|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02565 |
PLN02565 |
cysteine synthase |
1-322 |
0e+00 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 588.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 1 MASRIAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGESVLIEPTSGNTGV 80
Cdd:PLN02565 1 EKSSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVLIEPTSGNTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 81 GLAFTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYET 160
Cdd:PLN02565 81 GLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 161 TGPEIWKGTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLI 240
Cdd:PLN02565 161 TGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 241 DEVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPENAGKLFVAIFPSFGERYLSTVLFDATRKEAEAMTF 320
Cdd:PLN02565 241 DEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKEAENMVF 320
|
..
gi 15233613 321 EA 322
Cdd:PLN02565 321 EP 322
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
9-308 |
4.59e-173 |
|
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: 481.48 E-value: 4.59e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 9 VTELIGNTPLVYLNNVaEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGEsVLIEPTSGNTGVGLAFTAAA 88
Cdd:TIGR01139 1 ISELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGK-TIVEPTSGNTGIALAMVAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 89 KGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGY-MLQQFENPANPKIHYETTGPEIWK 167
Cdd:TIGR01139 79 RGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 168 GTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLIDEVVQVS 247
Cdd:TIGR01139 159 DTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVS 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233613 248 SDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPEnAGKLFVAIFPSFGERYLSTVLF 308
Cdd:TIGR01139 239 DEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
4-305 |
1.92e-159 |
|
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: 447.19 E-value: 1.92e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 4 RIAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGeSVLIEPTSGNTGVGLA 83
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPG-GTIVEATSGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 84 FTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETTGP 163
Cdd:COG0031 81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 164 EIWKGTGGKIDGFV------------SgigtggtitgagKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFI 231
Cdd:COG0031 161 EIWEQTDGKVDAFVagvgtggtitgvG------------RYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFV 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233613 232 PSVLNVDLIDEVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRpENAGKLFVAIFPSFGERYLST 305
Cdd:COG0031 229 PKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
14-304 |
4.22e-148 |
|
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: 418.07 E-value: 4.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 14 GNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGeSVLIEPTSGNTGVGLAFTAAAKGYKL 93
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPG-TTIIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 94 IITMPASMSTERRIILLAFGVELVLTDPAK--GMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETTGPEIWKGTGG 171
Cdd:cd01561 80 IIVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 172 KIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLIDEVVQVSSDES 251
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15233613 252 IDMARQLALKEGLLVGISSGAAAAAAIKLAQRPEnAGKLFVAIFPSFGERYLS 304
Cdd:cd01561 240 FAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-271 |
4.57e-62 |
|
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: 199.07 E-value: 4.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 9 VTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKpgesVLIEPTSGNTGVGLAFTAAA 88
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGK----TVVEASSGNHGRALAAAAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 89 KGYKLIITMPASMSTERRIILLAFGVELVLTDPakGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIhYETTGPEIWKG 168
Cdd:pfam00291 77 LGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEILEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 169 TGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGG---------KPGPHKIQGIGAGFIPSVLNVDL 239
Cdd:pfam00291 154 LGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDL 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 15233613 240 I----DEVVQVSSDESIDMARQLALKEGLLVGISSG 271
Cdd:pfam00291 234 LdeyvGEVVTVSDEEALEAMRLLARREGIVVEPSSA 269
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02565 |
PLN02565 |
cysteine synthase |
1-322 |
0e+00 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 588.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 1 MASRIAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGESVLIEPTSGNTGV 80
Cdd:PLN02565 1 EKSSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVLIEPTSGNTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 81 GLAFTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYET 160
Cdd:PLN02565 81 GLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 161 TGPEIWKGTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLI 240
Cdd:PLN02565 161 TGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 241 DEVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPENAGKLFVAIFPSFGERYLSTVLFDATRKEAEAMTF 320
Cdd:PLN02565 241 DEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKEAENMVF 320
|
..
