|
Name |
Accession |
Description |
Interval |
E-value |
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
73-554 |
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: 776.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 73 ILPDILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLA 152
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 153 LAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDD 232
Cdd:TIGR01137 79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 233 TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEELNQTEQTAYEVEGIGYDFIPTVL 312
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 313 DRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAA-RELQEGQRCVVILPDSVRNYMSKFLSDKWMLQK 391
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAeDELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 392 GFMKEE-LSVKRPWWWRLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVR 470
Cdd:TIGR01137 319 GFLDDEdLTVKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 471 PSDEVCKVLYKQFKPIHLTDTLGTLSHILEMDHFALVVHEQIQsrdqawsgvvggptdcsngmsskqqmvFGVVTAIDLL 550
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKP---------------------------IGVVTKIDLL 451
|
....
gi 21450071 551 NFVA 554
Cdd:TIGR01137 452 SFLA 455
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
82-380 |
5.41e-165 |
|
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: 470.46 E-value: 5.41e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 82 GNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd01561 1 GNTPLVRLNRLSP--GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQC 241
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 242 DGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWF 321
Cdd:cd01561 158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21450071 322 KSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 380
Cdd:cd01561 233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
72-381 |
3.84e-161 |
|
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: 461.05 E-value: 3.84e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 72 KILPDILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGL 151
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPG--AEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYD 231
Cdd:COG0031 80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 232 DTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTV 311
Cdd:COG0031 157 TTGPEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 312 LDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSK 381
Cdd:COG0031 232 LDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
71-393 |
1.87e-116 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 348.00 E-value: 1.87e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 71 PKILPDILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIG 150
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 151 LALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASN 225
Cdd:PRK10717 79 LALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 226 PLAHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEV----- 300
Cdd:PRK10717 158 REAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAL-----YSYYKTGELKAegssi 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 301 -EGIGYDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYM 379
Cdd:PRK10717 233 tEGIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQ 312
|
330
....*....|....
gi 21450071 380 SKFLSDKWMLQKGF 393
Cdd:PRK10717 313 SKLFNPDFLREKGL 326
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
77-380 |
3.49e-113 |
|
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: 338.57 E-value: 3.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 77 ILRKIGNTPMVRINKISKNAGlkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01139 1 ISELIGNTPLVRLNRIEGCNA---NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDDTAE 235
Cdd:TIGR01139 78 ARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 236 EILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRA 315
Cdd:TIGR01139 155 EIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21450071 316 VVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 380
Cdd:TIGR01139 230 VIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
77-380 |
1.12e-109 |
|
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: 329.63 E-value: 1.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 77 ILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAP--GCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDD 232
Cdd:TIGR01136 79 ARGYKLILTMPETMSLERRKLLRAYGAELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 233 TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPTVL 312
Cdd:TIGR01136 152 TGPEIWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKIL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21450071 313 DRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQ-EGQRCVVILPDSVRNYMS 380
Cdd:TIGR01136 227 DLSLIDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
84-374 |
2.23e-82 |
|
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: 257.44 E-value: 2.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGnLKPGDTIIEPTSGNTGIGLALAAAVKGYRCI 163
Cdd:cd00640 1 TPLVRLKRLSK--LGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEG-KLPKGVIIESTGGNTGIALAAAAARLGLKCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 164 IVMPEKMSMEKVDVLRALGAEIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdDTAEEILQQCDG 243
Cdd:cd00640 78 IVMPEGASPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 244 -KLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEgsilaepeelnqteqtAYEVegigydfiptvldravvdkwfk 322
Cdd:cd00640 152 qKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE----------------VVTV---------------------- 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 21450071 323 sNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDS 374
Cdd:cd00640 194 -SDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
75-380 |
1.50e-81 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 257.11 E-value: 1.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 75 PDILRKIGNTPMVRINKISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALA 154
Cdd:PRK11761 4 PTLEDTIGNTPLVKLQRLPPDRGN--TILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 155 AAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDDTA 234
Cdd:PRK11761 82 AAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 235 EEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDP-EGS----ILAEPEElnqteqtayevegigydFIP 309
Cdd:PRK11761 158 PEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21450071 310 TVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELqEGQRCVVILPDSVRNYMS 380
Cdd:PRK11761 221 KIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLS 290
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
77-373 |
5.95e-81 |
|
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: 255.31 E-value: 5.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 77 ILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAgnlKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdDTAEE 236
Cdd:pfam00291 76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 237 ILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS-ILAEPEELNQTEQTA---YEVEGIGYDFIPTVL 312
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGAL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450071 313 DRAVVDKWFKS----NDEDSFAFARMLIAQEGLLCGGSSGSAMAVA-VKAARELQEGQRCVVILPD 373
Cdd:pfam00291 230 ALDLLDEYVGEvvtvSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
77-387 |
3.79e-79 |
|
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: 250.97 E-value: 3.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 77 ILRKIGNTPMVRINKIskNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR03945 1 ILSLIGNTPLVKLERL--FPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLA 228
Cdd:TIGR03945 79 YKGLRFICVVDPNISPQNLKLLRAYGAEVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 229 HYDDTAEEILQQCDgKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSIL--AEPeelnqteqTAYEVEGIGYD 306
Cdd:TIGR03945 152 HYHGTGREIARAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGAS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 307 FIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSKFLSDK 386
Cdd:TIGR03945 223 VVPELLDESLIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDE 302
|
.
