|
Name |
Accession |
Description |
Interval |
E-value |
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
12-314 |
0e+00 |
|
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: 526.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDApfRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEI 169
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 170 VETIKQPiDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHV 249
Cdd:TIGR03945 161 ARAFPTL-DYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVHV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492954 250 DDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:TIGR03945 240 PEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEWV 304
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
17-306 |
8.21e-141 |
|
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: 399.58 E-value: 8.21e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 17 GQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIKGLKLT 94
Cdd:cd01561 1 GNTPLVRLNRLSPgtGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 95 CVVDPKISPTNLKIIKSYGANVEMVEEPDAHGgyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVETIK 174
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEADG--MKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 175 QPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIF-GDKPINRELPGIGASRVPEILNRSEINQVIHVDDYQ 253
Cdd:cd01561 159 GKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFsGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446492954 254 SALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLD 306
Cdd:cd01561 239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
9-306 |
1.00e-130 |
|
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: 374.38 E-value: 1.00e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 9 HDSLLDSVGQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:COG0031 4 YDSILELIGNTPLVRLNRLSPgpGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYlmtrIAKVQELLATIDDAYWINQYANELNWQSHYHGAG 166
Cdd:COG0031 84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGA----IDKAEELAAETPGAFWPNQFENPANPEAHYETTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 167 TEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIF-GDKPINRELPGIGASRVPEILNRSEINQ 245
Cdd:COG0031 160 PEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDPSLIDE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492954 246 VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLD 306
Cdd:COG0031 240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLS 300
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
12-299 |
2.39e-75 |
|
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: 233.36 E-value: 2.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGlitENTHLIESTSGNLGIALAMIAKIK 89
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELgvDVYLKLESLNPTGSFKDRGALNLLLRLKEGE---GGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVeepdahGGYLMTRIAKVQELLATIDDAYWINQYANELNWQShYHGAGTEI 169
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV------GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 170 VETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGD----------KPINRELPGIGASRVPEILN 239
Cdd:pfam00291 151 LEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARslaagrpvpvPVADTIADGLGVGDEPGALA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492954 240 RSEINQ----VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLI-TSIEEGATIVTILPD 299
Cdd:pfam00291 231 LDLLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALaGELKGGDRVVVVLTG 295
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
9-314 |
1.75e-65 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 209.33 E-value: 1.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 9 HDSLLDSVGQTPMVQLHQL--FPKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:PRK10717 4 FEDVSDTIGNTPLIRLNRAseATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEE-PDAHGG-YLMTRIAKVQELLAT-IDDAYWINQYANELNWQSHYH 163
Cdd:PRK10717 84 AARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAaPYANPNnYVKGAGRLAEELVASePNGAIWANQFDNPANREAHYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 164 GAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFG-------DKPINRELPGIGASRVPE 236
Cdd:PRK10717 164 TTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktgelKAEGSSITEGIGQGRITA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446492954 237 ILNRSEINQVIHVDDyQSALG-CRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:PRK10717 244 NLEGAPIDDAIRIPD-EEALStAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFL 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
12-314 |
0e+00 |
|
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: 526.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDApfRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEI 169
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 170 VETIKQPiDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHV 249
Cdd:TIGR03945 161 ARAFPTL-DYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVHV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492954 250 DDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:TIGR03945 240 PEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEWV 304
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
17-306 |
8.21e-141 |
|
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: 399.58 E-value: 8.21e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 17 GQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIKGLKLT 94
Cdd:cd01561 1 GNTPLVRLNRLSPgtGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 95 CVVDPKISPTNLKIIKSYGANVEMVEEPDAHGgyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVETIK 174
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEADG--MKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 175 QPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIF-GDKPINRELPGIGASRVPEILNRSEINQVIHVDDYQ 253
