|
Name |
Accession |
Description |
Interval |
E-value |
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
76-544 |
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: 818.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 76 ILPDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLA 155
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 156 LAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDT 235
Cdd:TIGR01137 79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 236 TADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVL 315
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 316 DRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ-ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQK 394
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 395 GFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQ 474
Cdd:TIGR01137 319 GFLDDEDLTVKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 475 PSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQyhstgkssqrqmvFGVVTAIDLLNFVA 544
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKP-------------IGVVTKIDLLSFLA 455
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
85-383 |
8.60e-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: 469.30 E-value: 8.60e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 85 GDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYR 164
Cdd:cd01561 1 GNTPLVRLNRLSP--GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 165 CIIVMPEKMSSEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQC 244
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 245 DGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWF 324
Cdd:cd01561 158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 295821200 325 KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 383
Cdd:cd01561 233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
75-384 |
2.10e-157 |
|
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: 451.04 E-value: 2.10e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 75 KILPDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGL 154
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSP--GPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 155 ALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYD 234
Cdd:COG0031 80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 235 TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTV 314
Cdd:COG0031 157 TTGPEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 315 LDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 384
Cdd:COG0031 232 LDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
74-396 |
8.80e-117 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 348.77 E-value: 8.80e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 74 PKILPDILKKIGDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIG 153
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 154 LALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASN 228
Cdd:PRK10717 79 LALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 229 PLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL----AEPEELNQTEQTTyevE 304
Cdd:PRK10717 158 REAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGELKAEGSSIT---E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 305 GIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 384
Cdd:PRK10717 235 GIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK 314
|
330
....*....|..
gi 295821200 385 FLSDRWMLQKGF 396
Cdd:PRK10717 315 LFNPDFLREKGL 326
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
84-383 |
1.55e-112 |
|
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: 336.65 E-value: 1.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 84 IGDTPMVRINKIgkkFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGY 163
Cdd:TIGR01139 5 IGNTPLVRLNRI---EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 164 RCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDTTADEILQ 242
Cdd:TIGR01139 82 KLILTMPETMSIERRKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 243 QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDK 322
Cdd:TIGR01139 159 DTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRSVIDE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295821200 323 WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 383
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
80-383 |
2.15e-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: 328.47 E-value: 2.15e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 80 ILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAA 159
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAP--GCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 160 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDT 235
Cdd:TIGR01136 79 ARGYKLILTMPETMSLERRKLLRAYGAELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 236 TADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVL 315
Cdd:TIGR01136 152 TGPEIWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKIL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295821200 316 DRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMT 383
Cdd:TIGR01136 227 DLSLIDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
87-377 |
6.22e-84 |
|
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: 260.91 E-value: 6.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 87 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLkPGDTIIEPTSGNTGIGLALAAAVRGYRCI 166
Cdd:cd00640 1 TPLVRLKRLSKLGG--ANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 167 IVMPEKMSSEKVDVLRALGAEIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDG 246
Cdd:cd00640 78 IVMPEGASPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 247 -KLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEgsilaepeelnqteqttyevegigydfiptvldrtvvdkWFK 325
Cdd:cd00640 152 qKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE---------------------------------------VVT 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 295821200 326 SNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDS 377
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
84-376 |
5.94e-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: 5.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 84 IGDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERdgtLKPGDTIIEPTSGNTGIGLALAAAVRGY 163
Cdd:pfam00291 5 IGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 164 RCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQ 243
Cdd:pfam00291 80 KVTIVVPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 244 CDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS-ILAEPEELNQTEQTT---YEVEGIGYDFIPTVLDRTV 319
Cdd:pfam00291 154 LGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGALALDL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295821200 320 VDKWFKS----NDEEAFTFARMLIAQEGLLCGGSAGSTVAVA-VKAAQELQEGQRCVVILPD 376
Cdd:pfam00291 234 LDEYVGEvvtvSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
80-390 |
2.94e-80 |
|
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: 253.66 E-value: 2.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 80 ILKKIGDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAA 159
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAP--FRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 160 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLA 231
Cdd:TIGR03945 79 YKGLRFICVVDPNISPQNLKLLRAYGAEVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 232 HYDTTADEILQQCDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL--AEPeelnqteqTTYEVEGIGYD 309
Cdd:TIGR03945 152 HYHGTGREIARAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGAS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 310 FIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDR 389
Cdd:TIGR03945 223 VVPELLDESLIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDE 302
|
.
