|
Name |
Accession |
Description |
Interval |
E-value |
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
15-319 |
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: 509.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 15 VLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQICAY 94
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPG-TTIIESSSGNLGIALAMICAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 95 YGIRFICVVDPRTNRQNIAIMRAYGAEVEVVTDIDPNsGEYLPVRIRRVRELVDSITHAYCPNQYANPLNPQAH-HSTVR 173
Cdd:TIGR03945 80 KGLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDET-GGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHyHGTGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 174 EVLDALPTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIFGSPVGGRLIPGHGASVRPSLYADGLADVVIR 253
Cdd:TIGR03945 159 EIARAFPTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVH 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501131759 254 VDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDRGERYLDTIYDDDWV 319
Cdd:TIGR03945 239 VPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEWV 304
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
20-311 |
2.50e-123 |
|
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: 356.05 E-value: 2.50e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 20 GATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQICAYYGIRF 99
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPG-TTIIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 100 ICVVDPRTNRQNIAIMRAYGAEVEVVTdidPNSGEYLPVRIRRVRELVDSITHAYCPNQYANPLNPQAH-HSTVREVLDA 178
Cdd:cd01561 80 IIVMPETMSEEKRKLLRALGAEVILTP---EAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHyETTAPEIWEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 179 LP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIF-GSPVGGRLIPGHGASVRPSLYADGLADVVIRVDD 256
Cdd:cd01561 157 LDgKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFsGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSD 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 501131759 257 LDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDRGERYLD 311
Cdd:cd01561 237 EEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
15-312 |
7.20e-119 |
|
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: 344.72 E-value: 7.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 15 VLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQICAY 94
Cdd:COG0031 7 ILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPG-GTIVEATSGNTGIGLAMVAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 95 YGIRFICVVDPRTNRQNIAIMRAYGAEVEVV-TDIDPNSgeylpvRIRRVRELVDSITHAYCPNQYANPLNPQAH-HSTV 172
Cdd:COG0031 86 KGYRLILVMPETMSKERRALLRAYGAEVVLTpGAEGMKG------AIDKAEELAAETPGAFWPNQFENPANPEAHyETTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 173 REVLDALP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIF-GSPVGGRLIPGHGASVRPSLYADGLADV 250
Cdd:COG0031 160 PEIWEQTDgKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDPSLIDE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501131759 251 VIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDRGERYLDT 312
Cdd:COG0031 240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
15-304 |
5.01e-66 |
|
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: 209.86 E-value: 5.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 15 VLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRdRIRDGRlvpGKSTVIESSSGNLGIGLAQICAY 94
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLL-RLKEGE---GGKTVVEASSGNHGRALAAAAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 95 YGIRFICVVDPRTNRQNIAIMRAYGAEVEVVtdidpnsGEYLPVRIRRVRELVDSITHAYCPNQYANPLNPQAHHSTVRE 174
Cdd:pfam00291 77 LGLKVTIVVPEDAPPGKLLLMRALGAEVVLV-------GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 175 VLDAL-PTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIFGS----------PVGGRLIPGHGASVRPSLY 243
Cdd:pfam00291 150 ILEQLgGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARslaagrpvpvPVADTIADGLGVGDEPGAL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501131759 244 A----DGLADVVIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALG-TMRDRIPPGATCALVFPD 304
Cdd:pfam00291 230 AldllDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKlALAGELKGGDRVVVVLTG 295
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
13-320 |
2.81e-56 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 185.84 E-value: 2.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 13 PGVLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGKsTVIESSSGNLGIGLAQIC 92
Cdd:PRK10717 5 EDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGG-TIVEGTAGNTGIGLALVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 93 AYYGIRFIcVVDPRTNRQ-NIAIMRAYGAE---VEVVTDIDPNSgeYLPVRIRRVRELVDSITH-AYCPNQYANPLNPQA 167
Cdd:PRK10717 84 AARGYKTV-IVMPETQSQeKKDLLRALGAElvlVPAAPYANPNN--YVKGAGRLAEELVASEPNgAIWANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 168 H-HSTVREVLDALP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIFG-------SPVGGRLIPGHGASV 238
Cdd:PRK10717 161 HyETTGPEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktgelKAEGSSITEGIGQGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 239 RPSLYADGLADVVIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDRGERYLDTIYDDDW 318
Cdd:PRK10717 241 ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDF 320
|
..
