|
Name |
Accession |
Description |
Interval |
E-value |
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
8-311 |
3.77e-180 |
|
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: 499.20 E-value: 3.77e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 8 NSQTIGHTPLVRLNRI--GNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALAFVAAARG 85
Cdd:TIGR01139 1 ISELIGNTPLVRLNRIegCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 86 YKLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADPQRNLLLQQFNNPANPEIHEKTTGPEIWQDT 165
Cdd:TIGR01139 81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 166 DGEIDVFIAGVGTGGTLTGVSRYIKNTKGkKIISVAVEPTDSPVISQAlageelKPGPHKIQGIGAGFIPGNLDLSLIDR 245
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKP-NIKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827402719 246 VEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEfADKNIVVILPSSGERYLSTPLF 311
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
8-311 |
7.43e-169 |
|
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: 471.00 E-value: 7.43e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 8 NSQTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALAFVAAAR 84
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLApgcDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 85 GYKLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADPqRNLLLQQFNNPANPEIHEKTTGPEIWQD 164
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETN-KYVMLDQFENPANPEAHYKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 165 TDGEIDVFIAGVGTGGTLTGVSRYIKNTKGkKIISVAVEPTDSPVISQAlageelKPGPHKIQGIGAGFIPGNLDLSLID 244
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLKEQNP-NIQIVAVEPAESPVLSGG------EPGPHKIQGIGAGFIPKILDLSLID 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827402719 245 RVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEFADKNIVVILPSSGERYLSTPLF 311
Cdd:TIGR01136 233 EVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
3-308 |
6.05e-161 |
|
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: 450.65 E-value: 6.05e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 3 KIYEDNSQTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALAF 79
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGpgaEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 80 VAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADPqRNLLLQQFNNPANPEIHEKTTGP 159
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETP-GAFWPNQFENPANPEAHYETTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 160 EIWQDTDGEIDVFIAgvgtggtltgvSRYIKNtKGKKIISVAVEPTDSPVISQAlageelKPGPHKIQGIGAGFIPGNLD 239
Cdd:COG0031 161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLKE-RNPDIKIVAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKILD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 240 LSLIDRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLI-ELPEfaDKNIVVILPSSGERYLST 308
Cdd:COG0031 234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAkRLGP--GKTIVTILPDSGERYLST 301
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
2-322 |
5.77e-160 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 449.70 E-value: 5.77e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 2 TKIYEDNSQTIGHTPLVRLNRIGN---GRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALA 78
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEatgCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 79 FVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAA------KGMKGAIAKAEEIVAADPQRNLLLQQFNNPANPEI 152
Cdd:PRK10717 81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 153 HEKTTGPEIWQDTDGEIDVFIAGVGTGGTLTGVSRYIKNTKGKKIIsVAVEPTDSPVISQALAGEELKPGPHKIQGIGAG 232
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKI-VLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 233 FIPGNLDLSLIDRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIElPEFADKNIVVILPSSGERYLSTPLFA 312
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAR-ELGPGHTIVTILCDSGERYQSKLFNP 318
|
330
....*....|
gi 827402719 313 DLFTEKELQQ 322
Cdd:PRK10717 319 DFLREKGLPV 328
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
