|
Name |
Accession |
Description |
Interval |
E-value |
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
1-439 |
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: 777.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:TIGR01137 29 LAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKCIIVLPEKMSSEKVDVLRALG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 81 AEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:TIGR01137 109 AEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 161 RKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:TIGR01137 189 RYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 241 CGGSAGSTVAVAVKAAQ-ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLT 319
Cdd:TIGR01137 269 VGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDNGFLDDEDLTVKDVLWWHARVKDLHLPAPVT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 320 VLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILE 399
Cdd:TIGR01137 349 VHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQPSDAVSKVMSKKFIQIGLGETLSDLSKFLE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1007358255 400 MDHFALVVHEQIQyhstgkssqrqmvFGVVTAIDLLNFVA 439
Cdd:TIGR01137 429 MDSSAIVVEEGKP-------------IGVVTKIDLLSFLA 455
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
1-278 |
3.28e-157 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 446.19 E-value: 3.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:cd01561 20 YAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 81 AEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:cd01561 100 AEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGKVDAFVAGVGTGGTITGVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 161 RKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:cd01561 179 RYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEAFAMARRLAREEGLL 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 1007358255 241 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 278
Cdd:cd01561 254 VGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
2-279 |
2.54e-144 |
|
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: 413.68 E-value: 2.54e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:COG0031 32 AKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:COG0031 112 EVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIWEQTDGKVDAFVAGVGTGGTITGVGR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 162 KLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLC 241
Cdd:COG0031 189 YLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILV 263
|
250 260 270
....*....|....*....|....*....|....*...
gi 1007358255 242 GGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 279
Cdd:COG0031 264 GISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
2-278 |
1.18e-106 |
|
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273465 Cd Length: 298 Bit Score: 317.77 E-value: 1.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:TIGR01139 25 VKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGYKLILTMPETMSIERRKLLKAYGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:TIGR01139 105 ELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWRDTDGKLDAFVAGVGTGGTITGVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 161 RKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:TIGR01139 182 EVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSDEEAIETARRLAAEEGIL 256
|
250 260 270
....*....|....*....|....*....|....*...
gi 1007358255 241 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 278
Cdd:TIGR01139 257 VGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
2-291 |
1.76e-106 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 318.73 E-value: 1.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:PRK10717 32 GKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTI 156
Cdd:PRK10717 112 ELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPANREAHYETTGPEIWEQTDGKVDGFVCAVGTGGTL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 157 TGIARKLKEKCPGCRIIGVDPEGSIL----AEPEELNQTEQTTyevEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARM 232
Cdd:PRK10717 191 AGVSRYLKETNPKVKIVLADPTGSALysyyKTGELKAEGSSIT---EGIGQGRITANLEGAPIDDAIRIPDEEALSTAYR 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1007358255 233 LIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGF 291
Cdd:PRK10717 268 LLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLREKGL 326
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
2-278 |
3.53e-102 |
|
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: 306.52 E-value: 3.53e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:TIGR01136 26 AKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAARGYKLILTMPETMSLERRKLLRAYGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTIT 157
Cdd:TIGR01136 106 ELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKTTGPEIWRDTDGRIDHFVAGVGTGGTIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 158 GIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQE 237
Cdd:TIGR01136 179 GVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDEDAIETARRLAREE 253
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1007358255 238 GLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMT 278
Cdd:TIGR01136 254 GILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
2-272 |
4.14e-78 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 242.81 E-value: 4.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLkPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:cd00640 19 LKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDG-KLDMLVASVGTGGTITGIA 160
Cdd:cd00640 98 EVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqKPDAVVVPVGGGGNIAGIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 161 RKLKEKCPGCRIIGVDPEgsilaepeelnqteqttyevegigydfiptvldrtvvdkWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:cd00640 172 RALKELLPNVKVIGVEPE---------------------------------------VVTVSDEEALEAIRLLAREEGIL 212
|
250 260 270
....*....|....*....|....*....|..
gi 1007358255 241 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDS 272
Cdd:cd00640 213 VEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
2-271 |
6.27e-74 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 233.74 E-value: 6.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERdgtLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:pfam00291 26 LKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:pfam00291 103 EVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQLGGDPDAVVVPVGGGGLIAGIAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 162 KLKEKCPGCRIIGVDPEGS-ILAEPEELNQTEQTT---YEVEGIGYDFIPTVLDRTVVDKWFKS----NDEEAFTFARML 233
Cdd:pfam00291 177 GLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGALALDLLDEYVGEvvtvSDEEALEAMRLL 256
|
250 260 270
....*....|....*....|....*....|....*....
