|
Name |
Accession |
Description |
Interval |
E-value |
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
26-489 |
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: 778.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 26 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 105
Cdd:TIGR01137 18 NKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKCIIVLPEKMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 106 SEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVAS 185
Cdd:TIGR01137 98 SEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEILEQCEGKLDMFVAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 186 VGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTF 265
Cdd:TIGR01137 178 VGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDEWIKTDDKESFTM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 266 ARMLIAQEGLLCGGSAGSTVAVAVKAAQ-ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLR 344
Cdd:TIGR01137 258 ARRLIKEEGLLVGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDNGFLDDEDLTVKDVLWWHAR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 345 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLT 424
Cdd:TIGR01137 338 VKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQPSDAVSKVMSKKFIQIGLG 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583420 425 DTLGRLSHILEMDHFALVVHEQIQsqdqawagvvggpadhstgkssqrqmvFGVVTAIDLLNFVA 489
Cdd:TIGR01137 418 ETLSDLSKFLEMDSSAIVVEEGKP---------------------------IGVVTKIDLLSFLA 455
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
26-314 |
3.25e-159 |
|
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: 453.12 E-value: 3.25e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 26 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 105
Cdd:cd01561 9 NRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETMS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 106 SEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVAS 185
Cdd:cd01561 89 EEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGKVDAFVAG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 186 VGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTF 265
Cdd:cd01561 168 VGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEAFAM 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462583420 266 ARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 314
Cdd:cd01561 243 ARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
26-315 |
2.29e-145 |
|
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: 418.30 E-value: 2.29e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 26 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 105
Cdd:COG0031 20 NRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAKGYRLILVMPETMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 106 SEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVAS 185
Cdd:COG0031 100 KERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIWEQTDGKVDAFVAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 186 VGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTF 265
Cdd:COG0031 177 VGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKILDPSLIDEVITVSDEEAFAM 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462583420 266 ARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 315
Cdd:COG0031 252 ARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
34-327 |
8.71e-107 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 321.04 E-value: 8.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 34 CRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLR 113
Cdd:PRK10717 28 CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 114 ALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGT 188
Cdd:PRK10717 108 ALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPANREAHYETTGPEIWEQTDGKVDGFVCAVGT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 189 GGTITGIARKLKEKCPGCRIIGVDPEGSIL----AEPEELNQTEQTTyevEGIGYDFIPTVLDRTVVDKWFKSNDEEAFT 264
Cdd:PRK10717 187 GGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGELKAEGSSIT---EGIGQGRITANLEGAPIDDAIRIPDEEALS 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462583420 265 FARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGF 327
Cdd:PRK10717 264 TAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLREKGL 326
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
29-314 |
2.38e-106 |
|
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: 318.93 E-value: 2.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 29 VPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEK 108
Cdd:TIGR01139 16 IEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGYKLILTMPETMSIER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 109 VDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVG 187
Cdd:TIGR01139 96 RKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWRDTDGKLDAFVAGVG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 188 TGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFAR 267
Cdd:TIGR01139 173 TGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSDEEAIETAR 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462583420 268 MLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 314
Cdd:TIGR01139 248 RLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
26-314 |
9.73e-105 |
|
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: 314.60 E-value: 9.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 26 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 105
Cdd:TIGR01136 14 NRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAARGYKLILTMPETMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 106 SEKVDVLRALGAEIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDTTADEILQQCDGKLDM 181
Cdd:TIGR01136 94 LERRKLLRAYGAELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKTTGPEIWRDTDGRIDH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 182 LVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEE 261
Cdd:TIGR01136 167 FVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDED 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462583420 262 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMT 314