gi 21450071 387 W 387
Cdd:TIGR03945 303 W 303
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
73-385 |
2.24e-78 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 249.84 E-value: 2.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 73 ILPDILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTI-IEPTSGNTGIGL 151
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVD--GCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHY 230
Cdd:PLN02565 83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 231 DDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPT 310
Cdd:PLN02565 159 ETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450071 311 VLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVK-AARELQEGQRCVVILPDSVRNYMSKFLSD 385
Cdd:PLN02565 234 VLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKiAKRPENAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
77-380 |
2.66e-72 |
|
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: 232.88 E-value: 2.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 77 ILRKIGNTPMVRINKISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGS--EVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDDTAEE 236
Cdd:TIGR01138 80 LKGYRMKLLMPDNMSQERKAAMRAYGAELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 237 ILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEgsilaEPeelnqteqtaYEVEGIGY---DFIPTVLD 313
Cdd:TIGR01138 156 IWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFD 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21450071 314 RAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQrCVVILPDSVRNYMS 380
Cdd:TIGR01138 221 ASLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
76-385 |
4.24e-70 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 228.35 E-value: 4.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 76 DILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPG-DTIIEPTSGNTGIGLALA 154
Cdd:PLN00011 10 DVTELIGNTPMVYLNNIVD--GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 155 AAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLA 228
Cdd:PLN00011 88 GAARGYKVILVMPSTMSLERRIILRALGAEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 229 HYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFI 308
Cdd:PLN00011 159 HYRTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGII 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21450071 309 PTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAA-RELQEGQRCVVILPDSVRNYMSKFLSD 385
Cdd:PLN00011 234 PFNLDLTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAkRPENAGKLIVVIFPSGGERYLSTKLFE 311
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
73-380 |
4.20e-67 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 223.89 E-value: 4.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 73 ILPDILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTI-IEPTSGNTGIGL 151
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAK--GCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPL 227
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 228 AHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDF 307
Cdd:PLN03013 264 IHYETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGF 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450071 308 IPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 380
Cdd:PLN03013 339 IPKNLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIY 411
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
56-386 |
3.38e-66 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 219.45 E-value: 3.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 56 AMADSPHYHTVLTKSPKILP------DILRKIGNTPMVRINKISKNAGLKceLLAKCEFFNAGGSVKDRISLRMIEDAER 129
Cdd:PLN02556 26 STVGSPSFAQRLRDLPKDLPgtkiktDASQLIGKTPLVYLNKVTEGCGAY--IAAKQEMFQPTSSIKDRPALAMIEDAEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 130 AGNLKPGDT-IIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNARFDSpeshVGVAWRL 207
Cdd:PLN02556 104 KNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTdPTKGMGGT----VKKAYEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 208 KNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEP 287
Cdd:PLN02556 180 LESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP-----AES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 288 EELNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQ-EGQR 366
Cdd:PLN02556 255 NVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPEnKGKL 334
|
330 340
....*....|....*....|
gi 21450071 367 CVVILPDSVRNYMSKFLSDK 386
Cdd:PLN02556 335 IVTVHPSFGERYLSSVLFQE 354
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
77-393 |
1.73e-59 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 203.30 E-value: 1.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 77 ILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:PLN02356 47 LIDAIGNTPLIRINSLSEATG--CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNarFDSPESHVGVAWRL---KNEIP-----------------NSH 215