Cdd:cd01561 159 GKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFsGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446492954 254 SALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLD 306
Cdd:cd01561 239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
9-306 |
1.00e-130 |
|
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: 374.38 E-value: 1.00e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 9 HDSLLDSVGQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:COG0031 4 YDSILELIGNTPLVRLNRLSPgpGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYlmtrIAKVQELLATIDDAYWINQYANELNWQSHYHGAG 166
Cdd:COG0031 84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGA----IDKAEELAAETPGAFWPNQFENPANPEAHYETTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 167 TEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIF-GDKPINRELPGIGASRVPEILNRSEINQ 245
Cdd:COG0031 160 PEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDPSLIDE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492954 246 VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLD 306
Cdd:COG0031 240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLS 300
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
12-305 |
1.69e-86 |
|
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: 261.83 E-value: 1.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCdaRVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVeepDAHGGyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEI 169
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILT---PGEEG-MKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 170 VETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIH 248
Cdd:TIGR01136 157 WRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEpAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVIT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446492954 249 VDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIE-EGATIVTILPDRGDRYL 305
Cdd:TIGR01136 237 VSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYL 294
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
14-305 |
5.76e-80 |
|
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: 245.35 E-value: 5.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 14 DSVGQTPMVQLHQLFPKH-EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIKGLK 92
Cdd:TIGR01139 3 ELIGNTPLVRLNRIEGCNaNVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 93 LTCVVDPKISPTNLKIIKSYGANVEMVeePDAHGGYLMtrIAKVQELLATIDDAYWI-NQYANELNWQSHYHGAGTEIVE 171
Cdd:TIGR01139 83 LILTMPETMSIERRKLLKAYGAELVLT--PGAEGMKGA--IAKAEEIAASTPNSYFMlQQFENPANPEIHRKTTGPEIWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 172 TIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGS-VIFGDKPINRELPGIGASRVPEILNRSEINQVIHVD 250
Cdd:TIGR01139 159 DTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESpVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446492954 251 DYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYL 305
Cdd:TIGR01139 239 DEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYL 293
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
12-299 |
2.39e-75 |
|
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: 233.36 E-value: 2.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGlitENTHLIESTSGNLGIALAMIAKIK 89
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELgvDVYLKLESLNPTGSFKDRGALNLLLRLKEGE---GGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVeepdahGGYLMTRIAKVQELLATIDDAYWINQYANELNWQShYHGAGTEI 169
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV------GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 170 VETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGD----------KPINRELPGIGASRVPEILN 239
Cdd:pfam00291 151 LEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARslaagrpvpvPVADTIADGLGVGDEPGALA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492954 240 RSEINQ----VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLI-TSIEEGATIVTILPD 299
Cdd:pfam00291 231 LDLLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALaGELKGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
19-300 |
2.76e-69 |
|
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: 216.23 E-value: 2.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 19 TPMVQLHQLF--PKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLItENTHLIESTSGNLGIALAMIAKIKGLKLTCV 96
Cdd:cd00640 1 TPLVRLKRLSklGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 97 VDPKISPTNLKIIKSYGANVEMVEepdahgGYLMTRIAKVQELLATIDDAYWINQYANELNWQSHYhGAGTEIVETIK-Q 175
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVP------GDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGgQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 176 PIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKgsvifgdkpinrelpgigasrvpeilnrseinqVIHVDDYQSA 255
Cdd:cd00640 153 KPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE---------------------------------VVTVSDEEAL 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446492954 256 LGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDR 300
Cdd:cd00640 200 EAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
9-316 |
6.19e-69 |
|
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: 221.98 E-value: 6.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 9 HDSLLDSVGQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:TIGR01137 2 LDNILDLIGNTPLVRLNKVSKglKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMV------EEPDAHGGylmtrIAKvqELLATIDDAYWINQYANELNWQS 160
Cdd:TIGR01137 82 AIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTptaaafDSPESHIG-----VAK--RLVREIPGAHILDQYRNPSNPLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 161 HYHGAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGDKPINR------ELPGIGASRV 234
Cdd:TIGR01137 155 HYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQtgrtpyKVEGIGYDFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 235 PEILNRSEINQVIHVDDYQSALGCRKLIDYEGIFAGGSTGS-IIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTW 313
Cdd:TIGR01137 235 PTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSaVVAALKAAEDELQEGQRCVVLLPDSIRNYMTKFLNDEW 314
|
...