gi 501131759 319 VA 320
Cdd:PRK10717 321 LR 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
15-319 |
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: 509.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 15 VLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQICAY 94
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPG-TTIIESSSGNLGIALAMICAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 95 YGIRFICVVDPRTNRQNIAIMRAYGAEVEVVTDIDPNsGEYLPVRIRRVRELVDSITHAYCPNQYANPLNPQAH-HSTVR 173
Cdd:TIGR03945 80 KGLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDET-GGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHyHGTGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 174 EVLDALPTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIFGSPVGGRLIPGHGASVRPSLYADGLADVVIR 253
Cdd:TIGR03945 159 EIARAFPTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVH 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501131759 254 VDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDRGERYLDTIYDDDWV 319
Cdd:TIGR03945 239 VPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEWV 304
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
20-311 |
2.50e-123 |
|
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: 356.05 E-value: 2.50e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 20 GATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQICAYYGIRF 99
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPG-TTIIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 100 ICVVDPRTNRQNIAIMRAYGAEVEVVTdidPNSGEYLPVRIRRVRELVDSITHAYCPNQYANPLNPQAH-HSTVREVLDA 178
Cdd:cd01561 80 IIVMPETMSEEKRKLLRALGAEVILTP---EAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHyETTAPEIWEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 179 LP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIF-GSPVGGRLIPGHGASVRPSLYADGLADVVIRVDD 256
Cdd:cd01561 157 LDgKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFsGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSD 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 501131759 257 LDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDRGERYLD 311
Cdd:cd01561 237 EEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
15-312 |
7.20e-119 |
|
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: 344.72 E-value: 7.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 15 VLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQICAY 94
Cdd:COG0031 7 ILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPG-GTIVEATSGNTGIGLAMVAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 95 YGIRFICVVDPRTNRQNIAIMRAYGAEVEVV-TDIDPNSgeylpvRIRRVRELVDSITHAYCPNQYANPLNPQAH-HSTV 172
Cdd:COG0031 86 KGYRLILVMPETMSKERRALLRAYGAEVVLTpGAEGMKG------AIDKAEELAAETPGAFWPNQFENPANPEAHyETTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 173 REVLDALP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIF-GSPVGGRLIPGHGASVRPSLYADGLADV 250
Cdd:COG0031 160 PEIWEQTDgKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDPSLIDE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501131759 251 VIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDRGERYLDT 312
Cdd:COG0031 240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
15-304 |
5.01e-66 |
|
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: 209.86 E-value: 5.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 15 VLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRdRIRDGRlvpGKSTVIESSSGNLGIGLAQICAY 94
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLL-RLKEGE---GGKTVVEASSGNHGRALAAAAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 95 YGIRFICVVDPRTNRQNIAIMRAYGAEVEVVtdidpnsGEYLPVRIRRVRELVDSITHAYCPNQYANPLNPQAHHSTVRE 174
Cdd:pfam00291 77 LGLKVTIVVPEDAPPGKLLLMRALGAEVVLV-------GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 175 VLDAL-PTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIFGS----------PVGGRLIPGHGASVRPSLY 243
Cdd:pfam00291 150 ILEQLgGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARslaagrpvpvPVADTIADGLGVGDEPGAL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501131759 244 A----DGLADVVIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALG-TMRDRIPPGATCALVFPD 304
Cdd:pfam00291 230 AldllDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKlALAGELKGGDRVVVVLTG 295
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
11-320 |
8.05e-65 |
|
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: 211.58 E-value: 8.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 11 SVPGVLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQ 90
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPG-DTIIEPTSGNTGIGLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 91 ICAYYGIRFICVVDPRTNRQNIAIMRAYGAEVEVV-TDIDPNSGE-YLPVRIRRVRElvdsITHAYCPNQYANPLNPQAH 168
Cdd:TIGR01137 80 VAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTpTAAAFDSPEsHIGVAKRLVRE----IPGAHILDQYRNPSNPLAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 169 -HSTVREVLDALP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSaIFGSPVG----GR---LIPGHGASVR 239
Cdd:TIGR01137 156 yDTTGPEILEQCEgKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtGRtpyKVEGIGYDFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 240 PSLYADGLADVVIRVDDLDTVVGCRRLAAREAILAGGSSG-AVVSALGTMRDRIPPGATCALVFPDRGERYLDTIYDDDW 318
Cdd:TIGR01137 235 PTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGsAVVAALKAAEDELQEGQRCVVLLPDSIRNYMTKFLNDEW 314
|
..