gi 15233613 321 EA 322
Cdd:PLN02565 321 EP 322
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
9-308 |
4.59e-173 |
|
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: 481.48 E-value: 4.59e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 9 VTELIGNTPLVYLNNVaEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGEsVLIEPTSGNTGVGLAFTAAA 88
Cdd:TIGR01139 1 ISELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGK-TIVEPTSGNTGIALAMVAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 89 KGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGY-MLQQFENPANPKIHYETTGPEIWK 167
Cdd:TIGR01139 79 RGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 168 GTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLIDEVVQVS 247
Cdd:TIGR01139 159 DTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVS 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233613 248 SDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPEnAGKLFVAIFPSFGERYLSTVLF 308
Cdd:TIGR01139 239 DEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
9-308 |
4.36e-166 |
|
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: 463.68 E-value: 4.36e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 9 VTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGEsVLIEPTSGNTGVGLAFTAAA 88
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGD-TIIEATSGNTGIALAMVAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 89 KGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETTGPEIWKG 168
Cdd:TIGR01136 80 RGYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 169 TGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLIDEVVQVSS 248
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 249 DESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPENAGKLFVAIFPSFGERYLSTVLF 308
Cdd:TIGR01136 240 EDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
5-321 |
6.85e-162 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 454.08 E-value: 6.85e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 5 IAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGESVLIEPTSGNTGVGLAF 84
Cdd:PLN00011 7 IKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEATAGNTGIGLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 85 TAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETTGPE 164
Cdd:PLN00011 87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 165 IWKGTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLIDEVV 244
Cdd:PLN00011 167 IWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEII 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233613 245 QVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPENAGKLFVAIFPSFGERYLSTVLFDATRKEAEAMTFE 321
Cdd:PLN00011 247 QVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAENLPIE 323
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
4-305 |
1.92e-159 |
|
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: 447.19 E-value: 1.92e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 4 RIAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGeSVLIEPTSGNTGVGLA 83
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPG-GTIVEATSGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 84 FTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETTGP 163
Cdd:COG0031 81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 164 EIWKGTGGKIDGFV------------SgigtggtitgagKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFI 231
Cdd:COG0031 161 EIWEQTDGKVDAFVagvgtggtitgvG------------RYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFV 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233613 232 PSVLNVDLIDEVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRpENAGKLFVAIFPSFGERYLST 305
Cdd:COG0031 229 PKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
5-321 |
3.33e-153 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 436.52 E-value: 3.33e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 5 IAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGESVLIEPTSGNTGVGLAF 84
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVLVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 85 TAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETTGPE 164
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTGPE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 165 IWKGTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLIDEVV 244
Cdd:PLN03013 273 IWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVI 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233613 245 QVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPENAGKLFVAIFPSFGeRYLSTVLFDATRKEAEAMTFE 321
