|
Name |
Accession |
Description |
Interval |
E-value |
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
73-540 |
0e+00 |
|
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273464 [Multi-domain] Cd Length: 455 Bit Score: 778.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 73 ILPDILRKIGNTPMVRINRISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLA 152
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 153 LAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDD 232
Cdd:TIGR01137 79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 233 TAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEELNQTEQTAYEVEGIGYDFIPTVL 312
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 313 DRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQ-ELKEGQRCVVILPDSVRNYMSKFLSDKWMLQK 391
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 392 GFMKEE-LSVKRPWWWHLRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVR 470
Cdd:TIGR01137 319 GFLDDEdLTVKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 471 PSDEVCKVLYKQFKPIHLTDTLGMLSHILEMDHFALVVHEQIQyrnngvsskqlmvFGVVTAIDLLNFVA 540
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKP-------------IGVVTKIDLLSFLA 455
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
82-380 |
1.83e-166 |
|
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: 473.54 E-value: 1.83e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 82 GNTPMVRINRISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd01561 1 GNTPLVRLNRLSP--GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQC 241
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 242 DGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRAVVDRWF 321
Cdd:cd01561 158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 158186659 322 KSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVILPDSVRNYMS 380
Cdd:cd01561 233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
72-381 |
4.43e-162 |
|
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: 462.60 E-value: 4.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 72 KILPDILRKIGNTPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGL 151
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPG--AEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYD 231
Cdd:COG0031 80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 232 DTAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTV 311
Cdd:COG0031 157 TTGPEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 312 LDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVILPDSVRNYMSK 381
Cdd:COG0031 232 LDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
71-393 |
6.43e-118 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 351.47 E-value: 6.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 71 PKILPDILRKIGNTPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIG 150
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 151 LALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASN 225
Cdd:PRK10717 79 LALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 226 PLAHYDDTAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEV----- 300
Cdd:PRK10717 158 REAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAL-----YSYYKTGELKAegssi 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 301 -EGIGYDFIPTVLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVILPDSVRNYM 379
Cdd:PRK10717 233 tEGIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQ 312
|
330
....*....|....
gi 158186659 380 SKFLSDKWMLQKGF 393
Cdd:PRK10717 313 SKLFNPDFLREKGL 326
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
77-380 |
1.43e-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: 338.96 E-value: 1.43e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 77 ILRKIGNTPMVRINRISKNAGlkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01139 1 ISELIGNTPLVRLNRIEGCNA---NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDDTAE 235
Cdd:TIGR01139 78 ARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 236 EILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRA 315
Cdd:TIGR01139 155 EIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158186659 316 VVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVILPDSVRNYMS 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 |
3.85e-110 |
|
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: 330.40 E-value: 3.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 77 ILRKIGNTPMVRINRISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAP--GCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDD 232
Cdd:TIGR01136 79 ARGYKLILTMPETMSLERRKLLRAYGAELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 233 TAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPTVL 312
Cdd:TIGR01136 152 TGPEIWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKIL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158186659 313 DRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELK-EGQRCVVILPDSVRNYMS 380
Cdd:TIGR01136 227 DLSLIDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
75-380 |
3.30e-84 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 263.66 E-value: 3.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 75 PDILRKIGNTPMVRINRISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLALA 154
Cdd:PRK11761 4 PTLEDTIGNTPLVKLQRLPPDRGN--TILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 155 AAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDDTA 234
Cdd:PRK11761 82 AAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 235 EEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDP-EGS----ILAEPEElnqteqtayevegigydFIP 309
Cdd:PRK11761 158 PEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158186659 310 TVLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELkEGQRCVVILPDSVRNYMS 380
Cdd:PRK11761 221 KIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLS 290
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
84-374 |
7.69e-83 |
|
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: 258.21 E-value: 7.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 84 TPMVRINRISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLkPGDTIIEPTSGNTGIGLALAAAVKGYRCI 163