Cdd:TIGR01136 242 AIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
25-308 |
4.35e-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: 246.66 E-value: 4.35e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 25 SDRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLkPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKM 104
Cdd:cd00640 6 LKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIVMPEGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 105 SSEKVDVLRALGAEIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDG-KLDMLV 183
Cdd:cd00640 85 SPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqKPDAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 184 ASVGTGGTITGIARKLKEKCPGCRIIGVDPEgsilaepeelnqteqttyevegigydfiptvldrtvvdkWFKSNDEEAF 263
Cdd:cd00640 159 VPVGGGGNIAGIARALKELLPNVKVIGVEPE---------------------------------------VVTVSDEEAL 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2462583420 264 TFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDS 308
Cdd:cd00640 200 EAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
26-319 |
9.61e-75 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 238.67 E-value: 9.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 26 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGLALAAAVRGYRCIIVMPEKM 104
Cdd:PLN02565 22 NNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAFMAAAKGYKLIITMPASM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 105 SSEKVDVLRALGAEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLV 183
Cdd:PLN02565 102 SLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEIWKGTGGKVDAFV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 184 ASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAF 263
Cdd:PLN02565 178 SGIGTGGTITGAGKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQVSSDEAI 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583420 264 TFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 319
Cdd:PLN02565 253 ETAKLLALKEGLLVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
25-307 |
1.40e-74 |
|
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: 237.21 E-value: 1.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 25 SDRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERdgtLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKM 104
Cdd:pfam00291 13 LPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 105 SSEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDGKLDMLVA 184
Cdd:pfam00291 90 PPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQLGGDPDAVVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 185 SVGTGGTITGIARKLKEKCPGCRIIGVDPEGS-ILAEPEELNQTEQTT---YEVEGIGYDFIPTVLDRTVVDKWFKS--- 257
Cdd:pfam00291 164 PVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGALALDLLDEYVGEvvt 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462583420 258 -NDEEAFTFARMLIAQEGLLCGGSAGSTVAVA-VKAAQELQEGQRCVVILPD 307
Cdd:pfam00291 244 vSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
27-307 |
1.15e-73 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 234.77 E-value: 1.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 27 RLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSS 106
Cdd:PRK11761 20 RLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYRMKLIMPENMSQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 107 EKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASV 186
Cdd:PRK11761 100 ERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTGPEIWRQTEGRITHFVSSM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 187 GTGGTITGIARKLKEKCPGCRIIGVDP-EGS----ILAEPEElnqteqttyevegigydFIPTVLDRTVVDKWFKSNDEE 261
Cdd:PRK11761 176 GTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLPKIFDASRVDRVLDVSQQE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462583420 262 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELqEGQRCVVILPD 307
Cdd:PRK11761 239 AENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICD 283
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
26-321 |
8.18e-73 |
|
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme. [Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274872 [Multi-domain] Cd Length: 304 Bit Score: 232.86 E-value: 8.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 26 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 105
Cdd:TIGR03945 14 ERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYKGLRFICVVDPNIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 106 SEKVDVLRALGAEIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDg 177
Cdd:TIGR03945 94 PQNLKLLRAYGAEVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRAHYHGTGREIARAFP- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 178 KLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL--AEPeelnqteqTTYEVEGIGYDFIPTVLDRTVVDKWF 255
Cdd:TIGR03945 166 TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGASVVPELLDESLIDDVV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462583420 256 KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRW 321
Cdd:TIGR03945 238 HVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEW 303
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
26-319 |
1.79e-67 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 219.49 E-value: 1.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 26 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPG-DTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKM 104
Cdd:PLN00011 24 NNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGAARGYKVILVMPSTM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 105 SSEKVDVLRALGAEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGK 178
Cdd:PLN00011 104 SLERRIILRALGAEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEIHYRTTGPEIWRDSAGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 179 LDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSN 258
Cdd:PLN00011 175 VDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQVT 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462583420 259 DEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQE-GQRCVVILPDSVRNYMTKFLSD 319