Cdd:PLN03013 353 AISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRWRKCSL 428
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
2-318 |
8.44e-152 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 430.54 E-value: 8.44e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 2 ASRIAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGESVLIEPTSGNTGVG 81
Cdd:PLN02556 46 GTKIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLIEPTSGNMGIS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 82 LAFTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETT 161
Cdd:PLN02556 126 LAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 162 GPEIWKGTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLID 241
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVME 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233613 242 EVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPENAGKLFVAIFPSFGERYLSTVLFDATRKEAEAM 318
Cdd:PLN02556 286 KVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAENM 362
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
14-304 |
4.22e-148 |
|
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: 418.07 E-value: 4.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 14 GNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGeSVLIEPTSGNTGVGLAFTAAAKGYKL 93
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPG-TTIIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 94 IITMPASMSTERRIILLAFGVELVLTDPAK--GMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETTGPEIWKGTGG 171
Cdd:cd01561 80 IIVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 172 KIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLIDEVVQVSSDES 251
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15233613 252 IDMARQLALKEGLLVGISSGAAAAAAIKLAQRPEnAGKLFVAIFPSFGERYLS 304
Cdd:cd01561 240 FAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
3-308 |
2.02e-108 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 318.73 E-value: 2.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 3 SRIAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGeSVLIEPTSGNTGVGL 82
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPG-GTIVEGTAGNTGIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 83 AFTAAAKGYKLIITMPASMSTERRIILLAFGVELVLT------DPAKGMKGAIAKAEEILAKTPNGY-MLQQFENPANPK 155
Cdd:PRK10717 80 ALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVpaapyaNPNNYVKGAGRLAEELVASEPNGAiWANQFDNPANRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 156 IHYETTGPEIWKGTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAI----LSG--GKPGPHKIQGIGAG 229
Cdd:PRK10717 160 AHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGelKAEGSSITEGIGQG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15233613 230 FIPSVLNVDLIDEVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAqRPENAGKLFVAIFPSFGERYLSTVLF 308
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLA-RELGPGHTIVTILCDSGERYQSKLFN 317
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
11-310 |
5.44e-96 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 286.00 E-value: 5.44e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 11 ELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGEsVLIEPTSGNTGVGLAFTAAAKG 90
Cdd:PRK11761 8 DTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGD-TLIEATSGNTGIALAMIAAIKG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 91 YKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTpNGYMLQQFENPANPKIHYETTGPEIWKGTG 170
Cdd:PRK11761 87 YRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEG-EGKVLDQFANPDNPLAHYETTGPEIWRQTE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 171 GKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVE-SAIlsggkPGphkIQGIGAGFIPSVLNVDLIDEVVQVSSD 249
Cdd:PRK11761 166 GRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEgSSI-----PG---IRRWPEEYLPKIFDASRVDRVLDVSQQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233613 250 ESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPENAgkLFVAIFPSFGERYLSTVLFDA 310
Cdd:PRK11761 238 EAENTMRRLAREEGIFCGVSSGGAVAAALRIARENPNA--VIVAIICDRGDRYLSTGVFPA 296
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
5-310 |
7.60e-91 |
|
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: 278.22 E-value: 7.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 5 IAKDVTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGeSVLIEPTSGNTGVGLAF 84