gi 501131759 319 VA 320
Cdd:TIGR01137 315 ML 316
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
22-305 |
3.20e-64 |
|
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: 203.52 E-value: 3.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 22 TPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLvpGKSTVIESSSGNLGIGLAQICAYYGIRFIC 101
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL--PKGVIIESTGGNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 102 VVDPRTNRQNIAIMRAYGAEVEVVtdidpnsGEYLPVRIRRVRELVDSITHAYCPNQYANPLNPQAHHSTVREVLDALP- 180
Cdd:cd00640 79 VMPEGASPEKVAQMRALGAEVVLV-------PGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLGg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 181 -TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDAlgsaifgspvggrlipghgasvrpslyadgladVVIRVDDLDT 259
Cdd:cd00640 152 qKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEP---------------------------------EVVTVSDEEA 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 501131759 260 VVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDR 305
Cdd:cd00640 199 LEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
13-320 |
2.81e-56 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 185.84 E-value: 2.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 13 PGVLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGKsTVIESSSGNLGIGLAQIC 92
Cdd:PRK10717 5 EDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGG-TIVEGTAGNTGIGLALVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 93 AYYGIRFIcVVDPRTNRQ-NIAIMRAYGAE---VEVVTDIDPNSgeYLPVRIRRVRELVDSITH-AYCPNQYANPLNPQA 167
Cdd:PRK10717 84 AARGYKTV-IVMPETQSQeKKDLLRALGAElvlVPAAPYANPNN--YVKGAGRLAEELVASEPNgAIWANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 168 H-HSTVREVLDALP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIFG-------SPVGGRLIPGHGASV 238
Cdd:PRK10717 161 HyETTGPEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktgelKAEGSSITEGIGQGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 239 RPSLYADGLADVVIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALVFPDRGERYLDTIYDDDW 318
Cdd:PRK10717 241 ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDF 320
|
..
gi 501131759 319 VA 320
Cdd:PRK10717 321 LR 322
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
13-312 |
2.23e-46 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 159.27 E-value: 2.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 13 PGVLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQIC 92
Cdd:PRK11761 4 PTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPG-DTLIEATSGNTGIALAMIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 93 AYYGIRFICVVDPRTNRQNIAIMRAYGAEVEVVtdidPNSG--EYlpvrirrVRELVDSITHA---YCPNQYANPLNPQA 167
Cdd:PRK11761 83 AIKGYRMKLIMPENMSQERRAAMRAYGAELILV----PKEQgmEG-------ARDLALQMQAEgegKVLDQFANPDNPLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 168 H-HSTVREVL-DALPTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVdalgsaifgSPVGGRLIPGhgasVR------ 239
Cdd:PRK11761 152 HyETTGPEIWrQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGL---------QPEEGSSIPG----IRrwpeey 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501131759 240 -PSLYADGLADVVIRVDDLDTVVGCRRLAAREAILAGGSS-GAVVSALgtmrdRIP---PGATCALVFPDRGERYLDT 312
Cdd:PRK11761 219 lPKIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSgGAVAAAL-----RIArenPNAVIVAIICDRGDRYLST 291
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
19-312 |
6.96e-45 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 156.32 E-value: 6.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 19 IGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGKSTVIESSSGNLGIGLAQICAYYGIR 98
Cdd:PLN00011 15 IGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEATAGNTGIGLACIGAARGYK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 99 FICVVDPRTNRQNIAIMRAYGAEVEVVtdiDPNSGeyLPVRIRRVRELVDSITHAYCPNQYANPLNPQAHHSTVREVL-- 176
Cdd:PLN00011 95 VILVMPSTMSLERRIILRALGAEVHLT---DQSIG--LKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGPEIwr 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 177 DALPTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIF-GSPVGGRLIPGHGASVRPSLYADGLADVVIRVD 255