gi 295821200 390 W 390
Cdd:TIGR03945 303 W 303
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
78-376 |
6.55e-80 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 252.49 E-value: 6.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 78 PDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALA 157
Cdd:PRK11761 4 PTLEDTIGNTPLVKLQRLPP--DRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 158 AAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDTTA 237
Cdd:PRK11761 82 AAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 238 DEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP-EGS----ILAEPEElnqteqttyevegigydFIP 312
Cdd:PRK11761 158 PEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLP 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295821200 313 TVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELqEGQRCVVILPD 376
Cdd:PRK11761 221 KIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICD 283
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
76-388 |
3.08e-76 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 244.06 E-value: 3.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 76 ILPDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGL 154
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVD--GCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 155 ALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHY 233
Cdd:PLN02565 83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 234 DTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPT 313
Cdd:PLN02565 159 ETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295821200 314 VLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 388
Cdd:PLN02565 234 VLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
80-383 |
1.22e-71 |
|
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: 230.96 E-value: 1.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 80 ILKKIGDTPMVRINKIGKKFGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAA 159
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGS--EVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 160 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDTTADE 239
Cdd:TIGR01138 80 LKGYRMKLLMPDNMSQERKAAMRAYGAELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 240 ILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEgsilaEPeelnqteqttYEVEGIGY---DFIPTVLD 316
Cdd:TIGR01138 156 IWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFD 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295821200 317 RTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQrCVVILPDSVRNYMT 383
Cdd:TIGR01138 221 ASLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
79-388 |
4.10e-70 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 227.96 E-value: 4.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 79 DILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPG-DTIIEPTSGNTGIGLALA 157
Cdd:PLN00011 10 DVTELIGNTPMVYLNNIVD--GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 158 AAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLA 231
Cdd:PLN00011 88 GAARGYKVILVMPSTMSLERRIILRALGAEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 232 HYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFI 311
Cdd:PLN00011 159 HYRTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGII 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295821200 312 PTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQE-GQRCVVILPDSVRNYMTKFLSD 388
Cdd:PLN00011 234 PFNLDLTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYLSTKLFE 311
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
76-383 |
2.19e-67 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 224.27 E-value: 2.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 76 ILPDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGL 154
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAK--GCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 155 ALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPL 230
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 231 AHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDF 310
Cdd:PLN03013 264 IHYETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGF 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295821200 311 IPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 383
Cdd:PLN03013 339 IPKNLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIY 411
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
59-388 |
4.15e-64 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 213.67 E-value: 4.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 59 PASESPHHHTAPAKSPKILP------DILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAER 132
Cdd:PLN02556 26 STVGSPSFAQRLRDLPKDLPgtkiktDASQLIGKTPLVYLNKVTE--GCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 133 DGTLKPGDT-IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRT-PTNARFDSpeshVGVAWRL 210
Cdd:PLN02556 104 KNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTdPTKGMGGT----VKKAYEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 211 KNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEP 290
Cdd:PLN02556 180 LESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP-----AES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 291 EELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQR 369
Cdd:PLN02556 255 NVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPEnKGKL 334
|
330
....*....|....*....
gi 295821200 370 CVVILPDSVRNYMTKFLSD 388
Cdd:PLN02556 335 IVTVHPSFGERYLSSVLFQ 353
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
80-396 |
5.38e-56 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 194.05 E-value: 5.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 80 ILKKIGDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAA 159
Cdd:PLN02356 47 LIDAIGNTPLIRINSLSEATG--CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 160 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRT-PTNarFDSPESHVGVAWRL---KNEIP-----------------NSH 218
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVrPVS--ITHKDHYVNIARRRaleANELAskrrkgsetdgihlektNGC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 219 IL-------------------DQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIG 279
Cdd:PLN02356 203 ISeeekenslfsssctggffaDQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 280 VDPEGSIL--------------AEPEELNQTEQTTyeVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 345
Cdd:PLN02356 283 IDPPGSGLfnkvtrgvmytreeAEGRRLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLF 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 295821200 346 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGF 396