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPG-DTIIEPTSGNTGIGLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 85 TAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGM---KGAIAKAEEILAKTPNGYMLQQFENPANPKIHYETT 161
Cdd:TIGR01137 80 VAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 162 GPEIWKGTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPvESAILSGGKP------GPHKIQGIGAGFIPSVL 235
Cdd:TIGR01137 160 GPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADP-EGSILAQPEElnqtgrTPYKVEGIGYDFIPTVL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233613 236 NVDLIDEVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPENAGKLFVAIFPSFGERYLSTVLFDA 310
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMTKFLNDE 313
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
9-308 |
3.97e-88 |
|
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: 265.62 E-value: 3.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 9 VTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGEsVLIEPTSGNTGVGLAFTAAA 88
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGD-VLIEATSGNTGIALAMIAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 89 KGYKLIITMPASMSTERRIILLAFGVELVLTDPAKGMKGAIAKAEEILAKTPnGYMLQQFENPANPKIHYETTGPEIWKG 168
Cdd:TIGR01138 81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGE-GKLLDQFNNPDNPYAHYTSTGPEIWQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 169 TGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGgkpgphkIQGIGAGFIPSVLNVDLIDEVVQVSS 248
Cdd:TIGR01138 160 TGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDIHQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 249 DESIDMARQLALKEGLLVGISSGAAAAAAIKLAQrpENAGKLFVAIFPSFGERYLSTVLF 308
Cdd:TIGR01138 233 RDAENTMRELAVREGIFCGVSSGGAVAAALRLAR--ELPDAVVVAIICDRGDRYLSTGVF 290
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-271 |
4.57e-62 |
|
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: 199.07 E-value: 4.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 9 VTELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKpgesVLIEPTSGNTGVGLAFTAAA 88
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGK----TVVEASSGNHGRALAAAAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 89 KGYKLIITMPASMSTERRIILLAFGVELVLTDPakGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIhYETTGPEIWKG 168
Cdd:pfam00291 77 LGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEILEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 169 TGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGG---------KPGPHKIQGIGAGFIPSVLNVDL 239
Cdd:pfam00291 154 LGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDL 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 15233613 240 I----DEVVQVSSDESIDMARQLALKEGLLVGISSG 271
Cdd:pfam00291 234 LdeyvGEVVTVSDEEALEAMRLLARREGIVVEPSSA 269
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
16-296 |
1.77e-61 |
|
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: 195.81 E-value: 1.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 16 TPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGesVLIEPTSGNTGVGLAFTAAAKGYKLII 95
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKG--VIIESTGGNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 96 TMPASMSTERRIILLAFGVELVLTDPakGMKGAIAKAEEILAKTPNGYMLQQFENPANPKIHYeTTGPEIWK-------- 167
Cdd:cd00640 79 VMPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEqlggqkpd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 168 ------GTGGKIDGFVsgigtggtitgagKYLKEQNANVKLYGVEPvesailsggkpgphkiqgigagfipsvlnvdlid 241
Cdd:cd00640 156 avvvpvGGGGNIAGIA-------------RALKELLPNVKVIGVEP---------------------------------- 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15233613 242 EVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQRPeNAGKLFVAIFP 296
Cdd:cd00640 189 EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL-GKGKTVVVILT 242
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
11-304 |
2.01e-32 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 124.72 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 11 ELIGNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMISDAEKKGLIKPGeSVLIEPTSGNTGVGLAFTAAAKG 90
Cdd:PLN02356 49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPG-GVVTEGSAGSTAISLATVAPAYG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 91 YKLIITMPASMSTERRIILLAFG--VELVL-----------------TDPAKGMKGAIAKAEEILAK------------- 138