Cdd:PLN00011 250 GEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYLSTKLFE 311
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
38-314 |
2.32e-65 |
|
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: 212.85 E-value: 2.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 38 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 117
Cdd:TIGR01138 27 LKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERKAAMRAYGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 118 EIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 197
Cdd:TIGR01138 107 ELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPEIWQQTGGRITHFVSSMGTTGTIMGVSR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 198 KLKEKCPGCRIIGVDPEgsilaEPeelnqteqttYEVEGIGY---DFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEG 274
Cdd:TIGR01138 183 FLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFDASLVDRVLDIHQRDAENTMRELAVREG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462583420 275 LLCGGSAGSTVAVAVKAAQELQEGQrCVVILPDSVRNYMT 314
Cdd:TIGR01138 248 IFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
32-325 |
1.94e-63 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 212.33 E-value: 1.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 32 CRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVD 110
Cdd:PLN03013 136 CVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAFIAASRGYRLILTMPASMSMERRV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 111 VLRALGAEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASV 186
Cdd:PLN03013 216 LLKAFGAELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPKIHYETTGPEIWDDTKGKVDIFVAGI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 187 GTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFA 266
Cdd:PLN03013 289 GTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVIAISSEEAIETA 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462583420 267 RMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK--FLSDRWMLQK 325
Cdd:PLN03013 364 KQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIYTprCSSLSGKRWR 424
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
32-319 |
3.07e-60 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 202.11 E-value: 3.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 32 CRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDT-IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVD 110
Cdd:PLN02556 72 CGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 111 VLRALGAEIVRT-PTNARFDSpeshVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTG 189
Cdd:PLN02556 152 TMRAFGAELVLTdPTKGMGGT----VKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 190 GTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARML 269
Cdd:PLN02556 228 GTVSGVGKYLKSKNPNVKIYGVEP-----AESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMAREL 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462583420 270 IAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 319
Cdd:PLN02556 303 ALKEGLMVGISSGANTVAALRLAKMPEnKGKLIVTVHPSFGERYLSSVLFQ 353
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
343-487 |
3.38e-54 |
|
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: 177.72 E-value: 3.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 343 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 422
Cdd:cd04608 2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583420 423 LTDTLGRLSHILEMDHFALVVHEQiqsqdqawagvvggpadhstgkssqrQMVFGVVTAIDLLNF 487
Cdd:cd04608 82 LDTPLGALSRILERDHFALVVDGQ--------------------------GKVLGIVTRIDLLNY 120
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
34-327 |
2.86e-48 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 172.10 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 34 CRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLR 113
Cdd:PLN02356 68 CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKCHVVIPDDVAIEKSQILE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 114 ALGAEIVRT-PTNarFDSPESHVGVAWRLK---NEIP-----------------NSHIL-------------------DQ 153
Cdd:PLN02356 148 ALGATVERVrPVS--ITHKDHYVNIARRRAleaNELAskrrkgsetdgihlektNGCISeeekenslfsssctggffaDQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 154 YRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL--------------A 219
Cdd:PLN02356 226 FENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGSGLfnkvtrgvmytreeA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 220 EPEELNQTEQTTyeVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQ 299
Cdd:PLN02356 306 EGRRLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNCVGAVRVAQSLGPGH 383
|
330 340
....*....|....*....|....*...
gi 2462583420 300 RCVVILPDSVRNYMTKFLSDRWMLQKGF 327
Cdd:PLN02356 384 TIVTILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
25-305 |
2.73e-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: 111.42 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 25 SDRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMI----EDAERDGtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVM 100
Cdd:cd01562 23 SPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLGIPATIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 101 PEKMSSEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD------TTAD 169
Cdd:cd01562 96 PETAPAAKVDATRAYGAEVVL--YGEDFDEAEAK---ARELAEEegltfIH-------------PFDDPDviagqgTIGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 170 EILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTEQTtyeVEGIGydfI 242
Cdd:cd01562 158 EILEQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTI---ADGLA---V 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462583420 243 PTVLDRT------VVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 305
Cdd:cd01562 231 KRPGELTfeiirkLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
39-305 |
3.79e-26 |
|
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: 108.59 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDR------ISLRmieDAERDGTlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVL 112