Cdd:PLN02356 361 VGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
412-542 |
6.94e-56 |
|
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: 183.50 E-value: 6.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 412 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 491
Cdd:cd04608 2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 295821200 492 LTDTLGRLSHILEMDHFALVVHEQiqyhstgkssqrQMVFGVVTAIDLLNF 542
Cdd:cd04608 82 LDTPLGALSRILERDHFALVVDGQ------------GKVLGIVTRIDLLNY 120
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
87-374 |
3.40e-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: 117.20 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 87 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMI----EDAERDGtlkpgdtIIEPTSGNTGIGLALAAAVRG 162
Cdd:cd01562 18 TPLLTSPTLSELLG--AEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 163 YRCIIVMPEKMSSEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD--- 234
Cdd:cd01562 89 IPATIVMPETAPAAKVDATRAYGAEVVL--YGEDFDEAEAK---ARELAEEegltfIH-------------PFDDPDvia 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 235 ---TTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTEQTtyeVE 304
Cdd:cd01562 151 gqgTIGLEILEQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTI---AD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295821200 305 GIGydfIPTVLDRT------VVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 374
Cdd:cd01562 227 GLA---VKRPGELTfeiirkLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
87-374 |
4.15e-29 |
|
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: 117.44 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 87 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDR------ISLRmieDAERDGTlkpgdtIIEPTSGNTGIGLALAAAV 160
Cdd:COG1171 25 TPLLRSPTLSERLG--AEVYLKLENLQPTGSFKLRgaynalASLS---EEERARG------VVAASAGNHAQGVAYAARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 161 RGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD- 234
Cdd:COG1171 94 LGIPATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAA---AAELAEEegatfVH-------------PFDDPDv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 235 -----TTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTeQT--- 299
Cdd:COG1171 156 iagqgTIALEILEQL-PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTiad 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295821200 300 ---TYEVEGIGYDFIPTVLDRTV-VDkwfksnDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 374
Cdd:COG1171 234 glaVGRPGELTFEILRDLVDDIVtVS------EDEIAAAMRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVVL 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
87-374 |
1.17e-27 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 113.25 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 87 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGY 163
Cdd:PRK06815 21 TPLEHSPLLSQHTG--CEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 164 RCIIVMPEKMSSEKVDVLRALGAEIVRTPTNArfDSPESHvgvAWRLKNEIPNSHIlDQYrNASNPLAHYDTTADEILQQ 243
Cdd:PRK06815 93 PVTVYAPEQASAIKLDAIRALGAEVRLYGGDA--LNAELA---ARRAAEQQGKVYI-SPY-NDPQVIAGQGTIGMELVEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 244 CDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA----EPEELNQTEQTTyeVEGIGYDFIPT 313
Cdd:PRK06815 166 QP-DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTLSDGT--AGGVEPGAITF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295821200 314 VLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQeGQRCVVIL 374
Cdd:PRK06815 243 PLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
77-374 |
6.97e-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: 93.81 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 77 LPDILKKI-----GDTPMVRINKIGKKFGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTG 151
Cdd:cd01563 8 LPVTEDDIvslgeGNTPLVRAPRLGERLGGK-NLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 152 IGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLA 231
Cdd:cd01563 83 ASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 232 H--YDTTADEILQQCDGKL-DMLVASVGTGGTITGIARKLKE--------KCPgcRIIGVDPEGS------ILAEPEELN 294
Cdd:cd01563 153 LegQKTIAFEIAEQLGWEVpDYVVVPVGNGGNITAIWKGFKElkelglidRLP--RMVGVQAEGAapivraFKEGKDDIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 295 QTEQTTYEVEGIGydfIPT-VLDRTVVDKWFKSN------DEEAFTFARMLIAQ-EGLLCGGSAGSTVAVAVKAAQE--L 364
Cdd:cd01563 231 PVENPETIATAIR---IGNpASGPKALRAVRESGgtavavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiI 307
|
330
....*....|
gi 295821200 365 QEGQRCVVIL 374
Cdd:cd01563 308 DKGERVVVVL 317
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
82-374 |
4.05e-19 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 88.22 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 82 KKIGDTPMVRINKIGKKFGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVR 161
Cdd:PRK06381 11 KPPGGTPLLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 162 GYRCIIVMPEKMSSEKVDVLRALGAEIVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDTTAD 238
Cdd:PRK06381 86 GLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 239 EILQQCDGKLDMLVASVGTGGTITGIARKLKE--------KCPgcRIIGVDPEGS--------------ILAEPEELNQT 296
Cdd:PRK06381 158 EIYEALGDVPDAVAVPVGNGTTLAGIYHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 297 EQTTYEVEGIGYDFiPTVLD--RTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVIL 374
Cdd:PRK06381 236 AVNEPLVSYRSFDG-DNALEaiYDSHGYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
85-381 |
1.65e-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: 81.40 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 85 GDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDR-----ISLrmiedAERDGTlkpgDTIIEPTSGNTGIGLALAAA 159
Cdd:COG0498 65 GGTPLVKAPRLADELG--KNLYVKEEGHNPTGSFKDRamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 160 VRGYRCIIVMPE-KMSSEKVDVLRALGAEIVRTPTNarFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPLAH--YDT 235
Cdd:COG0498 134 RAGIEVFVFVPEgKVSPGQLAQMLTYGAHVIAVDGN--FD-------DAQRLVKELAADEGL--YaVNSINPARLegQKT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 236 TADEILQQCDGKLDMLVASVGTGGTITGI--ARK------LKEKCPgcRIIGVDPEGS--ILAEPEelnqTEQTTYEVEG 305
Cdd:COG0498 203 YAFEIAEQLGRVPDWVVVPTGNGGNILAGykAFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPER 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 306 ---------IGydfIPT-------VLDRTvvDKWF-KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQE 366
Cdd:COG0498 277 petiapsmdIG---NPSngeralfALRES--GGTAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDP 351
|
330 340
....*....|....*....|..