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVrPVS--ITHKDHYVNIARRRaleANELAskrrkgsetdgihlektNGC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 216 IL-------------------DQYRNASNPLAHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIG 276
Cdd:PLN02356 203 ISeeekenslfsssctggffaDQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 277 VDPEGSIL--------------AEPEELNQTEQTAyeVEGIGYDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLL 342
Cdd:PLN02356 283 IDPPGSGLfnkvtrgvmytreeAEGRRLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLF 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 21450071 343 CGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSKFLSDKWMLQKGF 393
Cdd:PLN02356 361 VGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
408-552 |
6.11e-50 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 168.09 E-value: 6.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIH 487
Cdd:cd04608 2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21450071 488 LTDTLGTLSHILEMDHFALVVHEqiqsrdqawsgvvggptdcsngmsskQQMVFGVVTAIDLLNF 552
Cdd:cd04608 82 LDTPLGALSRILERDHFALVVDG--------------------------QGKVLGIVTRIDLLNY 120
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
84-371 |
2.34e-28 |
|
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: 114.89 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMI----EDAERAGnlkpgdtIIEPTSGNTGIGLALAAAVKG 159
Cdd:cd01562 18 TPLLTSPTLSELLG--AEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 160 YRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHVgvawrlkneipnsHILDQYRNAsnPLAH-YDD------ 232
Cdd:cd01562 89 IPATIVMPETAPAAKVDATRAYGAEVVL--YGEDFDEAEAKA-------------RELAEEEGL--TFIHpFDDpdviag 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 233 ---TAEEILQQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA-EPEELNQTEQTAyevEG 302
Cdd:cd01562 152 qgtIGLEILEQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTIA---DG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21450071 303 IGydfIPTVLD------RAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAvAVKAARELQEGQRCVVIL 371
Cdd:cd01562 228 LA---VKRPGEltfeiiRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
84-371 |
8.43e-27 |
|
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: 110.90 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDR------ISLRmieDAERAGnlkpgdTIIEPTSGNTGIGLALAAAV 157
Cdd:COG1171 25 TPLLRSPTLSERLG--AEVYLKLENLQPTGSFKLRgaynalASLS---EEERAR------GVVAASAGNHAQGVAYAARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 158 KGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNEipnshildqyRNASnpLAH-YDDT--- 233
Cdd:COG1171 94 LGIPATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAA---AAELAEE----------EGAT--FVHpFDDPdvi 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 234 ------AEEILQQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA-EPEELNQTeQTAyeV 300
Cdd:COG1171 157 agqgtiALEILEQL-PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTI--A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 301 EGIG--------YDFIPTVLDRAV-VdkwfksnDEDSFAFA-RMLIAQEGLLCGGSSGSAMAvAVKAARELQEGQRCVVI 370
Cdd:COG1171 233 DGLAvgrpgeltFEILRDLVDDIVtV-------SEDEIAAAmRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVV 304
|
.
gi 21450071 371 L 371
Cdd:COG1171 305 L 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
84-371 |
2.68e-25 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 106.70 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERagnlKPGdtIIEPTSGNTGIGLALAAAVKGY 160
Cdd:PRK06815 21 TPLEHSPLLSQHTG--CEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 161 RCIIVMPEKMSMEKVDVLRALGAEIVRTPTNArfdspeshvgvawrLKNEI-PNSHILDQYRNASNPlahYDD------- 232
Cdd:PRK06815 93 PVTVYAPEQASAIKLDAIRALGAEVRLYGGDA--------------LNAELaARRAAEQQGKVYISP---YNDpqviagq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 233 --TAEEILQQCDgKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA----EPEELNQ-TEQTAYE 299
Cdd:PRK06815 156 gtIGMELVEQQP-DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTlSDGTAGG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21450071 300 VEGigyDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQeGQRCVVIL 371
Cdd:PRK06815 235 VEP---GAITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
82-371 |
1.80e-20 |
|
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: 92.66 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 82 GNTPMVRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd01563 21 GNTPLVRAPRLGERLGGK-NLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLAH--YDDTAEEILQ 239
Cdd:cd01563 96 CVVFLPAGKALGKLAQALAYGATVLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYRLegQKTIAFEIAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 240 QCDGKL-DMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEGS-----------ILAEPEELNQTEQTAYE 299
Cdd:cd01563 166 QLGWEVpDYVVVPVGNGGNITAIWKGFKElkelglidRLP--RMVGVQAEGAapivrafkegkDDIEPVENPETIATAIR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 300 vegIGYdfiPtVLDRAVVDKWFKSN------DEDSFAFARMLIAQ-EGLLCGGSSGSAMAVAVKAARE--LQEGQRCVVI 370
Cdd:cd01563 244 ---IGN---P-ASGPKALRAVRESGgtavavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiIDKGERVVVV 316
|
.
