASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHRATT 161
Cdd:PLN02556 126 LAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 162 GPEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYD 241
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVME 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547292877 242 EVLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAGKNIVVLLPDTGDRYLSTALFAD 310
Cdd:PLN02556 286 KVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQE 354
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
5-308 |
1.12e-96 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 287.15 E-value: 1.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 5 YESVTELIGGTPILNAKNFAkqAGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGLAS 84
Cdd:PRK11761 3 YPTLEDTIGNTPLVKLQRLP--PDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 85 IAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEIEGaFIPSQFENPANPAAHRATTGPE 164
Cdd:PRK11761 81 IAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEG-KVLDQFANPDNPLAHYETTGPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 165 IWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPatspvlskgEAGPHkIQGI---GAGFVPdtlntKIY- 240
Cdd:PRK11761 160 IWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQP---------EEGSS-IPGIrrwPEEYLP-----KIFd 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547292877 241 ----DEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAgkNIVVLLPDTGDRYLSTALF 308
Cdd:PRK11761 225 asrvDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENPNA--VIVAIICDRGDRYLSTGVF 294
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
4-304 |
2.56e-95 |
|
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: 289.39 E-value: 2.56e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 4 IYESVTELIGGTPILNAKNFAKqaGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGLA 83
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 84 SIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGM---KGAIAKAEELAKEIEGAFIPSQFENPANPAAHRAT 160
Cdd:TIGR01137 79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 161 TGPEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSpVLSKGEA------GPHKIQGIGAGFVPDT 234
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTV 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 235 LNTKIYDEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAGKNIVVLLPDTGDRYLS 304
Cdd:TIGR01137 238 LDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMT 307
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
7-308 |
1.59e-83 |
|
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 253.68 E-value: 1.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 7 SVTELIGGTPILNAKNFAKQAGAnaTLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGLASIA 86
Cdd:TIGR01138 1 TIEQTVGNTPLVRLQRMGPENGS--EVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 87 AAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAEELAKEIEGAFIpSQFENPANPAAHRATTGPEIW 166
Cdd:TIGR01138 79 ALKGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLL-DQFNNPDNPYAHYTSTGPEIW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 167 KDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATspvlskgeagPHKIQGIG---AGFVPDTLNTKIYDEV 243
Cdd:TIGR01138 158 QQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEE----------GSSIPGIRrwpTEYLPGIFDASLVDRV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547292877 244 LPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANrpENAGKNIVVLLPDTGDRYLSTALF 308
Cdd:TIGR01138 228 LDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLAR--ELPDAVVVAIICDRGDRYLSTGVF 290
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
8-305 |
7.19e-76 |
|
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: 234.40 E-value: 7.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 8 VTELIGGTPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGIGLASIAA 87
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFR--LFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 88 AKGYR-IILTMPETMSVErRNLLKAYGAELVLTE---GAKGMKGA-IAKAEELAKEIEGAFIPSQFENPANPAAHRATTG 162