gi 295821200 367 GQRCVVIL-------PDSVRNY 381
Cdd:COG0498 352 DEPVVVLStghglkfPDAVREA 373
|
|
| PLN02970 |
PLN02970 |
serine racemase |
104-285 |
4.35e-16 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 79.34 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 104 ELLAKCEFFNAGGSVKDRISLRMI-----EDAERDgtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKV 178
Cdd:PLN02970 43 SLFFKCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 179 DVLRALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDTTADEILQQCDGkLDMLVASVGT 257
Cdd:PLN02970 115 DAVIRYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLEQVPE-LDVIIVPISG 185
|
170 180
....*....|....*....|....*...
gi 295821200 258 GGTITGIARKLKEKCPGCRIIGVDPEGS 285
Cdd:PLN02970 186 GGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
104-285 |
1.87e-14 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 74.22 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 104 ELLAKCEFFNAGGSVKDRISLRMIEDAErdgtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRA 183
Cdd:PRK08246 38 PVWLKLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 184 LGAEIVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDTTADEILQQCdGKLDMLVASVGTG 258
Cdd:PRK08246 113 LGAEVVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGGG 179
|
170 180
....*....|....*....|....*..
gi 295821200 259 GTITGIARKLKekcPGCRIIGVDPEGS 285
Cdd:PRK08246 180 GLIAGIAAWFE---GRARVVAVEPEGA 203
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
104-283 |
4.51e-14 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 73.13 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 104 ELLAKCEFFNAGGSVKDR---ISLRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV 180
Cdd:PRK07048 40 QVFFKCENFQRMGAFKFRgayNALSQFSPEQR----RAG--VVTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 181 LRALGAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKL 248
Cdd:PRK07048 114 TRGYGGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELFEEV-GPL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 295821200 249 DMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 283
Cdd:PRK07048 174 DALFVCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
148-285 |
6.07e-14 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 74.40 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 148 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 222
Cdd:PRK09224 77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295821200 223 yrnasnPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 285
Cdd:PRK09224 145 ------PFDDPDviagqgTIAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
142-285 |
6.35e-13 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 70.98 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 142 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEIPNS--HI 219
Cdd:PRK12483 88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAH---ALKLAEEEGLTfvPP 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295821200 220 LDQyrnaSNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 285
Cdd:PRK12483 163 FDD----PDVIAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
80-282 |
1.53e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 65.95 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 80 ILKKIGDTPMVRINKIGKKFGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERDGtlKPGDTIIEPTSGNTGIGLALAAA 159
Cdd:PRK06608 17 IKQYLHLTPIVHSESLNEMLGH--EIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 160 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDTT 236
Cdd:PRK06608 93 LFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 295821200 237 ADEILQQCDGKLDMLVASVGTGGTITG--IARKLKEkcPGCRIIGVDP 282
Cdd:PRK06608 161 CYEALQQLGFSPDAIFASCGGGGLISGtyLAKELIS--PTSLLIGSEP 206
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
75-271 |
2.66e-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: 65.10 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 75 KILPDILKKI-----GDTPMVRINKIGKKFGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGN 149
Cdd:TIGR00260 6 EFLPVTEKDLvdlgeGVTPLFRAPALAANVGIK-NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 150 TGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVLRALGAEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnSHIL 220
Cdd:TIGR00260 81 TGAAAAAYAGKAGLKVVVLYPAgKISLGKLAQALGYNAEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-YRLE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 295821200 221 DQYrnasnplahydTTADEILQQCDGKL-DMLVASVGTGGTITGIARKLKEK 271
Cdd:TIGR00260 158 GQK-----------TYAFEAVEQLGWEApDKVVVPVPNSGNFGAIWKGFKEK 198
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
80-283 |
1.02e-10 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 63.22 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 80 ILKKIGDTPMVRINKIGKKfgLKCELLAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLAL 156
Cdd:PRK08638 21 LAGRIRKTPLPRSNYLSER--CKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEK----RKG--VVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 157 AAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILDQYrNASNPLAHYDTT 236
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIPPY-DDPKVIAGQGTI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 295821200 237 ADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 283
Cdd:PRK08638 166 GLEILEDL-WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| CBS |
smart00116 |
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
422-469 |
1.33e-09 |
|
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.
Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 53.67 E-value: 1.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 295821200 422 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 469
Cdd:smart00116 2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
87-285 |
3.52e-09 |
|
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: 58.46 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 87 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDR-ISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRC 165
Cdd:cd06448 2 TPLIESTALSKTAG--CNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 166 IIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDTTADEILQQ 243
Cdd:cd06448 78 TIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 295821200 244 C--DGKLDMLVASVGTGGTITGIARKLkEKCPGCR--IIGVDPEGS 285
Cdd:cd06448 151 LqsQEKVDAIVCSVGGGGLLNGIVQGL-ERNGWGDipVVAVETEGA 195
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
422-505 |
3.80e-09 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 54.56 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 422 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTlgrLSH 501
Cdd:cd02205 4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTD---LEE 80
|
....
gi 295821200 502 ILEM 505
Cdd:cd02205 81 ALEL 84
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
86-282 |
1.60e-08 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 57.24 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 86 DTPMVRINKIGKKFGLKceLLAKCEFFNAGGSVKDRISLRMIEDAERDgTLKPGdtIIEPTSGNTGIGLALAAAVRGYRC 165
Cdd:PLN02550 109 ESPLQLAKKLSERLGVK--VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 166 IIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYD------TTADE 239
Cdd:PLN02550 184 VIAMPVTTPEIKWQSVERLGATVVLVGDS--YDEAQAYA-----------KQRALEEGRTFIPPFDHPDviagqgTVGME 250
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 295821200 240 ILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP 282
Cdd:PLN02550 251 IVRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEP 293
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
235-284 |
2.07e-08 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 56.35 E-value: 2.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 295821200 235 TTADEILQQCD--GKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG 284
Cdd:PRK08639 165 TVAVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
87-283 |
2.57e-08 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 56.04 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 87 TPMVRINKIGKKFGLKcELLAKCE---F----FNA-GGS------VKDRISLRMIE---DAERDGTLKP--GD-TIIEPT 146
Cdd:PRK08206 45 TPLVALPDLAAELGVG-SILVKDEsyrFglnaFKAlGGAyavarlLAEKLGLDISElsfEELTSGEVREklGDiTFATAT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 147 SGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDspEShVGVAWRLKNEipNSHILDQyrNA 226
Cdd:PRK08206 124 DGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN--YD--DS-VRLAAQEAQE--NGWVVVQ--DT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295821200 227 SNP---------LAHYDTTADEILQQCDGKLD-----MLVASVGT--GGTITGIARKLKEKCPgcRIIGVDPE 283
Cdd:PRK08206 195 AWEgyeeiptwiMQGYGTMADEAVEQLKEMGVppthvFLQAGVGSlaGAVLGYFAEVYGEQRP--HFVVVEPD 265
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
75-283 |
5.12e-08 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 54.74 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 75 KILPDILKKI----GDTPMVRINKIgkKFglkcellaKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNT 150
Cdd:PRK06450 43 KNFPYIKHFIslgeGRTPLIKKGNI--WF--------KLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 151 GIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYRN 225
Cdd:PRK06450 109 GASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFRD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295821200 226 ASNPLAHydttadEILQQCDGKL-DMLVASVGTGGTITGIARKLK--------EKCPgcRIIGVDPE 283
Cdd:PRK06450 179 GIRTLAY------EIAKDLDWKIpNYVFIPVSAGTLLLGVYSGFKhlldsgviSEMP--KIVAVQTE 237
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
422-550 |
8.15e-08 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 51.40 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 422 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQ------PSDQVGKVIYKQFKQIRLTDT 495
Cdd:COG3448 12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlLDLPVEDVMTRPVVTVTPDTP 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 295821200 496 LGRLSHILeMD---HFALVVHEQiqyhstGKssqrqmVFGVVTAIDLLNFVAAQERDQ 550
Cdd:COG3448 92 LEEAAELM-LEhgiHRLPVVDDD------GR------LVGIVTRTDLLRALARLLEEE 136
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
412-546 |
9.18e-08 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 51.02 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 412 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQI 490
Cdd:COG0517 1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTpVSEVMTRPPVTV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 295821200 491 RLTDTLGRLSHILEMDHF--ALVVHEqiqyhstgkssQRQMVfGVVTAIDLLNFVAAQ 546
Cdd:COG0517 81 SPDTSLEEAAELMEEHKIrrLPVVDD-----------DGRLV-GIITIKDLLKALLEP 126
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
101-189 |
9.66e-08 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 53.84 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 101 LKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV 180
Cdd:PRK06110 34 LGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAA 111
|
....*....