Cdd:cd00640 1 TPLVRLKRLSK--LGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 164 IVMPEKMSMEKVDVLRALGAEIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdDTAEEILQQCDG 243
Cdd:cd00640 78 IVMPEGASPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 244 -KVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEgsilaepeelnqteqtAYEVegigydfiptvldravvdrwfk 322
Cdd:cd00640 152 qKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE----------------VVTV---------------------- 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 158186659 323 sNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVILPDS 374
Cdd:cd00640 194 -SDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
77-373 |
1.30e-82 |
|
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: 259.55 E-value: 1.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 77 ILRKIGNTPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAgtlKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdDTAEE 236
Cdd:pfam00291 76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 237 ILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS-ILAEPEELNQTEQTA---YEVEGIGYDFIPTVL 312
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGAL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158186659 313 DRAVVDRWFKS----NDDDSFAFARMLISQEGLLCGGSSGSAMAVA-VKAAQELKEGQRCVVILPD 373
Cdd:pfam00291 230 ALDLLDEYVGEvvtvSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
73-385 |
7.68e-79 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 250.61 E-value: 7.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 73 ILPDILRKIGNTPMVRINRISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTI-IEPTSGNTGIGL 151
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVD--GCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHY 230
Cdd:PLN02565 83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 231 DDTAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPT 310
Cdd:PLN02565 159 ETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158186659 311 VLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELK-EGQRCVVILPDSVRNYMSKFLSD 385
Cdd:PLN02565 234 VLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
77-387 |
3.00e-78 |
|
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: 248.27 E-value: 3.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 77 ILRKIGNTPMVRINRIskNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR03945 1 ILSLIGNTPLVKLERL--FPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLA 228
Cdd:TIGR03945 79 YKGLRFICVVDPNISPQNLKLLRAYGAEVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 229 HYDDTAEEILQQCDgKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSIL--AEPeelnqteqTAYEVEGIGYD 306
Cdd:TIGR03945 152 HYHGTGREIARAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGAS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 307 FIPTVLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVILPDSVRNYMSKFLSDK 386
Cdd:TIGR03945 223 VVPELLDESLIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDE 302
|
.
gi 158186659 387 W 387
Cdd:TIGR03945 303 W 303
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
77-380 |
1.42e-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: 233.27 E-value: 1.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 77 ILRKIGNTPMVRINRISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGS--EVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDDTAEE 236
Cdd:TIGR01138 80 LKGYRMKLLMPDNMSQERKAAMRAYGAELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 237 ILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEgsilaEPeelnqteqtaYEVEGIGY---DFIPTVLD 313
Cdd:TIGR01138 156 IWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFD 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158186659 314 RAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQrCVVILPDSVRNYMS 380
Cdd:TIGR01138 221 ASLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
76-385 |
2.36e-69 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 226.04 E-value: 2.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 76 DILRKIGNTPMVRINRISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPG-DTIIEPTSGNTGIGLALA 154
Cdd:PLN00011 10 DVTELIGNTPMVYLNNIVD--GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 155 AAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLA 228
Cdd:PLN00011 88 GAARGYKVILVMPSTMSLERRIILRALGAEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 229 HYDDTAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFI 308
Cdd:PLN00011 159 HYRTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGII 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158186659 309 PTVLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKE-GQRCVVILPDSVRNYMSKFLSD 385
Cdd:PLN00011 234 PFNLDLTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYLSTKLFE 311
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
73-380 |
1.39e-66 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 221.96 E-value: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 73 ILPDILRKIGNTPMVRINRISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTI-IEPTSGNTGIGL 151
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAK--GCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPL 227
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 228 AHYDDTAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDF 307
Cdd:PLN03013 264 IHYETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGF 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158186659 308 IPTVLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVILPDSVRNYMS 380
Cdd:PLN03013 339 IPKNLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIY 411
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
56-386 |
3.39e-65 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 216.36 E-value: 3.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 56 PMADSPHYHTVPTKSPKILP------DILRKIGNTPMVRINRISKNAGLKceLLAKCEFFNAGGSVKDRISLRMIEDAER 129
Cdd:PLN02556 26 STVGSPSFAQRLRDLPKDLPgtkiktDASQLIGKTPLVYLNKVTEGCGAY--IAAKQEMFQPTSSIKDRPALAMIEDAEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 130 AGTLKPGDT-IIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNARFDSpeshVGVAWRL 207
Cdd:PLN02556 104 KNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTdPTKGMGGT----VKKAYEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 208 KNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEP 287
Cdd:PLN02556 180 LESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP-----AES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 288 EELNQTEQTAYEVEGIGYDFIPTVLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELK-EGQR 366
Cdd:PLN02556 255 NVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPEnKGKL 334
|
330 340
....*....|....*....|
gi 158186659 367 CVVILPDSVRNYMSKFLSDK 386
Cdd:PLN02556 335 IVTVHPSFGERYLSSVLFQE 354
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
77-393 |
1.17e-59 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 203.68 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 77 ILRKIGNTPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:PLN02356 47 LIDAIGNTPLIRINSLSEATG--CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNarFDSPESHVGVAWRL---KNEIP-----------------NSH 215
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVrPVS--ITHKDHYVNIARRRaleANELAskrrkgsetdgihlektNGC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 216 IL-------------------DQYRNASNPLAHYDDTAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIG 276
Cdd:PLN02356 203 ISeeekenslfsssctggffaDQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 277 VDPEGSIL--------------AEPEELNQTEQTAyeVEGIGYDFIPTVLDRAVVDRWFKSNDDDSFAFARMLISQEGLL 342
Cdd:PLN02356 283 IDPPGSGLfnkvtrgvmytreeAEGRRLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLF 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 158186659 343 CGGSSGSAMAVAVKAAQELKEGQRCVVILPDSVRNYMSKFLSDKWMLQKGF 393
Cdd:PLN02356 361 VGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
408-538 |
2.55e-51 |
|
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: 171.18 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 408 LRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIH 487
Cdd:cd04608 2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 158186659 488 LTDTLGMLSHILEMDHFALVVHEqiqyrnngvsskQLMVFGVVTAIDLLNF 538
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 |
7.56e-29 |
|
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: 116.05 E-value: 7.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 84 TPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDRISLRMI----EDAERAGtlkpgdtIIEPTSGNTGIGLALAAAVKG 159
Cdd:cd01562 18 TPLLTSPTLSELLG--AEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 160 YRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHVgvawrlkneipnsHILDQYRNAsnPLAH-YDD------ 232
Cdd:cd01562 89 IPATIVMPETAPAAKVDATRAYGAEVVL--YGEDFDEAEAKA-------------RELAEEEGL--TFIHpFDDpdviag 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 233 ---TAEEILQQCdGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA-EPEELNQTEQTAyevEG 302
Cdd:cd01562 152 qgtIGLEILEQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTIA---DG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158186659 303 IGydfIPTVLD------RAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAvAVKAAQELKEGQRCVVIL 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 |
1.40e-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: 110.13 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 84 TPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDR------ISLRmieDAERAGTlkpgdtIIEPTSGNTGIGLALAAAV 157
Cdd:COG1171 25 TPLLRSPTLSERLG--AEVYLKLENLQPTGSFKLRgaynalASLS---EEERARG------VVAASAGNHAQGVAYAARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 158 KGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNEipnshildqyRNASnpLAH-YDDT--- 233
Cdd:COG1171 94 LGIPATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAA---AAELAEE----------EGAT--FVHpFDDPdvi 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 234 ------AEEILQQCdGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA-EPEELNQTeQTAyeV 300
Cdd:COG1171 157 agqgtiALEILEQL-PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTI--A 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158186659 301 EGIG--------YDFIptvldRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKeGQRCVVIL 371
Cdd:COG1171 233 DGLAvgrpgeltFEIL-----RDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLK-GKRVVVVL 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
84-371 |
4.25e-25 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 105.93 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 84 TPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERagtlKPGdtIIEPTSGNTGIGLALAAAVKGY 160
Cdd:PRK06815 21 TPLEHSPLLSQHTG--CEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 161 RCIIVMPEKMSMEKVDVLRALGAEIVRTPTNArfdspeshvgvawrLKNEI-PNSHILDQYRNASNPlahYDD------- 232
Cdd:PRK06815 93 PVTVYAPEQASAIKLDAIRALGAEVRLYGGDA--------------LNAELaARRAAEQQGKVYISP---YNDpqviagq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 233 --TAEEILQQCDGKVDMLVASAGtGGTITGIARKLKEKCPGCKIIGVDPEG------SILA----EPEELNQ-TEQTAYE 299
Cdd:PRK06815 156 gtIGMELVEQQPDLDAVFVAVGG-GGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTlSDGTAGG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158186659 300 VEGigyDFIPTVLDRAVVDRWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKeGQRCVVIL 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 |
3.23e-21 |
|
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: 94.58 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 82 GNTPMVRINRISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGTlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd01563 21 GNTPLVRAPRLGERLGGK-NLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLAH--YDDTAEEILQ 239
Cdd:cd01563 96 CVVFLPAGKALGKLAQALAYGATVLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYRLegQKTIAFEIAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 240 QCDGKV-DMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEGS-----------ILAEPEELNQTEQTAYE 299
Cdd:cd01563 166 QLGWEVpDYVVVPVGNGGNITAIWKGFKElkelglidRLP--RMVGVQAEGAapivrafkegkDDIEPVENPETIATAIR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 300 vegIGYdfiPtVLDRAVVDRWFKSN------DDDSFAFA-RMLISQEGLLCGGSSGSAMAVAVKAAQE--LKEGQRCVVI 370
Cdd:cd01563 244 ---IGN---P-ASGPKALRAVRESGgtavavSDEEILEAqKLLARTEGIFVEPASAASLAGLKKLREEgiIDKGERVVVV 316
|
.
