|
Name |
Accession |
Description |
Interval |
E-value |
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
112-575 |
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: 779.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 112 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 191
Cdd:TIGR01137 18 NKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKCIIVLPEKMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 192 SEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVAS 271
Cdd:TIGR01137 98 SEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEILEQCEGKLDMFVAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 272 VGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTF 351
Cdd:TIGR01137 178 VGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDEWIKTDDKESFTM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 352 ARMLIAQEGLLCGGSAGSTVAVAVKAAQ-ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLR 430
Cdd:TIGR01137 258 ARRLIKEEGLLVGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDNGFLDDEDLTVKDVLWWHAR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 431 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLT 510
Cdd:TIGR01137 338 VKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQPSDAVSKVMSKKFIQIGLG 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021845 511 DTLGRLSHILEMDHFALVVHEQIQsqdqawagvvggpadhstgkssqrqmvFGVVTAIDLLNFVA 575
Cdd:TIGR01137 418 ETLSDLSKFLEMDSSAIVVEEGKP---------------------------IGVVTKIDLLSFLA 455
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
112-400 |
2.30e-157 |
|
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: 451.58 E-value: 2.30e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 112 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 191
Cdd:cd01561 9 NRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETMS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 192 SEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVAS 271
Cdd:cd01561 89 EEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGKVDAFVAG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 272 VGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTF 351
Cdd:cd01561 168 VGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEAFAM 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 768021845 352 ARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 400
Cdd:cd01561 243 ARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
112-401 |
1.03e-143 |
|
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: 417.14 E-value: 1.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 112 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 191
Cdd:COG0031 20 NRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAKGYRLILVMPETMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 192 SEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVAS 271
Cdd:COG0031 100 KERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIWEQTDGKVDAFVAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 272 VGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTF 351
Cdd:COG0031 177 VGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKILDPSLIDEVITVSDEEAFAM 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 768021845 352 ARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 401
Cdd:COG0031 252 ARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
115-400 |
3.16e-105 |
|
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: 3.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 115 VPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEK 194
Cdd:TIGR01139 16 IEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGYKLILTMPETMSIER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 195 VDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVG 273
Cdd:TIGR01139 96 RKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWRDTDGKLDAFVAGVG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 274 TGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFAR 353
Cdd:TIGR01139 173 TGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSDEEAIETAR 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 768021845 354 MLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 400
Cdd:TIGR01139 248 RLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
120-413 |
4.65e-105 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 319.50 E-value: 4.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 120 CRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLR 199
Cdd:PRK10717 28 CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 200 ALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGT 274
Cdd:PRK10717 108 ALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPANREAHYETTGPEIWEQTDGKVDGFVCAVGT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 275 GGTITGIARKLKEKCPGCRIIGVDPEGSIL----AEPEELNQTEQTTyevEGIGYDFIPTVLDRTVVDKWFKSNDEEAFT 350
Cdd:PRK10717 187 GGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGELKAEGSSIT---EGIGQGRITANLEGAPIDDAIRIPDEEALS 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021845 351 FARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGF 413
Cdd:PRK10717 264 TAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLREKGL 326
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
112-400 |
1.12e-103 |
|
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: 314.99 E-value: 1.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 112 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 191
Cdd:TIGR01136 14 NRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAARGYKLILTMPETMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 192 SEKVDVLRALGAEIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDTTADEILQQCDGKLDM 267
Cdd:TIGR01136 94 LERRKLLRAYGAELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKTTGPEIWRDTDGRIDH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 268 LVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEE 347