Cdd:COG1171 44 KLENLQPTGSFKLRgaynalASLS---EEERARG------VVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAAT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 113 RALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKLDM 181
Cdd:COG1171 115 RAYGAEVVLHGDT--YDDAEAA---AAELAEEegatfVH-------------PFDDPDviagqgTIALEILEQL-PDLDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 182 LVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTeQT------TYEVEGIGYDFIPTVLDR 248
Cdd:COG1171 176 VFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTiadglaVGRPGELTFEILRDLVDD 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583420 249 TV-VDkwfksnDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 305
Cdd:COG1171 255 IVtVS------EDEIAAAMRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVVL 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
25-305 |
6.51e-26 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 107.86 E-value: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 25 SDRLVPRCRCRGVAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMP 101
Cdd:PRK06815 26 SPLLSQHTGCEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGIPVTVYAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 102 EKMSSEKVDVLRALGAEIVRTPTNArfDSPESHvgvAWRLKNEIPNSHIlDQYrNASNPLAHYDTTADEILQQCDgKLDM 181
Cdd:PRK06815 100 EQASAIKLDAIRALGAEVRLYGGDA--LNAELA---ARRAAEQQGKVYI-SPY-NDPQVIAGQGTIGMELVEQQP-DLDA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 182 LVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA----EPEELNQTEQTTyeVEGIGYDFIPTVLDRTVV 251
Cdd:PRK06815 172 VFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTLSDGT--AGGVEPGAITFPLCQQLI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462583420 252 DKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQeGQRCVVIL 305
Cdd:PRK06815 250 DQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
|
|
| PLN02970 |
PLN02970 |
serine racemase |
23-216 |
3.06e-16 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 79.72 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 23 RSSDRLVPRcrcRGVAKCEFFNAGGSVKDRISLRMI-----EDAERDgtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCI 97
Cdd:PLN02970 34 SSLDALAGR---SLFFKCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLRGIPAY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 98 IVMPEKMSSEKVDVLRALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDTTADEILQQCD 176
Cdd:PLN02970 103 IVVPKNAPACKVDAVIRYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLEQVP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462583420 177 GkLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 216
Cdd:PLN02970 175 E-LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
39-305 |
3.05e-15 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 76.48 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 118
Cdd:cd01563 43 KDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGAT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 119 IVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLAH--YDTTADEILQQCDGKL-DMLVASVGTGGTITGI 195
Cdd:cd01563 119 VLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYRLegQKTIAFEIAEQLGWEVpDYVVVPVGNGGNITAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 196 ARKLKE--------KCPgcRIIGVDPEGS------ILAEPEELNQTEQTTYEVEGIGydfIPT-VLDRTVVDKWFKSN-- 258
Cdd:cd01563 189 WKGFKElkelglidRLP--RMVGVQAEGAapivraFKEGKDDIEPVENPETIATAIR---IGNpASGPKALRAVRESGgt 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462583420 259 ----DEEAFTFARMLIAQ-EGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVIL 305
Cdd:cd01563 264 avavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiIDKGERVVVVL 317
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
39-305 |
1.56e-14 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 74.36 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 118
Cdd:PRK06381 36 KFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 119 IVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGI 195
Cdd:PRK06381 112 IIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAYEIYEALGDVPDAVAVPVGNGTTLAGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 196 ARKLKE--------KCPgcRIIGVDPEGS--------------ILAEPEELNQTEQTTYEVEGIGYDFiPTVLD--RTVV 251
Cdd:PRK06381 184 YHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRETAVNEPLVSYRSFDG-DNALEaiYDSH 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462583420 252 DKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVIL 305
Cdd:PRK06381 261 GYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
39-216 |
4.64e-14 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 73.07 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDRISLRMIEDAErdgtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 118
Cdd:PRK08246 42 KLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 119 IVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDTTADEILQQCdGKLDMLVASVGTGGTIT 193
Cdd:PRK08246 117 VVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGGGGLIA 183
|
170 180
....*....|....*....|...
gi 2462583420 194 GIARKLKekcPGCRIIGVDPEGS 216
Cdd:PRK08246 184 GIAAWFE---GRARVVAVEPEGA 203
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
79-216 |
6.39e-14 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 74.02 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 79 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 153
Cdd:PRK09224 77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462583420 154 yrnasnPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 216
Cdd:PRK09224 145 ------PFDDPDviagqgTIAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
39-214 |
1.21e-13 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 71.59 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDR---ISLRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRAL 115
Cdd:PRK07048 44 KCENFQRMGAFKFRgayNALSQFSPEQR----RAG--VVTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 116 GAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKLDMLV 183
Cdd:PRK07048 118 GGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELFEEV-GPLDALF 177
|
170 180 190
....*....|....*....|....*....|.