13-307 |
5.60e-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: 399.97 E-value: 5.60e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 13 GHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALAFVAAARGYKLT 89
Cdd:cd01561 1 GNTPLVRLNRLSPGtgaEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 90 LTMPESMSLERRKLLKALGANLVLTEAAK--GMKGAIAKAEEIVAADPqRNLLLQQFNNPANPEIHEKTTGPEIWQDTDG 167
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETP-NAFWLNQFENPANPEAHYETTAPEIWEQLDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 168 EIDVFIAGVGTGGTLTGVSRYIKNtKGKKIISVAVEPTDSPVISQalageeLKPGPHKIQGIGAGFIPGNLDLSLIDRVE 247
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKE-KNPNVRIVGVDPVGSVLFSG------GPPGPHKIEGIGAGFIPENLDRSLIDEVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 248 KITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEfADKNIVVILPSSGERYLS 307
Cdd:cd01561 233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
4-319 |
9.15e-118 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 342.29 E-value: 9.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 4 IYEDNSQTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQI-VEPTSGNTGIALAF 79
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVDGcvaRIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 80 VAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADPQrNLLLQQFNNPANPEIHEKTTGP 159
Cdd:PLN02565 85 MAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPN-SYILQQFENPANPKIHYETTGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 160 EIWQDTDGEIDVFIAGVGTGGTLTGVSRYIKNtKGKKIISVAVEPTDSPVISQAlageelKPGPHKIQGIGAGFIPGNLD 239
Cdd:PLN02565 164 EIWKGTGGKVDAFVSGIGTGGTITGAGKYLKE-QNPDIKLYGVEPVESAVLSGG------KPGPHKIQGIGAGFIPGVLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 240 LSLIDRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEFADKNIVVILPSSGERYLSTPLFADLFTEKE 319
Cdd:PLN02565 237 VDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKEAE 316
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
4-319 |
5.25e-109 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 320.03 E-value: 5.25e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 4 IYEDNSQTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKG-VQIVEPTSGNTGIALAF 79
Cdd:PLN00011 7 IKNDVTELIGNTPMVYLNNIVDGcvaRIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 80 VAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADPQrNLLLQQFNNPANPEIHEKTTGP 159
Cdd:PLN00011 87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPG-GYIPQQFENPANPEIHYRTTGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 160 EIWQDTDGEIDVFIAGVGTGGTLTGVSRYIKNtKGKKIISVAVEPTDSPVISQAlageelKPGPHKIQGIGAGFIPGNLD 239
Cdd:PLN00011 166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLKE-KNKDIKVCVVEPVESAVLSGG------QPGPHLIQGIGSGIIPFNLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 240 LSLIDRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEFADKNIVVILPSSGERYLSTPLFADLFTEKE 319
Cdd:PLN00011 239 LTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAE 318
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
4-322 |
2.36e-107 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 319.80 E-value: 2.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 4 IYEDNSQTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQI-VEPTSGNTGIALAF 79
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGcvaNIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 80 VAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADPQRnLLLQQFNNPANPEIHEKTTGP 159
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDA-YMLQQFDNPANPKIHYETTGP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 160 EIWQDTDGEIDVFIAGVGTGGTLTGVSRYIKNtKGKKIISVAVEPTDSPVISQAlageelKPGPHKIQGIGAGFIPGNLD 239
Cdd:PLN03013 272 EIWDDTKGKVDIFVAGIGTGGTITGVGRFIKE-KNPKTQVIGVEPTESDILSGG------KPGPHKIQGIGAGFIPKNLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 240 LSLIDRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEFADKNIVVILPSSGeRYLSTPLFADLFTEKE 319
Cdd:PLN03013 345 QKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRW 423
|
...