gi 21450071 371 L 371
Cdd:cd01563 317 L 317
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
43-378 |
1.83e-15 |
|
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: 78.32 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 43 PDTPSRCTWQLGRAMADSPHYHTVLtkspkiLPDILRKI-----GNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKD 117
Cdd:COG0498 27 PDSYPALSREDLASRRGLWRYRELL------PFDDEEKAvslgeGGTPLVKAPRLADELG--KNLYVKEEGHNPTGSFKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 118 R-----ISLrmiedAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPE-KMSMEKVDVLRALGAEIVRTPTN 191
Cdd:COG0498 99 RamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQLAQMLTYGAHVIAVDGN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 192 arFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPL-------AHYddtaeEILQQCDGKLDMLVASAGTGGTITGI-- 261
Cdd:COG0498 170 --FD-------DAQRLVKELAADEGL--YaVNSINPArlegqktYAF-----EIAEQLGRVPDWVVVPTGNGGNILAGyk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 262 ARK------LKEKCPgcKIIGVDPEGS--ILAEPEelnqTEQTAYEVEG---------IGydfIPTVLDRAVVD-----K 319
Cdd:COG0498 234 AFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPERpetiapsmdIG---NPSNGERALFAlresgG 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21450071 320 WF-KSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARE--LQEGQRCVVIL-------PDSVRNY 378
Cdd:COG0498 305 TAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVVVLStghglkfPDAVREA 373
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
82-371 |
2.81e-15 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 77.05 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 82 GNTPMVRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:PRK06381 14 GGTPLLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 162 CIIVMPEKMSMEKVDVLRALGAEIVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDDTAEEIL 238
Cdd:PRK06381 89 AVIFIPRSYSNSRVKEMEKYGAEIIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAYEIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 239 QQCDGKLDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEGS--------------ILAEPEELNQTEQT 296
Cdd:PRK06381 161 EALGDVPDAVAVPVGNGTTLAGIYHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRETAVN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21450071 297 AYEVEGIGYDFIPTVldRAVVD---KWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVIL 371
Cdd:PRK06381 239 EPLVSYRSFDGDNAL--EAIYDshgYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| PLN02970 |
PLN02970 |
serine racemase |
84-282 |
1.62e-14 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 74.71 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKNAGLKCELlaKCEFFNAGGSVKDRISLRMI-----EDAERAgnlkpgdtIIEPTSGNTGIGLALAAAVK 158
Cdd:PLN02970 28 TPVLTSSSLDALAGRSLFF--KCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 159 GYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDDTAEEI 237
Cdd:PLN02970 98 GIPAYIVVPKNAPACKVDAVIRYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21450071 238 LQQCDGkLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 282
Cdd:PLN02970 170 LEQVPE-LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
95-280 |
2.77e-13 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 70.82 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 95 NAGLKCELLAKCEFFNAGGSVKDRIS----LRMIEDAERAGnlkpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKM 170
Cdd:PRK07048 34 DARTGAQVFFKCENFQRMGAFKFRGAynalSQFSPEQRRAG-------VVTFSSGNHAQAIALSARLLGIPATIVMPQDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 171 SMEKVDVLRALGAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------DTAEEIL 238
Cdd:PRK07048 107 PAAKVAATRGYGGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21450071 239 QQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE 280
Cdd:PRK07048 168 EEV-GPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
145-282 |
4.07e-12 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 68.63 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 145 GNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 219
Cdd:PRK09224 77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21450071 220 yrnasnPlahYDDT---------AEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 282
Cdd:PRK09224 145 ------P---FDDPdviagqgtiAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
101-282 |
1.02e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 66.13 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 101 ELLAKCEFFNAGGSVKDRISL-RMIedaeraGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLR 179
Cdd:PRK08246 38 PVWLKLEHLQHTGSFKARGAFnRLL------AAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 180 ALGAEIVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDDTAEEILQQCdGKLDMLVASAGT 254
Cdd:PRK08246 112 ALGAEVVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGG 178
|
170 180
....*....|....*....|....*...