Cdd:PLN00011 170 DSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLsGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQVT 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 501131759 256 DLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRiP--PGATCALVFPDRGERYLDT 312
Cdd:PLN00011 250 GEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKR-PenAGKLIVVIFPSGGERYLST 307
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
19-317 |
8.80e-45 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 157.04 E-value: 8.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 19 IGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGKSTVIESSSGNLGIGLAQICAYYGIR 98
Cdd:PLN02556 57 IGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLIEPTSGNMGISLAFMAAMKGYK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 99 FICVVDPRTNRQNIAIMRAYGAEVeVVTdiDPNSGeyLPVRIRRVRELVDSITHAYCPNQYANPLNPQAHHSTVREVL-- 176
Cdd:PLN02556 137 MILTMPSYTSLERRVTMRAFGAEL-VLT--DPTKG--MGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIwe 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 177 DALPTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIF-GSPVGGRLIPGHGASVRPSLYADGLADVVIRVD 255
Cdd:PLN02556 212 DTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLnGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVS 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501131759 256 DLDTVVGCRRLAAREAILAGGSSGA-VVSALGTMRDRIPPGATCALVFPDRGERYLDTIYDDD 317
Cdd:PLN02556 292 SEDAVNMARELALKEGLMVGISSGAnTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQE 354
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
7-313 |
3.76e-42 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 148.92 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 7 QGGSSVPGVLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGKSTVIESSSGNLGI 86
Cdd:PLN02565 1 EKSSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVLIEPTSGNTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 87 GLAQICAYYGIRFICVVDPRTNRQNIAIMRAYGAEVeVVTdiDPNSGeyLPVRIRRVRELVDSITHAYCPNQYANPLNPQ 166
Cdd:PLN02565 81 GLAFMAAAKGYKLIITMPASMSLERRIILLAFGAEL-VLT--DPAKG--MKGAVQKAEEILAKTPNSYILQQFENPANPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 167 AHHSTV-REVLDALP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIF-GSPVGGRLIPGHGASVRPSLY 243
Cdd:PLN02565 156 IHYETTgPEIWKGTGgKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLsGGKPGPHKIQGIGAGFIPGVL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501131759 244 ADGLADVVIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRiP--PGATCALVFPDRGERYLDTI 313
Cdd:PLN02565 236 DVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKR-PenAGKLIVVIFPSFGERYLSSV 306
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
15-312 |
5.77e-36 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 134.90 E-value: 5.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 15 VLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGKSTVIESSSGNLGIGLAQICAY 94
Cdd:PLN03013 117 VSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVLVEPTSGNTGIGLAFIAAS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 95 YGIRFICVVDPRTNRQNIAIMRAYGAEVeVVTdiDPNSGeyLPVRIRRVRELVDSITHAYCPNQYANPLNPQAHHSTVRE 174
Cdd:PLN03013 197 RGYRLILTMPASMSMERRVLLKAFGAEL-VLT--DPAKG--MTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTGP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 175 VL--DALPTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIF-GSPVGGRLIPGHGASVRPSLYADGLADVV 251
Cdd:PLN03013 272 EIwdDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILsGGKPGPHKIQGIGAGFIPKNLDQKIMDEV 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501131759 252 IRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIP-PGATCALVFPDRGeRYLDT 312
Cdd:PLN03013 352 IAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPEnAGKLIAVSLFASG-RDIYT 412
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
14-322 |
2.05e-19 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 88.51 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 14 GVLSTIGATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkSTVIESSSGNLGIGLAQICA 93
Cdd:PLN02356 46 GLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPG-GVVTEGSAGSTAISLATVAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 94 YYGIRFICVVDPRTNRQNIAIMRAYGAEVEVVTDID-PNSGEYLPVRIRRVRE--------------------------- 145