Cdd:TIGR01136 167 FVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDED 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 768021845 348 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMT 400
Cdd:TIGR01136 242 AIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
111-394 |
1.54e-78 |
|
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: 247.81 E-value: 1.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 111 SDRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLkPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKM 190
Cdd:cd00640 6 LKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIVMPEGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 191 SSEKVDVLRALGAEIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDG-KLDMLV 269
Cdd:cd00640 85 SPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqKPDAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 270 ASVGTGGTITGIARKLKEKCPGCRIIGVDPEgsilaepeelnqteqttyevegigydfiptvldrtvvdkWFKSNDEEAF 349
Cdd:cd00640 159 VPVGGGGNIAGIARALKELLPNVKVIGVEPE---------------------------------------VVTVSDEEAL 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 768021845 350 TFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDS 394
Cdd:cd00640 200 EAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
112-405 |
9.31e-74 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 238.28 E-value: 9.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 112 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGLALAAAVRGYRCIIVMPEKM 190
Cdd:PLN02565 22 NNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAFMAAAKGYKLIITMPASM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 191 SSEKVDVLRALGAEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLV 269
Cdd:PLN02565 102 SLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEIWKGTGGKVDAFV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 270 ASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAF 349
Cdd:PLN02565 178 SGIGTGGTITGAGKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQVSSDEAI 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 768021845 350 TFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 405
Cdd:PLN02565 253 ETAKLLALKEGLLVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
111-393 |
1.33e-73 |
|
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: 236.82 E-value: 1.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 111 SDRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERdgtLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKM 190
Cdd:pfam00291 13 LPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 191 SSEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDGKLDMLVA 270
Cdd:pfam00291 90 PPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQLGGDPDAVVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 271 SVGTGGTITGIARKLKEKCPGCRIIGVDPEGS-ILAEPEELNQTEQTT---YEVEGIGYDFIPTVLDRTVVDKWFKS--- 343
Cdd:pfam00291 164 PVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGALALDLLDEYVGEvvt 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 768021845 344 -NDEEAFTFARMLIAQEGLLCGGSAGSTVAVA-VKAAQELQEGQRCVVILPD 393
Cdd:pfam00291 244 vSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
113-393 |
1.83e-72 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 234.00 E-value: 1.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 113 RLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSS 192
Cdd:PRK11761 20 RLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYRMKLIMPENMSQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 193 EKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASV 272
Cdd:PRK11761 100 ERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTGPEIWRQTEGRITHFVSSM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 273 GTGGTITGIARKLKEKCPGCRIIGVDP-EGS----ILAEPEElnqteqttyevegigydFIPTVLDRTVVDKWFKSNDEE 347
Cdd:PRK11761 176 GTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLPKIFDASRVDRVLDVSQQE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 768021845 348 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELqEGQRCVVILPD 393
Cdd:PRK11761 239 AENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICD 283
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
112-407 |
2.20e-71 |
|
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: 231.32 E-value: 2.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 112 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMS 191
Cdd:TIGR03945 14 ERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYKGLRFICVVDPNIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 192 SEKVDVLRALGAEIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDg 263
Cdd:TIGR03945 94 PQNLKLLRAYGAEVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRAHYHGTGREIARAFP- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 264 KLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL--AEPeelnqteqTTYEVEGIGYDFIPTVLDRTVVDKWF 341
Cdd:TIGR03945 166 TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGASVVPELLDESLIDDVV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021845 342 KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRW 407
Cdd:TIGR03945 238 HVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEW 303
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
112-405 |
2.52e-66 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 219.10 E-value: 2.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 112 DRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPG-DTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKM 190
Cdd:PLN00011 24 NNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGAARGYKVILVMPSTM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 191 SSEKVDVLRALGAEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGK 264