gi 2462583420 184 ASVGTGGTITGIARKLKEKCPGCRIIGVDPE 214
Cdd:PRK07048 178 VCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
73-216 |
6.40e-13 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 70.98 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 73 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEIPNS--HI 150
Cdd:PRK12483 88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAH---ALKLAEEEGLTfvPP 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462583420 151 LDQyrnaSNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 216
Cdd:PRK12483 163 FDD----PDVIAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
39-312 |
1.86e-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: 68.69 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDR-----ISLrmiedAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVL 112
Cdd:COG0498 86 KEEGHNPTGSFKDRamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQLAQM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 113 RALGAEIVRTPTNarFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPLAH--YDTTADEILQQCDGKLDMLVASVGTG 189
Cdd:COG0498 157 LTYGAHVIAVDGN--FD-------DAQRLVKELAADEGL--YaVNSINPARLegQKTYAFEIAEQLGRVPDWVVVPTGNG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 190 GTITGI--ARK------LKEKCPgcRIIGVDPEGS--ILAEPEelnqTEQTTYEVEG---------IGydfIPT------ 244
Cdd:COG0498 226 GNILAGykAFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPERpetiapsmdIG---NPSngeral 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462583420 245 -VLDRTvvDKWF-KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVIL-------PDSVRNY 312
Cdd:COG0498 297 fALRES--GGTAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVVVLStghglkfPDAVREA 373
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
39-213 |
7.75e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 63.25 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDRISLRMIEDAERDGtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 118
Cdd:PRK06608 43 KVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 119 IVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITG- 194
Cdd:PRK06608 121 VILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTLCYEALQQLGFSPDAIFASCGGGGLISGt 188
|
170 180
....*....|....*....|
gi 2462583420 195 -IARKLKEkcPGCRIIGVDP 213
Cdd:PRK06608 189 yLAKELIS--PTSLLIGSEP 206
|
|
| CBS |
smart00116 |
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
353-400 |
1.73e-09 |
|
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: 53.29 E-value: 1.73e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2462583420 353 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 400
Cdd:smart00116 2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
353-436 |
3.91e-09 |
|
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: 54.17 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 353 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTlgrLSH 432
Cdd:cd02205 4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTD---LEE 80
|
....
gi 2462583420 433 ILEM 436
Cdd:cd02205 81 ALEL 84
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
33-214 |
6.89e-09 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 57.44 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 33 RCRG--VAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSE 107
Cdd:PRK08638 39 RCKGeiFLKLENMQRTGSFKIRGAfnkLSSLTDAEK----RKG--VVACSAGNHAQGVALSCALLGIDGKVVMPKGAPKS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 108 KVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILDQYrNASNPLAHYDTTADEILQQCdGKLDMLVASVG 187
Cdd:PRK08638 113 KVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIPPY-DDPKVIAGQGTIGLEILEDL-WDVDTVIVPIG 184
|
170 180
....*....|....*....|....*..
gi 2462583420 188 TGGTITGIARKLKEKCPGCRIIGVDPE 214
Cdd:PRK08638 185 GGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
166-215 |
1.97e-08 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 56.35 E-value: 1.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462583420 166 TTADEILQQCD--GKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG 215
Cdd:PRK08639 165 TVAVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
72-214 |
5.10e-08 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 54.88 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 72 TIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDspEShVGVAWRLKNEipNSHIL 151
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN--YD--DS-VRLAAQEAQE--NGWVV 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462583420 152 DQyrNASNP---------LAHYDTTADEILQQCDGKLD-----MLVASVGT--GGTITGIARKLKEKCPgcRIIGVDPE 214
Cdd:PRK08206 191 VQ--DTAWEgyeeiptwiMQGYGTMADEAVEQLKEMGVppthvFLQAGVGSlaGAVLGYFAEVYGEQRP--HFVVVEPD 265
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
48-213 |
1.07e-07 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 54.54 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 48 SVKDRISLRMIEDAERDgTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNar 127
Cdd:PLN02550 138 SFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDS-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 128 FDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKE 201
Cdd:PLN02550 213 YDEAQAYA-----------KQRALEEGRTFIPPFDHPDviagqgTVGMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKR 281
|
170
....*....|..