gi 295821200 181 LRALGAEIV 189
Cdd:PRK06110 112 MRALGAELI 120
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
86-283 |
2.56e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 52.97 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 86 DTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRG 162
Cdd:PRK07334 23 RTPCVHSRTLSQITG--AEVWLKFENLQFTASFKERGAlnkLLLLTEEER----ARG--VIAMSAGNHAQGVAYHAQRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 163 YRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEipnshildQYRNASNPLAHYD------TT 236
Cdd:PRK07334 95 IPATIVMPRFTPTVKVERTRGFGAEVVLH--GETLDEARAH---ARELAEE--------EGLTFVHPYDDPAviagqgTV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 295821200 237 ADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 283
Cdd:PRK07334 162 ALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTE 207
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
412-543 |
3.78e-07 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 51.04 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 412 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEaGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 491
Cdd:COG2524 86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTVS 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 295821200 492 LTDTLGRLSHILEmDH---FALVVHEQiqyhstGKssqrqmVFGVVTAIDLLNFV 543
Cdd:COG2524 165 EDDSLEEALRLML-EHgigRLPVVDDD------GK------LVGIITRTDILRAL 206
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
75-377 |
4.92e-07 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 52.12 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 75 KILPDILKKI----GDTPMVRiNKIGKKFGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNT 150
Cdd:PRK05638 51 ELLPQVKKIIslgeGGTPLIR-ARISEKLGE--NVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 151 GIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnas 227
Cdd:PRK05638 124 AASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 228 npLAHYDTTADEILQQCDGklDMLVASVGTGGTITGIARKLKE--------KCPgcRIIGVDPE------GSILAEPEEL 293
Cdd:PRK05638 196 --LEGQKTIAFELWEEINP--THVIVPTGSGSYLYSIYKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKC 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 294 NQTeqttyevEGIGYDFIPTVLDRTVVDKWFKS------NDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQ 365
Cdd:PRK05638 270 NET-------KALGLYVKNPVMKEYVSEAIKESggtavvVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIE 342
|
330
....*....|..
gi 295821200 366 EGQRCVVILPDS 377
Cdd:PRK05638 343 KGDKVVLVVTGS 354
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
414-469 |
5.75e-07 |
|
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.
Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 46.44 E-value: 5.75e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 295821200 414 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 469
Cdd:pfam00571 1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
41-190 |
1.03e-06 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 51.15 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 41 PLWIRPD-APSRCTWQ----LGRPASESPHHHTAPAKSPKILPDILKkiGDTPMVRINKIGKKFGLKcELLAKCEFFNAG 115
Cdd:PRK08197 31 PLLVRYDlEAVKQAVTrealAGRPANLWRYHELLPVRDPEHIVSLGE--GMTPLLPLPRLGKALGIG-RLWVKDEGLNPT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295821200 116 GSVKDRISLRMIEDAERDGTLKpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVR 190
Cdd:PRK08197 108 GSFKARGLAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELYL 178
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
414-541 |
2.50e-06 |
|
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: 45.78 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 414 VQELGLSAPLTVLPTITCGHTIEILREK-GFDQAPVVDEAGvilgmVTLgNMLSSLLAGKVQPSdqvgkviykqfkqirl 492
Cdd:COG3620 1 VRDLMSRDVVTVSPDDTLGEALRLMRKElGLSQLPVAELVG-----VSQ-SDILRIESGKRDPT---------------- 58
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 295821200 493 TDTLGRLSHILEMDHFALVVHEQIQYHstgkssqrqmvfGVVTAIDLLN 541
Cdd:COG3620 59 VSTLEKIAEALGKELSAVLVVDDGKLV------------GIITRRDLLK 95
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
74-284 |
3.01e-06 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 49.44 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 74 PKILPDIlkkigdTPMVRINKigkkfglkcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIG 153
Cdd:PRK08329 58 PHLTPPI------TPTVKRSI---------KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 154 LALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRnasnpLA 231
Cdd:PRK08329 119 LALYSLSEGIKVHVFVSYNASKEKISLLSRLGAEL----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYF-----LE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295821200 232 HYDTTADEILQQCdGKLDMLVASVGTGGTITGIARKLKE--------KCPgcRIIGVDPEG 284
Cdd:PRK08329 190 GTKTIAYEIYEQI-GVPDYAFVPVGSGTLFLGIWKGFKElhemgeisKMP--KLVAVQAEG 247
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
87-280 |