gi 1007358255 234 IAQEGLLCGGSAGSTVAVA-VKAAQELQEGQRCVVILPD 271
Cdd:pfam00291 257 ARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
2-271 |
9.25e-74 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 233.23 E-value: 9.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:PRK11761 31 AKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYRMKLIMPENMSQERRAAMRAYGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:PRK11761 111 ELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTGPEIWRQTEGRITHFVSSMGTTGTIMGVSR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 162 KLKEKCPGCRIIGVDP-EGS----ILAEPEElnqteqttyevegigydFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQ 236
Cdd:PRK11761 187 YLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLPKIFDASRVDRVLDVSQQEAENTMRRLARE 249
|
250 260 270
....*....|....*....|....*....|....*
gi 1007358255 237 EGLLCGGSAGSTVAVAVKAAQELqEGQRCVVILPD 271
Cdd:PRK11761 250 EGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICD 283
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
2-283 |
2.91e-73 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 233.28 E-value: 2.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN02565 34 AKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAFMAAAKGYKLIITMPASMSLERRIILLAFG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 81 AEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGI 159
Cdd:PLN02565 114 AELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEIWKGTGGKVDAFVSGIGTGGTITGA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 160 ARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGL 239
Cdd:PLN02565 190 GKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQVSSDEAIETAKLLALKEGL 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1007358255 240 LCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 283
Cdd:PLN02565 265 LVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
2-285 |
5.24e-73 |
|
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme. [Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274872 [Multi-domain] Cd Length: 304 Bit Score: 231.71 E-value: 5.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:TIGR03945 26 AKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYKGLRFICVVDPNISPQNLKLLRAYGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDgKLDMLVASVGTG 153
Cdd:TIGR03945 106 EVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRAHYHGTGREIARAFP-TLDYLFVGVSTT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 154 GTITGIARKLKEKCPGCRIIGVDPEGSIL--AEPeelnqteqTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFAR 231
Cdd:TIGR03945 178 GTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGASVVPELLDESLIDDVVHVPEYDTVAGCR 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1007358255 232 MLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRW 285
Cdd:TIGR03945 250 RLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEW 303
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
2-283 |
6.03e-66 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 214.10 E-value: 6.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPG-DTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN00011 36 AKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIILRALG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 81 AEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGG 154
Cdd:PLN00011 116 AEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEIHYRTTGPEIWRDSAGKVDILVAGVGTGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 155 TITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLI 234
Cdd:PLN00011 187 TATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQVTGEEAIETAKLLA 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1007358255 235 AQEGLLCGGSAGSTVAVAVKAAQELQE-GQRCVVILPDSVRNYMTKFLSD 283
Cdd:PLN00011 262 LKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYLSTKLFE 311
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
2-278 |
7.51e-66 |
|
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 212.85 E-value: 7.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:TIGR01138 27 LKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERKAAMRAYGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:TIGR01138 107 ELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPEIWQQTGGRITHFVSSMGTTGTIMGVSR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 162 KLKEKCPGCRIIGVDPEgsilaEPeelnqteqttYEVEGIGY---DFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEG 238
Cdd:TIGR01138 183 FLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFDASLVDRVLDIHQRDAENTMRELAVREG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1007358255 239 LLCGGSAGSTVAVAVKAAQELQEGQrCVVILPDSVRNYMT 278
Cdd:TIGR01138 248 IFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
2-289 |
7.14e-64 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 211.94 E-value: 7.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN03013 142 AKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAFIAASRGYRLILTMPASMSMERRVLLKAFG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 81 AEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTI 156
Cdd:PLN03013 222 AELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPKIHYETTGPEIWDDTKGKVDIFVAGIGTGGTI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 157 TGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQ 236
Cdd:PLN03013 295 TGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVIAISSEEAIETAKQLALK 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1007358255 237 EGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK--FLSDRWMLQK 289
Cdd:PLN03013 370 EGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIYTprCSSLSGKRWR 424
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
2-283 |
