|
Name |
Accession |
Description |
Interval |
E-value |
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
1-469 |
0e+00 |
|
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: 755.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:TIGR01137 14 LVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKCIIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDGKL 160
Cdd:TIGR01137 92 LPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEILEQCEGKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 161 DMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKSND 240
Cdd:TIGR01137 172 DMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDEWIKTDD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 241 EDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAA-RELQEGQRCVVILPDSVRNYMSKFLSDKWMLQKGFMKEE-LSVKRP 318
Cdd:TIGR01137 252 KESFTMARRLIKEEGLLVGGSSGSAVVAALKAAeDELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDNGFLDDEdLTVKDV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 319 WWWRLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQF 398
Cdd:TIGR01137 332 LWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQPSDAVSKVMSKKF 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907122203 399 KPIHLTDTLGTLSHILEMDHFALVVHEQIQsrdqawsgvvggptdcsngmsskqqmvFGVVTAIDLLNFVA 469
Cdd:TIGR01137 412 IQIGLGETLSDLSKFLEMDSSAIVVEEGKP---------------------------IGVVTKIDLLSFLA 455
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
1-295 |
4.70e-161 |
|
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: 456.98 E-value: 4.70e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:cd01561 5 LVRLNRLSP--GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDGKL 160
Cdd:cd01561 83 MPETMSEEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 161 DMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKSND 240
Cdd:cd01561 162 DAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSD 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907122203 241 EDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 295
Cdd:cd01561 237 EEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
1-296 |
1.15e-152 |
|
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: 436.02 E-value: 1.15e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:COG0031 16 LVRLNRLSPGPG--AEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAKGYRLILV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDGKL 160
Cdd:COG0031 94 MPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIWEQTDGKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 161 DMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKSND 240
Cdd:COG0031 171 DAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKILDPSLIDEVITVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907122203 241 EDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSK 296
Cdd:COG0031 246 EEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
1-308 |
9.06e-110 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 327.97 E-value: 9.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:PRK10717 16 LIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAAARGYKTVIV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASNPLAHYDDTAEEILQQ 155
Cdd:PRK10717 94 MPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPANREAHYETTGPEIWEQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 156 CDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEV------EGIGYDFIPTVLDR 229
Cdd:PRK10717 173 TDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAL-----YSYYKTGELKAegssitEGIGQGRITANLEG 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907122203 230 AVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSKFLSDKWMLQKGF 308
Cdd:PRK10717 248 APIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLREKGL 326
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
1-295 |
1.45e-108 |
|
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: 323.93 E-value: 1.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGlkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:TIGR01139 10 LVRLNRIEGCNA---NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGYKLILT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDDTAEEILQQCDGK 159
Cdd:TIGR01139 87 MPETMSIERRKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWRDTDGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 160 LDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKSN 239
Cdd:TIGR01139 164 LDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907122203 240 DEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 295
Cdd:TIGR01139 239 DEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
1-295 |
3.73e-104 |
|
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: 312.68 E-value: 3.73e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:TIGR01136 10 LVRLNRLAP--GCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAARGYKLILT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDDTAEEILQQC 156
Cdd:TIGR01136 88 MPETMSLERRKLLRAYGAELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 157 DGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWF 236