gi 158186659 371 L 371
Cdd:cd01563 317 L 317
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
82-378 |
4.87e-16 |
|
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: 80.24 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 82 GNTPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDR-----ISLrmiedAERAGTlkpgDTIIEPTSGNTGIGLALAAA 156
Cdd:COG0498 65 GGTPLVKAPRLADELG--KNLYVKEEGHNPTGSFKDRamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVMPE-KMSMEKVDVLRALGAEIVRTPTNarFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPL------- 227
Cdd:COG0498 134 RAGIEVFVFVPEgKVSPGQLAQMLTYGAHVIAVDGN--FD-------DAQRLVKELAADEGL--YaVNSINPArlegqkt 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 228 AHYddtaeEILQQCDGKVDMLVASAGTGGTITGI--ARK------LKEKCPgcKIIGVDPEGS--ILAEPEelnqTEQTA 297
Cdd:COG0498 203 YAF-----EIAEQLGRVPDWVVVPTGNGGNILAGykAFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 298 YEVEG---------IGydfIPTVLDRAVVD------RWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQE-- 360
Cdd:COG0498 272 YEPERpetiapsmdIG---NPSNGERALFAlresggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEge 348
|
330 340
....*....|....*....|....*
gi 158186659 361 LKEGQRCVVIL-------PDSVRNY 378
Cdd:COG0498 349 IDPDEPVVVLStghglkfPDAVREA 373
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
82-371 |
8.00e-15 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 75.51 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 82 GNTPMVRINRISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGTlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:PRK06381 14 GGTPLLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 162 CIIVMPEKMSMEKVDVLRALGAEIVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDDTAEEIL 238
Cdd:PRK06381 89 AVIFIPRSYSNSRVKEMEKYGAEIIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAYEIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 239 QQCDGKVDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEGS--------------ILAEPEELNQTEQT 296
Cdd:PRK06381 161 EALGDVPDAVAVPVGNGTTLAGIYHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRETAVN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158186659 297 AYEVEGIGYDFIPTVldRAVVD---RWFKSNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQELKEGQRCVVIL 371
Cdd:PRK06381 239 EPLVSYRSFDGDNAL--EAIYDshgYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| PLN02970 |
PLN02970 |
serine racemase |
101-282 |
5.11e-14 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 73.17 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 101 ELLAKCEFFNAGGSVKDRISLRMI-----EDAERAgtlkpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKV 175
Cdd:PLN02970 43 SLFFKCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 176 DVLRALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDDTAEEILQQCDGkVDMLVASAGT 254
Cdd:PLN02970 115 DAVIRYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLEQVPE-LDVIIVPISG 185
|
170 180
....*....|....*....|....*...