gi 2462583420 202 KCPGCRIIGVDP 213
Cdd:PLN02550 282 VRPEVKIIGVEP 293
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
343-435 |
2.67e-07 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 49.48 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 343 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQI 421
Cdd:COG0517 1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTpVSEVMTRPPVTV 80
|
90
....*....|....
gi 2462583420 422 RLTDTLGRLSHILE 435
Cdd:COG0517 81 SPDTSLEEAAELME 94
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
345-400 |
6.04e-07 |
|
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: 46.44 E-value: 6.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462583420 345 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 400
Cdd:pfam00571 1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
38-202 |
6.07e-07 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 51.23 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 38 AKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVLRALG 116
Cdd:TIGR00260 42 VKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAgKISLGKLAQALGYN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 117 AEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnSHILDQYrnasnplahydTTADEILQQCDGKL-DMLVASVG 187
Cdd:TIGR00260 118 AEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-YRLEGQK-----------TYAFEAVEQLGWEApDKVVVPVP 183
|
170
....*....|....*
gi 2462583420 188 TGGTITGIARKLKEK 202
Cdd:TIGR00260 184 NSGNFGAIWKGFKEK 198
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
39-214 |
6.42e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 51.27 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 118
Cdd:PRK06450 70 KLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 119 IVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYRNASNPLAHydttadEILQQCDGKL-DMLVASVGTGGTI 192
Cdd:PRK06450 146 VVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFRDGIRTLAY------EIAKDLDWKIpNYVFIPVSAGTLL 209
|
170 180 190
....*....|....*....|....*....|
gi 2462583420 193 TGIARKLK--------EKCPgcRIIGVDPE 214
Cdd:PRK06450 210 LGVYSGFKhlldsgviSEMP--KIVAVQTE 237
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
28-120 |
9.30e-07 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 50.76 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 28 LVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSE 107
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVE 107
|
90
....*....|...
gi 2462583420 108 KVDVLRALGAEIV 120
Cdd:PRK06110 108 KNAAMRALGAELI 120
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
28-216 |
1.03e-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: 50.38 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 28 LVPRCRCRGVAKCEFFNAGGSVKDR-ISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSS 106
Cdd:cd06448 10 LSKTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTIVVPESTKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 107 EKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDTTADEILQQC--DGKLDML 182
Cdd:cd06448 88 RVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQQLqsQEKVDAI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462583420 183 VASVGTGGTITGIARKLkEKCPGCR--IIGVDPEGS 216
Cdd:cd06448 161 VCSVGGGGLLNGIVQGL-ERNGWGDipVVAVETEGA 195
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
73-214 |
1.54e-06 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 50.28 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 73 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEipnshild 152
Cdd:PRK07334 74 VIAMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLH--GETLDEARAH---ARELAEE-------- 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583420 153 QYRNASNPLAHYD------TTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 214
Cdd:PRK07334 141 EGLTFVHPYDDPAviagqgTVALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTE 207
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
343-435 |
3.56e-06 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 47.96 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 343 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEaGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 422
Cdd:COG2524 86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTVS 164
|
90
....*....|...
gi 2462583420 423 LTDTLGRLSHILE 435
Cdd:COG2524 165 EDDSLEEALRLML 177
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
353-434 |
7.92e-06 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 45.24 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 353 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQ------PSDQVGKVIYKQFKQIRLTDT 426
Cdd:COG3448 12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlLDLPVEDVMTRPVVTVTPDTP 91
|
....*...
gi 2462583420 427 LGRLSHIL 434
Cdd:COG3448 92 LEEAAELM 99
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
39-215 |
3.35e-05 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 45.97 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 118
Cdd:PRK08329 77 KLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 119 IvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRnasnpLAHYDTTADEILQQCdGKLDMLVASVGTGGTITGIA 196
Cdd:PRK08329 153 L----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYF-----LEGTKTIAYEIYEQI-GVPDYAFVPVGSGTLFLGIW 222
|
170 180
....*....|....*....|....*..