Cdd:TIGR01136 161 DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 237 KSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQ-EGQRCVVILPDSVRNYMS 295
Cdd:TIGR01136 236 TVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
1-289 |
1.95e-79 |
|
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: 247.04 E-value: 1.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGnLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:cd00640 3 LVRLKRLSK--LGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEG-KLPKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdDTAEEILQQCDG-K 159
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 160 LDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEgsilaepeelnqteqtAYEVegigydfiptvldravvdkwfksN 239
Cdd:cd00640 154 PDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE----------------VVTV-----------------------S 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907122203 240 DEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDS 289
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
1-295 |
2.47e-76 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 240.93 E-value: 2.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:PRK11761 15 LVKLQRLPPDRGN--TILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYRMKLI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDDTAEEILQQCDGKL 160
Cdd:PRK11761 93 MPENMSQERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTGPEIWRQTEGRI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 161 DMLVASAGTGGTITGIARKLKEKCPGCKIIGVDP-EGS----ILAEPEElnqteqtayevegigydFIPTVLDRAVVDKW 235
Cdd:PRK11761 169 THFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLPKIFDASRVDRV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 236 FKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELqEGQRCVVILPDSVRNYMS 295
Cdd:PRK11761 232 LDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLS 290
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
1-288 |
4.00e-76 |
|
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: 240.29 E-value: 4.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAgnlKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:pfam00291 10 LVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdDTAEEILQQCDGKL 160
Cdd:pfam00291 85 VPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQLGGDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 161 DMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS-ILAEPEELNQTEQTA---YEVEGIGYDFIPTVLDRAVVDKWF 236
Cdd:pfam00291 159 DAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGALALDLLDEYV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907122203 237 KS----NDEDSFAFARMLIAQEGLLCGGSSGSAMAVA-VKAARELQEGQRCVVILPD 288
Cdd:pfam00291 239 GEvvtvSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
1-302 |
1.60e-74 |
|
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: 236.72 E-value: 1.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKIskNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:TIGR03945 10 LVKLERL--FPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYKGLRFICV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLAHYDDTAEEI 152
Cdd:TIGR03945 88 VDPNISPQNLKLLRAYGAEVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 153 LQQCDgKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSIL--AEPeelnqteqTAYEVEGIGYDFIPTVLDRA 230
Cdd:TIGR03945 161 ARAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGASVVPELLDES 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907122203 231 VVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSKFLSDKW 302
Cdd:TIGR03945 232 LIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEW 303
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
1-300 |
2.42e-73 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 234.43 E-value: 2.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTI-IEPTSGNTGIGLALAAAVKGYRCII 79
Cdd:PLN02565 18 LVYLNNVVD--GCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAFMAAAKGYKLII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 80 VMPEKMSMEKVDVLRALGAEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDG 158
Cdd:PLN02565 96 TMPASMSLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEIWKGTGG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 159 KLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKS 238
Cdd:PLN02565 172 KVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQV 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907122203 239 NDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVK-AARELQEGQRCVVILPDSVRNYMSKFLSD 300
Cdd:PLN02565 247 SSDEAIETAKLLALKEGLLVGISSGAAAAAAIKiAKRPENAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
1-295 |
9.90e-68 |
|
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: 218.63 E-value: 9.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:TIGR01138 11 LVRLQRMGPENGS--EVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDDTAEEILQQCDGKL 160
Cdd:TIGR01138 89 MPDNMSQERKAAMRAYGAELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPEIWQQTGGRI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 161 DMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEgsilaEPeelnqteqtaYEVEGIGY---DFIPTVLDRAVVDKWFK 237
Cdd:TIGR01138 165 THFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFDASLVDRVLD 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907122203 238 SNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQrCVVILPDSVRNYMS 295
Cdd:TIGR01138 230 IHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
1-300 |
3.61e-65 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 212.94 E-value: 3.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPG-DTIIEPTSGNTGIGLALAAAVKGYRCII 79
Cdd:PLN00011 20 MVYLNNIVD--GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGAARGYKVIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 80 VMPEKMSMEKVDVLRALGAEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLAHYDDTAEEIL 153
Cdd:PLN00011 98 VMPSTMSLERRIILRALGAEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEIHYRTTGPEIW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 154 QQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVD 233
Cdd:PLN00011 169 RDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVD 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907122203 234 KWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAA-RELQEGQRCVVILPDSVRNYMSKFLSD 300
Cdd:PLN00011 244 EIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAkRPENAGKLIVVIFPSGGERYLSTKLFE 311
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
1-295 |
2.19e-64 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 214.26 E-value: 2.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTI-IEPTSGNTGIGLALAAAVKGYRCII 79
Cdd:PLN03013 126 MVYLNSIAK--GCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAFIAASRGYRLIL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 80 VMPEKMSMEKVDVLRALGAEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPLAHYDDTAEEILQQ 155
Cdd:PLN03013 204 TMPASMSMERRVLLKAFGAELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPKIHYETTGPEIWDD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 156 CDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVDKW 235
Cdd:PLN03013 277 TKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEV 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 236 FKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 295
Cdd:PLN03013 352 IAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIY 411
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
1-301 |
4.89e-62 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 206.35 E-value: 4.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGLKceLLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDT-IIEPTSGNTGIGLALAAAVKGYRCII 79
Cdd:PLN02556 62 LVYLNKVTEGCGAY--IAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMIL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 80 VMPEKMSMEKVDVLRALGAEIVRT-PTNARFDSpeshVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDG 158
Cdd:PLN02556 140 TMPSYTSLERRVTMRAFGAELVLTdPTKGMGGT----VKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 159 KLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKS 238
Cdd:PLN02556 216 QVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP-----AESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEV 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907122203 239 NDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQ-EGQRCVVILPDSVRNYMSKFLSDK 301
Cdd:PLN02556 291 SSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPEnKGKLIVTVHPSFGERYLSSVLFQE 354
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
1-308 |
1.24e-55 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 190.97 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:PLN02356 56 LIRINSLSEATG--CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKCHVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRT-PTNarFDSPESHVGVAWRLK---NEIP-----------------NSHIL------- 132
Cdd:PLN02356 134 IPDDVAIEKSQILEALGATVERVrPVS--ITHKDHYVNIARRRAleaNELAskrrkgsetdgihlektNGCISeeekens 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 133 ------------DQYRNASNPLAHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSIL- 199
Cdd:PLN02356 212 lfsssctggffaDQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGSGLf 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 200 -------------AEPEELNQTEQTAyeVEGIGYDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAM 266
Cdd:PLN02356 292 nkvtrgvmytreeAEGRRLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNC 369
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907122203 267 AVAVKAARELQEGQRCVVILPDSVRNYMSKFLSDKWMLQKGF 308
Cdd:PLN02356 370 VGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
323-467 |
3.48e-50 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 166.94 E-value: 3.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 323 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIH 402