1.05e-59 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 199.42 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDT-IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN02556 78 AKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 81 AEIVRT-PTNARFDSpeshVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGI 159
Cdd:PLN02556 158 AELVLTdPTKGMGGT----VKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 160 ARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGL 239
Cdd:PLN02556 234 GKYLKSKNPNVKIYGVEP-----AESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGL 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1007358255 240 LCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 283
Cdd:PLN02556 309 MVGISSGANTVAALRLAKMPEnKGKLIVTVHPSFGERYLSSVLFQ 353
|
|
| CBS_pair_CBS |
cd04608 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
307-437 |
7.93e-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: 180.81 E-value: 7.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 307 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 386
Cdd:cd04608 2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1007358255 387 LTDTLGRLSHILEMDHFALVVHEQiqyhstgkssqrQMVFGVVTAIDLLNF 437
Cdd:cd04608 82 LDTPLGALSRILERDHFALVVDGQ------------GKVLGIVTRIDLLNY 120
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
1-291 |
3.49e-48 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 170.56 E-value: 3.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN02356 71 LGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKCHVVIPDDVAIEKSQILEALG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 81 AEIVRT-PTNarFDSPESHVGVAWRLK---NEIP-----------------NSHIL-------------------DQYRN 120
Cdd:PLN02356 151 ATVERVrPVS--ITHKDHYVNIARRRAleaNELAskrrkgsetdgihlektNGCISeeekenslfsssctggffaDQFEN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 121 ASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL--------------AEPE 186
Cdd:PLN02356 229 LANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGSGLfnkvtrgvmytreeAEGR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 187 ELNQTEQTTyeVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCV 266
Cdd:PLN02356 309 RLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNCVGAVRVAQSLGPGHTIV 386
|
330 340
....*....|....*....|....*
gi 1007358255 267 VILPDSVRNYMTKFLSDRWMLQKGF 291
Cdd:PLN02356 387 TILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
3-269 |
2.28e-26 |
|
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: 107.96 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMI----EDAERDGtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRA 78
Cdd:cd01562 37 KCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 79 LGAEIVRTptNARFDSPESHvgvAWRLKNEIPNSHIldqyrnasNPLAHYD------TTADEILQQCdGKLDMLVASVGT 152
Cdd:cd01562 110 YGAEVVLY--GEDFDEAEAK---ARELAEEEGLTFI--------HPFDDPDviagqgTIGLEILEQV-PDLDAVFVPVGG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 153 GGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTEQTtyeVEGIGydfIPTVLDRT------VVDKWF 219
Cdd:cd01562 176 GGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTI---ADGLA---VKRPGELTfeiirkLVDDVV 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1007358255 220 KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 269
Cdd:cd01562 250 TVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
3-269 |
2.44e-26 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 108.59 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDR------ISLRmieDAERDGTlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVL 76
Cdd:COG1171 44 KLENLQPTGSFKLRgaynalASLS---EEERARG------VVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAAT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 77 RALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKLDM 145
Cdd:COG1171 115 RAYGAEVVLHGDT--YDDAEAA---AAELAEEegatfVH-------------PFDDPDviagqgTIALEILEQL-PDLDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 146 LVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTeQT------TYEVEGIGYDFIPTVLDR 212
Cdd:COG1171 176 VFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTiadglaVGRPGELTFEILRDLVDD 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1007358255 213 TV-VDkwfksnDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 269
Cdd:COG1171 255 IVtVS------EDEIAAAMRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVVL 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
3-269 |
1.43e-25 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 106.32 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRAL 79
Cdd:PRK06815 40 KCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 80 GAEIVRTPTNArfDSPESHvgvAWRLKNEIPNSHIlDQYrNASNPLAHYDTTADEILQQCDgKLDMLVASVGTGGTITGI 159
Cdd:PRK06815 114 GAEVRLYGGDA--LNAELA---ARRAAEQQGKVYI-SPY-NDPQVIAGQGTIGMELVEQQP-DLDAVFVAVGGGGLISGI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 160 ARKLKEKCPGCRIIGVDPEG------SILA----EPEELNQTEQTTyeVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTF 229
Cdd:PRK06815 186 ATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTLSDGT--AGGVEPGAITFPLCQQLIDQKVLVSEEEIKEA 263
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1007358255 230 ARMLIAQEGLLCGGSAGSTVAVAVKAAQELQeGQRCVVIL 269
Cdd:PRK06815 264 MRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
|
|
| PLN02970 |
PLN02970 |
serine racemase |
3-180 |
4.81e-16 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 78.95 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMI-----EDAERDgtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLR 77
Cdd:PLN02970 47 KCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 78 ALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDTTADEILQQCDGkLDMLVASVGTGGTI 156
Cdd:PLN02970 119 RYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLEQVPE-LDVIIVPISGGGLI 189
|
170 180
....*....|....*....|....