gi 446492954 314 LEK 316
Cdd:TIGR01137 315 MLD 317
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
9-314 |
1.75e-65 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 209.33 E-value: 1.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 9 HDSLLDSVGQTPMVQLHQL--FPKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:PRK10717 4 FEDVSDTIGNTPLIRLNRAseATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEE-PDAHGG-YLMTRIAKVQELLAT-IDDAYWINQYANELNWQSHYH 163
Cdd:PRK10717 84 AARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAaPYANPNnYVKGAGRLAEELVASePNGAIWANQFDNPANREAHYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 164 GAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFG-------DKPINRELPGIGASRVPE 236
Cdd:PRK10717 164 TTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktgelKAEGSSITEGIGQGRITA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446492954 237 ILNRSEINQVIHVDDyQSALG-CRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:PRK10717 244 NLEGAPIDDAIRIPD-EEALStAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFL 321
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
11-305 |
3.17e-64 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 204.72 E-value: 3.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 11 SLLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKI 88
Cdd:PRK11761 5 TLEDTIGNTPLVKLQRLPPDRgnTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 89 KGLKLTCVVdpkisPTNLKI-----IKSYGANVEMVEepdAHGGYLMTR---IAKVQELLATIddaywINQYANELNWQS 160
Cdd:PRK11761 85 KGYRMKLIM-----PENMSQerraaMRAYGAELILVP---KEQGMEGARdlaLQMQAEGEGKV-----LDQFANPDNPLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 161 HYHGAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIfgdkpinrelPGI---GASRVPE 236
Cdd:PRK11761 152 HYETTGPEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQpEEGSSI----------PGIrrwPEEYLPK 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446492954 237 ILNRSEINQVIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIeEGATIVTILPDRGDRYL 305
Cdd:PRK11761 222 IFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYL 289
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
16-323 |
4.51e-47 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 162.82 E-value: 4.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 16 VGQTPMVQLHQLFPKHEVF--AKLEYMNPGGSMKDRPAKYIIEHGIKHGLITE-NTHLIESTSGNLGIALAMIAKIKGLK 92
Cdd:PLN02556 57 IGKTPLVYLNKVTEGCGAYiaAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPgKTTLIEPTSGNMGISLAFMAAMKGYK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 93 LTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGylmtRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVET 172
Cdd:PLN02556 137 MILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGG----TVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWED 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 173 IKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHVDD 251
Cdd:PLN02556 213 TLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEpAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSS 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446492954 252 YQSALGCRKLIDYEGIFAGGSTGS-IIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWLEKMKSRQGV 323
Cdd:PLN02556 293 EDAVNMARELALKEGLMVGISSGAnTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAENMQPV 365
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
16-312 |
9.35e-44 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 152.77 E-value: 9.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 16 VGQTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTH-LIESTSGNLGIALAMIAKIKGLK 92
Cdd:PLN02565 13 IGKTPLVYLNNVVDGcvARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGLAFMAAAKGYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 93 LTCVVDPKISPTNLKIIKSYGAnvEMVEEPDAHGgyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVET 172
Cdd:PLN02565 93 LIITMPASMSLERRIILLAFGA--ELVLTDPAKG--MKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEIWKG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 173 IKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHVDD 251
Cdd:PLN02565 169 TGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEpVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQVSS 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446492954 252 YQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIE-EGATIVTILPDRGDRYLDLVYSDT 312
Cdd:PLN02565 249 DEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFES 310