Cdd:PLN00011 104 SLERRIILRALGAEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEIHYRTTGPEIWRDSAGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 265 LDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSN 344
Cdd:PLN00011 175 VDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQVT 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021845 345 DEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQE-GQRCVVILPDSVRNYMTKFLSD 405
Cdd:PLN00011 250 GEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYLSTKLFE 311
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
124-400 |
3.65e-64 |
|
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: 212.08 E-value: 3.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 124 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 203
Cdd:TIGR01138 27 LKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERKAAMRAYGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 204 EIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 283
Cdd:TIGR01138 107 ELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPEIWQQTGGRITHFVSSMGTTGTIMGVSR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 284 KLKEKCPGCRIIGVDPEgsilaEPeelnqteqttYEVEGIGY---DFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEG 360
Cdd:TIGR01138 183 FLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFDASLVDRVLDIHQRDAENTMRELAVREG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 768021845 361 LLCGGSAGSTVAVAVKAAQELQEGQrCVVILPDSVRNYMT 400
Cdd:TIGR01138 248 IFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
118-411 |
2.65e-62 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 211.56 E-value: 2.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 118 CRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVD 196
Cdd:PLN03013 136 CVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAFIAASRGYRLILTMPASMSMERRV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 197 VLRALGAEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASV 272
Cdd:PLN03013 216 LLKAFGAELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPKIHYETTGPEIWDDTKGKVDIFVAGI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 273 GTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFA 352
Cdd:PLN03013 289 GTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVIAISSEEAIETA 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768021845 353 RMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK--FLSDRWMLQK 411
Cdd:PLN03013 364 KQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIYTprCSSLSGKRWR 424
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
118-405 |
1.89e-59 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 202.11 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 118 CRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDT-IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVD 196
Cdd:PLN02556 72 CGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 197 VLRALGAEIVRT-PTNARFDSpeshVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTG 275
Cdd:PLN02556 152 TMRAFGAELVLTdPTKGMGGT----VKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 276 GTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARML 355
Cdd:PLN02556 228 GTVSGVGKYLKSKNPNVKIYGVEP-----AESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMAREL 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 768021845 356 IAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 405
Cdd:PLN02556 303 ALKEGLMVGISSGANTVAALRLAKMPEnKGKLIVTVHPSFGERYLSSVLFQ 353
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
429-573 |
1.45e-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: 180.42 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 429 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 508
Cdd:cd04608 2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021845 509 LTDTLGRLSHILEMDHFALVVHEQiqsqdqawagvvggpadhstgkssqrQMVFGVVTAIDLLNF 573
Cdd:cd04608 82 LDTPLGALSRILERDHFALVVDGQ--------------------------GKVLGIVTRIDLLNY 120
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
120-413 |
3.16e-47 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 170.94 E-value: 3.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 120 CRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLR 199
Cdd:PLN02356 68 CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKCHVVIPDDVAIEKSQILE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 200 ALGAEIVRT-PTNarFDSPESHVGVAWRLK---NEIPNSHIL------------------------------------DQ 239
Cdd:PLN02356 148 ALGATVERVrPVS--ITHKDHYVNIARRRAleaNELASKRRKgsetdgihlektngciseeekenslfsssctggffaDQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 240 YRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL--------------A 305
Cdd:PLN02356 226 FENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGSGLfnkvtrgvmytreeA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 306 EPEELNQTEQTTyeVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQ 385
Cdd:PLN02356 306 EGRRLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNCVGAVRVAQSLGPGH 383
|
330 340
....*....|....*....|....*...
gi 768021845 386 RCVVILPDSVRNYMTKFLSDRWMLQKGF 413
Cdd:PLN02356 384 TIVTILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
111-391 |
3.62e-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: 111.81 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 111 SDRLVPRCRCRGVAKCEFFNAGGSVKDRISLRMI----EDAERDGtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVM 186
Cdd:cd01562 23 SPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLGIPATIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 187 PEKMSSEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD------TTAD 255
Cdd:cd01562 96 PETAPAAKVDATRAYGAEVVL--YGEDFDEAEAK---ARELAEEegltfIH-------------PFDDPDviagqgTIGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 256 EILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTEQTtyeVEGIGydfI 328
Cdd:cd01562 158 EILEQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTI---ADGLA---V 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021845 329 PTVLDRT------VVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 391
Cdd:cd01562 231 KRPGELTfeiirkLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
125-391 |
5.56e-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: 108.97 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDR------ISLRmieDAERDGTlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVL 198
Cdd:COG1171 44 KLENLQPTGSFKLRgaynalASLS---EEERARG------VVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAAT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 199 RALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKLDM 267
Cdd:COG1171 115 RAYGAEVVLHGDT--YDDAEAA---AAELAEEegatfVH-------------PFDDPDviagqgTIALEILEQL-PDLDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 268 LVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTeQT------TYEVEGIGYDFIPTVLDR 334
Cdd:COG1171 176 VFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTiadglaVGRPGELTFEILRDLVDD 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 768021845 335 TV-VDkwfksnDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 391
Cdd:COG1171 255 IVtVS------EDEIAAAMRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVVL 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
111-391 |
1.67e-25 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 107.09 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 111 SDRLVPRCRCRGVAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMP 187
Cdd:PRK06815 26 SPLLSQHTGCEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGIPVTVYAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 188 EKMSSEKVDVLRALGAEIVRTPTNArfDSPESHvgvAWRLKNEIPNSHIlDQYrNASNPLAHYDTTADEILQQCDgKLDM 267
Cdd:PRK06815 100 EQASAIKLDAIRALGAEVRLYGGDA--LNAELA---ARRAAEQQGKVYI-SPY-NDPQVIAGQGTIGMELVEQQP-DLDA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 268 LVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA----EPEELNQTEQTTyeVEGIGYDFIPTVLDRTVV 337
Cdd:PRK06815 172 VFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTLSDGT--AGGVEPGAITFPLCQQLI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 768021845 338 DKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQeGQRCVVIL 391
Cdd:PRK06815 250 DQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
|
|
| PLN02970 |
PLN02970 |
serine racemase |
109-302 |
4.08e-16 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 79.72 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 109 RSSDRLVPRcrcRGVAKCEFFNAGGSVKDRISLRMI-----EDAERDgtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCI 183
Cdd:PLN02970 34 SSLDALAGR---SLFFKCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLRGIPAY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 184 IVMPEKMSSEKVDVLRALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDTTADEILQQCD 262
Cdd:PLN02970 103 IVVPKNAPACKVDAVIRYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLEQVP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768021845 263 GkLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 302
Cdd:PLN02970 175 E-LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
125-391 |
3.32e-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: 76.86 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 204
Cdd:cd01563 43 KDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGAT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 205 IVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLAH--YDTTADEILQQCDGKL-DMLVASVGTGGTITGI 281
Cdd:cd01563 119 VLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYRLegQKTIAFEIAEQLGWEVpDYVVVPVGNGGNITAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 282 ARKLKE--------KCPgcRIIGVDPEGS------ILAEPEELNQTEQTTYEVEGIGydfIPT-VLDRTVVDKWFKSN-- 344
Cdd:cd01563 189 WKGFKElkelglidRLP--RMVGVQAEGAapivraFKEGKDDIEPVENPETIATAIR---IGNpASGPKALRAVRESGgt 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 768021845 345 ----DEEAFTFARMLIAQ-EGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVIL 391
Cdd:cd01563 264 avavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiIDKGERVVVVL 317
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
125-391 |
2.04e-14 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 74.36 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 204
Cdd:PRK06381 36 KFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 205 IVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGI 281
Cdd:PRK06381 112 IIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAYEIYEALGDVPDAVAVPVGNGTTLAGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 282 ARKLKE--------KCPgcRIIGVDPEGS--------------ILAEPEELNQTEQTTYEVEGIGYDFiPTVLD--RTVV 337
Cdd:PRK06381 184 YHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRETAVNEPLVSYRSFDG-DNALEaiYDSH 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 768021845 338 DKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVIL 391
Cdd:PRK06381 261 GYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
165-302 |
8.67e-14 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 74.02 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 165 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 239
Cdd:PRK09224 77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021845 240 yrnasnPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 302
Cdd:PRK09224 145 ------PFDDPDviagqgTIAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
125-302 |
1.02e-13 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 72.29 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDRISLRMIEDAErdgtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 204
Cdd:PRK08246 42 KLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 205 IVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDTTADEILQQCdGKLDMLVASVGTGGTIT 279
Cdd:PRK08246 117 VVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGGGGLIA 183
|
170 180
....*....|....*....|...
