|
Name |
Accession |
Description |
Interval |
E-value |
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
41-345 |
1.32e-115 |
|
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: 341.00 E-value: 1.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 41 FGDISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALAL 120
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 121 SLHGKQLGVEVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEIL 200
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 201 EQIQMPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFAS 280
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537387 281 MIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNHlKGKTVVSILSGGNID 345
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL-KGKKVVVVLSGGNID 304
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
43-361 |
2.55e-90 |
|
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: 276.92 E-value: 2.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 43 DISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSL 122
Cdd:COG1171 10 DIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQGVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 123 HGKQLGVEVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQ 202
Cdd:COG1171 90 AARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 203 IQMPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFASMI 282
Cdd:COG1171 170 LPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEILR 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537387 283 GKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNhLKGKTVVSILSGGNIDSTSLGRCIERGLAYDH 361
Cdd:COG1171 250 DLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER-LKGKRVVVVLSGGNIDPDRLAEILERGLVGEG 327
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
36-439 |
1.55e-85 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 267.53 E-value: 1.55e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 36 PKILQFGDISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGN 115
Cdd:PRK07334 2 GLMVTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 116 HALALSLHGKQLGVEVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTT 195
Cdd:PRK07334 82 HAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 196 GIEILEQIQMPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQ-AGHPVYTptrPTLADGLAVPNAG 274
Cdd:PRK07334 162 ALEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKgVALPCGG---STIAEGIAVKQPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 275 VNAFASMIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKlNHLKGKTVVSILSGGNIDSTSLGRCIE 354
Cdd:PRK07334 239 QLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYP-ERFRGRKVGLVLSGGNIDTRLLANVLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 355 RGLAYDHRVIRLSVIIPDKPGGLSKLTGLVGELSGNVRDLYLERAFMrnDMSSQ--RVKMVIEVRGEEHEMQLKQKFQEV 432
Cdd:PRK07334 318 RGLVRAGRLARLRVDIRDRPGALARVTALIGEAGANIIEVSHQRLFT--DLPAKgaELELVIETRDAAHLQEVIAALRAA 395
|
....*..
gi 17537387 433 YDPSNCQ 439
Cdd:PRK07334 396 GFEARLV 402
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
62-431 |
2.07e-85 |
|
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: 266.61 E-value: 2.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 62 KSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPL 141
Cdd:TIGR01127 5 YSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPESAPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 142 MKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQIQMPDAILVPVGGGGLVAG 221
Cdd:TIGR01127 85 SKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGGLISG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 222 VATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFASMIGKVDRVISVPENDIAVAIL 301
Cdd:TIGR01127 165 VASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIANAIY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 302 RLIENEKVVCEGAGAIGIGAILSGKLNhLKGKTVVSILSGGNIDSTSLGRCIERGLAYDHRVIRLSVIIPDKPGGLSKLT 381
Cdd:TIGR01127 245 LLLERHKILAEGAGAAGVAALLEQKVD-VKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPGALYHLL 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17537387 382 GLVGELSGNVRDLYLERAFMRNDMSSQRVKMVIEVRGEEHEMQLKQKFQE 431
Cdd:TIGR01127 324 ESIAEARANIVKIDHDRLSKEIPPGFAMVEITLETRGKEHLDEILKILRD 373
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
38-360 |
1.30e-67 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 218.84 E-value: 1.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 38 ILQFGDISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHA 117
Cdd:PRK08638 8 PVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 118 LALSLHGKQLGVEVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGI 197
Cdd:PRK08638 88 QGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 198 EILEQIQMPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNA 277
Cdd:PRK08638 168 EILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 278 FASMIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNH-LKGKTVVSILSGGNIDSTSLGRCIERG 356
Cdd:PRK08638 248 YEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQyIQNKKVVAIISGGNVDLSRVSQITGHV 327
|
....
gi 17537387 357 LAYD 360
Cdd:PRK08638 328 VAAD 331
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
51-341 |
2.18e-66 |
|
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: 214.48 E-value: 2.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 51 IQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSLHGKQLGVE 130
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 131 VNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNG-TYINGYDHYDILAGAGTTGIEILEQIQ-MPDA 208
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLGgDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 209 ILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVP-NAGVNAFASMIGKVDR 287
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVGE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17537387 288 VISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNHLKGK-TVVSILSG 341
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGdRVVVVLTG 295
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
43-358 |
5.15e-57 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 190.95 E-value: 5.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 43 DISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSL 122
Cdd:PRK07476 5 DIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 123 HGKQLGVEVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEq 202
Cdd:PRK07476 85 AARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILE- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 203 iQMPDA--ILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLAD----GLAVPNAgvN 276
Cdd:PRK07476 164 -ALPDVatVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslggGIGLDNR--Y 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 277 AFASMIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNHLKGKTVVsILSGGNIDSTSLGRCIERG 356
Cdd:PRK07476 241 TFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVV-VVSGANIDMELHRRIINGE 319
|
..