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
10-305 |
1.51e-41 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 149.54 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 10 DSLLDSVGQTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITE-NTHLIESTSGNLGIALAMIA 86
Cdd:PLN03013 115 DNVSQLIGKTPMVYLNSIAKGcvANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPgKSVLVEPTSGNTGIGLAFIA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 87 KIKGLKLTCVVDPKISPTNLKIIKSYGAnvEMVEEPDAHGgyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAG 166
Cdd:PLN03013 195 ASRGYRLILTMPASMSMERRVLLKAFGA--ELVLTDPAKG--MTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 167 TEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGS-VIFGDKPINRELPGIGASRVPEILNRSEINQ 245
Cdd:PLN03013 271 PEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESdILSGGKPGPHKIQGIGAGFIPKNLDQKIMDE 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492954 246 VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEE-GATIVTILPDRGdRYL 305
Cdd:PLN03013 351 VIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENaGKLIAVSLFASG-RDI 410
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
10-305 |
7.79e-39 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 139.75 E-value: 7.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 10 DSLLDSVGQTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITE-NTHLIESTSGNLGIALAMIA 86
Cdd:PLN00011 9 NDVTELIGNTPMVYLNNIVDGcvARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPgKSTLIEATAGNTGIGLACIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGylmtRIAKVQELLATIDDAYWINQYANELNWQSHYHGAG 166
Cdd:PLN00011 89 AARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKG----MLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 167 TEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIFGDKPINRELPGIGASRVPEILNRSEINQ 245
Cdd:PLN00011 165 PEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEpVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492954 246 VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEE-GATIVTILPDRGDRYL 305
Cdd:PLN00011 245 IIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYL 305
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
12-314 |
3.56e-35 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 132.04 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:PLN02356 47 LIDAIGNTPLIRINSLSEATgcEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 90 GLKLTCVVDPKISPTNLKIIKSYGANVEMV--------------------------------EEPDAHG-----GYLMTR 132
Cdd:PLN02356 127 GCKCHVVIPDDVAIEKSQILEALGATVERVrpvsithkdhyvniarrraleanelaskrrkgSETDGIHlektnGCISEE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 133 IAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAK 212
Cdd:PLN02356 207 EKENSLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 213 GSVIFG------------------DKPINRELPGIGASRVPEILNRSEINQVIHVDDYQSALGCRKLIDYEGIFAGGSTG 274
Cdd:PLN02356 287 GSGLFNkvtrgvmytreeaegrrlKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSA 366
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446492954 275 SIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:PLN02356 367 MNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYL 406
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
17-297 |
3.35e-13 |
|
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: 69.16 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 17 GQTPMVQLHQLFPKH---EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLitenTHLIESTSGNLGIALAMIAKIKGLKl 93
Cdd:cd01563 21 GNTPLVRAPRLGERLggkNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 94 TCVVDPK-ISPTNLKIIKSYGANVEMVEepdahggylmTRIAKVQELLATIDDAYWInqYANelNWQSHYHGAGT----- 167
Cdd:cd01563 96 CVVFLPAgKALGKLAQALAYGATVLAVE----------GNFDDALRLVRELAEENWI--YLS--NSLNPYRLEGQktiaf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 168 EIVETIKQPI-DYFVAPVSTTGSIMGMSRKIKEVH--------PnaQIVAVDAKGS------VIFGDKPINR-ELP---- 227
Cdd:cd01563 162 EIAEQLGWEVpDYVVVPVGNGGNITAIWKGFKELKelglidrlP--RMVGVQAEGAapivraFKEGKDDIEPvENPetia 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446492954 228 -GI------GASRVPEILNRSEInQVIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITS--IEEGATIVTIL 297
Cdd:cd01563 240 tAIrignpaSGPKALRAVRESGG-TAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgiIDKGERVVVVL 317
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
16-297 |
4.92e-13 |
|
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: 69.07 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 16 VGQTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITenthLIESTSGNLGIALAMIAKIKGLKL 93