Cdd:cd04608 2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907122203 403 LTDTLGTLSHILEMDHFALVVHEqiqsrdqawsgvvggptdcsngmsskQQMVFGVVTAIDLLNF 467
Cdd:cd04608 82 LDTPLGALSRILERDHFALVVDG--------------------------QGKVLGIVTRIDLLNY 120
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
10-286 |
6.34e-27 |
|
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: 109.88 E-value: 6.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 10 NAGLKCELLAKCEFFNAGGSVKDRISLRMI----EDAERAGnlkpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKM 85
Cdd:cd01562 27 SELLGAEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLGIPATIVMPETA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 86 SMEKVDVLRALGAEIVRtpTNARFDSPESHVgvawrlkneipnsHILDQYRNAsnPLAH-YDD---------TAEEILQQ 155
Cdd:cd01562 100 PAAKVDATRAYGAEVVL--YGEDFDEAEAKA-------------RELAEEEGL--TFIHpFDDpdviagqgtIGLEILEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 156 CdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA-EPEELNQTEQTAyevEGIGydfIPTVLD 228
Cdd:cd01562 163 V-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTIA---DGLA---VKRPGE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907122203 229 ------RAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAvAVKAARELQEGQRCVVIL 286
Cdd:cd01562 236 ltfeiiRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
10-286 |
9.02e-25 |
|
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: 104.35 E-value: 9.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 10 NAGLKCELLAKCEFFNAGGSVKDR------ISLRmieDAERAGnlkpgdTIIEPTSGNTGIGLALAAAVKGYRCIIVMPE 83
Cdd:COG1171 34 SERLGAEVYLKLENLQPTGSFKLRgaynalASLS---EEERAR------GVVAASAGNHAQGVAYAARLLGIPATIVMPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 84 KMSMEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNEipnshildqyRNASnpLAH-YDDT---------AEEIL 153
Cdd:COG1171 105 TAPAVKVAATRAYGAEVVLHGDT--YDDAEAA---AAELAEE----------EGAT--FVHpFDDPdviagqgtiALEIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 154 QQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA-EPEELNQTeQTAyeVEGIG------- 219
Cdd:COG1171 168 EQL-PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTI--ADGLAvgrpgel 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 220 -YDFIPTVLDRAV-VdkwfksnDEDSFAFA-RMLIAQEGLLCGGSSGSAMAvAVKAARELQEGQRCVVIL 286
Cdd:COG1171 244 tFEILRDLVDDIVtV-------SEDEIAAAmRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVVL 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
15-286 |
3.23e-24 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 102.85 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 15 CELLAKCEFFNAGGSVKDRIS---LRMIEDAERagnlKPGdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVD 91
Cdd:PRK06815 35 CEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 92 VLRALGAEIVRTPTNArfdspeshvgvawrLKNEI-PNSHILDQYRNASNPlahYDD---------TAEEILQQCDgKLD 161
Cdd:PRK06815 109 AIRALGAEVRLYGGDA--------------LNAELaARRAAEQQGKVYISP---YNDpqviagqgtIGMELVEQQP-DLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 162 MLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA----EPEELNQ-TEQTAYEVEGigyDFIPTVLDRA 230
Cdd:PRK06815 171 AVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTlSDGTAGGVEP---GAITFPLCQQ 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907122203 231 VVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQeGQRCVVIL 286
Cdd:PRK06815 248 LIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
2-286 |
1.28e-16 |
|
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: 80.72 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 2 VRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIVM 81
Cdd:cd01563 26 VRAPRLGERLGGK-NLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKCVVFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 82 PEKMSMEKVDVLRALGAEIVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLAH--YDDTAEEILQQCDGK 159
Cdd:cd01563 101 PAGKALGKLAQALAYGATVLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYRLegQKTIAFEIAEQLGWE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 160 L-DMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEGS-----------ILAEPEELNQTEQTAYEvegIG 219
Cdd:cd01563 171 VpDYVVVPVGNGGNITAIWKGFKElkelglidRLP--RMVGVQAEGAapivrafkegkDDIEPVENPETIATAIR---IG 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907122203 220 YdfiPtVLDRAVVDKWFKSN------DEDSFAFARMLIAQ-EGLLCGGSSGSAMAVAVKAARE--LQEGQRCVVIL 286
Cdd:cd01563 246 N---P-ASGPKALRAVRESGgtavavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiIDKGERVVVVL 317
|
|
| PLN02970 |
PLN02970 |
serine racemase |
16-197 |
1.46e-14 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 74.71 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 16 ELLAKCEFFNAGGSVKDRISLRMI-----EDAERAgnlkpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKV 90
Cdd:PLN02970 43 SLFFKCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 91 DVLRALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDDTAEEILQQCDGkLDMLVASAGT 169
Cdd:PLN02970 115 DAVIRYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLEQVPE-LDVIIVPISG 185
|
170 180
....*....|....*....|....*...