6.40e-06 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 48.42 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 87 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDR----ISLRMIEDAERDGtlkpgdtIIEPTSGNTGIGLALAAAVRG 162
Cdd:PRK07476 20 TPLVASASLSARAG--VPVWLKLETLQPTGSFKLRgatnALLSLSAQERARG-------VVTASTGNHGRALAYAARALG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 163 YRCIIVMPEKMSSEKVDVLRALGAEIVRTPtnarfDSPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD--- 234
Cdd:PRK07476 91 IRATICMSRLVPANKVDAIRALGAEVRIVG-----RSQDDAQAEVERLVREegltmVP-------------PFDDPRiia 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 295821200 235 ---TTADEILQQCDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGV 280
Cdd:PRK07476 153 gqgTIGLEILEALP-DVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGV 200
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
87-345 |
1.13e-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: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 87 TPMVRINKIGKKFGLKCELLAKCEFFN---AGGSVKDRISLRMIEDAERDGTlkpgDTIIepTSG----NTGIGLALAAA 159
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVEIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKGA----DTLV--TVGgiqsNHTRQVAAVAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 160 VRGYRCIIVM--PEKMSSEKVD------VLRALGAEIvrtptnaRFDSPESHVGV-------AWRLKNE------IPNSh 218
Cdd:cd06449 75 KLGLKCVLVQenWVPYSDAVYDrvgnilLSRIMGADV-------RLVSAGFDIGIrksfeeaAEEVEAKggkpyvIPAG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 219 ildqyrNASNPLAH--YDTTADEILQQCDG---KLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEEL 293
Cdd:cd06449 147 ------GSEHPLGGlgYVGFVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQV 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 295821200 294 NQTEQTTYEVEGIGYdfipTVLDRTVVDKWF-----KSNDE--EAFtfaRMLIAQEGLL 345
Cdd:cd06449 221 LRIAQAKLAEEGLEV----KEEDVVLDDDYAapeygIPNDEtiEAI---KLCARLEGII 272
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
414-546 |
1.18e-05 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 44.82 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 414 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQIRL 492
Cdd:COG2905 1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 295821200 493 TDTLGRLSHILEMDHF-ALVVHEQiqyhstGKssqrqmVFGVVTAIDLLNFVAAQ 546
Cdd:COG2905 81 DDSLAEALELMEEHRIrHLPVVDD------GK------LVGIVSITDLLRALSEE 123
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
129-280 |
3.67e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 45.98 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 129 DAERDGTlkpgDTIIepTSGntGIG-----LALAAAVR-GYRCIIVMPEKMSSEKVDVL--------RALGAEIVRTPTN 194
Cdd:PRK03910 58 DALAQGA----DTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 195 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDTTADEILQQCDG---KLDMLVASVGTGGTITG 263
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
|
170
....*....|....*..
gi 295821200 264 IARKLKEKCPGCRIIGV 280
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV 216
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
395-469 |
5.23e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 43.36 E-value: 5.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295821200 395 GFLKEEDLTEKKPwwwHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 469
Cdd:COG4109 62 GIVTSKDILGKDD---DTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
402-469 |
5.31e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 42.93 E-value: 5.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295821200 402 LTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 469
Cdd:COG0517 57 LAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
331-468 |
6.59e-05 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 44.10 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 331 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRcVVILPDSVRNYMTKF---------LSD--RWMLQK----- 394
Cdd:COG2524 42 LLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL-GLVLKMKVKDIMTKDvitvspdttLEEalELMLEKgisgl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 395 ---------GFLKEEDL---TEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLG 462
Cdd:COG2524 121 pvvddgklvGIITERDLlkaLAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRT 200
|
....*.
gi 295821200 463 NMLSSL 468
Cdd:COG2524 201 DILRAL 206
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
125-191 |
6.76e-05 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 6.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 125 RMIEDAerdGTLKPGDTIIEpTSGNTGIGLALA--AAVRGYRCIIVMPEKMSSEK-VDVLRALGAEIVRT 191
Cdd:cd08290 136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
422-515 |
9.04e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 42.59 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 422 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLssllagKVQPSDQVGKVIYKQFKQIRLTDTLGRLSH 501
Cdd:COG4109 27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVTPDTSLASAAH 100
|
90
....*....|....*.