Cdd:TIGR03945 79 YKGLRfICVVDPNISPQN-LKLLRAYGAEVEKVTepdETGGYLGTrIARVRELLASIPDAYWPNQYANPDNPRAHYHGTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 163 PEIWKDTDgKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEpATSPVLSKGEAGPHKIQGIGAGFVPDTLNTKIYDE 242
Cdd:TIGR03945 158 REIARAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVD-AVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547292877 243 VLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAAT-ILANRPENAgkNIVVLLPDTGDRYLST 305
Cdd:TIGR03945 236 VVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKrLLPRIPEGS--TVVAILPDRGERYLDT 297
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
8-297 |
1.36e-70 |
|
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: 220.65 E-value: 1.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 8 VTELIGGTPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKlkeGSVIIEPTSGNTGIGLASIAA 87
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVD--VYLKLESLNPTGSFKDRGALNLLLRLKEGEG---GKTVVEASSGNHGRALAAAAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 88 AKGYRIILTMPETMSVERRNLLKAYGAELVLTEGakGMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHrATTGPEIWK 167
Cdd:pfam00291 76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEGY-GTIGLEILE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 168 DTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPVLSKGEAG---------PHKIQGIGAGFVPDTLNTK 238
Cdd:pfam00291 153 QLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAgrpvpvpvaDTIADGLGVGDEPGALALD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547292877 239 IY----DEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAGKNIVVLLPD 297
Cdd:pfam00291 233 LLdeyvGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
15-297 |
1.58e-68 |
|
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: 213.53 E-value: 1.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 15 TPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGsVIIEPTSGNTGIGLASIAAAKGYRII 94
Cdd:cd00640 1 TPLVRLKRLSKLGGAN--IYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKG-VIIESTGGNTGIALAAAAARLGLKCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 95 LTMPETMSVERRNLLKAYGAELVLTEGakGMKGAIAKAEELAKEIEGAFIPSQFENPANPAAHrATTGPEIWKDTDG-KV 173
Cdd:cd00640 78 IVMPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQ-GTIGLEILEQLGGqKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 174 DIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPatspvlskgeagphkiqgigagfvpdtlntkiydEVLPIENEDAFA 253
Cdd:cd00640 155 DAVVVPVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------EVVTVSDEEALE 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 547292877 254 AGRAFAKAEGVLVGISSGAALHAATILANRPeNAGKNIVVLLPD 297
Cdd:cd00640 201 AIRLLAREEGILVEPSSAAALAAALKLAKKL-GKGKTVVVILTG 243
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
1-304 |
1.10e-34 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 130.50 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 1 MAKIYESVTELIGGTPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEPTSGNTGI 80
Cdd:PLN02356 40 KKKPRNGLIDAIGNTPLIRINSLSEATGCE--ILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 81 GLASIAAAKGYRIILTMPETMSVERRNLLKAYGA--------------------------------ELVLTEGAKG---- 124
Cdd:PLN02356 118 SLATVAPAYGCKCHVVIPDDVAIEKSQILEALGAtvervrpvsithkdhyvniarrraleanelasKRRKGSETDGihle 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 125 -MKGAIAKAEE----LAKEIEGAFIPSQFENPANPAAHRATTGPEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPD 199
Cdd:PLN02356 198 kTNGCISEEEKenslFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 200 IKVVAVEPATSPVLSK---------GEAGPHKI--------QGIGAGFVPDTLNTKIYDEVLPIENEDAFAAGRAFAKAE 262
Cdd:PLN02356 278 IKCFLIDPPGSGLFNKvtrgvmytrEEAEGRRLknpfdtitEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKND 357
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 547292877 263 GVLVGISSGAALHAATILAnRPENAGKNIVVLLPDTGDRYLS 304
Cdd:PLN02356 358 GLFVGSSSAMNCVGAVRVA-QSLGPGHTIVTILCDSGMRHLS 398
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
15-295 |
2.87e-14 |
|
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: 71.75 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 15 TPILNAKNFAKQAGANATLlaKLEYFNPAGSVKDRIAKAMI----DEAEKSGklkegsvIIEPTSGNTGIGLASIAAAKG 90
