|
Name |
Accession |
Description |
Interval |
E-value |
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
9-314 |
0e+00 |
|
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: 526.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYF 88
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 89 GLRFICVVDPKTTKQNLNIIKVYGAELEMVLEPDpETGEYLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYEGTFPE 168
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPD-ETGGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 169 IVAALKEiPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGSIIFGGEKKARLVPGMGASIKSQFLEENLLNEYVH 248
Cdd:TIGR03945 160 IARAFPT-LDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVH 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152074665 249 VTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIPAGSNCVLIFADRGERYLDTIYSDGWV 314
Cdd:TIGR03945 239 VPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEWV 304
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
14-306 |
1.34e-124 |
|
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: 358.36 E-value: 1.34e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 14 GATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYFGLRFI 93
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 94 CVVDPKTTKQNLNIIKVYGAELEMVlepDPETGEYLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYEGTFPEIVAAL 173
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILT---PEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 174 KEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGSIIF-GGEKKARLVPGMGASIKSQFLEENLLNEYVHVTDL 252
Cdd:cd01561 158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFsGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 152074665 253 DCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIPAGSNCVLIFADRGERYLD 306
Cdd:cd01561 238 EAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
9-307 |
2.71e-123 |
|
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: 355.51 E-value: 2.71e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYF 88
Cdd:COG0031 7 ILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 89 GLRFICVVDPKTTKQNLNIIKVYGAELemVLEPDPETgeyLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYEGTFPE 168
Cdd:COG0031 87 GYRLILVMPETMSKERRALLRAYGAEV--VLTPGAEG---MKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 169 IVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGSIIF-GGEKKARLVPGMGASIKSQFLEENLLNEYV 247
Cdd:COG0031 162 IWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDPSLIDEVI 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 248 HVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIPAGSNCVLIFADRGERYLDT 307
Cdd:COG0031 242 TVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
9-307 |
2.01e-77 |
|
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: 238.72 E-value: 2.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYF 88
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 89 GLRFICVVDPKTTKQNLNIIKVYGAELEMVlepDPETGeyLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYEGTFPE 168
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILT---PGEEG--MKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 169 IVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVD-AVGSIIFGGEKKARLVPGMGASIKSQFLEENLLNEYV 247
Cdd:TIGR01136 156 IWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEpAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152074665 248 HVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKI-KDSIPAGSNCVLIFADRGERYLDT 307
Cdd:TIGR01136 236 TVSDEDAIETARRLAREEGILVGISSGAAVAAALKLaKRLENADKVIVAILPDTGERYLST 296
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-299 |
3.46e-69 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 217.56 E-value: 3.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAmEKGKigPNTVVIESSSGNLGIGLAQVCRYF 88
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRL-KEGE--GGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 89 GLRFICVVDPKTTKQNLNIIKVYGAELEMVlepdpetGEYLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAhYEGTFPE 168
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV-------GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 169 IVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGSIIFGG----------EKKARLVPGMGASIKSQFL 238
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARslaagrpvpvPVADTIADGLGVGDEPGAL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152074665 239 EENLLNEY----VHVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDS-IPAGSNCVLIFAD 299
Cdd:pfam00291 230 ALDLLDEYvgevVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGeLKGGDRVVVVLTG 295
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
9-307 |
3.81e-69 |
|
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: 217.62 E-value: 3.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPfRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYF 88
Cdd:TIGR01139 1 ISELIGNTPLVRLNRIEGCNA-NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 89 GLRFICVVDPKTTKQNLNIIKVYGAELEMVlepDPETGeyLPARLKRVQALMAKFSDSFW-PNQYLNEYNPRAHYEGTFP 167
Cdd:TIGR01139 80 GYKLILTMPETMSIERRKLLKAYGAELVLT---PGAEG--MKGAIAKAEEIAASTPNSYFmLQQFENPANPEIHRKTTGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 168 EIVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGS-IIFGGEKKARLVPGMGASIKSQFLEENLLNEY 246