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVRPVSiTHKDHYVNIARRRALEanelaskrrkgsetdgihlektngcis 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 146 --------LVDSITHAYCPNQYANPLNPQAHHS-TVREVLDALP-TLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVD 215
Cdd:PLN02356 205 eeekenslFSSSCTGGFFADQFENLANFRAHYEgTGPEIWEQTQgNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLID 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 216 ALGSAIFGSPVGGRLIPGHGASVRP-----SLYADGLA-------------DVVIRVDDLDTVVGCRRLAAREAILAGGS 277
Cdd:PLN02356 285 PPGSGLFNKVTRGVMYTREEAEGRRlknpfDTITEGIGinrltqnflmaklDGAFRGTDKEAVEMSRYLLKNDGLFVGSS 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 501131759 278 SGavVSALGTMR--DRIPPGATCALVFPDRGERYLDTIYDDDWVATH 322
Cdd:PLN02356 365 SA--MNCVGAVRvaQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQH 409
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
22-301 |
8.86e-15 |
|
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: 73.92 E-value: 8.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 22 TPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRdrirdgRLVP--GKSTVIESSSGNLGIGLAQICAYYGIR- 98
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALA------SLSEeeRARGVVAASAGNHAQGVAYAARLLGIPa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 99 FICVvdPRTN-RQNIAIMRAYGAEVEVVtdidpnsGEYLPVRIRRVRELVDS----ITHAYcpnqyanplNP------QA 167
Cdd:COG1171 99 TIVM--PETApAVKVAATRAYGAEVVLH-------GDTYDDAEAAAAELAEEegatFVHPF---------DDpdviagQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 168 hhsTV-REVLDALPTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSA-IFGSPVGGRLIPGHGasvrPSLYAD 245
Cdd:COG1171 161 ---TIaLEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAaMYRSLAAGEPVTLPG----VDTIAD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501131759 246 GLA----------------DVVIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIpPGATCALV 301
Cdd:COG1171 234 GLAvgrpgeltfeilrdlvDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERL-KGKRVVVV 304
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
20-311 |
1.73e-14 |
|
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: 73.70 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 20 GATPIVELTKLNPDNPFRTFAKLESHNPGGSIKDR---SALEMLRDRirdgrlvpGKSTVIESSSGNLGIGLAQICAYYG 96
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRamqVAVSLALER--------GAKTIVCASSGNGSAALAAYAARAG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 97 IR-FICVVDPRTNRQNIAIMRAYGAEVEVV-TDIDPnsgeylpvRIRRVRELVDSitHAYCPnqyANPLNP-----Q--A 167
Cdd:COG0498 137 IEvFVFVPEGKVSPGQLAQMLTYGAHVIAVdGNFDD--------AQRLVKELAAD--EGLYA---VNSINParlegQktY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 168 HHSTVrEVLDALPtlDFLFCATSSCGTLRGCAEYLRRRQ-------LPvQIVAVDALGSAifgsPV-----GGRLIPghg 235
Cdd:COG0498 204 AFEIA-EQLGRVP--DWVVVPTGNGGNILAGYKAFKELKelglidrLP-RLIAVQATGCN----PIltafeTGRDEY--- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 236 ASVRPSLYADGLA------------------DVVIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDR--IPPG 295
Cdd:COG0498 273 EPERPETIAPSMDignpsngeralfalresgGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPD 352
|
330 340
....*....|....*....|...
gi 501131759 296 ATCALV-------FPDRGERYLD 311
Cdd:COG0498 353 EPVVVLstghglkFPDAVREALG 375
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
22-301 |
3.48e-13 |
|
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: 69.05 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 22 TPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRlvpgKSTVIESSSGNLGIGLAQICAYYGIR-FI 100
Cdd:cd01562 18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEER----AKGVVAASAGNHAQGVAYAAKLLGIPaTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 101 CVvdPRTN-RQNIAIMRAYGAEVEVVtdidpnsGEYLPVRIRRVRELVDSITHAYCPnqyanPLN-PQ--AHHSTV-REV 175
Cdd:cd01562 94 VM--PETApAAKVDATRAYGAEVVLY-------GEDFDEAEAKARELAEEEGLTFIH-----PFDdPDviAGQGTIgLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 176 LDALPTLDFLFCATSSCGTLRGCAEYLRRRQLPVQIVAVDALGSAIFG-SPVGGRLIPghgaSVRPSLYADGLA------ 248