gi 768021845 280 GIARKLKekcPGCRIIGVDPEGS 302
Cdd:PRK08246 184 GIAAWFE---GRARVVAVEPEGA 203
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
125-300 |
2.25e-13 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 71.20 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDR---ISLRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRAL 201
Cdd:PRK07048 44 KCENFQRMGAFKFRgayNALSQFSPEQR----RAG--VVTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 202 GAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKLDMLV 269
Cdd:PRK07048 118 GGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELFEEV-GPLDALF 177
|
170 180 190
....*....|....*....|....*....|.
gi 768021845 270 ASVGTGGTITGIARKLKEKCPGCRIIGVDPE 300
Cdd:PRK07048 178 VCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
159-302 |
1.27e-12 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 70.21 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 159 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEIPNS--HI 236
Cdd:PRK12483 88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAH---ALKLAEEEGLTfvPP 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021845 237 LDQyrnaSNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 302
Cdd:PRK12483 163 FDD----PDVIAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
125-398 |
2.08e-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: 69.07 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDR-----ISLrmiedAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVL 198
Cdd:COG0498 86 KEEGHNPTGSFKDRamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQLAQM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 199 RALGAEIVRTPTNarFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPLAH--YDTTADEILQQCDGKLDMLVASVGTG 275
Cdd:COG0498 157 LTYGAHVIAVDGN--FD-------DAQRLVKELAADEGL--YaVNSINPARLegQKTYAFEIAEQLGRVPDWVVVPTGNG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 276 GTITGI--ARK------LKEKCPgcRIIGVDPEGS--ILAEPEelnqTEQTTYEVEG---------IGydfIPT------ 330
Cdd:COG0498 226 GNILAGykAFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPERpetiapsmdIG---NPSngeral 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021845 331 -VLDRTvvDKWF-KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVIL-------PDSVRNY 398
Cdd:COG0498 297 fALRES--GGTAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVVVLStghglkfPDAVREA 373
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
125-299 |
1.00e-10 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 63.25 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDRISLRMIEDAERDGtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 204
Cdd:PRK06608 43 KVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 205 IVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITG- 280
Cdd:PRK06608 121 VILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTLCYEALQQLGFSPDAIFASCGGGGLISGt 188
|
170 180
....*....|....*....|
gi 768021845 281 -IARKLKEkcPGCRIIGVDP 299
Cdd:PRK06608 189 yLAKELIS--PTSLLIGSEP 206
|
|
| CBS |
smart00116 |
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
439-486 |
1.04e-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: 54.06 E-value: 1.04e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 768021845 439 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 486
Cdd:smart00116 2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
439-522 |
2.32e-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: 55.33 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 439 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTlgrLSH 518
Cdd:cd02205 4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTD---LEE 80
|
....
gi 768021845 519 ILEM 522
Cdd:cd02205 81 ALEL 84
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
119-300 |
8.83e-09 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 57.44 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 119 RCRG--VAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSE 193
Cdd:PRK08638 39 RCKGeiFLKLENMQRTGSFKIRGAfnkLSSLTDAEK----RKG--VVACSAGNHAQGVALSCALLGIDGKVVMPKGAPKS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 194 KVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILDQYrNASNPLAHYDTTADEILQQCdGKLDMLVASVG 273
Cdd:PRK08638 113 KVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIPPY-DDPKVIAGQGTIGLEILEDL-WDVDTVIVPIG 184
|
170 180
....*....|....*....|....*..
gi 768021845 274 TGGTITGIARKLKEKCPGCRIIGVDPE 300
Cdd:PRK08638 185 GGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
252-301 |
2.26e-08 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 56.35 E-value: 2.26e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 768021845 252 TTADEILQQCD--GKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG 301
Cdd:PRK08639 165 TVAVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
158-300 |
6.13e-08 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 55.27 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 158 TIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDspEShVGVAWRLKNEipNSHIL 237
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN--YD--DS-VRLAAQEAQE--NGWVV 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021845 238 DQyrNASNP---------LAHYDTTADEILQQCDGKLD-----MLVASVGT--GGTITGIARKLKEKCPgcRIIGVDPE 300
Cdd:PRK08206 191 VQ--DTAWEgyeeiptwiMQGYGTMADEAVEQLKEMGVppthvFLQAGVGSlaGAVLGYFAEVYGEQRP--HFVVVEPD 265
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
134-299 |
1.49e-07 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 54.16 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 134 SVKDRISLRMIEDAERDgTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNar 213
Cdd:PLN02550 138 SFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDS-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 214 FDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKE 287
Cdd:PLN02550 213 YDEAQAYA-----------KQRALEEGRTFIPPFDHPDviagqgTVGMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKR 281
|
170
....*....|..