gi 17537387 357 LA 358
Cdd:PRK07476 320 VA 321
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
43-377 |
8.00e-55 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 188.09 E-value: 8.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 43 DISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSL 122
Cdd:PRK08639 11 DIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 123 HGKQLGVEVNVVMPKIAPLMKINRCQDLGAN---ILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEI 199
Cdd:PRK08639 91 ACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEfveIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 200 LEQIQ---MPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVN 276
Cdd:PRK08639 171 LEQLEkegSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 277 AFASMIGKVDRVISVPENDIAVAILRLIENEKVVCEGagaigigailSGKL---------NHLKGKTVVSILSGGNIDST 347
Cdd:PRK08639 251 TFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEP----------AGALsiaalelykDEIKGKTVVCVISGGNNDIE 320
|
330 340 350
....*....|....*....|....*....|...
gi 17537387 348 SLGRCIERGLAYD---HRVIrlsVIIPDKPGGL 377
Cdd:PRK08639 321 RMPEIKERSLIYEglkHYFI---VNFPQRPGAL 350
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
50-385 |
1.76e-53 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 186.48 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 50 RIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSLHGKQLGV 129
Cdd:TIGR01124 10 RVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 130 EVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQIQMP-DA 208
Cdd:TIGR01124 90 KALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANPlDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 209 ILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFASMIGKVDRV 288
Cdd:TIGR01124 170 VFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 289 ISVPENDIAVAILRLIENEKVVCEgagaIGIGAILSG-----KLNHLKGKTVVSILSGGNIDSTSLGRCIERGLAYDHRV 363
Cdd:TIGR01124 250 VTVDTDEVCAAIKDLFEDTRAVAE----PAGALALAGlkkyvALHGIRGQTLVAILSGANMNFHRLRYVSERCELGEQRE 325
|
330 340
....*....|....*....|..
gi 17537387 364 IRLSVIIPDKPGGLSKLTGLVG 385
Cdd:TIGR01124 326 ALLAVTIPEQPGSFLKFCELLG 347
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
44-344 |
7.08e-51 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 174.50 E-value: 7.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 44 ISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSLH 123
Cdd:PRK06815 7 ILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 124 GKQLGVEVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQI 203
Cdd:PRK06815 87 AKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 204 QMPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAvpnAGVNA----FA 279
Cdd:PRK06815 167 PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTA---GGVEPgaitFP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537387 280 SMIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKlNHLKGKTVVSILSGGNI 344
Cdd:PRK06815 244 LCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLA-PRYQGKKVAVVLCGKNI 307
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
35-345 |
6.71e-50 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 172.13 E-value: 6.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 35 NPKILQFGDISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAG 114
Cdd:PRK07048 2 DLLLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 115 NHALALSLHGKQLGVEVNVVMPKIAPLMKINRCQDLGANIlVQGEDIAESRE-IALRMAHDSNGTYINGYDHYDILAGAG 193
Cdd:PRK07048 82 NHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEV-VTYDRYTEDREeIGRRLAEERGLTLIPPYDHPHVIAGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 194 TTGIEILEQIQMPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNA 273
Cdd:PRK07048 161 TAAKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537387 274 GVNAFASMIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNhLKGKTVVSILSGGNID 345
Cdd:PRK07048 241 GNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVP-LKGKRVGVIISGGNVD 311
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
66-385 |
2.05e-45 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 164.54 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 66 LSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKIN 145
Cdd:PRK09224 29 LSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 146 RCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQIQMP-DAILVpvgggglvagvat 224
Cdd:PRK09224 109 AVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHPlDAVFV------------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 225 AV-------------KALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFASMIGKVDRVISV 291
Cdd:PRK09224 176 PVggggliagvaayiKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 292 PENDIAVAILRLIENEKVVCEGagaigigailSGKL-----------NHLKGKTVVSILSGGNIDSTSLGRCIERGLAYD 360
Cdd:PRK09224 256 DTDEICAAIKDVFEDTRSIAEP----------AGALalaglkkyvaqHGIEGETLVAILSGANMNFDRLRYVAERAELGE 325
|
330 340
....*....|....*....|....*
gi 17537387 361 HRVIRLSVIIPDKPGGLSKLTGLVG 385
Cdd:PRK09224 326 QREALLAVTIPEEPGSFLKFCELLG 350
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
56-386 |
6.67e-45 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 163.81 E-value: 6.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 56 VRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSLHGKQLGVEVNVVM 135
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 136 PKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQIQMP-DAILVPVG 214
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGPlDAIFVPVG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 215 GGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFASMIGKVDRVISVPEN 294
Cdd:PRK12483 196 GGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVDEVVTVSTD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 295 DIAVAILRLIENEKVVCEGagaigigailSGKL-----------NHLKGKTVVSILSGGNIDSTSLGRCIERGLAYDHRV 363
Cdd:PRK12483 276 ELCAAIKDIYDDTRSITEP----------AGALavagikkyaerEGIEGQTLVAIDSGANVNFDRLRHVAERAELGEQRE 345
|
330 340
....*....|....*....|...