Cdd:cd01562 18 TPLLTSPTLSELLGAEVYL--KCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 91 YRIILTMPETMSVERRNLLKAYGAELVLTEgaKGMKGAIAKAEELAKEIEGAFIPSqFENPANPAAHrATTGPEIWKDTD 170
Cdd:cd01562 89 IPATIVMPETAPAAKVDATRAYGAEVVLYG--EDFDEAEAKARELAEEEGLTFIHP-FDDPDVIAGQ-GTIGLEILEQVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 171 GKVDIF------------VAgvgtggtvtgigeYLKEQNPDIKVVAVEPATSPVLS----KGEAGPHKIQGI----GAGF 230
Cdd:cd01562 165 DLDAVFvpvggggliagiAT-------------AVKALSPNTKVIGVEPEGAPAMAqslaAGKPVTLPEVDTiadgLAVK 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547292877 231 VPDTLNTKIY----DEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALhaATILANRPENAGKNIVVLL 295
Cdd:cd01562 232 RPGELTFEIIrklvDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALAL--AALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
15-295 |
6.66e-12 |
|
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: 65.06 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 15 TPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDR-----IAKaMIDEAEKSGklkegsvIIEPTSGNTGIGLASIAAAK 89
Cdd:COG1171 25 TPLLRSPTLSERLGAE--VYLKLENLQPTGSFKLRgaynaLAS-LSEEERARG-------VVAASAGNHAQGVAYAARLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 90 GYRIILTMPETMSVERRNLLKAYGAELVLTEGAkgMKGAIAKAEELAKEiEGA-FIPsqfenpanPAAHR------ATTG 162
Cdd:COG1171 95 GIPATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAELAEE-EGAtFVH--------PFDDPdviagqGTIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 163 PEIWKDTdGKVD--------------IFVagvgtggtvtgigeYLKEQNPDIKVVAVEPATSPVLSKG-EAG-PHKIQGI 226
Cdd:COG1171 164 LEILEQL-PDLDavfvpvggggliagVAA--------------ALKALSPDIRVIGVEPEGAAAMYRSlAAGePVTLPGV 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547292877 227 G------AGFVPDTLNTKIY----DEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALhaATILANRPENAGKNIVVLL 295
Cdd:COG1171 229 DtiadglAVGRPGELTFEILrdlvDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAAL--AALLAGKERLKGKRVVVVL 305
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
1-122 |
9.43e-12 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 64.73 E-value: 9.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 1 MAKIYESVTELIGGTPILNAKNFAKQAGANATLLaKLEYFNPAGSVKDRIAKAMIDEAEKSGKlkegSVIIEPTSGNTGI 80
Cdd:PRK06381 2 EEELSSSEEKPPGGTPLLRARKLEEELGLRKIYL-KFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 547292877 81 GLASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGA 122
Cdd:PRK06381 77 SIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGK 118
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
15-295 |
1.03e-11 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 64.33 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 15 TPILNAKNFAKQAGANATLlaKLEYFNPAGSVKDRIA----KAMIDEAEKSGklkegsvIIEPTSGNTGIGLASIAAAKG 90
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYL--KCEHLQHTGSFKFRGAsnklRLLNEAQRQQG-------VITASSGNHGQGVALAAKLAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 91 YRIILTMPETMSVERRNLLKAYGAELVLTEGAkgMKGAIAKAEELAKEIEGAFIPSQfeNPANPAAHRATTGPEIWKDTD 170
Cdd:PRK06815 92 IPVTVYAPEQASAIKLDAIRALGAEVRLYGGD--ALNAELAARRAAEQQGKVYISPY--NDPQVIAGQGTIGMELVEQQP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 171 GKVDIFVAGVGTGGtVTGIGEYLKEQNPDIKVVAVEPATSPV------------------LSKGEAGphkiqGIGAGFVP 232
Cdd:PRK06815 168 DLDAVFVAVGGGGL-ISGIATYLKTLSPKTEIIGCWPANSPSlytsleageivevaeqptLSDGTAG-----GVEPGAIT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547292877 233 DTLNTKIYDEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILAnrPENAGKNIVVLL 295
Cdd:PRK06815 242 FPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLA--PRYQGKKVAVVL 302
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
13-172 |
2.18e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 63.60 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 13 GGTPILNAKNFAkqaganatllAKLEYFNPAGSVKDRIAKAMIDEAEKSGkLKEgsvIIEPTSGNTGIGLASIAAAKGYR 92
Cdd:PRK06450 57 GRTPLIKKGNIW----------FKLDFLNPTGSYKDRGSVTLISYLAEKG-IKQ---ISEDSSGNAGASIAAYGAAAGIE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 93 IILTMPETMSVERRNLLKAYGAELVLTEGAKgmkgaiakaEELAKEIE--GAFIPSQFENPANPAAHRaTTGPEIWKDTD 170
Cdd:PRK06450 123 VKIFVPETASGGKLKQIESYGAEVVRVRGSR---------EDVAKAAEnsGYYYASHVLQPQFRDGIR-TLAYEIAKDLD 192
|
..