gi 21450071 255 GGTITGIARKLKekcPGCKIIGVDPEGS 282
Cdd:PRK08246 179 GGLIAGIAAWFE---GRARVVAVEPEGA 203
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
77-279 |
1.71e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 65.56 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 77 ILRKIGNTPMVriNKISKNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGnlKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:PRK06608 17 IKQYLHLTPIV--HSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDDT 233
Cdd:PRK06608 93 LFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21450071 234 AEEILQQCDGKLDMLVASAGTGGTITG--IARKLKEkcPGCKIIGVDP 279
Cdd:PRK06608 161 CYEALQQLGFSPDAIFASCGGGGLISGtyLAKELIS--PTSLLIGSEP 206
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
139-282 |
1.89e-11 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 66.36 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 139 IIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNEIPNSHIld 218
Cdd:PRK12483 88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVL--HGESFPDALAH---ALKLAEEEGLTFV-- 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450071 219 qyrnasNPlahYDD---------TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 282
Cdd:PRK12483 161 ------PP---FDDpdviagqgtVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
82-278 |
3.32e-11 |
|
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: 64.71 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 82 GNTPMVRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:TIGR00260 21 GVTPLFRAPALAANVGIK-NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 162 CIIVMPE-KMSMEKVDVLRALGAEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnshildqYRNASNPLAHYdd 232
Cdd:TIGR00260 96 VVVLYPAgKISLGKLAQALGYNAEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-------YRLEGQKTYAF-- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21450071 233 taeEILQQCDGKL-DMLVASAGTGGTITGIARKLKEKcpgcKIIGVD 278
Cdd:TIGR00260 165 ---EAVEQLGWEApDKVVVPVPNSGNFGAIWKGFKEK----KMLGLD 204
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
77-280 |
9.23e-11 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 63.22 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 77 ILRKIGNTPMVRINKISKNAglKCELLAKCEFFNAGGSVKDRIS---LRMIEDAERAGNlkpgdtIIEPTSGNTGIGLAL 153
Cdd:PRK08638 21 LAGRIRKTPLPRSNYLSERC--KGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKRKG------VVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 154 AAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILDQYrNASNPLAHYDDT 233
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIPPY-DDPKVIAGQGTI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21450071 234 AEEILQQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE 280
Cdd:PRK08638 166 GLEILEDL-WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
72-280 |
6.99e-09 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 57.82 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 72 KILPDILRKI----GNTPMVRINKISknaglkcellAKCEFFNAGGSVKDRISLRMIED-AERAGNlkpgdTIIEPTSGN 146
Cdd:PRK06450 43 KNFPYIKHFIslgeGRTPLIKKGNIW----------FKLDFLNPTGSYKDRGSVTLISYlAEKGIK-----QISEDSSGN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 147 TGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYR 221
Cdd:PRK06450 108 AGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFR 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 222 NASNPLAHyddtaeEILQQCDGKLD---MLVASAGTggTITGIARKLK--------EKCPgcKIIGVDPE 280
Cdd:PRK06450 178 DGIRTLAY------EIAKDLDWKIPnyvFIPVSAGT--LLLGVYSGFKhlldsgviSEMP--KIVAVQTE 237
|
|
| CBS |
smart00116 |
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
418-465 |
7.49e-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: 51.74 E-value: 7.49e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 21450071 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:smart00116 2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
83-282 |
1.09e-08 |
|
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: 56.92 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 83 NTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDR-ISLRMIEDAERAGNLKPGdtIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd06448 1 KTPLIESTALSKTAG--CNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDDTAEEILQ 239
Cdd:cd06448 77 CTIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21450071 240 QC--DGKLDMLVASAGTGGTITGIARKLkEKCPGCK--IIGVDPEGS 282
Cdd:cd06448 150 QLqsQEKVDAIVCSVGGGGLLNGIVQGL-ERNGWGDipVVAVETEGA 195
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
83-303 |
6.56e-08 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 54.90 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 83 NTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERAGNlkpgdtIIEPTSGNTGIGLALAAAVKG 159
Cdd:PRK07334 23 RTPCVHSRTLSQITG--AEVWLKFENLQFTASFKERGAlnkLLLLTEEERARG------VIAMSAGNHAQGVAYHAQRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 160 YRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNEipnshildQYRNASNPlahYDD------- 232
Cdd:PRK07334 95 IPATIVMPRFTPTVKVERTRGFGAEVVL--HGETLDEARAH---ARELAEE--------EGLTFVHP---YDDpaviagq 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21450071 233 --TAEEILQQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG--SILAEPEELNQTEQTAYEVEGI 303
Cdd:PRK07334 159 gtVALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELypSMYAAIKGVALPCGGSTIAEGI 232
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
95-186 |
1.07e-07 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 53.84 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 95 NAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEK 174
Cdd:PRK06110 31 AERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEK 108
|
90
....*....|..