gi 17537387 364 IRLSVIIPDKPGGLSKLTGLVGE 386
Cdd:PRK12483 346 AIIAVTIPEQPGSFKAFCAALGK 368
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
43-350 |
1.30e-44 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 157.81 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 43 DISMAHHRIQNGIVRTDCRKSRcLSKLFDMNIYLKMEVNQDTGSFKERGARYALqnLPEEKKKAGVYAASAGNHALALSL 122
Cdd:PRK08246 9 DVRAAAQRIAPHIRRTPVLEAD-GAGFGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 123 HGKQLGVEVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQ 202
Cdd:PRK08246 86 AAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 203 IQMPDAILVPVGGGGLVAGVATAVKalsPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFASMI 282
Cdd:PRK08246 166 APGVDTVLVAVGGGGLIAGIAAWFE---GRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALAR 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17537387 283 GKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNHLKGKTVVSILSGGNIDSTSLG 350
Cdd:PRK08246 243 AHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGERVAVVLCGANTDPATLA 310
|
|
| PLN02970 |
PLN02970 |
serine racemase |
41-349 |
7.51e-44 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 156.38 E-value: 7.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 41 FGDISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALAL 120
Cdd:PLN02970 11 LSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 121 SLHGKQLGVEVNVVMPKIAPLMKINRCQDLGANIlVQGEDIAESRE-IALRMAHDSNGTYINGYDHYDILAGAGTTGIEI 199
Cdd:PLN02970 91 ALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGII-TWCEPTVESREaVAARVQQETGAVLIHPYNDGRVISGQGTIALEF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 200 LEQIQMPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVpNAGVNAFA 279
Cdd:PLN02970 170 LEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA-SLGDLTWP 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537387 280 SMIGKVDRVISVPENDIaVAILRLI-ENEKVVCEGAGAIGIGAILSG--KLNHL--KGKTVVSILSGGNIDSTSL 349
Cdd:PLN02970 249 VVRDLVDDVITVDDKEI-IEAMKLCyERLKVVVEPSGAIGLAAALSDsfRSNPAwkGCKNVGIVLSGGNVDLGVL 322
|
|
| COG2061 |
COG2061 |
Uncharacterized conserved protein, contains ACT domain [General function prediction only]; |
46-431 |
1.50e-43 |
|
Uncharacterized conserved protein, contains ACT domain [General function prediction only];
Pssm-ID: 441664 [Multi-domain] Cd Length: 401 Bit Score: 157.51 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 46 MAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNH----ALALS 121
Cdd:COG2061 8 EAAAAALAVVVVTTPLLLSSSSSLSVGLVVLLKEENLQTTGSFKRRGAYKLIALLLEEEEKGGVAAAAAGNaaqaAAAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 122 LHGKQLGVevnVVMPKIAPLMKINRCQDLGANILVQGEDIAESrEIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILE 201
Cdd:COG2061 88 ALGGISAI---VVMPPPPPLPKVAATRGGGAVVVVVGGDDDAA-AAAAAALQEEEGGFFHHPDDDDDVIAGGGGGGLEIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 202 QIQMPDAILVPVGGGG-LVAGVATAVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFAS 280
Cdd:COG2061 164 ELLPDVVVVVVGGGGGgGGGGAAAAAKAKRPPIVIVGVQAEAAAAAPSSLAAGIEVVPGGGTTIADGIAVVKPGGLTFII 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 281 MIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILsgKLNHLKGKTVVSILSGGNIDSTSLGRCIERGLAYD 360
Cdd:COG2061 244 IRKVVDDVVVVVEEEIAAALLLLLERKKKVVEGAAAAAAAAAL--KKKPLRGKKVVVVLSGGNIDDLLLLRIIIKGLLAA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537387 361 HRVIRLSVIIPDKPGGLSKLTGLVGELSGNVRDLYLERAFMRNDMSSQRVKMVIEVRGEEHEMQLKQKFQE 431
Cdd:COG2061 322 GRRLVLLVVLPDRPGQLLRVLQPIAELGANIISVVHERENSKTPRGEVEVEVVLETRGEEHLEEIIAALRE 392
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
58-342 |
5.58e-43 |
|
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: 151.51 E-value: 5.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 58 TDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAG--VYAASAGNHALALSLHGKQLGVEVNVVM 135
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 136 PKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHDSNG-TYINGYDHYDILAGAGTTGIEILEQI--QMPDAIlvp 212
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGTIGLEILEQLggQKPDAV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 213 vgggglvagvatavkalsptteVIGVVS-ETCQAIVKSLQAGHPVytptrptladglaVPNAGVNAfasmigkvdRVISV 291
Cdd:cd00640 158 ----------------------VVPVGGgGNIAGIARALKELLPN-------------VKVIGVEP---------EVVTV 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17537387 292 PENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNHLKGKTVVSILSGG 342
Cdd:cd00640 194 SDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
35-348 |
5.60e-38 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 141.06 E-value: 5.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 35 NPKILQFGDISMAHHRIQNGIVRTDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAG-VYAASA 113