gi 158186659 255 GGTITGIARKLKEKCPGCKIIGVDPEGS 282
Cdd:PLN02970 186 GGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
95-280 |
1.63e-12 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 68.51 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 95 NAGLKCELLAKCEFFNAGGSVKDRIS----LRMIEDAERAGtlkpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKM 170
Cdd:PRK07048 34 DARTGAQVFFKCENFQRMGAFKFRGAynalSQFSPEQRRAG-------VVTFSSGNHAQAIALSARLLGIPATIVMPQDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 171 SMEKVDVLRALGAEIVrtptnaRFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------DTAEEIL 238
Cdd:PRK07048 107 PAAKVAATRGYGGEVV------TYDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 158186659 239 QQCdGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE 280
Cdd:PRK07048 168 EEV-GPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
77-279 |
3.27e-12 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 67.87 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 77 ILRKIGNTPMVRINriSKNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGtlKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:PRK06608 17 IKQYLHLTPIVHSE--SLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDDT 233
Cdd:PRK06608 93 LFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158186659 234 AEEILQQCDGKVDMLVASAGTGGTITG--IARKLKEkcPGCKIIGVDP 279
Cdd:PRK06608 161 CYEALQQLGFSPDAIFASCGGGGLISGtyLAKELIS--PTSLLIGSEP 206
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
84-282 |
5.85e-12 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 66.90 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 84 TPMVRINRISKNAGlkcELLAKCEFFNAGGSVKDRISLRMIEDAEragtlKPGDTIIEPTSGNTGIGLALAAAVKGYRCI 163
Cdd:PRK08246 24 TPVLEADGAGFGPA---PVWLKLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 164 IVMPEKMSMEKVDVLRALGAEIVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDDTAEEIL 238
Cdd:PRK08246 96 VFVPETAPPAKVARLRALGAEVVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 158186659 239 QQCdGKVDMLVASAGTGGTITGIARKLKekcPGCKIIGVDPEGS 282
Cdd:PRK08246 164 EQA-PGVDTVLVAVGGGGLIAGIAAWFE---GRARVVAVEPEGA 203
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
145-282 |
9.32e-12 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 67.47 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 145 GNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 219
Cdd:PRK09224 77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158186659 220 yrnasnPlahYDDT---------AEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 282
Cdd:PRK09224 145 ------P---FDDPdviagqgtiAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
77-280 |
1.52e-11 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 65.91 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 77 ILRKIGNTPMVRINRISKNAglKCELLAKCEFFNAGGSVKDRIS---LRMIEDAERAgtlkpgDTIIEPTSGNTGIGLAL 153
Cdd:PRK08638 21 LAGRIRKTPLPRSNYLSERC--KGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKR------KGVVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 154 AAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILDQYrNASNPLAHYDDT 233
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIPPY-DDPKVIAGQGTI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158186659 234 AEEILQQCdGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE 280
Cdd:PRK08638 166 GLEILEDL-WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
63-282 |
2.24e-11 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 66.36 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 63 YHTVPTKSPKILPDILRKIGN---------TPMVRINRISknAGLKCELLAKCEFFNAGGSVKDR---ISLRMIEDAERA 130
Cdd:PRK12483 8 SPTTIAPRAALLADYLRKILAarvydvareTPLQRAPNLS--ARLGNQVLLKREDLQPVFSFKIRgayNKMARLPAEQLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 131 gtlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNE 210
Cdd:PRK12483 86 ------RGVITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVL--HGESFPDALAH---ALKLAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 211 IPNSHIldqyrnasNPlahYDD---------TAEEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG 281
Cdd:PRK12483 155 EGLTFV--------PP---FDDpdviagqgtVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDD 223
|
.
gi 158186659 282 S 282
Cdd:PRK12483 224 S 224
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
82-278 |
1.67e-10 |
|
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: 62.40 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 82 GNTPMVRINRISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGTlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:TIGR00260 21 GVTPLFRAPALAANVGIK-NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 162 CIIVMPE-KMSMEKVDVLRALGAEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnshildqYRNASNPLAHYdd 232
Cdd:TIGR00260 96 VVVLYPAgKISLGKLAQALGYNAEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-------YRLEGQKTYAF-- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158186659 233 taeEILQQCDGKV-DMLVASAGTGGTITGIARKLKEKcpgcKIIGVD 278
Cdd:TIGR00260 165 ---EAVEQLGWEApDKVVVPVPNSGNFGAIWKGFKEK----KMLGLD 204
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
72-280 |
9.36e-09 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 57.05 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 72 KILPDILRKI----GNTPMVRINRISknaglkcellAKCEFFNAGGSVKDRISLRMIEDAERAGTlkpgDTIIEPTSGNT 147
Cdd:PRK06450 43 KNFPYIKHFIslgeGRTPLIKKGNIW----------FKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 148 GIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYRN 222
Cdd:PRK06450 109 GASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFRD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158186659 223 ASNPLAHyddtaeEILQQCDGKVD---MLVASAGTggTITGIARKLK--------EKCPgcKIIGVDPE 280
Cdd:PRK06450 179 GIRTLAY------EIAKDLDWKIPnyvFIPVSAGT--LLLGVYSGFKhlldsgviSEMP--KIVAVQTE 237
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
83-282 |
1.12e-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: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 83 NTPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDR-ISLRMIEDAERAGTLKPGdtIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd06448 1 KTPLIESTALSKTAG--CNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDDTAEEILQ 239
Cdd:cd06448 77 CTIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158186659 240 QC--DGKVDMLVASAGTGGTITGIARKLkEKCPGCK--IIGVDPEGS 282
Cdd:cd06448 150 QLqsQEKVDAIVCSVGGGGLLNGIVQGL-ERNGWGDipVVAVETEGA 195
|
|
| CBS |
smart00116 |
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
418-465 |
3.50e-08 |
|
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.
Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 49.82 E-value: 3.50e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 158186659 418 PLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:smart00116 2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
95-186 |
3.76e-08 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 55.39 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 95 NAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTLKPGdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEK 174
Cdd:PRK06110 31 AERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEK 108
|
90
....*....|..
gi 158186659 175 VDVLRALGAEIV 186
Cdd:PRK06110 109 NAAMRALGAELI 120
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
83-303 |
4.10e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 52.20 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 83 NTPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERA-GtlkpgdtIIEPTSGNTGIGLALAAAVK 158
Cdd:PRK07334 23 RTPCVHSRTLSQITG--AEVWLKFENLQFTASFKERGAlnkLLLLTEEERArG-------VIAMSAGNHAQGVAYHAQRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 159 GYRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNEipnshildQYRNASNPlahYDD------ 232
Cdd:PRK07334 94 GIPATIVMPRFTPTVKVERTRGFGAEVVL--HGETLDEARAH---ARELAEE--------EGLTFVHP---YDDpaviag 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158186659 233 ---TAEEILQQCdGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG--SILAEPEELNQTEQTAYEVEGI 303
Cdd:PRK07334 158 qgtVALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELypSMYAAIKGVALPCGGSTIAEGI 232
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
418-511 |
4.43e-07 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 48.39 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 418 PLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIHLTDTLGM-LS 496
Cdd:cd02205 4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEaLE 83
|
90
....*....|....*.
gi 158186659 497 HILEMD-HFALVVHEQ 511
Cdd:cd02205 84 LMLEHGiRRLPVVDDD 99
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
84-191 |
6.43e-07 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 51.80 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 84 TPMVRINRISKNAGLKcELLAKCE---F----FNA-GGS------VKDRISLRmIED-----------AERAGTLkpgdT 138
Cdd:PRK08206 45 TPLVALPDLAAELGVG-SILVKDEsyrFglnaFKAlGGAyavarlLAEKLGLD-ISElsfeeltsgevREKLGDI----T 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 158186659 139 IIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTN 191
Cdd:PRK08206 119 FATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN 171
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
234-281 |
8.66e-07 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 51.35 E-value: 8.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 158186659 234 AEEILQQCD--GKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG 281
Cdd:PRK08639 167 AVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
126-342 |
1.66e-06 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 50.22 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 126 DAERAGTlkpgDTIIepTSGntGIG-----LALAAAVK-GYRCIIVMPEKMSMEKVDVL--------RALGAEIVRTPTN 191
Cdd:PRK03910 58 DALAQGA----DTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 192 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDDTAEEILQQCDG---KVDMLVASAGTGGTITG 260
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 261 IARKLKEKCPGCKIIGVdpegSILAEPEElnQTEQTAYEVEGI-GYDFIPTVLDRAVVDRWfksndDDSFA--------- 330
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV----TVSRSAAE--QEPKVAKLAQATaELLGLPTEIPRADIRLW-----DDYVGpgygvptde 268
|
250
....*....|....*
gi 158186659 331 ---FARMLISQEGLL 342
Cdd:PRK03910 269 mleAVKLLARTEGIL 283
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
84-342 |
2.36e-06 |
|
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: 49.73 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 84 TPMVRINRISKNAGLKCELLAKCEFFN---AGGSVKDRISLRMIEDAERAGTlkpgDTIIepTSG----NTGIGLALAAA 156
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVEIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKGA----DTLV--TVGgiqsNHTRQVAAVAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 157 VKGYRCIIVM--PEKMSMEKVD------VLRALGAEIvrtptnaRFDSPESHVGV-------AWRLKNE------IPNSh 215
Cdd:cd06449 75 KLGLKCVLVQenWVPYSDAVYDrvgnilLSRIMGADV-------RLVSAGFDIGIrksfeeaAEEVEAKggkpyvIPAG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 216 ildqyrNASNPLAH--YDDTAEEILQQCDG---KVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEEL 290
Cdd:cd06449 147 ------GSEHPLGGlgYVGFVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQV 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 158186659 291 NQTEQTAYEVEGIGYdfipTVLDRAVVDRWF-----KSNDDDSFAFaRMLISQEGLL 342
Cdd:cd06449 221 LRIAQAKLAEEGLEV----KEEDVVLDDDYAapeygIPNDETIEAI-KLCARLEGII 272
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
410-465 |
2.64e-06 |
|
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.
Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 44.51 E-value: 2.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 158186659 410 VQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:pfam00571 1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
72-374 |
4.16e-06 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 49.43 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 72 KILPDILRKI----GNTPMVRiNRISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGTlkpgDTIIEPTSGNT 147
Cdd:PRK05638 51 ELLPQVKKIIslgeGGTPLIR-ARISEKLGE--NVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 148 GIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnas 224
Cdd:PRK05638 124 AASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 225 npLAHYDDTAEEILQQCDGkvDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPE------GSILAEPEEL 290
Cdd:PRK05638 196 --LEGQKTIAFELWEEINP--THVIVPTGSGSYLYSIYKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKC 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 291 NQTEQTA-YEVEGIGYDFIPTVLDR----AVVdrwfksNDDDSFAFARMLISQEGLLCGGSSGSAMAVAVKAAQE--LKE 363
Cdd:PRK05638 270 NETKALGlYVKNPVMKEYVSEAIKEsggtAVV------VNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEK 343
|
330
....*....|.
gi 158186659 364 GQRCVVILPDS 374
Cdd:PRK05638 344 GDKVVLVVTGS 354
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
418-546 |
5.87e-06 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 46.01 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 418 PLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDE------VCKVLYKQFKPIHLTDT 491
Cdd:COG3448 12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEErlldlpVEDVMTRPVVTVTPDTP 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 158186659 492 LGMLSHIL-EMDHFALVVheqiqyrnngVSSKQLMVfGVVTAIDLLNFVAAREQTR 546
Cdd:COG3448 92 LEEAAELMlEHGIHRLPV----------VDDDGRLV-GIVTRTDLLRALARLLEEE 136
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
55-281 |
7.47e-06 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 48.28 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 55 RPMADSPHY-HTVPTKS---PKILPDIlrkignTPMVRINRisknaglkcELLAKCEFFNAGGSVKDRISLRMIEDAERA 130
Cdd:PRK08329 38 REYLDMRRYiDYLPVDEeflPHLTPPI------TPTVKRSI---------KVYFKLDYLQPTGSFKDRGTYVTVAKLKEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 131 GTlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIvrtpTNARFDSPESHV-GVAWRLKN 209
Cdd:PRK08329 103 GI----NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGAEL----HFVEGDRMEVHEeAVKFSKRN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 210 EIPN-SHILDQYRNASNPLAHYddtaeEILQQCdGKVDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPE 280
Cdd:PRK08329 175 NIPYvSHWLNPYFLEGTKTIAY-----EIYEQI-GVPDYAFVPVGSGTLFLGIWKGFKElhemgeisKMP--KLVAVQAE 246
|
.
gi 158186659 281 G 281
Cdd:PRK08329 247 G 247
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
139-279 |
8.14e-06 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 48.76 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 139 IIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVgvawrlkneipNSHILD 218
Cdd:PLN02550 160 VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDS--YDEAQAYA-----------KQRALE 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158186659 219 QYRNASNPLAHYDDTA------EEILQQCDGKVDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDP 279
Cdd:PLN02550 227 EGRTFIPPFDHPDVIAgqgtvgMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEP 293
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
408-473 |
9.03e-06 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 45.24 E-value: 9.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158186659 408 LRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSD 473
Cdd:COG0517 1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLD 66
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
84-188 |
1.74e-05 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 46.88 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 84 TPMVRINRISKNAGlkCELLAKCEFFNAGGSVKDR----ISLRMIEDAERAGtlkpgdtIIEPTSGNTGIGLALAAAVKG 159
Cdd:PRK07476 20 TPLVASASLSARAG--VPVWLKLETLQPTGSFKLRgatnALLSLSAQERARG-------VVTASTGNHGRALAYAARALG 90
|
90 100
....*....|....*....|....*....