gi 21450071 175 VDVLRALGAEIV 186
Cdd:PRK06110 109 NAAMRALGAELI 120
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
72-374 |
1.57e-07 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 54.05 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 72 KILPDILRKI----GNTPMVRiNKISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNT 147
Cdd:PRK05638 51 ELLPQVKKIIslgeGGTPLIR-ARISEKLGE--NVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 148 GIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnas 224
Cdd:PRK05638 124 AASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 225 npLAHYDDTAEEILQQCDGklDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPE------GSILAEPEEL 290
Cdd:PRK05638 196 --LEGQKTIAFELWEEINP--THVIVPTGSGSYLYSIYKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKC 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 291 NQTEQTA-YEVEGIGYDFIPTVLDR----AVVdkwfksNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARE--LQE 363
Cdd:PRK05638 270 NETKALGlYVKNPVMKEYVSEAIKEsggtAVV------VNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEK 343
|
330
....*....|.
gi 21450071 364 GQRCVVILPDS 374
Cdd:PRK05638 344 GDKVVLVVTGS 354
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
418-511 |
2.95e-07 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 49.17 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIHLTDTLGT-LS 496
Cdd:cd02205 4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEaLE 83
|
90
....*....|....*.
gi 21450071 497 HILEMD-HFALVVHEQ 511
Cdd:cd02205 84 LMLEHGiRRLPVVDDD 99
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
84-191 |
4.87e-07 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 52.19 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKNAGLKcELLAKCE---F----FNA-GGS------VKDRISLRMIE---DAERAGNLKP--GD-TIIEPT 143
Cdd:PRK08206 45 TPLVALPDLAAELGVG-SILVKDEsyrFglnaFKAlGGAyavarlLAEKLGLDISElsfEELTSGEVREklGDiTFATAT 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 21450071 144 SGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTN 191
Cdd:PRK08206 124 DGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN 171
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
84-279 |
9.01e-07 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 51.85 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKNAGLKceLLAKCEFFNAGGSVKDRISLRMIEDAERAgNLKPGdtIIEPTSGNTGIGLALAAAVKGYRCI 163
Cdd:PLN02550 110 SPLQLAKKLSERLGVK--VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 164 IVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYDDTA------EEI 237
Cdd:PLN02550 185 IAMPVTTPEIKWQSVERLGATVVLVGDS--YDEAQAYA-----------KQRALEEGRTFIPPFDHPDVIAgqgtvgMEI 251
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21450071 238 LQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDP 279
Cdd:PLN02550 252 VRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEP 293
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
410-465 |
9.48e-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: 46.05 E-value: 9.48e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21450071 410 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:pfam00571 1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
234-281 |
1.04e-06 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 51.35 E-value: 1.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 21450071 234 AEEILQQCD--GKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG 281
Cdd:PRK08639 167 AVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
408-473 |
1.41e-06 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 47.55 E-value: 1.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450071 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSD 473
Cdd:COG0517 1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLD 66
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
126-342 |
2.13e-06 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 49.83 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 126 DAERAGnlkpGDTIIepTSGntGIG-----LALAAAVK-GYRCIIVMPEKMSMEKVDVL--------RALGAEIVRTPTN 191
Cdd:PRK03910 58 DALAQG----ADTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 192 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDDTAEEILQQCDG---KLDMLVASAGTGGTITG 260
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 261 IARKLKEKCPGCKIIGVdpegSILAEPEElnQTEQTAYEVEGI-GYDFIPTVLDRAVV---DKWF-----KSNDEDsFAF 331
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV----TVSRSAAE--QEPKVAKLAQATaELLGLPTEIPRADIrlwDDYVgpgygVPTDEM-LEA 272
|
250
....*....|.