Cdd:TIGR01139 155 EIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESpVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEV 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152074665 247 VHVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIPAGSNCVLIFADRGERYLDT 307
Cdd:TIGR01139 235 ITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLST 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
16-300 |
2.44e-63 |
|
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: 200.82 E-value: 2.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 16 TPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIgPNTVVIESSSGNLGIGLAQVCRYFGLRFICV 95
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 96 VDPKTTKQNLNIIKVYGAELEMVlepdpetGEYLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYeGTFPEIVAALKE 175
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLV-------PGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 176 I-PNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAvgsiifggekkarlvpgmgasiksqfleenllnEYVHVTDLDC 254
Cdd:cd00640 152 QkPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEP---------------------------------EVVTVSDEEA 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 152074665 255 VIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIPAGSNCVLIFADR 300
Cdd:cd00640 199 LEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
7-317 |
2.67e-61 |
|
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: 201.95 E-value: 2.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 7 QGILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCR 86
Cdd:TIGR01137 3 DNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 87 YFGLRFICVVDPKTTKQNLNIIKVYGAELemVLEP------DPETGEYLPARLKRvqalmaKFSDSFWPNQYLNEYNPRA 160
Cdd:TIGR01137 83 IKGYKCIIVLPEKMSSEKVDVLRALGAEI--VRTPtaaafdSPESHIGVAKRLVR------EIPGAHILDQYRNPSNPLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 161 HYEGTFPEIVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGSIIFGGE------KKARLVPGMGASIK 234
Cdd:TIGR01137 155 HYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEelnqtgRTPYKVEGIGYDFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 235 SQFLEENLLNEYVHVTDLDCVIGCQRLLRTEAILAGGSSG-AVLMGFDKIKDSIPAGSNCVLIFADRGERYLDTIYSDGW 313
Cdd:TIGR01137 235 PTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGsAVVAALKAAEDELQEGQRCVVLLPDSIRNYMTKFLNDEW 314
|
....
gi 152074665 314 VTQH 317
Cdd:TIGR01137 315 MLDN 318
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
9-307 |
3.38e-51 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 171.21 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYF 88
Cdd:PRK11761 6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 89 GLRFICVVDPKTTKQNLNIIKVYGAELemVLEPDPETGEYlparlKRVQAL-MAKFSDSFWPNQYLNEYNPRAHYEGTFP 167
Cdd:PRK11761 86 GYRMKLIMPENMSQERRAAMRAYGAEL--ILVPKEQGMEG-----ARDLALqMQAEGEGKVLDQFANPDNPLAHYETTGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 168 EIVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVD-AVGSIIFGGEK--KARLvPGMgasiksqfLEENLLN 244
Cdd:PRK11761 159 EIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQpEEGSSIPGIRRwpEEYL-PKI--------FDASRVD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152074665 245 EYVHVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIPaGSNCVLIFADRGERYLDT 307
Cdd:PRK11761 230 RVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENP-NAVIVAIICDRGDRYLST 291
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
9-307 |
4.86e-50 |
|
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: 168.17 E-value: 4.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYF 88
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 89 GLRFICVVDPKTTKQNLNIIKVYGAELEMVLEPDPETGEYLPARlKRVQALMAKFSDsfwpnQYLNEYNPRAHYEGTFPE 168
Cdd:TIGR01138 82 GYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLAL-ELANRGEGKLLD-----QFNNPDNPYAHYTSTGPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 169 IVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVD-AVGSIIFGgekkARLVPgmgASIKSQFLEENLLNEYV 247
Cdd:TIGR01138 156 IWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQpEEGSSIPG----IRRWP---TEYLPGIFDASLVDRVL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 248 HVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIPAGSnCVLIFADRGERYLDT 307
Cdd:TIGR01138 229 DIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLST 287
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
7-316 |
3.98e-49 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 166.96 E-value: 3.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 7 QGILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCR 86
Cdd:PRK10717 5 EDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 87 YFGLRFIcVVDPKT-TKQNLNIIKVYGAELemVLEP-----DPETGEYLPARLkrVQALMAKFSD-SFWPNQYLNEYNPR 159
Cdd:PRK10717 85 ARGYKTV-IVMPETqSQEKKDLLRALGAEL--VLVPaapyaNPNNYVKGAGRL--AEELVASEPNgAIWANQFDNPANRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 160 AHYEGTFPEI-------VAAlkeipnyLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGSIIFG----GEKKAR---L 225
Cdd:PRK10717 160 AHYETTGPEIweqtdgkVDG-------FVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktGELKAEgssI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 226 VPGMGASIKSQFLEENLLNEYVHVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIPAGSNCVLIFADRGERYL 305
Cdd:PRK10717 233 TEGIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQ 312
|
330
....*....|.