gi 158186659 160 YRCIIVMPEKMSMEKVDVLRALGAEIVRT 188
Cdd:PRK07476 91 IRATICMSRLVPANKVDAIRALGAEVRIV 119
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
41-187 |
1.86e-05 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 46.92 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 41 ISPDTPSRCTWQLGRpmadsphYHTV-PTKSPKILPDILRkiGNTPMVRINRISKNAGLKcELLAKCEFFNAGGSVKDRI 119
Cdd:PRK08197 45 VTREALAGRPANLWR-------YHELlPVRDPEHIVSLGE--GMTPLLPLPRLGKALGIG-RLWVKDEGLNPTGSFKARG 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158186659 120 SLRMIEDAERAGTLKpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVR 187
Cdd:PRK08197 115 LAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELYL 178
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
408-539 |
2.63e-05 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 45.26 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 408 LRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNEsGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIH 487
Cdd:COG2524 86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTVS 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 158186659 488 LTDTLG-MLSHILEMD-HFALVVHEqiqyrnNGVsskqlmVFGVVTAIDLLNFV 539
Cdd:COG2524 165 EDDSLEeALRLMLEHGiGRLPVVDD------DGK------LVGIITRTDILRAL 206
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
405-465 |
2.66e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 43.70 E-value: 2.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158186659 405 WWHLRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG0517 64 LLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
82-276 |
9.80e-05 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 45.19 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 82 GNTPMVRINRISKNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGTL-KPGDTIIEPTSGNTGIGLALAAAVKGY 160
Cdd:PLN02569 132 GNSNLFWAERLGKEFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYCAAAGI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 161 RCIIVMPE-KMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIP----NShiLDQYRnasnpLAHYDDTAE 235
Cdd:PLN02569 212 PSIVFLPAdKISIAQLVQPIANGALVLSIDTD--FDGCMRLIR---EVTAELPiylaNS--LNSLR-----LEGQKTAAI 279
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 158186659 236 EILQQCDGKV-DMLVASAGTGGTITGIARKLKEkcpgCKIIG 276
Cdd:PLN02569 280 EILQQFDWEVpDWVIVPGGNLGNIYAFYKGFKM----CKELG 317
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
122-188 |
1.70e-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: 43.75 E-value: 1.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 122 RMIEDAeraGTLKPGDTIIEpTSGNTGIGLALA--AAVKGYRCIIVMPEKMSMEK-VDVLRALGAEIVRT 188
Cdd:cd08290 136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
410-540 |
3.09e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 40.58 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 410 VQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDE-VCKVLYKQFKPIHL 488
Cdd:COG2905 1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 158186659 489 TDTLGMLSHILEMDHF-ALVVheqiqyrnngVSSKQLMvfGVVTAIDLLNFVA 540
Cdd:COG2905 81 DDSLAEALELMEEHRIrHLPV----------VDDGKLV--GIVSITDLLRALS 121
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
406-464 |
1.19e-03 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 40.25 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 158186659 406 WHLRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSL 464
Cdd:COG2524 148 LDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
408-465 |
1.31e-03 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 39.08 E-value: 1.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 158186659 408 LRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG3448 73 LPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
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|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
407-461 |
1.37e-03 |
|
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: 38.76 E-value: 1.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 158186659 407 HLRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNML 461
Cdd:cd02205 58 DTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
408-465 |
1.79e-03 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 38.66 E-value: 1.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 158186659 408 LRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNEsGAILGMVTLGNMLSSLL 465
Cdd:COG2905 65 TPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
410-537 |
2.23e-03 |
|
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: 37.69 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158186659 410 VQELSLSAPLTVLPTVTCEHTIAILREK-GFDQAPVVNESGailgmVTLgNMLSSLLAGKVRPSdevckvlykqfkpihl 488
Cdd:COG3620 1 VRDLMSRDVVTVSPDDTLGEALRLMRKElGLSQLPVAELVG-----VSQ-SDILRIESGKRDPT---------------- 58
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 158186659 489 TDTLGMLSHILEMDHFALVVHEQIQYrnngvsskqlmvFGVVTAIDLLN 537
Cdd:COG3620 59 VSTLEKIAEALGKELSAVLVVDDGKL------------VGIITRRDLLK 95
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
407-465 |
3.10e-03 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 37.97 E-value: 3.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 158186659 407 HLRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG4109 75 DTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
407-465 |
3.39e-03 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 40.20 E-value: 3.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 158186659 407 HLRVQELSLSAPLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:PRK14869 67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
|
|
| CBS_pair_NTP_transferase_assoc |
cd04607 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
418-462 |
7.28e-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: 7.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 158186659 418 PLTVLPTVTCEHTIAILREKGFDQAPVVNESGAILGMVTLGNMLS 462
Cdd:cd04607 68 PITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLLA 112
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