gi 2462583420 197 RKLKE--------KCPgcRIIGVDPEG 215
Cdd:PRK08329 223 KGFKElhemgeisKMP--KLVAVQAEG 247
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
326-400 |
4.45e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 43.36 E-value: 4.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583420 326 GFLKEEDLTEKKPwwwHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 400
Cdd:COG4109 62 GIVTSKDILGKDD---DTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
60-211 |
4.88e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 45.21 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 60 DAERDGTlkpgDTIIepTSGntGIG-----LALAAAVR-GYRCIIVMPEKMSSEKVDVL--------RALGAEIVRTPTN 125
Cdd:PRK03910 58 DALAQGA----DTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 126 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDTTADEILQQCDG---KLDMLVASVGTGGTITG 194
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
|
170
....*....|....*..
gi 2462583420 195 IARKLKEKCPGCRIIGV 211
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV 216
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
56-122 |
5.92e-05 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 5.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 56 RMIEDAerdGTLKPGDTIIEpTSGNTGIGLALA--AAVRGYRCIIVMPEKMSSEK-VDVLRALGAEIVRT 122
Cdd:cd08290 136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
333-400 |
6.17e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 42.55 E-value: 6.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462583420 333 LTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 400
Cdd:COG0517 57 LAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
353-446 |
7.77e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 42.59 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 353 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLssllagKVQPSDQVGKVIYKQFKQIRLTDTLGRLSH 432
Cdd:COG4109 27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVTPDTSLASAAH 100
|
90
....*....|....*.
gi 2462583420 433 ILEMDHFAL--VVHEQ 446
Cdd:COG4109 101 KMIWEGIELlpVVDDD 116
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
79-211 |
8.32e-05 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 44.57 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 79 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPtnarfDSPESHVGVAWRLKNE-----IPnshildq 153
Cdd:PRK07476 76 GNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVG-----RSQDDAQAEVERLVREegltmVP------- 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462583420 154 yrnasnPLAHYD------TTADEILQQCDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGV 211
Cdd:PRK07476 144 ------PFDDPRiiagqgTIGLEILEALP-DVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGV 200
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
262-399 |
1.12e-04 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 43.33 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 262 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRcVVILPDSVRNYMTKF---------LSD--RWMLQK----- 325
Cdd:COG2524 42 LLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL-GLVLKMKVKDIMTKDvitvspdttLEEalELMLEKgisgl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 326 ---------GFLKEEDL---TEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLG 393
Cdd:COG2524 121 pvvddgklvGIITERDLlkaLAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRT 200
|
....*.
gi 2462583420 394 NMLSSL 399
Cdd:COG2524 201 DILRAL 206
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
326-396 |
1.18e-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: 41.46 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462583420 326 GFLKEEDLTEK---KPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNML 396
Cdd:cd02205 39 GIVTERDILRAlveGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
345-427 |
1.18e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 41.74 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 345 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQIRL 423
Cdd:COG2905 1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80
|
....
gi 2462583420 424 TDTL 427
Cdd:COG2905 81 DDSL 84
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
291-400 |
3.23e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 40.58 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 291 AAQELQE-GQRCVVILPDSvrNYMTKFLSDRWMLQKGFLKEEDLTEkkpwwwhLRVQELGLSAPLTVLPTITCGHTIEIL 369
Cdd:COG2905 21 AARLMTEkGVGSLVVVDDD--GRLVGIITDRDLRRRVLAEGLDPLD-------TPVSEVMTRPPITVSPDDSLAEALELM 91
|
90 100 110
....*....|....*....|....*....|.