gi 295821200 502 ILEMDHFAL--VVHEQ 515
Cdd:COG4109 101 KMIWEGIELlpVVDDD 116
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
395-465 |
1.07e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 41.85 E-value: 1.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295821200 395 GFLKEEDLTEK---KPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNML 465
Cdd:cd02205 39 GIVTERDILRAlveGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
360-469 |
2.08e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 41.35 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 360 AAQELQE-GQRCVVILPDSvrNYMTKFLSDRWMLQKGFLKEEDLTEKKpwwwhlrVQELGLSAPLTVLPTITCGHTIEIL 438
Cdd:COG2905 21 AARLMTEkGVGSLVVVDDD--GRLVGIITDRDLRRRVLAEGLDPLDTP-------VSEVMTRPPITVSPDDSLAEALELM 91
|
90 100 110
....*....|....*....|....*....|.
gi 295821200 439 REKGFDQAPVVDEaGVILGMVTLGNMLSSLL 469
Cdd:COG2905 92 EEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
|
|
| CBS_pair_Mg_transporter |
cd04606 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ... |
423-540 |
4.27e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 40.39 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 423 LTVLPTITCGHTIEILREKG-----FDQAPVVDEAGVILGMVTLGNMLSSllagkvQPSDQVGKVIYKQFKQIRLTDTLG 497
Cdd:cd04606 12 VAVRPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSLRDLLLA------DPDTKVSDIMDTDVISVSADDDQE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 295821200 498 RLSHILEM-DHFAL-VVHEqiqyhstgkssQRQMVfGVVT---AIDLL 540
Cdd:cd04606 86 EVARLFAKyDLLALpVVDE-----------EGRLV-GIITvddVLDVI 121
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
85-279 |
6.06e-04 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 42.49 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 85 GDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTL-KPGDTIIEPTSGNTGIGLALAAAVRGY 163
Cdd:PLN02569 132 GNSNLFWAERLGKEFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYCAAAGI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 164 RCIIVMPE-KMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIP----NShiLDQYRnasnpLAHYDTTAD 238
Cdd:PLN02569 212 PSIVFLPAdKISIAQLVQPIANGALVLSIDTD--FDGCMRLIR---EVTAELPiylaNS--LNSLR-----LEGQKTAAI 279
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 295821200 239 EILQQCDGKL-DMLVASVGTGGTITGIARKLKEkcpgCRIIG 279
Cdd:PLN02569 280 EILQQFDWEVpDWVIVPGGNLGNIYAFYKGFKM----CKELG 317
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
396-469 |
7.61e-04 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 39.85 E-value: 7.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295821200 396 FLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 469
Cdd:COG3448 57 ALLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
411-469 |
9.29e-04 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 42.13 E-value: 9.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 295821200 411 HLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 469
Cdd:PRK14869 67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
|
|
| CBS_pair_IMPDH |
cd04601 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
422-460 |
9.80e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 38.93 E-value: 9.80e-04
10 20 30
....*....|....*....|....*....|....*....
gi 295821200 422 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 460
Cdd:cd04601 4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT 42
|
|
| MgtE |
COG2239 |
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; |
423-543 |
5.23e-03 |
|
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 39.28 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295821200 423 LTVLPTITCGHTIEILREKG-----FDQAPVVDEAGVILGMVTLGNMLSSllagkvQPSDQVGKVIYKQFKQIRLTDTLG 497
Cdd:COG2239 140 VAVREDWTVGEALRYLRRQAedpetIYYIYVVDDDGRLVGVVSLRDLLLA------DPDTKVSDIMDTDVISVPADDDQE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 295821200 498 RLSHILEM-DHFAL-VVHEqiqyhstgkssQRQMVfGVVTAIDLLNFV 543
Cdd:COG2239 214 EVARLFERyDLLALpVVDE-----------EGRLV-GIITVDDVVDVI 249
|
|
| CBS_pair_NTP_transferase_assoc |
cd04607 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
395-466 |
6.99e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 36.65 E-value: 6.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295821200 395 GFLKEEDLTEKkpwwwhlrVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLS 466
Cdd:cd04607 49 GLLKGLSLDAP--------VEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLLA 112
|
|
| CBS_pair_BON_assoc |
cd04586 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
422-460 |
8.95e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 36.64 E-value: 8.95e-03
10 20 30
....*....|....*....|....*....|....*....
gi 295821200 422 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 460
Cdd:cd04586 5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVS 43
|
|
| CBS_pair_arch1_repeat2 |
cd04632 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
422-461 |
1.00e-02 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; 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: 341395 [Multi-domain] Cd Length: 127 Bit Score: 36.54 E-value: 1.00e-02
10 20 30 40
....*....|....*....|....*....|....*....|
gi 295821200 422 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTL 461
Cdd:cd04632 4 VITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTT 43
|
|
| |