Cdd:PRK06608 1 NLLLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPDkIVAYST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 114 GNHALALSLHGKQLGVEVNVVMPKIAPLMKINRCQDLGAN-ILVQGEDIAESReiaLRMAHDSNGTYINGYDHYDILAGA 192
Cdd:PRK06608 81 GNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEvILTNTRQEAEEK---AKEDEEQGFYYIHPSDSDSTIAGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 193 GTTGIEILEQIQM-PDAILVPVGGGGLVAGVATAVKALSPTTEVIGvvSETCQA--IVKSLQAGHPVYTPTRP-TLADGL 268
Cdd:PRK06608 158 GTLCYEALQQLGFsPDAIFASCGGGGLISGTYLAKELISPTSLLIG--SEPLNAndAYLSLKNNKIYRLNYSPnTIADGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 269 AVPNAGVNAFaSMIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILSGKLNHLKGKTVVSILSGGNIDSTS 348
Cdd:PRK06608 236 KTLSVSARTF-EYLKKLDDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKPQKLLVILSGGNIDPIL 314
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
66-388 |
2.32e-37 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 143.91 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 66 LSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKIN 145
Cdd:PLN02550 118 LSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 146 RCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQIQMP-DAILVPVGGGGLVAGVAT 224
Cdd:PLN02550 198 SVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPlHAIFVPVGGGGLIAGIAA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 225 AVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFASMIGKVDRVISVPENDIAVAILRLI 304
Cdd:PLN02550 278 YVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSRDAICASIKDMF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 305 ENEKVVCEgagaIGIGAILSG-----KLNHLKGKTVVSILSGGNIDSTSLGRCIERGLAYDHRVIRLSVIIPDKPGGLSK 379
Cdd:PLN02550 358 EEKRSILE----PAGALALAGaeaycKYYGLKDENVVAITSGANMNFDRLRIVTELADVGRQQEAVLATFMPEEPGSFKR 433
|
....*....
gi 17537387 380 LTGLVGELS 388
Cdd:PLN02550 434 FCELVGPMN 442
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
66-351 |
1.42e-31 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 123.18 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 66 LSKLFDMNIYLKMEVNQDTGSFKERGARYALQNL-PEEKKKAGVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKI 144
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLaRRGPRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 145 NRCQDLGANILVQGEDIAESREIALRMAHDSNGTYINGYdHYDILAGAGTTGIEILEQIQMPDAILVPVGGGGLVAGVAT 224
Cdd:PRK06110 110 AAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRAVPDLDVVYVPIGMGSGICGAIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 225 AVKALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNAGVNAFASMIGKVDRVISVPENDIAVAILRLI 304
Cdd:PRK06110 189 ARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAYF 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17537387 305 ENEKVVCEGAGAIGIGAILSGKlNHLKGKTVVSILSGGNIDSTSLGR 351
Cdd:PRK06110 269 TDTHNVAEGAGAAALAAALQER-ERLAGKRVGLVLSGGNIDRAVFAR 314
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
58-312 |
1.13e-26 |
|
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: 109.31 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 58 TDCRKSRCLSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEE--KKKAGVYAASAGNHALALSLHGKQLGVEVNVVM 135
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQglNECVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 136 PKIAPLMKINRCQDLGANILVQGEDIAESrEIALR---MAHDSNGTYINGYDHYDILAGAGTTGIEILEQIQ---MPDAI 209
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVWWEA-DNYLReelAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQsqeKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 210 LVpvgggglvagvatAV--------------KALSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRPTLADGLAVPNagV 275
Cdd:cd06448 161 VC-------------SVggggllngivqgleRNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKT--V 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 17537387 276 NAFASMIGKVDRVISVPENDIAV--AILRLIENEKVVCE 312
Cdd:cd06448 226 SSQALEYAQEHNIKSEVVSDRDAvqACLRFADDERILVE 264
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
74-349 |
1.14e-26 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 110.10 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 74 IYLKMEVNQDTGSFKERGARYALQNLPEEKKKAGVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKINRCQDLGAN 153
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 154 ILVQGEDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEIleQIQMPDAILVPVGGGGLVAGVATAVKalSPTT 233
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIEL--AAHAPDVVIVPIGGGGLASGVALALK--SQGV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 234 EVIGVVSETCQAIVKSLQAGHPVYTPTrPTLADGLAVPNAGVNAFASMIGKVDRVISVPENDIAVAILRLIENEKVVCEG 313
Cdd:PRK08813 206 RVVGAQVEGVDSMARAIRGDLREIAPV-ATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEG 284
|
250 260 270
....*....|....*....|....*....|....*.