gi 1007358255 157 TGIARKLKEKCPGCRIIGVDPEGS 180
Cdd:PLN02970 190 SGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
3-269 |
3.19e-15 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 76.09 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:cd01563 43 KDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGAT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 83 IVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLAH--YDTTADEILQQCDGKL-DMLVASVGTGGTITGI 159
Cdd:cd01563 119 VLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYRLegQKTIAFEIAEQLGWEVpDYVVVPVGNGGNITAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 160 ARKLKE--------KCPgcRIIGVDPEGS------ILAEPEELNQTEQTTYEVEGIGydfIPT-VLDRTVVDKWFKSN-- 222
Cdd:cd01563 189 WKGFKElkelglidRLP--RMVGVQAEGAapivraFKEGKDDIEPVENPETIATAIR---IGNpASGPKALRAVRESGgt 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1007358255 223 ----DEEAFTFARMLIAQ-EGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVIL 269
Cdd:cd01563 264 avavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiIDKGERVVVVL 317
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
3-269 |
1.26e-14 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 74.36 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK06381 36 KFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 83 IVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGI 159
Cdd:PRK06381 112 IIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAYEIYEALGDVPDAVAVPVGNGTTLAGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 160 ARKLKE--------KCPgcRIIGVDPEGS--------------ILAEPEELNQTEQTTYEVEGIGYDFiPTVLD--RTVV 215
Cdd:PRK06381 184 YHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRETAVNEPLVSYRSFDG-DNALEaiYDSH 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1007358255 216 DKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVIL 269
Cdd:PRK06381 261 GYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
3-180 |
1.86e-14 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 73.84 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMIEDAErdgtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK08246 42 KLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 83 IVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDTTADEILQQCdGKLDMLVASVGTGGTIT 157
Cdd:PRK08246 117 VVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGGGGLIA 183
|
170 180
....*....|....*....|...
gi 1007358255 158 GIARKLKekcPGCRIIGVDPEGS 180
Cdd:PRK08246 184 GIAAWFE---GRARVVAVEPEGA 203
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
43-180 |
6.45e-14 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 73.63 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 43 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 117
Cdd:PRK09224 77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007358255 118 yrnasnPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 180
Cdd:PRK09224 145 ------PFDDPDviagqgTIAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
3-178 |
9.50e-14 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 71.97 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDR---ISLRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRAL 79
Cdd:PRK07048 44 KCENFQRMGAFKFRgayNALSQFSPEQR----RAG--VVTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 80 GAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKLDMLV 147
Cdd:PRK07048 118 GGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELFEEV-GPLDALF 177
|
170 180 190
....*....|....*....|....*....|.
gi 1007358255 148 ASVGTGGTITGIARKLKEKCPGCRIIGVDPE 178
Cdd:PRK07048 178 VCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
37-180 |
4.20e-13 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 70.98 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 37 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEIPNS--HI 114
Cdd:PRK12483 88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAH---ALKLAEEEGLTfvPP 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1007358255 115 LDQyrnaSNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 180
Cdd:PRK12483 163 FDD----PDVIAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
3-276 |
1.52e-12 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 68.69 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDR-----ISLrmiedAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVL 76
Cdd:COG0498 86 KEEGHNPTGSFKDRamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQLAQM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 77 RALGAEIVRTPTNarFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPLAH--YDTTADEILQQCDGKLDMLVASVGTG 153
Cdd:COG0498 157 LTYGAHVIAVDGN--FD-------DAQRLVKELAADEGL--YaVNSINPARLegQKTYAFEIAEQLGRVPDWVVVPTGNG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 154 GTITGI--ARK------LKEKCPgcRIIGVDPEGS--ILAEPEelnqTEQTTYEVEG---------IGydfIPT------ 208
Cdd:COG0498 226 GNILAGykAFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPERpetiapsmdIG---NPSngeral 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007358255 209 -VLDRTvvDKWF-KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVIL-------PDSVRNY 276
Cdd:COG0498 297 fALRES--GGTAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVVVLStghglkfPDAVREA 373
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
3-177 |
6.41e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 63.25 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMIEDAERDGtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK06608 43 KVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 83 IVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITG- 158
Cdd:PRK06608 121 VILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTLCYEALQQLGFSPDAIFASCGGGGLISGt 188
|
170 180
....*....|....*....|
gi 1007358255 159 -IARKLKEkcPGCRIIGVDP 177
Cdd:PRK06608 189 yLAKELIS--PTSLLIGSEP 206
|
|
| CBS |
smart00116 |
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
317-364 |
3.08e-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: 52.52 E-value: 3.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1007358255 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:smart00116 2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
317-400 |
6.76e-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: 53.40 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTlgrLSH 396
Cdd:cd02205 4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTD---LEE 80
|
....