gi 152074665 306 DTIYSDGWVTQ 316
Cdd:PRK10717 313 SKLFNPDFLRE 323
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
9-308 |
7.34e-48 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 163.56 E-value: 7.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGP-NTVVIESSSGNLGIGLAQVCRY 87
Cdd:PLN02565 9 VTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPgESVLIEPTSGNTGIGLAFMAAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 88 FGLRFICVVDPKTTKQNLNIIKVYGAELEMVlepDPETGeyLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYEGTFP 167
Cdd:PLN02565 89 KGYKLIITMPASMSLERRIILLAFGAELVLT---DPAKG--MKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 168 EIVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGS-IIFGGEKKARLVPGMGASIKSQFLEENLLNEY 246
Cdd:PLN02565 164 EIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESaVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152074665 247 VHVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKI-KDSIPAGSNCVLIFADRGERYLDTI 308
Cdd:PLN02565 244 VQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIaKRPENAGKLIVVIFPSFGERYLSSV 306
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
9-307 |
2.55e-47 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 162.09 E-value: 2.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGP-NTVVIESSSGNLGIGLAQVCRY 87
Cdd:PLN00011 11 VTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPgKSTLIEATAGNTGIGLACIGAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 88 FGLRFICVVDPKTTKQNLNIIKVYGAELEMVlepDPETGeyLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYEGTFP 167
Cdd:PLN00011 91 RGYKVILVMPSTMSLERRIILRALGAEVHLT---DQSIG--LKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 168 EIVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGS-IIFGGEKKARLVPGMGASIKSQFLEENLLNEY 246
Cdd:PLN00011 166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESaVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEI 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152074665 247 VHVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKI-KDSIPAGSNCVLIFADRGERYLDT 307
Cdd:PLN00011 246 IQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVaKRPENAGKLIVVIFPSGGERYLST 307
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
12-307 |
4.62e-40 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 145.30 E-value: 4.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 12 LIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGP-NTVVIESSSGNLGIGLAQVCRYFGL 90
Cdd:PLN03013 120 LIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPgKSVLVEPTSGNTGIGLAFIAASRGY 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 91 RFICVVDPKTTKQNLNIIKVYGAELEMVlepDPETGeyLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYEGTFPEIV 170
Cdd:PLN03013 200 RLILTMPASMSMERRVLLKAFGAELVLT---DPAKG--MTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTGPEIW 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 171 AALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGS-IIFGGEKKARLVPGMGASIKSQFLEENLLNEYVHV 249
Cdd:PLN03013 275 DDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESdILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVIAI 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 152074665 250 TDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKI-KDSIPAGSNCVLIFADRGeRYLDT 307
Cdd:PLN03013 355 SSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVaKRPENAGKLIAVSLFASG-RDIYT 412
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
12-308 |
1.58e-38 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 140.10 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 12 LIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGP-NTVVIESSSGNLGIGLAQVCRYFGL 90
Cdd:PLN02556 56 LIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPgKTTLIEPTSGNMGISLAFMAAMKGY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 91 RFICVVDPKTTKQNLNIIKVYGAELEMVlepDPETGeyLPARLKRVQALMAKFSDSFWPNQYLNEYNPRAHYEGTFPEIV 170
Cdd:PLN02556 136 KMILTMPSYTSLERRVTMRAFGAELVLT---DPTKG--MGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIW 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 171 A-ALKEIPNYLFGaVSTCGTIMGCANYIHNQRLETKVIAVD-AVGSIIFGGEKKARLVPGMGASIKSQFLEENLLNEYVH 248
Cdd:PLN02556 211 EdTLGQVDIFVMG-IGSGGTVSGVGKYLKSKNPNVKIYGVEpAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLE 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152074665 249 VTDLDCVIGCQRLLRTEAILAGGSSGA-VLMGFDKIKDSIPAGSNCVLIFADRGERYLDTI 308