gi 17537387 314 AGAIGIGailSGKlnHLKGKTVVSILSGGNIDSTSL 349
Cdd:PRK08813 285 AGALALA---AGR--RVSGKRKCAVVSGGNIDATVL 315
|
|
| ACT_ThrD-II-like |
cd04886 |
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and ... |
366-431 |
2.07e-17 |
|
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains; This CD includes the C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains. The Escherichia coli tdcB gene product, ThrD-II, anaerobically catalyzes the pyridoxal phosphate-dependent dehydration of L-threonine and L-serine to ammonia and to alpha-ketobutyrate and pyruvate, respectively. Tetrameric ThrD-II is subject to allosteric activation by AMP, inhibition by alpha-keto acids, and catabolite inactivation by several metabolites of glycolysis and the citric acid cycle. Also included in this CD are N-terminal ACT domains present in smaller (~170 a.a.) archaeal proteins of unknown function. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153158 [Multi-domain] Cd Length: 73 Bit Score: 76.43 E-value: 2.07e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17537387 366 LSVIIPDKPGGLSKLTGLVGELSGNVRDLYLERAFMRNDMSSQRVKMVIEVRGEEHEMQLKQKFQE 431
Cdd:cd04886 1 LRVELPDRPGQLAKLLAVIAEAGANIIEVSHDRAFKTLPLGEVEVELTLETRGAEHIEEIIAALRE 66
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
66-312 |
4.50e-17 |
|
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: 82.56 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 66 LSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAgVYAASAGNHALALSLHGKQLGVEVNVVMPK-IAPLMKI 144
Cdd:COG0498 75 LADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKT-IVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 145 NRCQDLGA-NILVQGeDIAESREIALRMAHDSNGTYINGYDHYDILaGAGTTGIEILEQI-QMPDAILVpvgggglvagv 222
Cdd:COG0498 154 AQMLTYGAhVIAVDG-NFDDAQRLVKELAADEGLYAVNSINPARLE-GQKTYAFEIAEQLgRVPDWVVV----------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 223 atAV----------------KALSPTTEV---IGVVSETCQAIVKSLQAGHPVYTPTRP-TLADGLAVPNA-----GVNA 277
Cdd:COG0498 221 --PTgnggnilagykafkelKELGLIDRLprlIAVQATGCNPILTAFETGRDEYEPERPeTIAPSMDIGNPsngerALFA 298
|
250 260 270
....*....|....*....|....*....|....*
gi 17537387 278 FASMIGkvdRVISVPENDIAVAILRLIENEKVVCE 312
Cdd:COG0498 299 LRESGG---TAVAVSDEEILEAIRLLARREGIFVE 330
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
73-312 |
9.36e-15 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 74.94 E-value: 9.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 73 NIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAgVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKINRCQDLGA 152
Cdd:cd01563 39 NLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKA-VACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 153 NILVQGEDIAESREIALRMAhDSNGTYINGYDHYDILAGAGTTGIEILEQI--QMPDAIlvpvGGGGLVAGVATAV---- 226
Cdd:cd01563 118 TVLAVEGNFDDALRLVRELA-EENWIYLSNSLNPYRLEGQKTIAFEIAEQLgwEVPDYV----VVPVGNGGNITAIwkgf 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 227 ---KALSPTTEV---IGVVSETCQAIVKSLQAGHPVYTPTR--PTLADGLAVPNAgVNAFaSMIGKVDR----VISVPEN 294
Cdd:cd01563 193 kelKELGLIDRLprmVGVQAEGAAPIVRAFKEGKDDIEPVEnpETIATAIRIGNP-ASGP-KALRAVREsggtAVAVSDE 270
|
250
....*....|....*...