gi 827402719 320 LQQ 322
Cdd:PLN03013 424 RKC 426
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
2-322 |
8.41e-98 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 293.02 E-value: 8.41e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 2 TKIYEDNSQTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKG-VQIVEPTSGNTGIAL 77
Cdd:PLN02556 47 TKIKTDASQLIGKTPLVYLNKVTEGcgaYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGNMGISL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 78 AFVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADPQRnLLLQQFNNPANPEIHEKTT 157
Cdd:PLN02556 127 AFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDA-FMLQQFSNPANTQVHFETT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 158 GPEIWQDTDGEIDVFIAGVGTGGTLTGVSRYIKnTKGKKIISVAVEPTDSPVISQAlageelKPGPHKIQGIGAGFIPGN 237
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLK-SKNPNVKIYGVEPAESNVLNGG------KPGPHHITGNGVGFKPDI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 238 LDLSLIDRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEFADKNIVVILPSSGERYLSTPLFADLFTE 317
Cdd:PLN02556 279 LDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKE 358
|
....*
gi 827402719 318 KELQQ 322
Cdd:PLN02556 359 AENMQ 363
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
10-311 |
2.62e-96 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 286.77 E-value: 2.62e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 10 QTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALAFVAAARGY 86
Cdd:PRK11761 8 DTIGNTPLVKLQRLPpdrGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 87 KLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADpqRNLLLQQFNNPANPEIHEKTTGPEIWQDTD 166
Cdd:PRK11761 88 RMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEG--EGKVLDQFANPDNPLAHYETTGPEIWRQTE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 167 GEIDVFIAGVGTGGTLTGVSRYIKnTKGKKIISVAVEPTDSPVIsqalageelkPGphkIQGIGAGFIPGNLDLSLIDRV 246
Cdd:PRK11761 166 GRITHFVSSMGTTGTIMGVSRYLK-EQNPAVQIVGLQPEEGSSI----------PG---IRRWPEEYLPKIFDASRVDRV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827402719 247 EKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIElpEFADKNIVVILPSSGERYLSTPLF 311
Cdd:PRK11761 232 LDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAR--ENPNAVIVAIICDRGDRYLSTGVF 294
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
10-311 |
3.65e-80 |
|
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 245.59 E-value: 3.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 10 QTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALAFVAAARGY 86
Cdd:TIGR01138 4 QTVGNTPLVRLQRMGpenGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 87 KLTLTMPESMSLERRKLLKALGANLVLTEAAKGMKGAIAKAEEIVAADPQRnlLLQQFNNPANPEIHEKTTGPEIWQDTD 166
Cdd:TIGR01138 84 RMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGK--LLDQFNNPDNPYAHYTSTGPEIWQQTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 167 GEIDVFIAGVGTGGTLTGVSRYIKnTKGKKIISVAVEPTDSPVIsqalageelkPGphkIQGIGAGFIPGNLDLSLIDRV 246
Cdd:TIGR01138 162 GRITHFVSSMGTTGTIMGVSRFLK-EQNPPVQIVGLQPEEGSSI----------PG---IRRWPTEYLPGIFDASLVDRV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827402719 247 EKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIElpEFADKNIVVILPSSGERYLSTPLF 311
Cdd:TIGR01138 228 LDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLAR--ELPDAVVVAIICDRGDRYLSTGVF 290
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
4-307 |
6.59e-79 |
|
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: 247.41 E-value: 6.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 4 IYEDNSQTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALAFV 80
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSKGlkcELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 81 AAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAAKGM---KGAIAKAEEIVAADPQrNLLLQQFNNPANPEIHEKTT 157
Cdd:TIGR01137 81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPG-AHILDQYRNPSNPLAHYDTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 158 GPEIWQDTDGEIDVFIAGVGTGGTLTGVSRYIKNtKGKKIISVAVEPTDSpVISQALAGEELKPGPHKIQGIGAGFIPGN 237
Cdd:TIGR01137 160 GPEILEQCEGKLDMFVAGVGTGGTITGIARYLKE-SCPGCRIVGADPEGS-ILAQPEELNQTGRTPYKVEGIGYDFIPTV 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 238 LDLSLIDRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEFADKNIVVILPSSGERYLS 307
Cdd:TIGR01137 238 LDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMT 307