Cdd:cd01562 160 LEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAqSLAAGKPVT----LPEVDTIADGLAvkrpge 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501131759 249 ----------DVVIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDRIPPGATCALV 301
Cdd:cd01562 236 ltfeiirklvDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVL 298
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
22-282 |
5.93e-13 |
|
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: 68.48 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 22 TPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRlvPGKSTVIESSSGNLGIGLAQICAYYGIRFIC 101
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGL--NECVHVVCSSGGNAGLAAAYAARKLGVPCTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 102 VVDPRTNRQNIAIMRAYGAEVEVVTDIDPNSGEYLPVrirrvrELVDS-ITHAYCPnQYANPLNPQAHHSTVREVLDAL- 179
Cdd:cd06448 80 VVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLRE------ELAENdPGPVYVH-PFDDPLIWEGHSSMVDEIAQQLq 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 180 --PTLDFLFCATSSCGTLRGCAEYLRRRQL-PVQIVAVDALGSAIFGSPV-GGRLIP-GHGASVRPSLYADGLAD----- 249
Cdd:cd06448 153 sqEKVDAIVCSVGGGGLLNGIVQGLERNGWgDIPVVAVETEGAHSLNASLkAGKLVTlPKITSVATSLGAKTVSSqaley 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 501131759 250 ------VVIRVDDLDTVVGCRRLAAREAIL---AGGSSGAVV 282
Cdd:cd06448 233 aqehniKSEVVSDRDAVQACLRFADDERILvepACGAALAVV 274
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
20-301 |
5.34e-11 |
|
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: 62.61 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 20 GATPIVELTKLNPDNPFRT-FAKLESHNPGGSIKDR-------SALEMlrdrirdgrlvpGKSTVIESSSGNLGIGLAQI 91
Cdd:cd01563 21 GNTPLVRAPRLGERLGGKNlYVKDEGLNPTGSFKDRgmtvavsKAKEL------------GVKAVACASTGNTSASLAAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 92 CAYYGIRFICVVDPRTNRQNIAIMRAYGAEV-EVVTDIDpnsgeylpVRIRRVRELVDSitHAYCPNQYANPLNPQAHHS 170
Cdd:cd01563 89 AARAGIKCVVFLPAGKALGKLAQALAYGATVlAVEGNFD--------DALRLVRELAEE--NWIYLSNSLNPYRLEGQKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 171 TVREVLDAL----PtlDFLFCATSSCGTLRG-------------------------------CAEYLRRRQLPVQIVAVD 215
Cdd:cd01563 159 IAFEIAEQLgwevP--DYVVVPVGNGGNITAiwkgfkelkelglidrlprmvgvqaegaapiVRAFKEGKDDIEPVENPE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 216 ALGSAI-FGSPVGGRLIPghgASVRPSlyaDGLAdvvIRVDDLDTVVGCRRLAAREAILAGGSSGAVVSALGTMRDR--I 292
Cdd:cd01563 237 TIATAIrIGNPASGPKAL---RAVRES---GGTA---VAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgiI 307
|
....*....
gi 501131759 293 PPGATCALV 301
Cdd:cd01563 308 DKGERVVVV 316
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
41-260 |
4.80e-09 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 56.62 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 41 KLESHNPGGSIKDRSALEMLRdrirdgrLVPG---KSTVIESSSGNLGIGLAQICAYYGIRFICVVDPRTNRQNIAIMRA 117
Cdd:PRK06815 40 KCEHLQHTGSFKFRGASNKLR-------LLNEaqrQQGVITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 118 YGAEVEVVTDiDPNSGEYLPVRIRRVRELVdsithaycpnqYANPLN-PQ--AHHSTV-REVLDALPTLDFLFCATSSCG 193
Cdd:PRK06815 113 LGAEVRLYGG-DALNAELAARRAAEQQGKV-----------YISPYNdPQviAGQGTIgMELVEQQPDLDAVFVAVGGGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501131759 194 TLRGCAEYLRRRQLPVQIVAVDalgsaifgspvggrliPGHGasvrPSLYADGLADVVIRVDDLDTV 260
Cdd:PRK06815 181 LISGIATYLKTLSPKTEIIGCW----------------PANS----PSLYTSLEAGEIVEVAEQPTL 227
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
20-122 |
1.94e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 52.02 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 20 GATPIVELTKL-NPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRlvpgkSTVIESSSGNLGIGLAQICAYYGIR 98
Cdd:PRK06381 14 GGTPLLRARKLeEELGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY-----SGITVGTCGNYGASIAYFARLYGLK 88
|
90 100
....*....|....*....|....*.
gi 501131759 99 FICVVdPR--TNRQnIAIMRAYGAEV 122
Cdd:PRK06381 89 AVIFI-PRsySNSR-VKEMEKYGAEI 112
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
22-123 |
9.50e-07 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 49.77 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 22 TPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSALEMLRDRIRDGRLvPGKstVIESSSGNLGIGLAQICAYYGIRFIC 101
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKL-PDK--IVAYSTGNHGQAVAYASKLFGIKTRI 100
|
90 100
....*....|....*....|..