gi 17537387 295 DIAVAILRLIENEKVVCE 312
Cdd:cd01563 271 EILEAQKLLARTEGIFVE 288
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
73-272 |
1.50e-14 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 74.48 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 73 NIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAgVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKINRCQDLGA 152
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINE-VVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 153 NI-LVQGeDIAESREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQIQMPDAILVPVGGGGLVAGVATAVKALSP 231
Cdd:PRK08329 152 ELhFVEG-DRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIWKGFKELHE 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17537387 232 TTEV------IGVVSETCQAIVKSlqaghpvyTPTRPTLADGLAVPN 272
Cdd:PRK08329 231 MGEIskmpklVAVQAEGYESLCKR--------SKSENKLADGIAIPE 269
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
49-341 |
1.61e-11 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 65.99 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 49 HRIQNGIVRTDCRKSRCLSKLfDMNIYLKMEVNQDTGSFKERGARYALQN-LPEEKKkaGVYAASAGNHALALSLHGKQL 127
Cdd:PRK05638 58 KIISLGEGGTPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYgLPYAAN--GFIVASDGNAAASVAAYSARA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 128 GVEVNVVMPKIAPLMKINRCQDLGANILVQGEDIAESREIALRMAHdSNGTYiNGYDHYDILA--GAGTTGIEILEQIQ- 204
Cdd:PRK05638 135 GKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELAR-LNGLY-NVTPEYNIIGleGQKTIAFELWEEINp 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 205 ----MPDAILVPVGGGGLVAGVATAVKALSPTTEVIGVVSETCQAIVKSLqagHPVYTPTRPTLADGLAVPNAGVNAFAS 280
Cdd:PRK05638 213 thviVPTGSGSYLYSIYKGFKELLEIGVIEEIPKLIAVQTERCNPIASEI---LGNKTKCNETKALGLYVKNPVMKEYVS 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537387 281 -MIGKVDRVISVPENDIAVAILRLIENEKVVCEGAGAIGIGAILS--GKLNHLKGKTVVSILSG 341
Cdd:PRK05638 290 eAIKESGGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKlgEEGYIEKGDKVVLVVTG 353
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
73-273 |
3.61e-11 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 64.64 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 73 NIYLKMEVNQDTGSFKERGARYALQnlpeEKKKAGVYA---ASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKINRCQD 149
Cdd:PRK08197 96 RLWVKDEGLNPTGSFKARGLAVGVS----RAKELGVKHlamPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECAL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 150 LGAN-ILVQGEdIAESREIALRMAHDSngtyinGYdhYDI--------LAGAGTTGIEILEQI--QMPDAILVPVGGGGL 218
Cdd:PRK08197 172 AGAElYLVDGL-ISDAGKIVAEAVAEY------GW--FDVstlkepyrIEGKKTMGLELAEQLgwRLPDVILYPTGGGVG 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537387 219 VAGVATAVKAL-------SPTTEVIGVVSETCQAIVKSLQAG--HPVYTPTRPTLADGLAVPNA 273
Cdd:PRK08197 243 LIGIWKAFDELealgwigGKRPRLVAVQAEGCAPIVKAWEEGkeESEFWEDAHTVAFGIRVPKA 306
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
66-311 |
3.74e-10 |
|
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: 60.61 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 66 LSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEE---KKKAGVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLM 142
Cdd:cd01561 11 LSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRgllKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETMSEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 143 KINRCQDLGAN-ILVQGED-------IAESREIAlrmAHDSNGTYINGYD-------HYDilagagTTGIEILEQIQ-MP 206
Cdd:cd01561 91 KRKLLRALGAEvILTPEAEadgmkgaIAKARELA---AETPNAFWLNQFEnpanpeaHYE------TTAPEIWEQLDgKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 207 DAILVPVGGGGLVAGVATAVKALSPTTEVIGVvsETCQAIVKSLQAGHPVYTP-----TRPTLADglavpnagvnafasm 281
Cdd:cd01561 162 DAFVAGVGTGGTITGVARYLKEKNPNVRIVGV--DPVGSVLFSGGPPGPHKIEgigagFIPENLD--------------- 224
|
250 260 270
....*....|....*....|....*....|
gi 17537387 282 IGKVDRVISVPENDIAVAILRLIENEKVVC 311
Cdd:cd01561 225 RSLIDEVVRVSDEEAFAMARRLAREEGLLV 254
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
73-209 |