gi 547292877 171 GK 172
Cdd:PRK06450 193 WK 194
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
13-121 |
3.13e-11 |
|
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: 63.30 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 13 GGTPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLkegsVIIEPTSGNTGIGLASIAAAKGYR 92
Cdd:COG0498 65 GGTPLVKAPRLADELGKN--LYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAARAGIE 138
|
90 100 110
....*....|....*....|....*....|
gi 547292877 93 IILTMPET-MSVERRNLLKAYGAELVLTEG 121
Cdd:COG0498 139 VFVFVPEGkVSPGQLAQMLTYGAHVIAVDG 168
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
13-151 |
1.85e-08 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 55.01 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 13 GGTPILNAKNFAKQAGANaTLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGkLKEgsvIIEPTSGNTGIGLASIAAAKGYR 92
Cdd:PRK08197 78 GMTPLLPLPRLGKALGIG-RLWVKDEGLNPTGSFKARGLAVGVSRAKELG-VKH---LAMPTNGNAGAAWAAYAARAGIR 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 547292877 93 IILTMPETMSVERRNLLKAYGAELVLTEGAKGMKGAIAKAeelAKEIEGAFIPSQFENP 151
Cdd:PRK08197 153 ATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAE---AVAEYGWFDVSTLKEP 208
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
2-210 |
4.35e-08 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 54.03 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 2 AKIYESVTEliggTPILNAKNFAKQAGaNATLLaKLEYFNPAGSVK-----DRIAKAMIDEAEKSgklkegsvIIEPTSG 76
Cdd:PRK12483 29 ARVYDVARE----TPLQRAPNLSARLG-NQVLL-KREDLQPVFSFKirgayNKMARLPAEQLARG--------VITASAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 77 NTGIGLASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTegAKGMKGAIAKAEELAKEIEGAFIPSqFENPaNPAA 156
Cdd:PRK12483 95 NHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEEGLTFVPP-FDDP-DVIA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 547292877 157 HRATTGPEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATS 210
Cdd:PRK12483 171 GQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
32-151 |
7.07e-08 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 53.29 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 32 TLLAKLEYFNPAGSVKDRIAKAMIdeaeksGKLKEGSV--IIEPTSGNTGIGLASIAAAKGYRIILTMPETMSVERRNLL 109
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTV------AKLKEEGIneVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLL 146
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 547292877 110 KAYGAELVLTEGAKgMKgAIAKAEELAKEIEGAFIpSQFENP 151
Cdd:PRK08329 147 SRLGAELHFVEGDR-ME-VHEEAVKFSKRNNIPYV-SHWLNP 185
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
13-295 |
8.59e-08 |
|
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: 52.60 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 13 GGTPILNAKNFAKQAGANaTLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKlkegSVIIEPTSGNTGIGLASIAAAKGYR 92
Cdd:cd01563 21 GNTPLVRAPRLGERLGGK-NLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 93 IILTMPETMSVERRNLLKAYGAELVLTEGakGMKGAIAKAEELAKEIEGAFIPSqfENPanpaaHRA----TTGPEIWKD 168
Cdd:cd01563 96 CVVFLPAGKALGKLAQALAYGATVLAVEG--NFDDALRLVRELAEENWIYLSNS--LNP-----YRLegqkTIAFEIAEQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 169 TDGKV-D-IFV---AGVGTGGTVTGIGEYLK----EQNPdiKVVAVEPA-TSPVLSKGEAGPHKIQGIGAgfvPDTLNTK 238
Cdd:cd01563 167 LGWEVpDyVVVpvgNGGNITAIWKGFKELKElgliDRLP--RMVGVQAEgAAPIVRAFKEGKDDIEPVEN---PETIATA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547292877 239 I-------YDEVL-----------PIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPENAGKNIVVLL 295
Cdd:cd01563 242 IrignpasGPKALravresggtavAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDKGERVVVV 316
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