Cdd:COG0498 64 EGGTPLVKAPRLADElgKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKT----IVCASSGNGSAALAAYAARAGIEV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 94 TCVVdP--KISPTNLKIIKSYGANVEMVEepdahGGYlMTRIAKVQELLAtidDAYWINqyANELNWqshY--HGAGT-- 167
Cdd:COG0498 140 FVFV-PegKVSPGQLAQMLTYGAHVIAVD-----GNF-DDAQRLVKELAA---DEGLYA--VNSINP---ArlEGQKTya 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 168 -EIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVH--------PnaQIVAVDAKGSV-IF-----GDKPINRELPG---- 228
Cdd:COG0498 205 fEIAEQLGRVPDWVVVPTGNGGNILAGYKAFKELKelglidrlP--RLIAVQATGCNpILtafetGRDEYEPERPEtiap 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446492954 229 ---IGAS----RVPEILNRSEiNQVIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLI--TSIEEGATIVTIL 297
Cdd:COG0498 283 smdIGNPsngeRALFALRESG-GTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLReeGEIDPDEPVVVLS 359
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
19-213 |
1.53e-12 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 67.54 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 19 TPMVQLHQlfpkhEVFAKLEYMNPGGSMKDRpAKYIIEHGIKHGLITENThlIEStSGNLGIALAMIAKIKGLKLTCVVD 98
Cdd:PRK08329 65 TPTVKRSI-----KVYFKLDYLQPTGSFKDR-GTYVTVAKLKEEGINEVV--IDS-SGNAALSLALYSLSEGIKVHVFVS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 99 PKISPTNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQELLATiddAYWINQYANElnwqshyhgaGT-----EIVETI 173
Cdd:PRK08329 136 YNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYV---SHWLNPYFLE----------GTktiayEIYEQI 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446492954 174 KQPiDYFVAPVSTTGSIMGMSRKIKEVHPNAQI------VAVDAKG 213
Cdd:PRK08329 203 GVP-DYAFVPVGSGTLFLGIWKGFKELHEMGEIskmpklVAVQAEG 247
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
18-280 |
7.17e-12 |
|
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: 65.01 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 18 QTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLiTENTHLIESTSGNLGIALAMIAKIKGLKLTC 95
Cdd:cd06448 1 KTPLIESTALSKTagCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGL-NECVHVVCSSGGNAGLAAAYAARKLGVPCTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 96 VVDPKISPTNLKIIKSYGANVEMV-----EEPDAHGgylmtriakvQELLATIDDAYWINQYANELNWQSHyhgagTEIV 170
Cdd:cd06448 80 VVPESTKPRVVEKLRDEGATVVVHgkvwwEADNYLR----------EELAENDPGPVYVHPFDDPLIWEGH-----SSMV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 171 ETIKQ------PIDYFVAPVSTTGSIMGMSRKIKEVHPN-AQIVAVDAKGSVIF-----GDKPInrELPGI-------GA 231
Cdd:cd06448 145 DEIAQqlqsqeKVDAIVCSVGGGGLLNGIVQGLERNGWGdIPVVAVETEGAHSLnaslkAGKLV--TLPKItsvatslGA 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446492954 232 SRVPEILNRSEINQVIH---VDDYQSALGCRKLIDYEGIFAGGSTGSIIAAI 280
Cdd:cd06448 223 KTVSSQALEYAQEHNIKsevVSDRDAVQACLRFADDERILVEPACGAALAVV 274
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
17-120 |
7.94e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 62.06 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 17 GQTPMVQlhqlfpKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLitenTHLIESTSGNLGIALAMIAKIKGLKLTCV 96
Cdd:PRK06450 57 GRTPLIK------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKIF 126
|
90 100
....*....|....*....|....
gi 446492954 97 VDPKISPTNLKIIKSYGANVEMVE 120
Cdd:PRK06450 127 VPETASGGKLKQIESYGAEVVRVR 150
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
17-301 |
1.24e-09 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 59.06 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 17 GQTPMVQLHQLFPKHE-VFAKLEYMNPGGSMKDRPAKYIIEHGIKHGliteNTHLIESTSGNLGIALAMIAKIKGLKLTC 95
Cdd:PRK05638 65 GGTPLIRARISEKLGEnVYIKDETRNPTGSFRDRLATVAVSYGLPYA----ANGFIVASDGNAAASVAAYSARAGKEAFV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 96 VVDPKISPTNLKIIKSYGANVEMVEEpdahggylmtriaKVQELLatiddaywinQYANEL-------NWQSHYHGAGTE 168
Cdd:PRK05638 141 VVPRKVDKGKLIQMIAFGAKIIRYGE-------------SVDEAI----------EYAEELarlnglyNVTPEYNIIGLE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 169 IVETIKQPI------DYFVAPVSTTGSIMGMSRKIKEVHPNAQI------VAVDAK-----GSVIFGDKPINRELPGIG- 230
Cdd:PRK05638 198 GQKTIAFELweeinpTHVIVPTGSGSYLYSIYKGFKELLEIGVIeeipklIAVQTErcnpiASEILGNKTKCNETKALGl 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 231 -------ASRVPEILNRS-EINQVIHVDDYQSAlgcRKLIDYEGIFAGGSTGSIIAAIEQLITS--IEEGATIVTILPDR 300
Cdd:PRK05638 278 yvknpvmKEYVSEAIKESgGTAVVVNEEEIMAG---EKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGS 354
|
.