Cdd:PLN02356 128 CKCHVVIPDDVAIEKSQILEALGatVERVRpvsithkdhyvniarrrALEANELASKRRKGSETDGIhlektngciseee 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 139 ---------TPNGYMLQQFENPANPKIHYETTGPEIWKGTGGKIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVE 209
Cdd:PLN02356 208 kenslfsssCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 210 SAILSG-------------GK----PGPHKIQGIGAGFIPSVLNVDLIDEVVQVSSDESIDMARQLALKEGLLVGISSGA 272
Cdd:PLN02356 288 SGLFNKvtrgvmytreeaeGRrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAM 367
|
330 340 350
....*....|....*....|....*....|..
gi 15233613 273 AAAAAIKLAQRPeNAGKLFVAIFPSFGERYLS 304
Cdd:PLN02356 368 NCVGAVRVAQSL-GPGHTIVTILCDSGMRHLS 398
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
2-266 |
5.23e-10 |
|
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: 59.42 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 2 ASRIAKDVTElignTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMIS----DAEKKGLIKPgesvliepTSGN 77
Cdd:cd01562 8 AARIKPVVRR----TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLslseEERAKGVVAA--------SAGN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 78 TGVGLAFTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPakGMKGAIAKAEEILAKTpnGYMlqqFENPANpkiH 157
Cdd:cd01562 76 HAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGE--DFDEAEAKARELAEEE--GLT---FIHPFD---D 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 158 YE------TTGPEIWK------------GTGGKIDGfVSGigtggtitgagkYLKEQNANVKLYGVEPVESAILS----G 215
Cdd:cd01562 146 PDviagqgTIGLEILEqvpdldavfvpvGGGGLIAG-IAT------------AVKALSPNTKVIGVEPEGAPAMAqslaA 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15233613 216 GKPGPHKIQGI----GAGFIPSVLNVDLI----DEVVQVSSDESIDMARQLALKEGLLV 266
Cdd:cd01562 213 GKPVTLPEVDTiadgLAVKRPGELTFEIIrklvDDVVTVSEDEIAAAMLLLFEREKLVA 271
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
14-283 |
5.51e-10 |
|
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: 59.53 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 14 GNTPLVYLNNVAE-GCVGRVAAKLEMMEPCSSVKDRiGFSM-ISDAekKGLikpGESVLIEPTSGNTGVGLAFTAAAKGY 91
Cdd:cd01563 21 GNTPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDR-GMTVaVSKA--KEL---GVKAVACASTGNTSASLAAYAARAGI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 92 KLIITMPASMSTERRIILLAFGVELVltdPAKGMKGAIAKAEEILAKTPNGYMLqqfeNPANP-KIH-YETTGPEIWK-- 167
Cdd:cd01563 95 KCVVFLPAGKALGKLAQALAYGATVL---AVEGNFDDALRLVRELAEENWIYLS----NSLNPyRLEgQKTIAFEIAEql 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 168 ------------GTGGKI----DGFvsgigtggtitgagKYLKEQ---NANVKLYGV-----EPVESAILSGGK-----P 218
Cdd:cd01563 168 gwevpdyvvvpvGNGGNItaiwKGF--------------KELKELgliDRLPRMVGVqaegaAPIVRAFKEGKDdiepvE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233613 219 GPHKI-QGIGAGFIPS-VLNVDLIDE----VVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQR 283
Cdd:cd01563 234 NPETIaTAIRIGNPASgPKALRAVREsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREE 304
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
14-120 |
3.22e-06 |
|
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: 48.27 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 14 GNTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRiGFSM-ISDAEKKglikpGESVLIEPTSGNTGVGLAFTAAAKGYK 92
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDR-AMQVaVSLALER-----GAKTIVCASSGNGSAALAAYAARAGIE 138
|
90 100
....*....|....*....|....*....
gi 15233613 93 LIITMPAS-MSTERRIILLAFGVELVLTD 120
Cdd:COG0498 139 VFVFVPEGkVSPGQLAQMLTYGAHVIAVD 167
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
2-267 |
2.88e-05 |
|
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: 45.03 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 2 ASRIAKDVTElignTPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMI---SDAEKKglikpgeSVLIEPTSGNT 78
Cdd:COG1171 15 AARIAGVVRR----TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALaslSEEERA-------RGVVAASAGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 79 GVGLAFTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDPAkgMKGAIAKAEEiLAKTPNGYMLQQFENPAnpKIH- 157
Cdd:COG1171 84 AQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAE-LAEEEGATFVHPFDDPD--VIAg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 158 YETTGPEIWK------------GTGGKIDGFVSgigtggtitgagkYLKEQNANVKLYGVEPVESAI----LSGGKP--- 218
Cdd:COG1171 159 QGTIALEILEqlpdldavfvpvGGGGLIAGVAA-------------ALKALSPDIRVIGVEPEGAAAmyrsLAAGEPvtl 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15233613 219 -GPHKI-QGIGAGfIPSVLNVDLI----DEVVQVSSDESIDMARQLALKEGLLVG 267