15-295 |
1.07e-07 |
|
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: 52.83 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 15 TPILNAKNFAKQAGANATLlaKLEYFNPAGSVKDRIAKAMIDEAEKSGKlKEGsvIIEPTSGNTGIGLASIAAAKGYRII 94
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYL--KLENLQKTGSFKIRGALNKIANLSEDQR-QRG--VVAASAGNHAQGVAYAAKKFGIKAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 95 LTMPETMSVERRNLLKAYGAELVLtEGAKgMKGAIAKAEELAKEiEGAFIPSQFENPaNPAAHRATTGPEIWKDTdGKVD 174
Cdd:TIGR01127 76 IVMPESAPPSKVKATKSYGAEVIL-HGDD-YDEAYAFATSLAEE-EGRVFVHPFDDE-FVMAGQGTIGLEIMEDI-PDVD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 175 IFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPATSPV----LSKGEAGPHK-IQGIGAGFV---PDTLNTKI----YDE 242
Cdd:TIGR01127 151 TVIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSmyesLREGKIKAVEsVRTIADGIAvkkPGDLTFNIikeyVDD 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 547292877 243 VLPI-ENEDAFAAGRAFAKAEGVLVGisSGAALHAAtILANRPENAGKNIVVLL 295
Cdd:TIGR01127 231 VVTVdEEEIANAIYLLLERHKILAEG--AGAAGVAA-LLEQKVDVKGKKIAVVL 281
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
15-293 |
2.54e-07 |
|
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: 51.15 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 15 TPILNAKNFAKQAGANATLlaKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIEpTSGNTGIGLASIAAAKGYRII 94
Cdd:cd06448 2 TPLIESTALSKTAGCNVFL--KLENLQPSGSFKIRGIGHLCQKSAKQGLNECVHVVCS-SGGNAGLAAAYAARKLGVPCT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 95 LTMPET---MSVERrnlLKAYGAELVLtEGAKGMKGAIAKAEELAK-EIEGAFIPSqFENPANPAAHrATTGPEIWKD-- 168
Cdd:cd06448 79 IVVPEStkpRVVEK---LRDEGATVVV-HGKVWWEADNYLREELAEnDPGPVYVHP-FDDPLIWEGH-SSMVDEIAQQlq 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 169 TDGKVDIFVAGVGTGGTVTGIGEYLKE-QNPDIKVVAVEPATSPVLSKG-EAGPH----KIQGI----GAGFVPD-TL-- 235
Cdd:cd06448 153 SQEKVDAIVCSVGGGGLLNGIVQGLERnGWGDIPVVAVETEGAHSLNASlKAGKLvtlpKITSVatslGAKTVSSqALey 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547292877 236 --NTKIYDEVlpIENEDAFAAGRAFAKAEGVLVGISSGAALHAA---TILANRPEN---AGKNIVV 293
Cdd:cd06448 233 aqEHNIKSEV--VSDRDAVQACLRFADDERILVEPACGAALAVVysgKILDLQLEVlltPLDNVVV 296
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
2-208 |
1.76e-06 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 49.15 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 2 AKIYESVTEliggTPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSgKLKEGsvIIEPTSGNTGIG 81
Cdd:PLN02550 101 AKVYDVAIE----SPLQLAKKLSERLGVK--VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 82 LASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTegAKGMKGAIAKAEELAKEIEGAFIPSqFENPaNPAAHRATT 161
Cdd:PLN02550 172 VALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLV--GDSYDEAQAYAKQRALEEGRTFIPP-FDHP-DVIAGQGTV 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 547292877 162 GPEIWKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPA 208
Cdd:PLN02550 248 GMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPS 294
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
13-299 |
6.25e-06 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 47.50 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 13 GGTPILNAKNFAKqagANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKlkegSVIIEPTSGNTGIGLASIAAAKGYR 92
Cdd:PRK05638 65 GGTPLIRARISEK---LGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 93 IILTMPETMSVERRNLLKAYGAELVLTEgaKGMKGAIAKAEELAKeIEGAFIPSQFENPANPAAHRaTTGPEIWKDTDGK 172
Cdd:PRK05638 138 AFVVVPRKVDKGKLIQMIAFGAKIIRYG--ESVDEAIEYAEELAR-LNGLYNVTPEYNIIGLEGQK-TIAFELWEEINPT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 173 VDIFVAGVGTGGTVTGI--GEYLK----EQNPdiKVVAVE-----PATSPVLS-KGEAGPHKIQGIgagFVPDTLN---- 236