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-299 |
2.39e-67 |
|
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: 212.56 E-value: 2.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 9 SQTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRgvlKKGVQIVEPTSGNTGIALAFVAAARG 85
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSkelGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 86 YKLTLTMPESMSLERRKLLKALGANLVLTEAakGMKGAIAKAEEIvAADPQRNLLLQQFNNPANPEIHeKTTGPEIWQDT 165
Cdd:pfam00291 79 LKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAAREL-AAEGPGAYYINQYDNPLNIEGY-GTIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 166 DGEIDVFIAGVGTGGTLTGVSRYIKNTKGK-KIIsvAVEPTDSPVISQALAG---EELKPGPHKIQGIGAGFIPGNLDLS 241
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDvRVI--GVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827402719 242 LIDR----VEKITNEEAISTARRLMEEEGILAGISSGAAVaAALKLIELPEF-ADKNIVVILP 299
Cdd:pfam00291 233 LLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAAL-AALKLALAGELkGGDRVVVVLT 294
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
15-301 |
2.16e-66 |
|
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: 208.52 E-value: 2.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 15 TPLVRLNRI---GNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVqIVEPTSGNTGIALAFVAAARGYKLTLT 91
Cdd:cd00640 1 TPLVRLKRLsklGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGV-IIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 92 MPESMSLERRKLLKALGANLVLTEAakGMKGAIAKAEEIVAADPqRNLLLQQFNNPANPEIHeKTTGPEIWQDTDGE-ID 170
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDP-GAYYVNQFDNPANIAGQ-GTIGLEILEQLGGQkPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 171 VFIAgvgtggtltgvsryikntkgkkiisvaveptdsPVISQALAGeelkpgphkiqGIGAGFIPGNLDLSLI---DRVE 247
Cdd:cd00640 156 AVVV---------------------------------PVGGGGNIA-----------GIARALKELLPNVKVIgvePEVV 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 827402719 248 KITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEfADKNIVVILPSS 301
Cdd:cd00640 192 TVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTGG 244
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
10-307 |
6.67e-30 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 117.78 E-value: 6.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 10 QTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVQIVEPTSGNTGIALAFVAAARGY 86
Cdd:PLN02356 49 DAIGNTPLIRINSLSEAtgcEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 87 KLTLTMPESMSLERRKLLKALGA---------------------------NLVLTEAAKGMK----------GAIAKAEE 129
Cdd:PLN02356 129 KCHVVIPDDVAIEKSQILEALGAtvervrpvsithkdhyvniarrraleaNELASKRRKGSEtdgihlektnGCISEEEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 130 ---IVAADPQRNLLLQQFNNPANPEIHEKTTGPEIWQDTDGEIDVFIAGVGTGGTLTGVSRYIKNtKGKKIISVAVEPTD 206
Cdd:PLN02356 209 ensLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQE-KNPNIKCFLIDPPG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 207 SPVISQALAG-----EE-----LK-PGPHKIQGIGAGFIPGNLDLSLIDRVEKITNEEAISTARRLMEEEGILAGISSGA 275
Cdd:PLN02356 288 SGLFNKVTRGvmytrEEaegrrLKnPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAM 367
|
330 340 350
....*....|....*....|....*....|....
gi 827402719 276 AVAAALKLIEL--PefaDKNIVVILPSSGERYLS 307
Cdd:PLN02356 368 NCVGAVRVAQSlgP---GHTIVTILCDSGMRHLS 398
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
9-302 |
2.95e-18 |
|
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: 83.31 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 9 SQTIGHTPLVR---LNRIGNGRILAKVESRNPSFSVKCRiGA-NMIW--DAEKRgvlKKGVqiVEPTSGNTGIALAFVAA 82
Cdd:cd01562 12 KPVVRRTPLLTsptLSELLGAEVYLKCENLQKTGSFKIR-GAyNKLLslSEEER---AKGV--VAASAGNHAQGVAYAAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 83 ARGYKLTLTMPESMSLERRKLLKALGANLVLTEAakGMKGAIAKAEEIVAadpQRNLLlqqFNNPANpeiHEK------T 156
Cdd:cd01562 86 LLGIPATIVMPETAPAAKVDATRAYGAEVVLYGE--DFDEAEAKARELAE---EEGLT---FIHPFD---DPDviagqgT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 157 TGPEIWQDTdGEID-VF-----------IAGvgtggtltgvsrYIKNTKGK-KIIsvAVEPTDSPVISQAL-AGE--ELK 220
Cdd:cd01562 155 IGLEILEQV-PDLDaVFvpvggggliagIAT------------AVKALSPNtKVI--GVEPEGAPAMAQSLaAGKpvTLP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 221 PGPHKIQGIgAGFIPGNLDLSLI----DRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIElpEFADKNIVV 296
Cdd:cd01562 220 EVDTIADGL-AVKRPGELTFEIIrklvDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKL--DLKGKKVVV 296
|
....*.