gi 1007358255 397 ILEM 400
Cdd:cd02205 81 ALEL 84
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
37-178 |
9.98e-09 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 56.67 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 37 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILD 116
Cdd:PRK08638 78 VVACSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIP 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007358255 117 QYrNASNPLAHYDTTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 178
Cdd:PRK08638 152 PY-DDPKVIAGQGTIGLEILEDL-WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
130-179 |
1.94e-08 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 55.97 E-value: 1.94e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1007358255 130 TTADEILQQCD--GKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG 179
Cdd:PRK08639 165 TVAVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
36-178 |
4.36e-08 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 54.88 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 36 TIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDspEShVGVAWRLKNEipNSHIL 115
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN--YD--DS-VRLAAQEAQE--NGWVV 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007358255 116 DQyrNASNP---------LAHYDTTADEILQQCDGKLD-----MLVASVGT--GGTITGIARKLKEKCPgcRIIGVDPE 178
Cdd:PRK08206 191 VQ--DTAWEgyeeiptwiMQGYGTMADEAVEQLKEMGVppthvFLQAGVGSlaGAVLGYFAEVYGEQRP--HFVVVEPD 265
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
12-177 |
9.37e-08 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 54.16 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 12 SVKDRISLRMIEDAERDgTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNar 91
Cdd:PLN02550 138 SFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDS-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 92 FDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKE 165
Cdd:PLN02550 213 YDEAQAYA-----------KQRALEEGRTFIPPFDHPDviagqgTVGMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKR 281
|
170
....*....|..
gi 1007358255 166 KCPGCRIIGVDP 177
Cdd:PLN02550 282 VRPEVKIIGVEP 293
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
307-441 |
2.18e-07 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 49.48 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 307 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQI 385
Cdd:COG0517 1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTpVSEVMTRPPVTV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1007358255 386 RLTDTLGRLSHILEMDHF--ALVVHEQIQyhstgkssqrqmVFGVVTAIDLLNFVAAQ 441
Cdd:COG0517 81 SPDTSLEEAAELMEEHKIrrLPVVDDDGR------------LVGIITIKDLLKALLEP 126
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
317-445 |
2.45e-07 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 49.48 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQ------PSDQVGKVIYKQFKQIRLTDT 390
Cdd:COG3448 12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlLDLPVEDVMTRPVVTVTPDTP 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1007358255 391 LGRLSHILeMD---HFALVVHEQiqyhstGKssqrqmVFGVVTAIDLLNFVAAQERDQ 445
Cdd:COG3448 92 LEEAAELM-LEhgiHRLPVVDDD------GR------LVGIVTRTDLLRALARLLEEE 136
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
2-166 |
5.13e-07 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 51.23 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 2 AKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVLRALG 80
Cdd:TIGR00260 42 VKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAgKISLGKLAQALGYN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 81 AEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnSHILDQYrnasnplahydTTADEILQQCDGKL-DMLVASVG 151
Cdd:TIGR00260 118 AEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-YRLEGQK-----------TYAFEAVEQLGWEApDKVVVPVP 183
|
170
....*....|....*
gi 1007358255 152 TGGTITGIARKLKEK 166
Cdd:TIGR00260 184 NSGNFGAIWKGFKEK 198
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
3-178 |
5.43e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 51.27 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK06450 70 KLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 83 IVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYRNASNPLAHydttadEILQQCDGKL-DMLVASVGTGGTI 156
Cdd:PRK06450 146 VVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFRDGIRTLAY------EIAKDLDWKIpNYVFIPVSAGTLL 209
|
170 180 190
....*....|....*....|....*....|
gi 1007358255 157 TGIARKLK--------EKCPgcRIIGVDPE 178
Cdd:PRK06450 210 LGVYSGFKhlldsgviSEMP--KIVAVQTE 237
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
3-180 |
8.05e-07 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 50.76 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDR-ISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:cd06448 21 KLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 82 EIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDTTADEILQQC--DGKLDMLVASVGTGGTIT 157
Cdd:cd06448 99 TVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQQLqsQEKVDAIVCSVGGGGLLN 171
|
170 180
....*....|....*....|....*
gi 1007358255 158 GIARKLkEKCPGCR--IIGVDPEGS 180
Cdd:cd06448 172 GIVQGL-ERNGWGDipVVAVETEGA 195
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
11-84 |
8.62e-07 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 50.76 E-value: 8.62e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007358255 11 GSVKDRISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIV 84
Cdd:PRK06110 49 GAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELI 120
|
|
| CBS |
pfam00571 |