Cdd:PLN02556 290 VSSEDAVNMARELALKEGLMVGISSGAnTVAALRLAKMPENKGKLIVTVHPSFGERYLSSV 350
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
7-317 |
6.40e-31 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 120.48 E-value: 6.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 7 QGILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVVIESSSGNLGIGLAQVCR 86
Cdd:PLN02356 45 NGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 87 YFGLRFICVVDPKTTKQNLNIIKVYGAELEMVlEPDPETGEYLPARLKRVQALMAK------------------------ 142
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERV-RPVSITHKDHYVNIARRRALEANelaskrrkgsetdgihlektngci 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 143 ---------FSDS----FWPNQYLNEYNPRAHYEGTFPEIVAALKEIPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAV 209
Cdd:PLN02356 204 seeekenslFSSSctggFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 210 DAVGSIIFGG----------EKKAR--------LVPGMGASIKSQFLEENLLNEYVHVTDLDCVIGCQRLLRTEAILAGG 271
Cdd:PLN02356 284 DPPGSGLFNKvtrgvmytreEAEGRrlknpfdtITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGS 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 152074665 272 SSGAVLMGFDKIKDSIPAGSNCVLIFADRGERYLDTIYSDGWVTQH 317
Cdd:PLN02356 364 SSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQH 409
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
14-181 |
1.73e-13 |
|
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: 69.93 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 14 GATPLIQLTQIYKDLPF-RVFAKLEGFNPSGSIKDRP---AISMIKQamekgkIGPNTVVIeSSSGNLGIGLAQVCRYFG 89
Cdd:cd01563 21 GNTPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGmtvAVSKAKE------LGVKAVAC-ASTGNTSASLAAYAARAG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 90 LRFICVVDPKTTKQNLNIIKVYGAELEMVlepdpeTGEYLPArLKRVQALMAKfsdsFWPnqYL-NEYNP-RahYEGT-- 165
Cdd:cd01563 94 IKCVVFLPAGKALGKLAQALAYGATVLAV------EGNFDDA-LRLVRELAEE----NWI--YLsNSLNPyR--LEGQkt 158
|
170
....*....|....*....
gi 152074665 166 --FpEIVAAL-KEIPNYLF 181
Cdd:cd01563 159 iaF-EIAEQLgWEVPDYVV 176
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
14-118 |
8.89e-12 |
|
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: 65.22 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 14 GATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIgpntVVIESSSGNLGIGLAQVCRYFGLRFI 93
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAARAGIEVF 140
|
90 100
....*....|....*....|....*..
gi 152074665 94 CVVdP--KTTKQNLNIIKVYGAELEMV 118
Cdd:COG0498 141 VFV-PegKVSPGQLAQMLTYGAHVIAV 166
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
16-114 |
9.49e-12 |
|
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: 64.63 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 16 TPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPNTVViESSSGNLGIGLAQVCRYFGLRfiC- 94
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECVHVV-CSSGGNAGLAAAYAARKLGVP--Ct 78
|
90 100
....*....|....*....|.
gi 152074665 95 VVDPKTTKQNL-NIIKVYGAE 114
Cdd:cd06448 79 IVVPESTKPRVvEKLRDEGAT 99
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
16-296 |
1.88e-10 |
|
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: 60.82 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 16 TPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQ-AMEKGKIGpntvVIESSSGNLGIGLAQVCRYFGLR-FI 93
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASlSEEERARG----VVAASAGNHAQGVAYAARLLGIPaTI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 94 CVvdPKTT-KQNLNIIKVYGAELEmvlepdpETGEYLPARLKRVQALMAK--------FSDsfwpnqylneynprahyeg 164
Cdd:COG1171 101 VM--PETApAVKVAATRAYGAEVV-------LHGDTYDDAEAAAAELAEEegatfvhpFDD------------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 165 tfPEIVA--------ALKEIPN--YLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGSiifggekkarlvPGMGASIK 234
Cdd:COG1171 153 --PDVIAgqgtialeILEQLPDldAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGA------------AAMYRSLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 235 S---QFLEE----------------------NLLNEYVHVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDSIpA 289
Cdd:COG1171 219 AgepVTLPGvdtiadglavgrpgeltfeilrDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERL-K 297
|
....*..