Cdd:COG1171 226 pGVDTIaDGLAVG-RPGELTFEILrdlvDDIVTVSEDEIAAAMRLLLERTKIVVE 279
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
31-120 |
3.50e-05 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 44.70 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 31 RVAAKLEMMEPCSSVKDRIGFSMISDAekkglIKPGESVLIEPTSGNTGVGLAFTAAAKGYKLIITMPASMSTERRIILL 110
Cdd:PRK06381 32 KIYLKFEGANPTGTQKDRIAEAHVRRA-----MRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEME 106
|
90
....*....|
gi 15233613 111 AFGVELVLTD 120
Cdd:PRK06381 107 KYGAEIIYVD 116
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
16-139 |
4.53e-05 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 44.73 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 16 TPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMIS---DAEK-KGLIKpgesvliePTSGNTGVGLAFTAAAKGY 91
Cdd:PRK08638 28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSsltDAEKrKGVVA--------CSAGNHAQGVALSCALLGI 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15233613 92 KLIITMPASMSTERRIILLAFGVELVLTdpAKGMKGAIAKAEEILAKT 139
Cdd:PRK08638 100 DGKVVMPKGAPKSKVAATCGYGAEVVLH--GDNFNDTIAKVEEIVEEE 145
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
65-117 |
1.42e-03 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 39.98 E-value: 1.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15233613 65 PGESVLIEPTSGNTGVGLAFTAAAKGYKLIITMPASMSTERRIILLAFGVELV 117
Cdd:PRK06110 68 PRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELI 120
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
1-134 |
4.07e-03 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 38.40 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 1 MASRIAKdvteLIGNTPLVYLNNVAEGCVGrVAAKLEMMEPCSSVKDRIGFSMISDAEKkglikPGESVLIePTSGNTGV 80
Cdd:PRK08246 13 AAQRIAP----HIRRTPVLEADGAGFGPAP-VWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVA-ASGGNAGL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15233613 81 GLAFTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTDP--AKGMKGAIAKAEE 134
Cdd:PRK08246 82 AVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAE 137
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
49-120 |
6.47e-03 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 37.94 E-value: 6.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233613 49 IGFSMISDAEKKGLIkpGESVLIEPTSGNTGVGLAFTAAAKGYKLIITMPASMSTERRIILLAFGVELVLTD 120
Cdd:PRK08206 100 LSFEELTSGEVREKL--GDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITD 169
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
16-250 |
7.90e-03 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 37.85 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 16 TPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMIS----DAEKKGLIKPgesvliepTSGNTGVGLAFTAAAKGY 91
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMArlpaEQLARGVITA--------SAGNHAQGVALAAARLGV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 92 KLIITMPASMSTERRIILLAFGVELVLTDPAkgMKGAIAKAEEiLAKTPNGYMLQQFENPaNPKIHYETTGPEIWKGTGG 171
Cdd:PRK12483 110 KAVIVMPRTTPQLKVDGVRAHGGEVVLHGES--FPDALAHALK-LAEEEGLTFVPPFDDP-DVIAGQGTVAMEILRQHPG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 172 KIDGFVSGIGTGGTITGAGKYLKEQNANVKLYGVEPVESAILSGGKPGPHKIQGIGAGFIPSVLNVDLI----------- 240
Cdd:PRK12483 186 PLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIgehtfelcrhy 265
|
250
....*....|.
gi 15233613 241 -DEVVQVSSDE 250
Cdd:PRK12483 266 vDEVVTVSTDE 276
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
16-283 |
9.77e-03 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 37.36 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 16 TPLVYLNNVAEGCVGRVAAKLEMMEPCSSVKDRIGFSMI---SDAEKKGLIkpgesvlIEPTSGNTGVGLAFTAAAKGYK 92
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLrllNEAQRQQGV-------ITASSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 93 LIITMPASMSTERRIILLAFGVEL-VLTDPAKGMKGAIAKAEEILAKTpngymlqqFENPAN-PKI--HYETTGPEIWK- 167
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVrLYGGDALNAELAARRAAEQQGKV--------YISPYNdPQViaGQGTIGMELVEq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233613 168 -----------GTGGKIDGfvsgigtggtitgAGKYLKEQNANVKLYGVEPVESAI------------------LSGGKP 218
Cdd:PRK06815 166 qpdldavfvavGGGGLISG-------------IATYLKTLSPKTEIIGCWPANSPSlytsleageivevaeqptLSDGTA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233613 219 GphkiqGIGAGFIPSVLNVDLIDEVVQVSSDESIDMARQLALKEGLLVGISSGAAAAAAIKLAQR 283
Cdd:PRK06815 233 G-----GVEPGAITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPR 292
|
|
| |