gi 1907122203 170 GGTITGIARKLKEKCPGCKIIGVDPEGS 197
Cdd:PLN02970 186 GGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
10-195 |
2.09e-13 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 70.82 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 10 NAGLKCELLAKCEFFNAGGSVKDRIS----LRMIEDAERAGnlkpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKM 85
Cdd:PRK07048 34 DARTGAQVFFKCENFQRMGAFKFRGAynalSQFSPEQRRAG-------VVTFSSGNHAQAIALSARLLGIPATIVMPQDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 86 SMEKVDVLRALGAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------DTAEEIL 153
Cdd:PRK07048 107 PAAKVAATRGYGGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907122203 154 QQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE 195
Cdd:PRK07048 168 EEV-GPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
1-286 |
2.31e-13 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 70.89 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIV 80
Cdd:PRK06381 18 LLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKAVIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 81 MPEKMSMEKVDVLRALGAEIVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDDTAEEILQQCD 157
Cdd:PRK06381 93 IPRSYSNSRVKEMEKYGAEIIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAYEIYEALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 158 GKLDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEGS--------------ILAEPEELNQTEQTAYEV 215
Cdd:PRK06381 165 DVPDAVAVPVGNGTTLAGIYHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRETAVNEPLV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907122203 216 EGIGYDFIPTVldRAVVD---KWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVIL 286
Cdd:PRK06381 243 SYRSFDGDNAL--EAIYDshgYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
2-293 |
2.23e-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: 68.30 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 2 VRINKISKNAGlkCELLAKCEFFNAGGSVKDR-----ISLrmiedAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYR 76
Cdd:COG0498 70 VKAPRLADELG--KNLYVKEEGHNPTGSFKDRamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAARAGIE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 77 CIIVMPE-KMSMEKVDVLRALGAEIVRTPTNarFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPL-------AHYdd 147
Cdd:COG0498 139 VFVFVPEgKVSPGQLAQMLTYGAHVIAVDGN--FD-------DAQRLVKELAADEGL--YaVNSINPArlegqktYAF-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 148 taeEILQQCDGKLDMLVASAGTGGTITGI--ARK------LKEKCPgcKIIGVDPEGS--ILAEPEelnqTEQTAYEVEG 217
Cdd:COG0498 206 ---EIAEQLGRVPDWVVVPTGNGGNILAGykAFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPER 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 218 ---------IGydfIPTVLDRAVVD-----KWF-KSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARE--LQEGQ 280
Cdd:COG0498 277 petiapsmdIG---NPSNGERALFAlresgGTAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDE 353
|
330 340
....*....|....*....|
gi 1907122203 281 RCVVIL-------PDSVRNY 293
Cdd:COG0498 354 PVVVLStghglkfPDAVREA 373
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
60-197 |
4.98e-12 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 67.86 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 60 GNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 134
Cdd:PRK09224 77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907122203 135 yrnasnPlahYDDT---------AEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 197
Cdd:PRK09224 145 ------P---FDDPdviagqgtiAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
54-197 |
1.41e-11 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 66.36 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 54 IIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNEIPNSHIld 133
Cdd:PRK12483 88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVL--HGESFPDALAH---ALKLAEEEGLTFV-- 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907122203 134 qyrnasNPlahYDD---------TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 197
Cdd:PRK12483 161 ------PP---FDDpdviagqgtVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
16-197 |
1.57e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 64.98 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 16 ELLAKCEFFNAGGSVKDRISLRMIEdaeraGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRA 95
Cdd:PRK08246 38 PVWLKLEHLQHTGSFKARGAFNRLL-----AAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 96 LGAEIVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDDTAEEILQQCdGKLDMLVASAGTG 170
Cdd:PRK08246 113 LGAEVVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGGG 179
|
170 180
....*....|....*....|....*..
gi 1907122203 171 GTITGIARKLKekcPGCKIIGVDPEGS 197
Cdd:PRK08246 180 GLIAGIAAWFE---GRARVVAVEPEGA 203
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
10-194 |
5.40e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 63.64 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 10 NAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGnlKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEK 89
Cdd:PRK06608 33 NEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 90 VDVLRALGAEIVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDDTAEEILQQCDGKLDMLVAS 166
Cdd:PRK06608 111 QQAALYYGGEVILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTLCYEALQQLGFSPDAIFAS 178
|
170 180 190
....*....|....*....|....*....|
gi 1907122203 167 AGTGGTITG--IARKLKEkcPGCKIIGVDP 194
Cdd:PRK06608 179 CGGGGLISGtyLAKELIS--PTSLLIGSEP 206
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
2-193 |
5.84e-09 |
|
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: 57.39 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 2 VRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIVM 81
Cdd:TIGR00260 26 FRAPALAANVGIK-NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKVVVLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 82 PE-KMSMEKVDVLRALGAEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnshildqYRNASNPLAHYddtaeEI 152
Cdd:TIGR00260 101 PAgKISLGKLAQALGYNAEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-------YRLEGQKTYAF-----EA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907122203 153 LQQCDGKL-DMLVASAGTGGTITGIARKLKEKcpgcKIIGVD 193
Cdd:TIGR00260 167 VEQLGWEApDKVVVPVPNSGNFGAIWKGFKEK----KMLGLD 204
|
|
| CBS |
smart00116 |
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
333-380 |
1.12e-08 |
|
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.
Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 50.97 E-value: 1.12e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907122203 333 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 380
Cdd:smart00116 2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
1-195 |
1.89e-08 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 55.90 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 1 MVRINKISKNAglKCELLAKCEFFNAGGSVKDRIS---LRMIEDAERAGNlkpgdtIIEPTSGNTGIGLALAAAVKGYRC 77
Cdd:PRK08638 30 LPRSNYLSERC--KGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKRKG------VVACSAGNHAQGVALSCALLGIDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 78 IIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILDQYrNASNPLAHYDDTAEEILQQCd 157
Cdd:PRK08638 102 KVVMPKGAPKSKVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIPPY-DDPKVIAGQGTIGLEILEDL- 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907122203 158 GKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE 195
Cdd:PRK08638 174 WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
10-101 |
1.01e-07 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 53.46 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 10 NAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEK 89
Cdd:PRK06110 31 AERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEK 108
|
90
....*....|..
gi 1907122203 90 VDVLRALGAEIV 101
Cdd:PRK06110 109 NAAMRALGAELI 120
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
333-426 |
3.72e-07 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 48.78 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 333 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIHLTDTLGT-LS 411
Cdd:cd02205 4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEaLE 83
|
90
....*....|....*.
gi 1907122203 412 HILEMD-HFALVVHEQ 426
Cdd:cd02205 84 LMLEHGiRRLPVVDDD 99
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
20-195 |
5.27e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 51.66 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 20 KCEFFNAGGSVKDRISLRMIED-AERAGNlkpgdTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGA 98
Cdd:PRK06450 70 KLDFLNPTGSYKDRGSVTLISYlAEKGIK-----QISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 99 EIVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYRNASNPLAHyddtaeEILQQCDGKLD---MLVASAGTg 170
Cdd:PRK06450 145 EVVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFRDGIRTLAY------EIAKDLDWKIPnyvFIPVSAGT- 207
|
170 180 190
....*....|....*....|....*....|...
gi 1907122203 171 gTITGIARKLK--------EKCPgcKIIGVDPE 195
Cdd:PRK06450 208 -LLLGVYSGFKhlldsgviSEMP--KIVAVQTE 237
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
15-218 |
8.74e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 51.05 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 15 CELLAKCEFFNAGGSVKDRIS---LRMIEDAERAGNlkpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVD 91
Cdd:PRK07334 38 AEVWLKFENLQFTASFKERGAlnkLLLLTEEERARG------VIAMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 92 VLRALGAEIVRTptNARFDSPESHvgvAWRLKNEipnshildQYRNASNPlahYDD---------TAEEILQQCdGKLDM 162
Cdd:PRK07334 112 RTRGFGAEVVLH--GETLDEARAH---ARELAEE--------EGLTFVHP---YDDpaviagqgtVALEMLEDA-PDLDT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907122203 163 LVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG--SILAEPEELNQTEQTAYEVEGI 218
Cdd:PRK07334 175 LVVPIGGGGLISGMATAAKALKPDIEIIGVQTELypSMYAAIKGVALPCGGSTIAEGI 232
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
53-106 |
8.83e-07 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 51.03 E-value: 8.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907122203 53 TIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTN 106
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN 171
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
149-196 |
9.88e-07 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 50.96 E-value: 9.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907122203 149 AEEILQQCD--GKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG 196
Cdd:PRK08639 167 AVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
325-380 |
1.28e-06 |
|
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.
Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 45.28 E-value: 1.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907122203 325 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 380
Cdd:pfam00571 1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
6-194 |
1.33e-06 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 50.69 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 6 KISKNAGLKceLLAKCEFFNAGGSVKDRISLRMIEDAERAgNLKPGdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKM 85
Cdd:PLN02550 117 KLSERLGVK--VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 86 SMEKVDVLRALGAEIVRTPTNarFDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYDDTA------EEILQQCDGK 159
Cdd:PLN02550 192 PEIKWQSVERLGATVVLVGDS--YDEAQAYA-----------KQRALEEGRTFIPPFDHPDVIAgqgtvgMEIVRQHQGP 258
|
170 180 190
....*....|....*....|....*....|....*
gi 1907122203 160 LDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDP 194
Cdd:PLN02550 259 LHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEP 293
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
323-388 |
1.64e-06 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 47.17 E-value: 1.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907122203 323 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSD 388
Cdd:COG0517 1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLD 66
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
7-197 |
1.82e-06 |
|
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: 49.60 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 7 ISKNAGlkCELLAKCEFFNAGGSVKDR-ISLRMIEDAERAGNLKPGdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKM 85
Cdd:cd06448 10 LSKTAG--CNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTIVVPEST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 86 SMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDDTAEEILQQC--DGKLD 161
Cdd:cd06448 86 KPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQQLqsQEKVD 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907122203 162 MLVASAGTGGTITGIARKLkEKCPGCK--IIGVDPEGS 197
Cdd:cd06448 159 AIVCSVGGGGLLNGIVQGL-ERNGWGDipVVAVETEGA 195
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
41-257 |
2.61e-06 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 49.44 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 41 DAERAGnlkpGDTIIepTSGntGIG-----LALAAAVK-GYRCIIVMPEKMSMEKVDVL--------RALGAEIVRTPTN 106
Cdd:PRK03910 58 DALAQG----ADTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 107 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDDTAEEILQQCDG---KLDMLVASAGTGGTITG 175
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 176 IARKLKEKCPGCKIIGVdpegSILAEPEElnQTEQTAYEVEGI-GYDFIPTVLDRAVV---DKWF-----KSNDEDsFAF 246
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV----TVSRSAAE--QEPKVAKLAQATaELLGLPTEIPRADIrlwDDYVgpgygVPTDEM-LEA 272
|
250
....*....|.
gi 1907122203 247 ARMLIAQEGLL 257
Cdd:PRK03910 273 VKLLARTEGIL 283
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
322-415 |
8.86e-06 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 46.42 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 322 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNEsGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPI 401
Cdd:COG2524 85 KMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTV 163
|
90
....*....|....
gi 1907122203 402 HLTDTLGTLSHILE 415
Cdd:COG2524 164 SEDDSLEEALRLML 177
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
320-380 |
1.60e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 44.47 E-value: 1.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907122203 320 WWRLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 380
Cdd:COG0517 64 LLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
325-388 |
6.15e-05 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 42.51 E-value: 6.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907122203 325 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSD 388
Cdd:COG2905 1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLD 64
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
333-414 |
6.81e-05 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 42.55 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 333 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDE------VCKVLYKQFKPIHLTDT 406
Cdd:COG3448 12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEErlldlpVEDVMTRPVVTVTPDTP 91
|
....*...
gi 1907122203 407 LGTLSHIL 414
Cdd:COG3448 92 LEEAAELM 99
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
20-289 |
1.16e-04 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 44.42 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 20 KCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAE 99
Cdd:PRK05638 85 KDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 100 IVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnasnpLAHYDDTAEEILQQCDGklDMLVASAGTGGTITGI 176
Cdd:PRK05638 161 IIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG--------LEGQKTIAFELWEEINP--THVIVPTGSGSYLYSI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 177 ARKLKE--------KCPgcKIIGVDPE------GSILAEPEELNQTEQTA-YEVEGIGYDFIPTVLDR----AVVdkwfk 237
Cdd:PRK05638 229 YKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKCNETKALGlYVKNPVMKEYVSEAIKEsggtAVV----- 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907122203 238 sNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARE--LQEGQRCVVILPDS 289
Cdd:PRK05638 302 -VNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGS 354
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
37-103 |
1.34e-04 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 44.13 E-value: 1.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 37 RMIEDAeraGNLKPGDTIIEpTSGNTGIGLALA--AAVKGYRCIIVMPEKMSMEK-VDVLRALGAEIVRT 103
Cdd:cd08290 136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