gi 152074665 290 GSNCVLI 296
Cdd:COG1171 298 GKRVVVV 304
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
16-214 |
7.41e-10 |
|
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: 59.04 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 16 TPLIQ---LTQIYKDlpfRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGPntvVIESSSGNLGIGLAQVCRYFGLR- 91
Cdd:cd01562 18 TPLLTsptLSELLGA---EVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 92 FICVvdPKTT-KQNLNIIKVYGAELemVLepdpeTGEYLPARLKRVQALmAKFSDSFwpnqYLNEYNpraHYE-----GT 165
Cdd:cd01562 92 TIVM--PETApAAKVDATRAYGAEV--VL-----YGEDFDEAEAKAREL-AEEEGLT----FIHPFD---DPDviagqGT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 152074665 166 FP-EIVAALKEIpNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVGS 214
Cdd:cd01562 155 IGlEILEQVPDL-DAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGA 203
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
14-192 |
3.03e-09 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 57.41 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 14 GATPLIQLTQIYKDLPFR-VFAKLEGFNPSGSIKDRPAISMIKQAMEKGKigpNTVVIeSSSGNLGIGLAQVCRYFGLRF 92
Cdd:PRK06381 14 GGTPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY---SGITV-GTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 93 ICVVDPKTTKQNLNIIKVYGAElemVLEPDpetGEYLPARLKRVqalmaKFS-DSFWPNQYLNEYNPRAHYEG---TFPE 168
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAE---IIYVD---GKYEEAVERSR-----KFAkENGIYDANPGSVNSVVDIEAysaIAYE 158
|
170 180
....*....|....*....|....
gi 152074665 169 IVAALKEIPNYLFGAVSTCGTIMG 192
Cdd:PRK06381 159 IYEALGDVPDAVAVPVGNGTTLAG 182
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
14-312 |
4.60e-08 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 54.05 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 14 GATPLIQlTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKIGpntvVIESSSGNLGIGLAQVCRYFGLRFI 93
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANG----FIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 94 CVVDPKTTKQNLNIIKVYGAELeMVLEPDPETGEYLPARLKRVQALMAKFSDS--------------FWpnqylNEYNPR 159
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKI-IRYGESVDEAIEYAEELARLNGLYNVTPEYniiglegqktiafeLW-----EEINPT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 160 AHYEGT------------FPEI--VAALKEIPNYLfgAVSTcgtimGCANyihnqrletkviavdAVGSIIFGGEKKARL 225
Cdd:PRK05638 214 HVIVPTgsgsylysiykgFKELleIGVIEEIPKLI--AVQT-----ERCN---------------PIASEILGNKTKCNE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 226 VPGMGASIKSQFLEENLLN------EYVHVTDLDCVIGCQRLLRTEAILAGGSSGAVLMGFDKIKDS--IPAGSNCVLIF 297
Cdd:PRK05638 272 TKALGLYVKNPVMKEYVSEaikesgGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVV 351
|
330
....*....|....*
gi 152074665 298 ADRGeryLDTIYSDG 312
Cdd:PRK05638 352 TGSG---LKGYGEGG 363
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
21-190 |
2.93e-07 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 51.37 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 21 LTQIYKDlPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKigpNTVVIEsSSGNLGIGLAQVCRYFGLRFICVVDPKT 100
Cdd:PRK08329 64 ITPTVKR-SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI---NEVVID-SSGNAALSLALYSLSEGIKVHVFVSYNA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 101 TKQNLNIIKVYGAELEMVlEPDpetgeylpaRLKrVQALMAKFSD-------SFWPNQYLNEYNPRAHYEgTFPEIvaal 173
Cdd:PRK08329 139 SKEKISLLSRLGAELHFV-EGD---------RME-VHEEAVKFSKrnnipyvSHWLNPYFLEGTKTIAYE-IYEQI---- 202
|
170
....*....|....*..