1.38e-06 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 50.12 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 73 NIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAgVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKINRCQDLGA 152
Cdd:PRK06450 66 NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQ-ISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGA 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 153 NIL-VQGediaeSREIALRMAHDSNGTYINGYDHYDILAGAGTTGIEILEQI--QMPDAI 209
Cdd:PRK06450 145 EVVrVRG-----SREDVAKAAENSGYYYASHVLQPQFRDGIRTLAYEIAKDLdwKIPNYV 199
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
67-312 |
5.08e-05 |
|
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: 45.07 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 67 SKLFDMNIYLKMEVNQDTGSFKERGARYALQNLPEEKKKAgVYAASAGNHALALSLHGKQLGVEVNVVMP--KIApLMKI 144
Cdd:TIGR00260 33 ANVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDT-VLCASTGNTGAAAAAYAGKAGLKVVVLYPagKIS-LGKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 145 nrCQDLGANILVQGED------------IAESREIALRMAhdsngtyINGYDHYdiLAGAGTTGIEILEQI--QMPDAIL 210
Cdd:TIGR00260 111 --AQALGYNAEVVAIDgnfddaqrlvkqLFEDKPALGLNS-------ANSIPYR--LEGQKTYAFEAVEQLgwEAPDKVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 211 VPVGGGGLVAGVATAVKA-----LSPTTEVIGVVSETCQAIVKSLQAGHPVYTPTRP-TLADGLAV--PNAGVNA---FA 279
Cdd:TIGR00260 180 VPVPNSGNFGAIWKGFKEkkmlgLDSLPVKRGIQAEGAADIVRAFLEGGQWEPIETPeTLSTAMDIgnPANWPRAleaFR 259
|
250 260 270
....*....|....*....|....*....|...
gi 17537387 280 SMIGKVDrviSVPENDIAVAILRLIENEKVVCE 312
Cdd:TIGR00260 260 RSNGYAE---DLSDEEILEAIKLLAREEGYFVE 289
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
66-302 |
5.41e-05 |
|
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: 45.04 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 66 LSKLFDMNIYLKMEVNQDTGSFKERGARYALQNLpeEKK---KAG--VYAASAGNHALALSLHGKQLGVEVNVVMPKIAP 140
Cdd:COG0031 22 LSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDA--EKRgllKPGgtIVEATSGNTGIGLAMVAAAKGYRLILVMPETMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 141 LMKINRCQDLGAN-ILVQGED-----IAESREIAlrmAHDSNGTYINGYD-------HYDilagagTTGIEILEQIQM-P 206
Cdd:COG0031 100 KERRALLRAYGAEvVLTPGAEgmkgaIDKAEELA---AETPGAFWPNQFEnpanpeaHYE------TTGPEIWEQTDGkV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 207 DAIlvpvgggglVAGVATAVKALSPTTEVIGVvsETCQAIVKSLQAGHPVYTPtrptladGLAvpnagvnafASMIGK-- 284
Cdd:COG0031 171 DAFvagvgtggtITGVGRYLKERNPDIKIVAV--EPEGSPLLSGGEPGPHKIE-------GIG---------AGFVPKil 232
|
250 260
....*....|....*....|..
gi 17537387 285 ----VDRVISVPENDiAVAILR 302
Cdd:COG0031 233 dpslIDEVITVSDEE-AFAMAR 253
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
62-211 |
2.32e-04 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 43.16 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 62 KSRCLSKLFDMN-IYLKMEVNQDTGSFKERGARYALQNLPEEKKKaGVYAASAGNHALALSLHGKQLGVEVNVVMPKIAP 140
Cdd:PRK06381 20 RARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYS-GITVGTCGNYGASIAYFARLYGLKAVIFIPRSYS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17537387 141 LMKINRCQDLGANIL-VQG---EDIAESREIALRMA-HDSNGTYINgyDHYDILAGAGTTgIEILEQI-QMPDAILV 211
Cdd:PRK06381 99 NSRVKEMEKYGAEIIyVDGkyeEAVERSRKFAKENGiYDANPGSVN--SVVDIEAYSAIA-YEIYEALgDVPDAVAV 172
|
|
| diampropi_NH3ly |
TIGR01747 |
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ... |
86-204 |
3.18e-04 |
|
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]
Pssm-ID: 130808 Cd Length: 376 Bit Score: 42.96 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 86 SFKERGARYALQNLPEEK----------------------KKAGVYAASAGNHALALSLHGKQLGVEVNVVMPKIAPLMK 143
Cdd:TIGR01747 53 AFKMLGGSYAIAQYLAEKlhldietlsfehlkndaigekmGQATFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQER 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17537387 144 INRCQDLGANILVQGEDIAESREIALRMAHDSNGTYIN--GYDHYD-----ILAGAGTTGIEILEQIQ 204
Cdd:TIGR01747 133 VENILNLGAECTITDMNYDDTVRLAMQMAQQHGWVVVQdtAWEGYEkiptwIMQGYATLADEAVEQLR 200
|
|
| 2_3_DAP_am_ly |
TIGR03528 |
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ... |
10-204 |
3.78e-04 |
|
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.