gi 446492954 301 G 301
Cdd:PRK05638 355 G 355
|
|
| PLN02970 |
PLN02970 |
serine racemase |
32-214 |
8.06e-09 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 56.23 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 32 EVFAKLEYMNPGGSMKDRPAKYIIEHGI----KHGLITentHliesTSGNLGIALAMIAKIKGLKLTCVVdPKISPtNLK 107
Cdd:PLN02970 43 SLFFKCECFQKGGAFKFRGACNAIFSLSddqaEKGVVT---H----SSGNHAAALALAAKLRGIPAYIVV-PKNAP-ACK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 108 I--IKSYGANVEMVEEpdahggYLMTRIAKVQELLATIDdAYWINQYanelNWQSHYHGAGT---EIVETIKQpIDYFVA 182
Cdd:PLN02970 114 VdaVIRYGGIITWCEP------TVESREAVAARVQQETG-AVLIHPY----NDGRVISGQGTialEFLEQVPE-LDVIIV 181
|
170 180 190
....*....|....*....|....*....|..
gi 446492954 183 PVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGS 214
Cdd:PLN02970 182 PISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
1-209 |
1.55e-08 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 55.08 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 1 MIEKSQACHDSLLDSVGQTPM---VQLHQLfPKHEVFAKLEYMNPGGSMKDRPAKYII----EHGIKHGLITenthlieS 73
Cdd:PRK06815 3 LFDAILEAHQRLRPQVRVTPLehsPLLSQH-TGCEVYLKCEHLQHTGSFKFRGASNKLrllnEAQRQQGVIT-------A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 74 TSGNLGIALAMIAKIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEpDAHGGYLMTRI-AKVQELLatiddayWINQY 152
Cdd:PRK06815 75 SSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGG-DALNAELAARRaAEQQGKV-------YISPY 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 153 aNELNWQShyhGAGT---EIVETIKQPIDYFVApVSTTGSIMGMSRKIKEVHPNAQIVAV 209
Cdd:PRK06815 147 -NDPQVIA---GQGTigmELVEQQPDLDAVFVA-VGGGGLISGIATYLKTLSPKTEIIGC 201
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
16-208 |
7.33e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 53.24 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 16 VGQTPMVQ---LHQLFpKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITEntHLIESTSGNLGIALAMIAKIKGLK 92
Cdd:PRK06608 21 LHLTPIVHsesLNEML-GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPD--KIVAYSTGNHGQAVAYASKLFGIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 93 LTCVVDPKISPTNLKIIKSYGANVEmveepdahggYLMTRI-AKVQELLATIDDAYWINQYanelNWQSHYHGAGT---E 168
Cdd:PRK06608 98 TRIYLPLNTSKVKQQAALYYGGEVI----------LTNTRQeAEEKAKEDEEQGFYYIHPS----DSDSTIAGAGTlcyE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446492954 169 IVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVA 208
Cdd:PRK06608 164 ALQQLGFSPDAIFASCGGGGLISGTYLAKELISPTSLLIG 203
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
18-211 |
2.26e-05 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 45.50 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 18 QTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHgikhglITENTH---LIESTSGNLGIALAMIAKIKGLK 92
Cdd:PRK08638 27 KTPLPRSNYLSErcKGEIFLKLENMQRTGSFKIRGAFNKLSS------LTDAEKrkgVVACSAGNHAQGVALSCALLGID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 93 LTcVVDPKISP-TNLKIIKSYGANVEMveepdaHGGYLMTRIAKVQElLATIDDAYWINQYANELNwqshYHGAGT---E 168
Cdd:PRK08638 101 GK-VVMPKGAPkSKVAATCGYGAEVVL------HGDNFNDTIAKVEE-IVEEEGRTFIPPYDDPKV----IAGQGTiglE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446492954 169 IVETIKQpIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDA 211
Cdd:PRK08638 169 ILEDLWD-VDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQS 210
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
33-116 |
3.74e-05 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 44.70 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 33 VFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENThlieSTSGNLGIALAMIAKIKGLKLTCVVDPKISPTNLKIIKSY 112
Cdd:PRK06381 33 IYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITV----GTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKY 108
|
....