gi 21450071 332 ARMLIAQEGLL 342
Cdd:PRK03910 273 VKLLARTEGIL 283
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
407-500 |
5.77e-06 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 47.57 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 407 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNEsGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPI 486
Cdd:COG2524 85 KMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTV 163
|
90
....*....|....
gi 21450071 487 HLTDTLGTLSHILE 500
Cdd:COG2524 164 SEDDSLEEALRLML 177
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
84-342 |
1.21e-05 |
|
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: 47.42 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKNAGLKCELLAKCEFFN---AGGSVKDRISLRMIEDAERAGnlkpGDTIIepTSG----NTGIGLALAAA 156
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVEIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKG----ADTLV--TVGgiqsNHTRQVAAVAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 157 VKGYRCIIVM--PEKMSMEKVD------VLRALGAEIvrtptnaRFDSPESHVGV-------AWRLKNE------IPNSh 215
Cdd:cd06449 75 KLGLKCVLVQenWVPYSDAVYDrvgnilLSRIMGADV-------RLVSAGFDIGIrksfeeaAEEVEAKggkpyvIPAG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 216 ildqyrNASNPLAH--YDDTAEEILQQCDG---KLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEEL 290
Cdd:cd06449 147 ------GSEHPLGGlgYVGFVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQV 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 21450071 291 NQTEQTAYEVEGIGYdfipTVLDRAVVDKWF-----KSNDEDSFAFaRMLIAQEGLL 342
Cdd:cd06449 221 LRIAQAKLAEEGLEV----KEEDVVLDDDYAapeygIPNDETIEAI-KLCARLEGII 272
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
405-465 |
1.48e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 44.47 E-value: 1.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21450071 405 WWRLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG0517 64 LLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
84-371 |
2.04e-05 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 46.88 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 84 TPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMI---EDAERAGNlkpgdtIIEPTSGNTGIGLALAAAVKGY 160
Cdd:PRK07476 20 TPLVASASLSARAG--VPVWLKLETLQPTGSFKLRGATNALlslSAQERARG------VVTASTGNHGRALAYAARALGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 161 RCIIVMPEKMSMEKVDVLRALGAEIVRTPtnarfDSPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYDDTAE 235
Cdd:PRK07476 92 RATICMSRLVPANKVDAIRALGAEVRIVG-----RSQDDAQAEVERLVREegltmVP-------------PFDDPRIIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 236 ------EILQQCDgKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE-GSILAEPEELNQTEQTAyEVE------- 301
Cdd:PRK07476 154 qgtiglEILEALP-DVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMErGAAMHASLAAGRPVQVE-EVPtladslg 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450071 302 -GIGYDFIPTV-LDRAVVDKWFKSnDEDSFAFA-RMLIAQEGLLCGGSSGSAMAvAVKAARELQEGQRCVVIL 371
Cdd:PRK07476 232 gGIGLDNRYTFaMCRALLDDVVLL-DEAEIAAGiRHAYREERLVVEGAGAVGIA-ALLAGKIAARDGPIVVVV 302
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
410-473 |
5.50e-05 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 42.89 E-value: 5.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21450071 410 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSD 473
Cdd:COG2905 1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLD 64
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
418-499 |
6.18e-05 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 42.93 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDE------VCKVLYKQFKPIHLTDT 491
Cdd:COG3448 12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEErlldlpVEDVMTRPVVTVTPDTP 91
|
....*...