Pssm-ID: 274631 Cd Length: 396 Bit Score: 42.40 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 10 SIFYSLAHRRHVASVPLKDVFCDPENPKILQFgdismahHRIQNGIVRTDCRKSRCLSKLFDMN-IYLKMEVNQ-DTGSF 87
Cdd:TIGR03528 1 SIKIIINDNKKATNGTDLSLLSKEEAEKVRAF-------HQSFPGYQPTPLAELDNLAKHLGVGsILVKDESYRfGLNAF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 88 KERGARYALQNL-------------------PEEKKKAG--VYA-ASAGNHALALSLHGKQLGVEVNVVMPKIAPLMKIN 145
Cdd:TIGR03528 74 KVLGGSYAIGKYlaeklgkdiselsfeklksNEIREKLGdiTFVtATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17537387 146 RCQDLGANILVQGEDIAESREIALRMAHDsNG------TYINGYDHYD--ILAGAGTTGIEILEQIQ 204
Cdd:TIGR03528 154 NIRAEGAECTITDLNYDDAVRLAWKMAQE-NGwvmvqdTAWEGYEKIPtwIMQGYGTLALEALEQLK 219
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
366-430 |
1.33e-03 |
|
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.
Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 36.89 E-value: 1.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17537387 366 LSVIIPDKPGGLSKLTGLVGELSGNVRDLYlerafMRNDMSSQRVKMVIEVRGEEHEMQLKQKFQ 430
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIE-----QRTSGDGGEADIFIVVDGDGDLEKLLEALE 60
|
|
| ACT_CBS |
cd04884 |
C-terminal ACT domain of the cystathionine beta-synthase (CBS) domain protein found in ... |
365-433 |
1.78e-03 |
|
C-terminal ACT domain of the cystathionine beta-synthase (CBS) domain protein found in Thermotoga maritima, Tm0935, and delta proteobacteria; This CD includes the C-terminal ACT domain of the cystathionine beta-synthase (CBS) domain protein found in Thermotoga maritima, Tm0935, and delta proteobacteria. This protein has two N-terminal tandem CBS domains and a single C-terminal ACT domain. The CBS domain is found in a wide range of proteins, often in tandem arrangements and together with a variety of other functional domains. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153156 Cd Length: 72 Bit Score: 37.08 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537387 365 RLSVIIPDKPGGLSKLTGLVGELSGNVRDLYLERAFMRNDMSSQRVKMVIEVRGEEHEM--QLKQKFQEVY 433
Cdd:cd04884 1 RFTFLLEDKPGTLKPVVDTLREFNARIISILTAFEDAPDGMRRVFIRVTPMDRSKENELieELKAKFTVVY 71
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
71-211 |
2.13e-03 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 40.18 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 71 DMN-IYLKMEVNQDTGSFKERGARYALQNLPEEKKKA----GVYAASAGNHALALSLHGKQLGVEVNVVMPKIAP-LMKI 144
Cdd:PLN02569 148 GMNdLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAkpvvGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKIsIAQL 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537387 145 NRCQDLGANILVQGEDIAES----REIALRMA-HDSNGtyINGYDhydiLAGAGTTGIEILEQI--QMPDAILV 211
Cdd:PLN02569 228 VQPIANGALVLSIDTDFDGCmrliREVTAELPiYLANS--LNSLR----LEGQKTAAIEILQQFdwEVPDWVIV 295
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
66-202 |
3.41e-03 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 39.46 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537387 66 LSKLFDMNIYLKMEVNQDTGSFKERGARYALQNlpEEKK---KAG--VYAASAGNHALALSLHGKQLGVEVNVVMPKIAP 140
Cdd:PRK10717 22 ASEATGCEILGKAEFLNPGGSVKDRAALNIIWD--AEKRgllKPGgtIVEGTAGNTGIGLALVAAARGYKTVIVMPETQS 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17537387 141 LMKINRCQDLGAN-ILVQGEDIAESR---EIALRMAHDSNGTYINGY---DHYDILAGA----GTTGIEILEQ 202
Cdd:PRK10717 100 QEKKDLLRALGAElVLVPAAPYANPNnyvKGAGRLAEELVASEPNGAiwaNQFDNPANReahyETTGPEIWEQ 172
|
|
| |