4-257 |
2.81e-04 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 42.79 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 4 INKISKNAGLKCELLAKCEFFN---AGGSVKDRISLRMIEDAERAGnlkpGDTIIepTSG----NTGIGLALAAAVKGYR 76
Cdd:cd06449 6 LPRLSEHLGGKVEIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKG----ADTLV--TVGgiqsNHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 77 CIIVM--PEKMSMEKVD------VLRALGAEIvrtptnaRFDSPESHVGV-------AWRLKNE------IPNShildqy 135
Cdd:cd06449 80 CVLVQenWVPYSDAVYDrvgnilLSRIMGADV-------RLVSAGFDIGIrksfeeaAEEVEAKggkpyvIPAG------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 136 rNASNPLAH--YDDTAEEILQQCDG---KLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEELNQTEQ 210
Cdd:cd06449 147 -GSEHPLGGlgYVGFVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQ 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907122203 211 TAYEVEGIGYdfipTVLDRAVVDKWF-----KSNDEDSFAFaRMLIAQEGLL 257
Cdd:cd06449 226 AKLAEEGLEV----KEEDVVLDDDYAapeygIPNDETIEAI-KLCARLEGII 272
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
322-380 |
3.51e-04 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 40.62 E-value: 3.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907122203 322 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 380
Cdd:COG3448 72 DLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
16-196 |
3.82e-04 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 42.51 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 16 ELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRA 95
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 96 LGAEIvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRNASNPLAHYddtaeEILQQCdGKLDMLVASAGTGGTI 173
Cdd:PRK08329 149 LGAEL----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYFLEGTKTIAY-----EIYEQI-GVPDYAFVPVGSGTLF 218
|
170 180 190
....*....|....*....|....*....|.
gi 1907122203 174 TGIARKLKE--------KCPgcKIIGVDPEG 196
Cdd:PRK08329 219 LGIWKGFKElhemgeisKMP--KLVAVQAEG 247
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
322-380 |
5.10e-04 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 42.51 E-value: 5.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907122203 322 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 380
Cdd:PRK14869 67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
333-426 |
5.99e-04 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 39.90 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907122203 333 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLssllagKVRPSDEVCKVLYKQFKPIHLTDTLGTLSH 412
Cdd:COG4109 27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVTPDTSLASAAH 100
|
90
....*....|....*.
gi 1907122203 413 ILEMDHFAL--VVHEQ 426
Cdd:COG4109 101 KMIWEGIELlpVVDDD 116
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
323-379 |
7.44e-04 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 40.64 E-value: 7.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907122203 323 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSL 379
Cdd:COG2524 150 APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
323-380 |
7.55e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 39.43 E-value: 7.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907122203 323 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNEsGAILGMVTLGNMLSSLL 380
Cdd:COG2905 65 TPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
323-376 |
8.21e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 39.15 E-value: 8.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907122203 323 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNML 376
Cdd:cd02205 59 TPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
60-103 |
1.27e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 40.72 E-value: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1907122203 60 GNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT 103
Cdd:PRK07476 76 GNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIV 119
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
323-380 |
1.74e-03 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 38.74 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907122203 323 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 380
Cdd:COG4109 76 TPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
|
|
| CBS_pair_IMPDH |
cd04601 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
333-371 |
1.84e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 37.78 E-value: 1.84e-03
10 20 30
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gi 1907122203 333 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVT 371
Cdd:cd04601 4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT 42
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| CBS_pair_plant_CBSX |
cd17789 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ... |
325-376 |
2.71e-03 |
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Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341425 [Multi-domain] Cd Length: 141 Bit Score: 38.22 E-value: 2.71e-03
10 20 30 40 50
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gi 1907122203 325 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNML 376
Cdd:cd17789 88 VGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVV 139
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| CBS_pair_ParBc_assoc |
cd04610 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ... |
335-376 |
7.38e-03 |
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Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 36.14 E-value: 7.38e-03
10 20 30 40
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gi 1907122203 335 TVLPTVTCEDTIAILREKGFDQAPVVnESGAILGMVTLGNML 376
Cdd:cd04610 7 TVSPDDTVKDVIKLIKETGHDGFPVV-DDGKVVGYVTAKDLL 47
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