Cdd:PRK05638 214 HVIVPTGSGSYLYSIYKgfKELLEigviEEIP--KLIAVQtercnPIASEILGnKTKCNETKALGL---YVKNPVMkeyv 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547292877 237 ---TKIYDEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALHAATILANRPE-NAGKNIVVLLPDTG 299
Cdd:PRK05638 289 seaIKESGGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYiEKGDKVVLVVTGSG 355
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
195-304 |
1.95e-05 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 45.94 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 195 EQNPDIKVVAVEPATSPVLSKGE--------AG--P-HKIQGIGAGFVPD-------------TLNTKIYDEVL----PI 246
Cdd:PRK12391 280 EGKKDTRFIAVEPAACPTLTKGEyaydfgdtAGltPlLKMYTLGHDFVPPpihagglryhgmaPLVSLLVHEGLiearAY 359
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547292877 247 ENEDAFAAGRAFAKAEGVLVGISSGAALhAATI---LANRPENAGKNIVVLLPDTG-------DRYLS 304
Cdd:PRK12391 360 PQTEVFEAAVLFARTEGIVPAPESSHAI-AAAIdeaLKAKEEGEEKVILFNLSGHGlldlaayDAYLA 426
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
8-139 |
1.34e-04 |
|
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: 43.14 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 8 VTELIGGTPILNAKNFAKQAGANaTLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKlkegSVIIEPTSGNTGIGLASIAA 87
Cdd:TIGR00260 16 VDLGEGVTPLFRAPALAANVGIK-NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAG 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 547292877 88 AKGYRIILTMPETmSVERRNLLKA--YGAELVltegakGMKGAIAKAEELAKEI 139
Cdd:TIGR00260 91 KAGLKVVVLYPAG-KISLGKLAQAlgYNAEVV------AIDGNFDDAQRLVKQL 137
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
1-138 |
3.27e-04 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 41.68 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 1 MAKIYESVTELIGGTPILNAKNFAKQAGANatLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGsvIIEPTSGNTGI 80
Cdd:PRK06608 10 IAAAHNRIKQYLHLTPIVHSESLNEMLGHE--IFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPDK--IVAYSTGNHGQ 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 547292877 81 GLASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTEGAkgmkgaiAKAEELAKE 138
Cdd:PRK06608 86 AVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTR-------QEAEEKAKE 136
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
31-146 |
6.73e-04 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 40.75 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 31 ATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGsvIIEPTSGNTGIGLASIAAAKGYRIILTMPETMSVERRNLLK 110
Cdd:PRK06110 36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMR 113
|
90 100 110
....*....|....*....|....*....|....*.
gi 547292877 111 AYGAELVltEGAKGMKGAIAKAEELAKEIEGAFIPS 146
Cdd:PRK06110 114 ALGAELI--EHGEDFQAAREEAARLAAERGLHMVPS 147
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
15-134 |
7.16e-04 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 40.71 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 15 TPILNAKNFAkqaGANATLLAKLEYFNPAGSVKDRIAKAMIdeaeKSGKLKEGSVIIePTSGNTGIGLASIAAAKGYRII 94
Cdd:PRK08246 24 TPVLEADGAG---FGPAPVWLKLEHLQHTGSFKARGAFNRL----LAAPVPAAGVVA-ASGGNAGLAVAYAAAALGVPAT 95
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 547292877 95 LTMPETMSVERRNLLKAYGAELVLTEG--AKGMKGAIAKAEE 134
Cdd:PRK08246 96 VFVPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAE 137
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
6-206 |
1.40e-03 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 39.72 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 6 ESVTELIGGTPILNAKNFAKQAGANATLlaKLEYFNPAGSVKDRIAKAMID---EAEKsgklKEGsvIIEPTSGNTGIGL 82