gi 21450071 492 LGTLSHIL 499
Cdd:COG3448 92 LEEAAELM 99
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
41-187 |
6.24e-05 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 45.38 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 41 IRPDTPSRCTWQLGRamadsphYHTVLtksPKILPDILRKIGN--TPMVRINKISKNAGLKcELLAKCEFFNAGGSVKDR 118
Cdd:PRK08197 45 VTREALAGRPANLWR-------YHELL---PVRDPEHIVSLGEgmTPLLPLPRLGKALGIG-RLWVKDEGLNPTGSFKAR 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21450071 119 ISLRMIEDAERAGnLKpgdTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVR 187
Cdd:PRK08197 114 GLAVGVSRAKELG-VK---HLAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELYL 178
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
71-281 |
8.89e-05 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 44.82 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 71 PKILPDIlrkignTPMVRINKisknaglkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIG 150
Cdd:PRK08329 58 PHLTPPI------TPTVKRSI---------KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 151 LALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRNASNPLA 228
Cdd:PRK08329 119 LALYSLSEGIKVHVFVSYNASKEKISLLSRLGAEL----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYFLEGTKTI 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21450071 229 HYddtaeEILQQCdGKLDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEG 281
Cdd:PRK08329 195 AY-----EIYEQI-GVPDYAFVPVGSGTLFLGIWKGFKElhemgeisKMP--KLVAVQAEG 247
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
122-188 |
1.34e-04 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 44.13 E-value: 1.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 122 RMIEDAeraGNLKPGDTIIEpTSGNTGIGLALA--AAVKGYRCIIVMPEKMSMEK-VDVLRALGAEIVRT 188
Cdd:cd08290 136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
407-465 |
3.37e-04 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 41.00 E-value: 3.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 21450071 407 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG3448 72 DLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
55-276 |
4.51e-04 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 42.88 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 55 RAMADS-------PHYHTVLTKSPKILP-----DILRKI-GNTPMVRINKISKNAGLKCELLAKCEFFNAGGSVKDRISL 121
Cdd:PLN02569 92 RALFDSrvgkttwPYGSGVWSKKEWVLPeidddDIVSLFeGNSNLFWAERLGKEFLGMNDLWVKHCGISHTGSFKDLGMT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 122 RMIEDAERAGNL-KPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPE-KMSMEKVDVLRALGAEIVRTPTNarFDSPES 199
Cdd:PLN02569 172 VLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPAdKISIAQLVQPIANGALVLSIDTD--FDGCMR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 200 HVGvawRLKNEIP----NShiLDQYRnasnpLAHYDDTAEEILQQCDGKL-DMLVASAGTGGTITGIARKLKEkcpgCKI 274
Cdd:PLN02569 250 LIR---EVTAELPiylaNS--LNSLR-----LEGQKTAAIEILQQFDWEVpDWVIVPGGNLGNIYAFYKGFKM----CKE 315
|
..
gi 21450071 275 IG 276
Cdd:PLN02569 316 LG 317
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
407-465 |
5.21e-04 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 42.90 E-value: 5.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 21450071 407 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:PRK14869 67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
408-464 |
5.42e-04 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 41.41 E-value: 5.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 21450071 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSL 464
Cdd:COG2524 150 APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
418-511 |
6.28e-04 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 40.28 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450071 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLssllagKVRPSDEVCKVLYKQFKPIHLTDTLGTLSH 497
Cdd:COG4109 27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVTPDTSLASAAH 100
|
90
....*....|....*.
gi 21450071 498 ILEMDHFAL--VVHEQ 511
Cdd:COG4109 101 KMIWEGIELlpVVDDD 116
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
408-465 |
7.02e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 39.81 E-value: 7.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 21450071 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNEsGAILGMVTLGNMLSSLL 465
Cdd:COG2905 65 TPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
408-461 |
7.31e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 39.54 E-value: 7.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 21450071 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNML 461
Cdd:cd02205 59 TPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
408-465 |
1.75e-03 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 38.74 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 21450071 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG4109 76 TPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
|
|
| CBS_pair_IMPDH |
cd04601 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
418-456 |
2.11e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 38.16 E-value: 2.11e-03
10 20 30
....*....|....*....|....*....|....*....
gi 21450071 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVT 456
Cdd:cd04601 4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT 42
|
|
| CBS_pair_plant_CBSX |
cd17789 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ... |
410-461 |
3.13e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341425 [Multi-domain] Cd Length: 141 Bit Score: 38.22 E-value: 3.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 21450071 410 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNML 461
Cdd:cd17789 88 VGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVV 139
|
|
| CBS_pair_ParBc_assoc |
cd04610 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ... |
420-461 |
8.68e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 36.14 E-value: 8.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 21450071 420 TVLPTVTCEDTIAILREKGFDQAPVVnESGAILGMVTLGNML 461
Cdd:cd04610 7 TVSPDDTVKDVIKLIKETGHDGFPVV-DDGKVVGYVTAKDLL 47
|
|
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