gi 768021845 288 KCPGCRIIGVDP 299
Cdd:PLN02550 282 VRPEVKIIGVEP 293
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
429-521 |
1.87e-07 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 50.25 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 429 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQI 507
Cdd:COG0517 1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTpVSEVMTRPPVTV 80
|
90
....*....|....
gi 768021845 508 RLTDTLGRLSHILE 521
Cdd:COG0517 81 SPDTSLEEAAELME 94
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
431-486 |
3.73e-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: 47.21 E-value: 3.73e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 768021845 431 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 486
Cdd:pfam00571 1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
124-288 |
7.68e-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: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 124 AKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVLRALG 202
Cdd:TIGR00260 42 VKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAgKISLGKLAQALGYN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 203 AEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnSHILDQYrnasnplahydTTADEILQQCDGKL-DMLVASVG 273
Cdd:TIGR00260 118 AEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-YRLEGQK-----------TYAFEAVEQLGWEApDKVVVPVP 183
|
170
....*....|....*
gi 768021845 274 TGGTITGIARKLKEK 288
Cdd:TIGR00260 184 NSGNFGAIWKGFKEK 198
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
125-300 |
8.14e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 51.27 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 204
Cdd:PRK06450 70 KLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 205 IVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYRNASNPLAHydttadEILQQCDGKL-DMLVASVGTGGTI 278
Cdd:PRK06450 146 VVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFRDGIRTLAY------EIAKDLDWKIpNYVFIPVSAGTLL 209
|
170 180 190
....*....|....*....|....*....|
gi 768021845 279 TGIARKLK--------EKCPgcRIIGVDPE 300
Cdd:PRK06450 210 LGVYSGFKhlldsgviSEMP--KIVAVQTE 237
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
114-302 |
1.31e-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: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 114 LVPRCRCRGVAKCEFFNAGGSVKDR-ISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSS 192
Cdd:cd06448 10 LSKTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTIVVPESTKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 193 EKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDTTADEILQQC--DGKLDML 268
Cdd:cd06448 88 RVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQQLqsQEKVDAI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 768021845 269 VASVGTGGTITGIARKLkEKCPGCR--IIGVDPEGS 302
Cdd:cd06448 161 VCSVGGGGLLNGIVQGL-ERNGWGDipVVAVETEGA 195
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
114-206 |
1.40e-06 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 50.38 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 114 LVPRCRCRGVAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSE 193
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVE 107
|
90
....*....|...
gi 768021845 194 KVDVLRALGAEIV 206
Cdd:PRK06110 108 KNAAMRALGAELI 120
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
429-521 |
1.84e-06 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 49.11 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 429 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEaGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 508
Cdd:COG2524 86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTVS 164
|
90
....*....|...