gi 501131759 102 VVDPRTNRQNIAIMRAYGAEVE 123
Cdd:PRK06608 101 YLPLNTSKVKQQAALYYGGEVI 122
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
20-146 |
8.45e-06 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 47.11 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 20 GATPIVE---LTKLNPDnpfrTFAKLESHNPGGSIKDRSALEMlrdrIRDGrLVPGKSTVIESSSGNLGIGLAQICAYYG 96
Cdd:PRK05638 65 GGTPLIRariSEKLGEN----VYIKDETRNPTGSFRDRLATVA----VSYG-LPYAANGFIVASDGNAAASVAAYSARAG 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501131759 97 IRFICVVDPRTNRQNIAIMRAYGAEVEVvtdidpnSGEYLPVRIRRVREL 146
Cdd:PRK05638 136 KEAFVVVPRKVDKGKLIQMIAFGAKIIR-------YGESVDEAIEYAEEL 178
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
37-126 |
1.17e-05 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 46.95 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 37 RTFAKLESHNPGGSIKDRSAL--EMLRDRIrdgrlvpGKSTVI-ESSSGNLGIGLAQICAYYGIR---FICVVDPRTNRQ 110
Cdd:PRK13802 348 RVFLKREDLNHTGAHKINNALgqALLVKRM-------GKTRVIaETGAGQHGVATATVCAMLGLKcriYMGQIDARRQAL 420
|
90
....*....|....*.
gi 501131759 111 NIAIMRAYGAEVEVVT 126
Cdd:PRK13802 421 NVARMRMLGAEVVEVT 436
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
18-125 |
4.45e-05 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 44.82 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 18 TIGATPIVELTKlnpdnpfRTFAKLESHNPGGSIKDRSA---LEMLRDRirdgrlvpGKSTVIESSSGNLGIGLAQICAY 94
Cdd:PRK08329 61 TPPITPTVKRSI-------KVYFKLDYLQPTGSFKDRGTyvtVAKLKEE--------GINEVVIDSSGNAALSLALYSLS 125
|
90 100 110
....*....|....*....|....*....|.
gi 501131759 95 YGIRFICVVDPRTNRQNIAIMRAYGAEVEVV 125
Cdd:PRK08329 126 EGIKVHVFVSYNASKEKISLLSRLGAELHFV 156
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
39-122 |
6.41e-05 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 44.21 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 39 FAKLESHNPGGSIKDRSALEMLRDRIRDGRLVPGkstVIESSSGNLGIGLAQICAYYGIRFICVVdPRTN-RQNIAIMRA 117
Cdd:PRK06110 39 WVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG---VISATRGNHGQSVAFAARRHGLAATIVV-PHGNsVEKNAAMRA 114
|
....*
gi 501131759 118 YGAEV 122
Cdd:PRK06110 115 LGAEL 119
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
41-135 |
7.78e-05 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 43.96 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 41 KLESHNPGGSIKDRSA---LEMLRDRirdgrlvpGKSTVIESSSGNLGIGLAQICAYYGIRFICVVdPRTNR-QNIAIMR 116
Cdd:PRK06450 70 KLDFLNPTGSYKDRGSvtlISYLAEK--------GIKQISEDSSGNAGASIAAYGAAAGIEVKIFV-PETASgGKLKQIE 140
|
90 100
....*....|....*....|....*.
gi 501131759 117 AYGAEV-------EVVTDIDPNSGEY 135
Cdd:PRK06450 141 SYGAEVvrvrgsrEDVAKAAENSGYY 166
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
37-122 |
1.48e-04 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 43.14 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 37 RTFAKLESHNPGGSIKDRsALEMLRDRIRDGrlvpGKSTVIESSSGNLGIGLAQICAYYGIRFICVV-DPRTNRQNIAIM 115
Cdd:TIGR00260 39 NLYVKELGHNPTLSFKDR-GMAVALTKALEL----GNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYpAGKISLGKLAQA 113
|
....*..
gi 501131759 116 RAYGAEV 122
Cdd:TIGR00260 114 LGYNAEV 120
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
22-126 |
5.40e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 41.72 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501131759 22 TPIVELTKLNPDNPFRTFAKLESHNPGGSIKDRSAL--EMLRDRIrdgrlvpGKSTVI-ESSSGNLGIGLAQICAYYGIR 98
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALgqALLAKRM-------GKTRIIaETGAGQHGVATATACALFGLK 344
|
90 100 110
....*....|....*....|....*....|.
gi 501131759 99 ---FICVVDPRTNRQNIAIMRAYGAEVEVVT 126
Cdd:PRK13803 345 ctiFMGEEDIKRQALNVERMKLLGANVIPVL 375
|
|
| |