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
309-364 |
1.08e-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: 45.67 E-value: 1.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1007358255 309 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:pfam00571 1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
37-178 |
1.66e-06 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 49.89 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 37 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEipnshild 116
Cdd:PRK07334 74 VIAMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLH--GETLDEARAH---ARELAEE-------- 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007358255 117 QYRNASNPLAHYD------TTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 178
Cdd:PRK07334 141 EGLTFVHPYDDPAviagqgTVALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTE 207
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
307-438 |
1.83e-06 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 48.34 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 307 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEaGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 386
Cdd:COG2524 86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTVS 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1007358255 387 LTDTLGRLSHILEmDH---FALVVHEQiqyhstGKssqrqmVFGVVTAIDLLNFV 438
Cdd:COG2524 165 EDDSLEEALRLML-EHgigRLPVVDDD------GK------LVGIITRTDILRAL 206
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
309-436 |
1.00e-05 |
|
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: 43.86 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 309 VQELGLSAPLTVLPTITCGHTIEILREK-GFDQAPVVDEAGvilgmVTLgNMLSSLLAGKVQPSdqvgkviykqfkqirl 387
Cdd:COG3620 1 VRDLMSRDVVTVSPDDTLGEALRLMRKElGLSQLPVAELVG-----VSQ-SDILRIESGKRDPT---------------- 58
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1007358255 388 TDTLGRLSHILEMDHFALVVHEQIQYHstgkssqrqmvfGVVTAIDLLN 436
Cdd:COG3620 59 VSTLEKIAEALGKELSAVLVVDDGKLV------------GIITRRDLLK 95
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
309-441 |
2.66e-05 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 43.28 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 309 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQIRL 387
Cdd:COG2905 1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1007358255 388 TDTLGRLSHILEMDHF-ALVVHEQiqyhstGKssqrqmVFGVVTAIDLLNFVAAQ 441
Cdd:COG2905 81 DDSLAEALELMEEHRIrHLPVVDD------GK------LVGIVSITDLLRALSEE 123
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
3-179 |
2.85e-05 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 45.97 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK08329 77 KLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 83 IvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRnasnpLAHYDTTADEILQQCdGKLDMLVASVGTGGTITGIA 160
Cdd:PRK08329 153 L----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYF-----LEGTKTIAYEIYEQI-GVPDYAFVPVGSGTLFLGIW 222
|
170 180
....*....|....*....|....*..
gi 1007358255 161 RKLKE--------KCPgcRIIGVDPEG 179
Cdd:PRK08329 223 KGFKElhemgeisKMP--KLVAVQAEG 247
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
24-175 |
4.20e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 45.21 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 24 DAERDGTlkpgDTIIepTSGntGIG-----LALAAAVR-GYRCIIVMPEKMSSEKVDVL--------RALGAEIVRTPTN 89
Cdd:PRK03910 58 DALAQGA----DTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 90 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDTTADEILQQCDG---KLDMLVASVGTGGTITG 158
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
|
170
....*....|....*..
gi 1007358255 159 IARKLKEKCPGCRIIGV 175
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV 216
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
20-86 |
5.57e-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: 44.90 E-value: 5.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 20 RMIEDAerdGTLKPGDTIIEpTSGNTGIGLALA--AAVRGYRCIIVMPEKMSSEK-VDVLRALGAEIVRT 86
Cdd:cd08290 136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
43-175 |
6.75e-05 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 44.57 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 43 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPtnarfDSPESHVGVAWRLKNE-----IPnshildq 117
Cdd:PRK07476 76 GNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVG-----RSQDDAQAEVERLVREegltmVP------- 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007358255 118 yrnasnPLAHYD------TTADEILQQCDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGV 175
Cdd:PRK07476 144 ------PFDDPRiiagqgTIGLEILEALP-DVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGV 200
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
297-364 |
7.78e-05 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 42.16 E-value: 7.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007358255 297 LTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:COG0517 57 LAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
290-364 |
8.39e-05 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 42.21 E-value: 8.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007358255 290 GFLKEEDLTEKKPwwwHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:COG4109 62 GIVTSKDILGKDD---DTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
317-410 |
1.51e-04 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 41.44 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLssllagKVQPSDQVGKVIYKQFKQIRLTDTLGRLSH 396
Cdd:COG4109 27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVTPDTSLASAAH 100
|
90
....*....|....*.