gi 152074665 174 kEIPNYLFGAVSTcGTI 190
Cdd:PRK08329 203 -GVPDYAFVPVGS-GTL 217
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
14-115 |
2.87e-06 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 48.19 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 14 GATPLIQltqiYKDLPFrvfaKLEGFNPSGSIKDRPAISMIKQAMEKGKigpnTVVIESSSGNLGIGLAQVCRYFGLRFI 93
Cdd:PRK06450 57 GRTPLIK----KGNIWF----KLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVK 124
|
90 100
....*....|....*....|...
gi 152074665 94 CVVdPKTTK-QNLNIIKVYGAEL 115
Cdd:PRK06450 125 IFV-PETASgGKLKQIESYGAEV 146
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
2-117 |
6.82e-06 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 47.07 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 2 IQQQNQGILSLIGATPLIQLTQIYKDLPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKigPNTVVIESSSGNLGIGL 81
Cdd:PRK06608 10 IAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGK--LPDKIVAYSTGNHGQAV 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 152074665 82 AQVCRYFGLrficvvdPKTTKQNLNIIKV-------YGAELEM 117
Cdd:PRK06608 88 AYASKLFGI-------KTRIYLPLNTSKVkqqaalyYGGEVIL 123
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
9-115 |
1.05e-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: 46.61 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 9 ILSLI-GATPLIQLTQIYKDL-PFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGkigpNTVVIESSSGNLGIGLAQVCR 86
Cdd:TIGR00260 15 LVDLGeGVTPLFRAPALAANVgIKNLYVKELGHNPTLSFKDRGMAVALTKALELG----NDTVLCASTGNTGAAAAAYAG 90
|
90 100 110
....*....|....*....|....*....|
gi 152074665 87 YFGLRFICVV-DPKTTKQNLNIIKVYGAEL 115
Cdd:TIGR00260 91 KAGLKVVVLYpAGKISLGKLAQALGYNAEV 120
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
14-118 |
1.07e-05 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 46.53 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 14 GATPLIQLTQIYKDLPF-RVFAKLEGFNPSGSIKDRP---AISMIKQAMEKGKIGPntvviesSSGNLGIGLAQVCRYFG 89
Cdd:PRK08197 78 GMTPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGlavGVSRAKELGVKHLAMP-------TNGNAGAAWAAYAARAG 150
|
90 100 110
....*....|....*....|....*....|
gi 152074665 90 LRFICVVdPKTTKQ-NLNIIKVYGAELEMV 118
Cdd:PRK08197 151 IRATIFM-PADAPEiTRLECALAGAELYLV 179
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
31-209 |
1.21e-05 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 46.22 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 31 RVFAKLEGFNPSGSIKDRPAISMIKQ-AMEKGKIGpntvVIESSSGNLGIGLAQVCRYFGLRFICVVDPKTTKQNLNIIK 109
Cdd:PRK06815 36 EVYLKCEHLQHTGSFKFRGASNKLRLlNEAQRQQG----VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 110 VYGAELEmVLEPDPETGEYLPARLKRVQALMakfsdsfwpnqYLNEYNPrahyegtfPEIVAA--------LKEIPNY-- 179
Cdd:PRK06815 112 ALGAEVR-LYGGDALNAELAARRAAEQQGKV-----------YISPYND--------PQVIAGqgtigmelVEQQPDLda 171
|
170 180 190
....*....|....*....|....*....|
gi 152074665 180 LFGAVSTCGTIMGCANYIHNQRLETKVIAV 209
Cdd:PRK06815 172 VFVAVGGGGLISGIATYLKTLSPKTEIIGC 201
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
2-213 |
4.39e-05 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 44.80 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 2 IQQQNQGILSLIGATPL---IQLTQIYKdlpFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKigpNTVVIESSSGNLG 78
Cdd:PRK08639 12 IDKAAKRLKDVVPETPLqrnDYLSEKYG---ANVYLKREDLQPVRSYKLRGAYNAISQLSDEEL---AAGVVCASAGNHA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 79 IGLAQVCRYFGLR---FIcvvdPKTT-KQNLNIIKVYGAE-LEMVLepdpeTGEYLPARLKRVQALMAKFSDSFWPnqyl 153
Cdd:PRK08639 86 QGVAYACRHLGIPgviFM----PVTTpQQKIDQVRFFGGEfVEIVL-----VGDTFDDSAAAAQEYAEETGATFIP---- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 152074665 154 neynPRAHY-----EGTFP-EIVAALKE--IPNYLFGAVSTCGTIMGCANYIHNQRLETKVIAVDAVG 213
Cdd:PRK08639 153 ----PFDDPdviagQGTVAvEILEQLEKegSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
16-114 |
4.89e-05 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 44.45 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 16 TPLI---QLTQIYKdlPFRVFAKLEGFNPSGSIKDRPAISMIKQAMEKGKigpNTVVIESSSGNLGIGLAQVCRYFGLRf 92
Cdd:cd06446 35 TPLYrakRLSEYLG--GAKIYLKREDLNHTGAHKINNALGQALLAKRMGK---KRVIAETGAGQHGVATATACALFGLE- 108
|
90 100
....*....|....*....|....*..