gi 768021845 509 LTDTLGRLSHILE 521
Cdd:COG2524 165 EDDSLEEALRLML 177
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
159-300 |
2.30e-06 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 50.28 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 159 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEipnshild 238
Cdd:PRK07334 74 VIAMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLH--GETLDEARAH---ARELAEE-------- 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021845 239 QYRNASNPLAHYD------TTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 300
Cdd:PRK07334 141 EGLTFVHPYDDPAviagqgTVALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTE 207
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
439-581 |
5.30e-06 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 46.01 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 439 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQ------PSDQVGKVIYKQFKQIRLTDT 512
Cdd:COG3448 12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlLDLPVEDVMTRPVVTVTPDTP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021845 513 LGRLSHILeMD---HFALVVHEQiqsqdqawagvvggpadhstGKssqrqmVFGVVTAIDLLNFVAAQERDQ 581
Cdd:COG3448 92 LEEAAELM-LEhgiHRLPVVDDD--------------------GR------LVGIVTRTDLLRALARLLEEE 136
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
125-301 |
4.20e-05 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 45.97 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 204
Cdd:PRK08329 77 KLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 205 IvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRnasnpLAHYDTTADEILQQCdGKLDMLVASVGTGGTITGIA 282
Cdd:PRK08329 153 L----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYF-----LEGTKTIAYEIYEQI-GVPDYAFVPVGSGTLFLGIW 222
|
170 180
....*....|....*....|....*..
gi 768021845 283 RKLKE--------KCPgcRIIGVDPEG 301
Cdd:PRK08329 223 KGFKElhemgeisKMP--KLVAVQAEG 247
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
348-485 |
4.40e-05 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 44.87 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 348 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRcVVILPDSVRNYMTKF---------LSD--RWMLQK----- 411
Cdd:COG2524 42 LLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL-GLVLKMKVKDIMTKDvitvspdttLEEalELMLEKgisgl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 412 ---------GFLKEEDL---TEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLG 479
Cdd:COG2524 121 pvvddgklvGIITERDLlkaLAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRT 200
|
....*.
gi 768021845 480 NMLSSL 485
Cdd:COG2524 201 DILRAL 206
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
412-486 |
4.64e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 43.36 E-value: 4.64e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021845 412 GFLKEEDLTEKKPwwwHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 486
Cdd:COG4109 62 GIVTSKDILGKDD---DTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
419-486 |
4.89e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 43.32 E-value: 4.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021845 419 LTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 486
Cdd:COG0517 57 LAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
142-208 |
6.73e-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: 6.73e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 142 RMIEDAerdGTLKPGDTIIEpTSGNTGIGLALA--AAVRGYRCIIVMPEKMSSEK-VDVLRALGAEIVRT 208
Cdd:cd08290 136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
439-532 |
7.42e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 42.98 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 439 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLssllagKVQPSDQVGKVIYKQFKQIRLTDTLGRLSH 518
Cdd:COG4109 27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVTPDTSLASAAH 100
|
90
....*....|....*.
gi 768021845 519 ILEMDHFAL--VVHEQ 532
Cdd:COG4109 101 KMIWEGIELlpVVDDD 116
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
412-482 |
8.05e-05 |
|
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: 42.23 E-value: 8.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021845 412 GFLKEEDLTEK---KPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNML 482
Cdd:cd02205 39 GIVTERDILRAlveGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
146-297 |
9.49e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 44.82 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 146 DAERDGTlkpgDTIIepTSGntGIG-----LALAAAVR-GYRCIIVMPEKMSSEKVDVL--------RALGAEIVRTPTN 211
Cdd:PRK03910 58 DALAQGA----DTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 212 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDTTADEILQQCDG---KLDMLVASVGTGGTITG 280
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
|
170
....*....|....*..
gi 768021845 281 IARKLKEKCPGCRIIGV 297
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV 216
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
431-513 |
1.02e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 42.12 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 431 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQIRL 509
Cdd:COG2905 1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80
|
....
gi 768021845 510 TDTL 513
Cdd:COG2905 81 DDSL 84
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
165-297 |
1.45e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 44.19 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 165 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPtnarfDSPESHVGVAWRLKNE-----IPnshildq 239
Cdd:PRK07476 76 GNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVG-----RSQDDAQAEVERLVREegltmVP------- 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021845 240 yrnasnPLAHYD------TTADEILQQCDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGV 297
Cdd:PRK07476 144 ------PFDDPRiiagqgTIGLEILEALP-DVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGV 200
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
377-486 |
2.32e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 40.97 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 377 AAQELQE-GQRCVVILPDSvrNYMTKFLSDRWMLQKGFLKEEDLTEKKpwwwhlrVQELGLSAPLTVLPTITCGHTIEIL 455
Cdd:COG2905 21 AARLMTEkGVGSLVVVDDD--GRLVGIITDRDLRRRVLAEGLDPLDTP-------VSEVMTRPPITVSPDDSLAEALELM 91
|
90 100 110
....*....|....*....|....*....|.