gi 446492954 113 GANV 116
Cdd:PRK06381 109 GAEI 112
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
17-308 |
6.91e-05 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 44.22 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 17 GQTPMVQLHQLFPK---HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLitenTHLIESTSGNLGIALAMIAKIKGLKL 93
Cdd:PRK08197 78 GMTPLLPLPRLGKAlgiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGV----KHLAMPTNGNAGAAWAAYAARAGIRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 94 TCVVdPKISP-TNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQEL--LATIDDAYWIN-------QYANELNWqshyh 163
Cdd:PRK08197 154 TIFM-PADAPeITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWfdVSTLKEPYRIEgkktmglELAEQLGW----- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 164 gagtEIVETIKQPidyfvapvstTG---SIMGMSRKIKEVH-------PNAQIVAVDAKGSVifgdkPINREL------- 226
Cdd:PRK08197 228 ----RLPDVILYP----------TGggvGLIGIWKAFDELEalgwiggKRPRLVAVQAEGCA-----PIVKAWeegkees 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 227 ----------PGIgasRVPEILNRSEINQV--------IHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITS-- 286
Cdd:PRK08197 289 efwedahtvaFGI---RVPKALGDFLVLDAvretggcaIAVSDDAILAAQRELAREEGLFACPEGAATFAAARQLRESgw 365
|
330 340
....*....|....*....|..
gi 446492954 287 IEEGATIVTILPDRGDRYLDLV 308
Cdd:PRK08197 366 LKGDERVVLFNTGSGLKYPDTV 387
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
164-213 |
1.70e-04 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 42.87 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446492954 164 GAGT---EIVETIKQP--IDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKG 213
Cdd:PRK08639 162 GQGTvavEILEQLEKEgsPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
18-121 |
2.04e-04 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 42.63 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 18 QTPMVQLH-QLFPKHEVFAKLEYMNPGGSMKDRPAKY-IIEHGI-KHGLITenthlieSTSGNLGIALAMIAKIKGLKLT 94
Cdd:PRK08246 23 RTPVLEADgAGFGPAPVWLKLEHLQHTGSFKARGAFNrLLAAPVpAAGVVA-------ASGGNAGLAVAYAAAALGVPAT 95
|
90 100
....*....|....*....|....*...
gi 446492954 95 CVVdPKISPTN-LKIIKSYGANVEMVEE 121
Cdd:PRK08246 96 VFV-PETAPPAkVARLRALGAEVVVVGA 122
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
71-214 |
6.18e-03 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 38.20 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 71 IESTSGN--LGIALAmiAKIKGLKLTCVVdPKISPtNLKI--IKSYGANVEMveepdaHGgylmtriakvqellATIDDA 146
Cdd:PRK09224 72 ITASAGNhaQGVALS--AARLGIKAVIVM-PVTTP-DIKVdaVRAFGGEVVL------HG--------------DSFDEA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492954 147 YwinQYANELNWQSHY---H---------GAGT---EIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDA 211
Cdd:PRK09224 128 Y---AHAIELAEEEGLtfiHpfddpdviaGQGTiamEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEP 204
|
...
gi 446492954 212 KGS 214
Cdd:PRK09224 205 EDS 207
|
|
| |