gi 827402719 297 ILpsSG 302
Cdd:cd01562 297 VL--SG 300
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
14-302 |
5.86e-18 |
|
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: 82.78 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCRIGANMIW--DAEKRgvlKKGVqiVEPTSGNTGIALAFVAAARGYKL 88
Cdd:COG1171 24 RTPLLRsptLSERLGAEVYLKLENLQPTGSFKLRGAYNALAslSEEER---ARGV--VAASAGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 89 TLTMPESMSLERRKLLKALGANLVLTEAAkgMKGAIAKAEEIVAadpQRNL-LLQQFNNP------AnpeihekTTGPEI 161
Cdd:COG1171 99 TIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAELAE---EEGAtFVHPFDDPdviagqG-------TIALEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 162 WQDTdGEID-VF-----------IAGvgtggtltgvsrYIKNTKgKKIISVAVEPTDSPVISQALAGEELK--PGPHKI- 226
Cdd:COG1171 167 LEQL-PDLDaVFvpvggggliagVAA------------ALKALS-PDIRVIGVEPEGAAAMYRSLAAGEPVtlPGVDTIa 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 227 QGIGAGfIPGNLDLSLI----DRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIElpEFADKNIVVILpsSG 302
Cdd:COG1171 233 DGLAVG-RPGELTFEILrdlvDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKE--RLKGKRVVVVL--SG 307
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
13-298 |
2.25e-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: 72.93 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 13 GHTPLVRLNRIGN---GRILAKVESRNPSFSVKCR---IGANMiwdAEKRGVLKkgvqIVEPTSGNTGIALAFVAAARGY 86
Cdd:COG0498 65 GGTPLVKAPRLADelgKNLYVKEEGHNPTGSFKDRamqVAVSL---ALERGAKT----IVCASSGNGSAALAAYAARAGI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 87 KLTLTMPES-MSLERRKLLKALGANLVLTE-----AAKGMKgAIAKAEEIVAAdpqrnlllqqfnNPANPEIHE--KTTG 158
Cdd:COG0498 138 EVFVFVPEGkVSPGQLAQMLTYGAHVIAVDgnfddAQRLVK-ELAADEGLYAV------------NSINPARLEgqKTYA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 159 PEIWQDTDGEIDVF----------IAGVgtggtltgvsryikntKGKK------IIS-----VAVEPTDSPVISQALAGE 217
Cdd:COG0498 205 FEIAEQLGRVPDWVvvptgnggniLAGY----------------KAFKelkelgLIDrlprlIAVQATGCNPILTAFETG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 218 ELKPGPHKIQ------GIGagfIPGNLD--LSLIDR----VEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIE 285
Cdd:COG0498 269 RDEYEPERPEtiapsmDIG---NPSNGEraLFALREsggtAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLRE 345
|
330
....*....|...
gi 827402719 286 LPEFADKNIVVIL 298
Cdd:COG0498 346 EGEIDPDEPVVVL 358
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
13-302 |
1.79e-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: 64.15 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 13 GHTPLVRLNRI----GNGRILAKVESRNPSFSVKCRiGANM-IWDAEKRGVlkkgVQIVEPTSGNTGIALAFVAAARGYK 87
Cdd:cd01563 21 GNTPLVRAPRLgerlGGKNLYVKDEGLNPTGSFKDR-GMTVaVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 88 LTLTMPESMSLErrKLLKAL--GANLVLTEaakgmkGAIAKAEEIVAADPQRNLLLqqFNNPANPEIHE--KTTGPEIWQ 163
Cdd:cd01563 96 CVVFLPAGKALG--KLAQALayGATVLAVE------GNFDDALRLVRELAEENWIY--LSNSLNPYRLEgqKTIAFEIAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 164 DTDGEI-DVFIAgvgtggTLTGVSRYIKNTKGKK------IIS-----VAVEPTDSPVISQAL--AGEELKPG--PHKI- 226
Cdd:cd01563 166 QLGWEVpDYVVV------PVGNGGNITAIWKGFKelkelgLIDrlprmVGVQAEGAAPIVRAFkeGKDDIEPVenPETIa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 227 QGIGAGFiPGNLDLSL--IDR----VEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEFA-DKNIVVILP 299
Cdd:cd01563 240 TAIRIGN-PASGPKALraVREsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDkGERVVVVLT 318
|
...