gi 768021845 456 REKGFDQAPVVDEaGVILGMVTLGNMLSSLL 486
Cdd:COG2905 92 EEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
431-572 |
4.03e-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: 39.62 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 431 VQELGLSAPLTVLPTITCGHTIEILREK-GFDQAPVVDEAGvilgmVTLgNMLSSLLAGKVQPSdqvgkviykqfkqirl 509
Cdd:COG3620 1 VRDLMSRDVVTVSPDDTLGEALRLMRKElGLSQLPVAELVG-----VSQ-SDILRIESGKRDPT---------------- 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021845 510 TDTLGRLSHILEMDHFALVVHEQiqsqdqawagvvggpadhstGKssqrqmVFGVVTAIDLLN 572
Cdd:COG3620 59 VSTLEKIAEALGKELSAVLVVDD--------------------GK------LVGIITRRDLLK 95
|
|
| CBS_pair_IMPDH |
cd04601 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
439-477 |
5.82e-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: 39.70 E-value: 5.82e-04
10 20 30
....*....|....*....|....*....|....*....
gi 768021845 439 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 477
Cdd:cd04601 4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT 42
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
428-486 |
7.16e-04 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 42.51 E-value: 7.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 768021845 428 HLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 486
Cdd:PRK14869 67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
125-394 |
7.24e-04 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 42.11 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 125 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 204
Cdd:PRK05638 85 KDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 205 IVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnasnpLAHYDTTADEILQQCDGKldMLVASVGTGGTITGI 281
Cdd:PRK05638 161 IIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG--------LEGQKTIAFELWEEINPT--HVIVPTGSGSYLYSI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 282 ARKLKE--------KCPgcRIIGVDPE------GSILAEPEELNQTeqttyevEGIGYDFIPTVLDRTVVDKWFKS---- 343
Cdd:PRK05638 229 YKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKCNET-------KALGLYVKNPVMKEYVSEAIKESggta 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 768021845 344 --NDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVILPDS 394
Cdd:PRK05638 300 vvVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGS 354
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
413-486 |
7.36e-04 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 39.85 E-value: 7.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021845 413 FLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 486
Cdd:COG3448 57 ALLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
|
|
| CBS_pair_Mg_transporter |
cd04606 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ... |
440-511 |
8.26e-04 |
|
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: 39.62 E-value: 8.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768021845 440 LTVLPTITCGHTIEILREKG-----FDQAPVVDEAGVILGMVTLGNMLSSllagkvQPSDQVGKVIYKQFKQIRLTD 511
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 ... |
412-483 |
6.12e-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: 36.65 E-value: 6.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021845 412 GFLKEEDLTEKkpwwwhlrVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLS 483
Cdd:cd04607 49 GLLKGLSLDAP--------VEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLLA 112
|
|
| MgtE |
COG2239 |
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; |
440-532 |
7.48e-03 |
|
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 38.89 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021845 440 LTVLPTITCGHTIEILREKG-----FDQAPVVDEAGVILGMVTLGNMLSSllagkvQPSDQVGKVIYKQFKQIRLTDTLG 514
Cdd:COG2239 140 VAVREDWTVGEALRYLRRQAedpetIYYIYVVDDDGRLVGVVSLRDLLLA------DPDTKVSDIMDTDVISVPADDDQE 213
|
90 100
....*....|....*....|
gi 768021845 515 RLSHILEM-DHFAL-VVHEQ 532
Cdd:COG2239 214 EVARLFERyDLLALpVVDEE 233
|
|
| CBS_pair_BON_assoc |
cd04586 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
439-477 |
9.71e-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: 9.71e-03
10 20 30
....*....|....*....|....*....|....*....
gi 768021845 439 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 477
Cdd:cd04586 5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVS 43
|
|
| |