gi 2462583420 370 REKGFDQAPVVDEaGVILGMVTLGNMLSSLL 400
Cdd:COG2905 92 EEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
39-308 |
5.80e-04 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 42.11 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 39 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 118
Cdd:PRK05638 85 KDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 119 IVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnasnpLAHYDTTADEILQQCDGKldMLVASVGTGGTITGI 195
Cdd:PRK05638 161 IIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG--------LEGQKTIAFELWEEINPT--HVIVPTGSGSYLYSI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 196 ARKLKE--------KCPgcRIIGVDPE------GSILAEPEELNQTeqttyevEGIGYDFIPTVLDRTVVDKWFKS---- 257
Cdd:PRK05638 229 YKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKCNET-------KALGLYVKNPVMKEYVSEAIKESggta 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462583420 258 --NDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVILPDS 308
Cdd:PRK05638 300 vvVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGS 354
|
|
| CBS_pair_IMPDH |
cd04601 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
353-391 |
6.52e-04 |
|
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: 39.32 E-value: 6.52e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2462583420 353 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 391
Cdd:cd04601 4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT 42
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
342-400 |
6.79e-04 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 42.13 E-value: 6.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462583420 342 HLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 400
Cdd:PRK14869 67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
345-486 |
7.12e-04 |
|
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];
Pssm-ID: 442838 [Multi-domain] Cd Length: 95 Bit Score: 38.85 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 345 VQELGLSAPLTVLPTITCGHTIEILREK-GFDQAPVVDEAGvilgmVTLgNMLSSLLAGKVQPSdqvgkviykqfkqirl 423
Cdd:COG3620 1 VRDLMSRDVVTVSPDDTLGEALRLMRKElGLSQLPVAELVG-----VSQ-SDILRIESGKRDPT---------------- 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462583420 424 TDTLGRLSHILEMDHFALVVHEQiqsqdqawagvvggpadhstGKssqrqmVFGVVTAIDLLN 486
Cdd:COG3620 59 VSTLEKIAEALGKELSAVLVVDD--------------------GK------LVGIITRRDLLK 95
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
327-400 |
9.15e-04 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 39.46 E-value: 9.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462583420 327 FLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 400
Cdd:COG3448 57 ALLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
|
|
| CBS_pair_Mg_transporter |
cd04606 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ... |
354-425 |
1.15e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain] Cd Length: 121 Bit Score: 38.85 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462583420 354 LTVLPTITCGHTIEILREKG-----FDQAPVVDEAGVILGMVTLGNMLSSllagkvQPSDQVGKVIYKQFKQIRLTD 425
Cdd:cd04606 12 VAVRPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSLRDLLLA------DPDTKVSDIMDTDVISVSADD 82
|
|
| CBS_pair_NTP_transferase_assoc |
cd04607 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
326-397 |
6.78e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) 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: 341381 [Multi-domain] Cd Length: 112 Bit Score: 36.27 E-value: 6.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462583420 326 GFLKEEDLTEKkpwwwhlrVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLS 397
Cdd:cd04607 49 GLLKGLSLDAP--------VEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLLA 112
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
86-276 |
7.74e-03 |
|
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: 38.56 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 86 ALAAAVRGYRCIIVM--PEKMSSEKVD------VLRALGAEIvrtptnaRFDSPESHVGV-------AWRLKNE------ 144
Cdd:cd06449 70 AAVAAKLGLKCVLVQenWVPYSDAVYDrvgnilLSRIMGADV-------RLVSAGFDIGIrksfeeaAEEVEAKggkpyv 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583420 145 IPNShildqyrNASNPLAH--YDTTADEILQQCDG---KLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILA 219
Cdd:cd06449 143 IPAG-------GSEHPLGGlgYVGFVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEK 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462583420 220 EPEELNQTEQTTYEVEGIGYdfipTVLDRTVVDKWF-----KSNDE--EAFtfaRMLIAQEGLL 276
Cdd:cd06449 216 TKAQVLRIAQAKLAEEGLEV----KEEDVVLDDDYAapeygIPNDEtiEAI---KLCARLEGII 272
|
|
| CBS_pair_BON_assoc |
cd04586 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
353-391 |
9.15e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. 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: 341362 [Multi-domain] Cd Length: 137 Bit Score: 36.64 E-value: 9.15e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2462583420 353 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 391
Cdd:cd04586 5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVS 43
|
|
| |