gi 152074665 93 iCVV-----DPKTTKQNLNIIKVYGAE 114
Cdd:cd06446 109 -CEIymgavDVERQPLNVFRMELLGAE 134
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
15-308 |
6.52e-05 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 44.36 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 15 ATPLI---QLTQIYKDLPFR---VFAKLEGFNPSGSIKDRPAISmikQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYF 88
Cdd:PLN02618 66 ETPLYfaeRLTEHYKRADGEgpeIYLKREDLNHTGAHKINNAVA---QALLAKRLGKKRIIAETGAGQHGVATATVCARF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 89 GLRFICVVDPK-TTKQNLNI--IKVYGAELEMVLEPDP-----------------ETGEYL----------PARLKRVQA 138
Cdd:PLN02618 143 GLECIVYMGAQdMERQALNVfrMRLLGAEVRPVHSGTAtlkdatseairdwvtnvETTHYIlgsvagphpyPMMVRDFHS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 139 LMAKFSDSfwpnQYLNEYnprahyeGTFPEIVAAlkeipnylfgAVSTCGTIMGCAN-YIHNQrlETKVIAVDAVGSIIF 217
Cdd:PLN02618 223 VIGKETRR----QAMEKW-------GGKPDVLVA----------CVGGGSNAMGLFHeFIDDE--DVRLIGVEAAGFGLD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 218 GGEKKARLV----------------------------------PGMGASIksQFLEENLLNEYVHVTDLDCVIGCQRLLR 263
Cdd:PLN02618 280 SGKHAATLTkgevgvlhgamsyllqdedgqiiephsisagldyPGVGPEH--SFLKDTGRAEYYSVTDEEALEAFQRLSR 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 152074665 264 TEAILAGGSSGAVLMGFDKIKDSIPAGSNCVLIFADRGERYLDTI 308
Cdd:PLN02618 358 LEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNTA 402
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
28-115 |
9.45e-05 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 43.86 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 28 LPFRVFAKLEGFNPSGSIKDRPAISmikQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYFGLR---FICVVDPKTTKQN 104
Cdd:PRK13802 345 LDARVFLKREDLNHTGAHKINNALG---QALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKcriYMGQIDARRQALN 421
|
90
....*....|.
gi 152074665 105 LNIIKVYGAEL 115
Cdd:PRK13802 422 VARMRMLGAEV 432
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
16-119 |
1.94e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 42.88 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152074665 16 TPLI---QLTQIYKDlpfRVFAKLEGFNPSGSIKDRPAISmikQAMEKGKIGPNTVVIESSSGNLGIGLAQVCRYFGLR- 91
Cdd:PRK13803 272 TPLTeakRLSDIYGA---RIYLKREDLNHTGSHKINNALG---QALLAKRMGKTRIIAETGAGQHGVATATACALFGLKc 345
|
90 100 110
....*....|....*....|....*....|
gi 152074665 92 --FICVVDPKTTKQNLNIIKVYGAELEMVL 119
Cdd:PRK13803 346 tiFMGEEDIKRQALNVERMKLLGANVIPVL 375
|
|
| |