gi 1007358255 397 ILEMDHFAL--VVHEQ 410
Cdd:COG4109 101 KMIWEGIELlpVVDDD 116
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
290-360 |
1.78e-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: 40.69 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007358255 290 GFLKEEDLTEK---KPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNML 360
Cdd:cd02205 39 GIVTERDILRAlveGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
226-363 |
3.09e-04 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 41.79 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 226 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRcVVILPDSVRNYMTKF---------LSD--RWMLQK----- 289
Cdd:COG2524 42 LLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL-GLVLKMKVKDIMTKDvitvspdttLEEalELMLEKgisgl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 290 ---------GFLKEEDL---TEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLG 357
Cdd:COG2524 121 pvvddgklvGIITERDLlkaLAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRT 200
|
....*.
gi 1007358255 358 NMLSSL 363
Cdd:COG2524 201 DILRAL 206
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
255-364 |
4.63e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 39.81 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 255 AAQELQE-GQRCVVILPDSvrNYMTKFLSDRWMLQKGFLKEEDLTEKKpwwwhlrVQELGLSAPLTVLPTITCGHTIEIL 333
Cdd:COG2905 21 AARLMTEkGVGSLVVVDDD--GRLVGIITDRDLRRRVLAEGLDPLDTP-------VSEVMTRPPITVSPDDSLAEALELM 91
|
90 100 110
....*....|....*....|....*....|.
gi 1007358255 334 REKGFDQAPVVDEaGVILGMVTLGNMLSSLL 364
Cdd:COG2905 92 EEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
3-272 |
7.88e-04 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 41.72 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK05638 85 KDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 83 IVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnasnpLAHYDTTADEILQQCDGklDMLVASVGTGGTITGI 159
Cdd:PRK05638 161 IIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG--------LEGQKTIAFELWEEINP--THVIVPTGSGSYLYSI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 160 ARKLKE--------KCPgcRIIGVDPE------GSILAEPEELNQTeqttyevEGIGYDFIPTVLDRTVVDKWFKS---- 221
Cdd:PRK05638 229 YKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKCNET-------KALGLYVKNPVMKEYVSEAIKESggta 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1007358255 222 --NDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVILPDS 272
Cdd:PRK05638 300 vvVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGS 354
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
306-364 |
8.57e-04 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 41.74 E-value: 8.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1007358255 306 HLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:PRK14869 67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
|
|
| CBS_pair_IMPDH |
cd04601 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
317-355 |
8.86e-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: 8.86e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1007358255 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 355
Cdd:cd04601 4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT 42
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
291-364 |
1.08e-03 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 39.08 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007358255 291 FLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:COG3448 57 ALLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
|
|
| CBS_pair_Mg_transporter |
cd04606 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ... |
318-435 |
1.68e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 38.08 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007358255 318 LTVLPTITCGHTIEILREKG-----FDQAPVVDEAGVILGMVTLGNMLSSllagkvQPSDQVGKVIYKQFKQIRLTDTLG 392
Cdd:cd04606 12 VAVRPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSLRDLLLA------DPDTKVSDIMDTDVISVSADDDQE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1007358255 393 RLSHILEM-DHFAL-VVHEqiqyhstgkssQRQMVfGVVT---AIDLL 435
Cdd:cd04606 86 EVARLFAKyDLLALpVVDE-----------EGRLV-GIITvddVLDVI 121
|
|
| CBS_pair_NTP_transferase_assoc |
cd04607 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
290-361 |
8.86e-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: 35.88 E-value: 8.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007358255 290 GFLKEEDLTEKkpwwwhlrVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLS 361
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 ... |
317-355 |
9.41e-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: 36.25 E-value: 9.41e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1007358255 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 355
Cdd:cd04586 5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVS 43
|
|
| |