Cdd:PRK08638 19 QRLAGRIRKTPLPRSNYLSERCKGEIFL--KLENMQRTGSFKIRGAFNKLSsltDAEK----RKG--VVACSAGNHAQGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 83 ASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLTegAKGMKGAIAKAEELAKEiEGAFIPSQFENPaNPAAHRATTG 162
Cdd:PRK08638 91 ALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLH--GDNFNDTIAKVEEIVEE-EGRTFIPPYDDP-KVIAGQGTIG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 547292877 163 PEIWKDTdGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVE 206
Cdd:PRK08638 167 LEILEDL-WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQ 209
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
15-306 |
1.72e-03 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 39.79 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 15 TPILNAKNFAKQAGANATLlaKLEYFNPAGSVK--DRIAKAMIdeAEKSGKLKegsVIIEPTSGNTGIGLASIAAAKGYR 92
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYL--KREDLNHTGSHKinNALGQALL--AKRMGKTR---IIAETGAGQHGVATATACALFGLK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 93 IILTMPET------MSVERRNLLkayGAELV-LTEGAKGMKGAIAKA--------EELAKEIEGAFIPSQFenPANPAAH 157
Cdd:PRK13803 345 CTIFMGEEdikrqaLNVERMKLL---GANVIpVLSGSKTLKDAVNEAirdwvasvPDTHYLIGSAVGPHPY--PEMVAYF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 158 RATTGPEI---WKDTDGKVDIFVAGVGTGGTVTGIGEYLKEQNPDIKVVAVEPA--------TSPVLSKGEAG------- 219
Cdd:PRK13803 420 QSVIGEEAkeqLKEQTGKLPDAIIACVGGGSNAIGIFYHFLDDPSVKLIGVEAGgkgvntgeHAATIKKGRKGvlhgsmt 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 220 ------------PHKIQ------GIGAGFVpdTLNTKIYDEVLPIENEDAFAAGRAFAKAEGVLVGISSGAALhaATILA 281
Cdd:PRK13803 500 ylmqdengqilePHSISagldypGIGPMHA--NLFETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHAL--AYLKE 575
|
330 340
....*....|....*....|....*.
gi 547292877 282 NRPENAGKNIVVL-LPDTGDRYLSTA 306
Cdd:PRK13803 576 GRKKFKKKDIVIVnLSGRGDKDIPTL 601
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
8-99 |
3.89e-03 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 38.64 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 8 VTELIGGTPILNAKNFAKQAGANATLLAKLEYFNPAGSVKDRIAKAMIDEAEKSGKLKEGSVIIE-PTSGNTGIGLASIA 86
Cdd:PLN02569 127 VSLFEGNSNLFWAERLGKEFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAKPVVGVGcASTGDTSAALSAYC 206
|
90
....*....|...
gi 547292877 87 AAKGYRIILTMPE 99
Cdd:PLN02569 207 AAAGIPSIVFLPA 219
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
59-136 |
4.41e-03 |
|
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: 38.35 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 59 EKSGKLKEGSVIIEpTSGNTGIGLASI--AAAKGYRIILTM---PETMSVERRnlLKAYGAELVLTEG-------AKGMK 126
Cdd:cd08290 139 EDFVKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVrdrPDLEELKER--LKALGADHVLTEEelrsllaTELLK 215
|
90
....*....|
gi 547292877 127 GAIAKAEELA 136
Cdd:cd08290 216 SAPGGRPKLA 225
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
2-219 |
6.57e-03 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 37.81 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 2 AKIYESVTEliggTPILNAKNFAKQAGaNATLLaKLEYFNPAGSVKDRIAKAMI----DEAEKSGklkegsvIIEPTSGN 77
Cdd:PRK09224 12 ARVYDVAQE----TPLEKAPKLSARLG-NQVLL-KREDLQPVFSFKLRGAYNKMaqltEEQLARG-------VITASAGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547292877 78 TGIGLASIAAAKGYRIILTMPETMSVERRNLLKAYGAELVLtegakgmKG-----AIAKAEELAKEIEGAFIPSqFENPA 152
Cdd:PRK09224 79 HAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVL-------HGdsfdeAYAHAIELAEEEGLTFIHP-FDDPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547292877 153 NPAAhRATTGPEIWKDTDGKVD-IFVAGVGTGGTVTGIGeYLKEQNPDIKVVAVEPATSPVLSKG-EAG 219
Cdd:PRK09224 151 VIAG-QGTIAMEILQQHPHPLDaVFVPVGGGGLIAGVAA-YIKQLRPEIKVIGVEPEDSACLKAAlEAG 217
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