gi 827402719 300 SSG 302
Cdd:cd01563 319 GHG 321
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
14-297 |
2.59e-11 |
|
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: 63.47 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCR-IGaNMIWDAEKRGvLKKGVQIVEPTSGNTGIALAFVAAARGYKLT 89
Cdd:cd06448 1 KTPLIEstaLSKTAGCNVFLKLENLQPSGSFKIRgIG-HLCQKSAKQG-LNECVHVVCSSGGNAGLAAAYAARKLGVPCT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 90 LTMPESMSLERRKLLKALGANLVLTEAAKGmKGAIAKAEEIVAADPqRNLLLQQFNNPANPEIHeKTTGPEIWQD--TDG 167
Cdd:cd06448 79 IVVPESTKPRVVEKLRDEGATVVVHGKVWW-EADNYLREELAENDP-GPVYVHPFDDPLIWEGH-SSMVDEIAQQlqSQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 168 EIDVFIAGVGTGGTLTGVSRYIKNTKGKKIISVAVEPTDSPVISQAL-AGE--ELKPGPHKIQGIGAGFIPgnlDLSLID 244
Cdd:cd06448 156 KVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLkAGKlvTLPKITSVATSLGAKTVS---SQALEY 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827402719 245 ------RVEKITNEEAISTARRLMEEEGILAGISSGAAVAAA------LKLIELPEFADKNIVVI 297
Cdd:cd06448 233 aqehniKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVysgkilDLQLEVLLTPLDNVVVV 297
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
15-298 |
3.99e-11 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 62.79 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 15 TPL---VRLNRIGNGRILAKVESRNPSFSVKCRIGANMI--WDAEKRgvlKKGVqiVEPTSGNTGIALAFVAAARGYKLT 89
Cdd:PRK06815 21 TPLehsPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLrlLNEAQR---QQGV--ITASSGNHGQGVALAAKLAGIPVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 90 LTMPESMSLERRKLLKALGANLVLTeaakGMKGAIAKAEEIVAADPQRNLLLQQFNnpaNPEI--HEKTTGPEIWQDTDG 167
Cdd:PRK06815 96 VYAPEQASAIKLDAIRALGAEVRLY----GGDALNAELAARRAAEQQGKVYISPYN---DPQViaGQGTIGMELVEQQPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 168 EIDVFIAGVGTGGTLTGVSrYIKnTKGKKIISVAVEPTDSPVISQAL-AGE--ELKPGPHKIQGIGAGFIPGNLDLSLID 244
Cdd:PRK06815 169 LDAVFVAVGGGGLISGIAT-YLK-TLSPKTEIIGCWPANSPSLYTSLeAGEivEVAEQPTLSDGTAGGVEPGAITFPLCQ 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 827402719 245 RV--EKIT-NEEAISTARRLM--EEEGILAGiSSGAAVAAALKLIelPEFADKNIVVIL 298
Cdd:PRK06815 247 QLidQKVLvSEEEIKEAMRLIaeTDRWLIEG-AAGVALAAALKLA--PRYQGKKVAVVL 302
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
13-302 |
9.13e-09 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 56.36 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 13 GHTPLVRlNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGvlKKGvqIVEPTSGNTGIALAFVAAARGYKLT 89
Cdd:PRK05638 65 GGTPLIR-ARISeklGENVYIKDETRNPTGSFRDRLATVAVSYGLPYA--ANG--FIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 90 LTMPESMSLERRKLLKALGANLV-----LTEAAKGMKGaIAKAEEIVAADPQRNLLLQQfnnpanpeiHEKTTGPEIWQD 164
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIrygesVDEAIEYAEE-LARLNGLYNVTPEYNIIGLE---------GQKTIAFELWEE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 165 TdGEIDVFIAGVGTGGTLTGV---SRYIKN---TKGKKIISVAVEPTdSPVISQALaGEELKPGPHKIQGIgagFIPGNL 238
Cdd:PRK05638 210 I-NPTHVIVPTGSGSYLYSIYkgfKELLEIgviEEIPKLIAVQTERC-NPIASEIL-GNKTKCNETKALGL---YVKNPV 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827402719 239 DLSLIDRVEK-------ITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIELPEFA-DKNIVVILPSSG 302
Cdd:PRK05638 284 MKEYVSEAIKesggtavVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIEkGDKVVLVVTGSG 355
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
9-114 |
1.46e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 55.16 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 9 SQTIGHTPLVR---LNRIGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKKgvQIVEPTSGNTGIALAFVAAARG 85
Cdd:PRK06608 18 KQYLHLTPIVHsesLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPD--KIVAYSTGNHGQAVAYASKLFG 95
|
90 100
....*....|....*....|....*....
gi 827402719 86 YKLTLTMPESMSLERRKLLKALGANLVLT 114
Cdd:PRK06608 96 IKTRIYLPLNTSKVKQQAALYYGGEVILT 124
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
13-133 |
1.66e-08 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 55.39 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 13 GHTPLVRLNR----IGNGRILAKVESRNPSFSVKCRiGANM-IWDAEKRGVlkkgVQIVEPTSGNTGIALAFVAAARGYK 87
Cdd:PRK08197 78 GMTPLLPLPRlgkaLGIGRLWVKDEGLNPTGSFKAR-GLAVgVSRAKELGV----KHLAMPTNGNAGAAWAAYAARAGIR 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 827402719 88 LTLTMPESMSLERRKLLKALGANLVLTEaakgmkGAIAKAEEIVAA 133
Cdd:PRK08197 153 ATIFMPADAPEITRLECALAGAELYLVD------GLISDAGKIVAE 192
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
13-302 |
3.91e-08 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 53.97 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 13 GHTPLVRlnrigNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkkgVQIVEPTSGNTGIALAFVAAARGYKLTLTM 92
Cdd:PRK06450 57 GRTPLIK-----KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKIFV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 93 PESMSLERRKLLKALGANLVlteAAKGMKGAIAKAEEIVAADPQRNLLLQQFNNPAnpeiheKTTGPEIWQDTDGEI--D 170
Cdd:PRK06450 128 PETASGGKLKQIESYGAEVV---RVRGSREDVAKAAENSGYYYASHVLQPQFRDGI------RTLAYEIAKDLDWKIpnY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 171 VFIAGVGTGGTLTGVS--RYIKNT----KGKKIISVAVEPTdSPVISQaLAGEELKPgPHKIQGIGAGFIPGNldLSLID 244
Cdd:PRK06450 199 VFIPVSAGTLLLGVYSgfKHLLDSgvisEMPKIVAVQTEQV-SPLCAK-FKGISYTP-PDKVTSIADALVSTR--PFLLD 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827402719 245 RVEKI---------TNEEAISTARRLMEEEGILAGISSgAAVAAALKLIELpefadKNIVVILPSSG 302
Cdd:PRK06450 274 YMVKAlseygecivVSDNEIVEAWKELAKKGLLVEYSS-ATVYAAYKKYSV-----NDSVLVLTGSG 334
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
13-285 |
5.24e-08 |
|
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: 53.54 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 13 GHTPLVRLNR----IGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkkgVQIVEPTSGNTGIALAFVAAARGYKL 88
Cdd:TIGR00260 21 GVTPLFRAPAlaanVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 89 TLTMPESmSLERRKLLKALGANLVLTeaakGMKGAIAKAEEIV--AADPQRNLLLQQFNN-PANPEiHEKTTGPEIWQDT 165
Cdd:TIGR00260 97 VVLYPAG-KISLGKLAQALGYNAEVV----AIDGNFDDAQRLVkqLFEDKPALGLNSANSiPYRLE-GQKTYAFEAVEQL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 166 DGEID---VFIAGVGTGGTLTGVSRYIKNTKGKKIISV--AVEPTD-SPVISQALAGEELKP--GPHKIQGIGAGFIPGN 237
Cdd:TIGR00260 171 GWEAPdkvVVPVPNSGNFGAIWKGFKEKKMLGLDSLPVkrGIQAEGaADIVRAFLEGGQWEPieTPETLSTAMDIGNPAN 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 827402719 238 LD--LSLIDR----VEKITNEEAISTARRLMEEEGILAGISSGAAVAAALKLIE 285
Cdd:TIGR00260 251 WPraLEAFRRsngyAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVE 304
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
1-135 |
7.11e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 50.09 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 1 MTKIYEDNSQTIGHTPLVRLNRIGN----GRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkKGVQIvePTSGNTGIA 76
Cdd:PRK06381 2 EEELSSSEEKPPGGTPLLRARKLEEelglRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY--SGITV--GTCGNYGAS 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827402719 77 LAFVAAARGYKLTLTMPESMSLERRKLLKALGANLVLT----EAAKGMKGAIAKAEEIVAADP 135
Cdd:PRK06381 78 IAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVdgkyEEAVERSRKFAKENGIYDANP 140
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
65-281 |
1.38e-05 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 46.10 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 65 IVEPTSGNTGIALAFVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEA--AKGMKGAIAKAEEIVAadpqrnLLLQ 142
Cdd:PRK08246 71 VVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAETGA------LLCH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 143 QFNnpaNPEI--HEKTTGPEIWQDTdGEID-VFIAGVGTGGTLTGVSRYikntkGKKIISVAVEPTDSPVISQALAGEEl 219
Cdd:PRK08246 145 AYD---QPEVlaGAGTLGLEIEEQA-PGVDtVLVAVGGGGLIAGIAAWF-----EGRARVVAVEPEGAPTLHAALAAGE- 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827402719 220 kPGPHKIQGIGAGFIP----GNLDLSLI---DRVEKITNEEAISTARRLMEEEGILAGISSGAAVAAAL 281
Cdd:PRK08246 215 -PVDVPVSGIAADSLGarrvGEIAFALArahVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAAL 282
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
22-218 |
8.43e-05 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 44.02 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 22 RIGNgRILAKVESRNPSFSVKCRIG----ANMIWDAEKRGVlkkgvqiVEPTSGNTGIALAFVAAARGYKLTLTMPESMS 97
Cdd:PRK12483 49 RLGN-QVLLKREDLQPVFSFKIRGAynkmARLPAEQLARGV-------ITASAGNHAQGVALAAARLGVKAVIVMPRTTP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 98 LERRKLLKALGANLVLteAAKGMKGAIAKAEEIvaADPQRNLLLQQFNNPaNPEIHEKTTGPEIWQDTDGEIDVFIAGVG 177
Cdd:PRK12483 121 QLKVDGVRAHGGEVVL--HGESFPDALAHALKL--AEEEGLTFVPPFDDP-DVIAGQGTVAMEILRQHPGPLDAIFVPVG 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 827402719 178 TGGTLTGVSRYIKNTKgKKIISVAVEPTDSPVISQALAGEE 218
Cdd:PRK12483 196 GGGLIAGIAAYVKYVR-PEIKVIGVEPDDSNCLQAALAAGE 235
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
249-302 |
5.04e-04 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 41.37 E-value: 5.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 827402719 249 ITNEEAISTARRLMEEEGILAGISSGAAVAAALKL-IELPEfaDKNIVVILpsSG 302
Cdd:cd06446 306 VTDEEALEAFKLLARTEGIIPALESSHAIAYAIKLaKKLGK--EKVIVVNL--SG 356
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
15-134 |
5.35e-04 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 41.26 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 15 TPLVRLNRIGN---GRILAKVESRNPSFSVKCRIGANMI---WDAEKRgvlkKGVqiVEPTSGNTGIALAFVAAARGYKL 88
Cdd:PRK08638 28 TPLPRSNYLSErckGEIFLKLENMQRTGSFKIRGAFNKLsslTDAEKR----KGV--VACSAGNHAQGVALSCALLGIDG 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 827402719 89 TLTMPESMSLERRKLLKALGANLVLteAAKGMKGAIAKAEEIVAAD 134
Cdd:PRK08638 102 KVVMPKGAPKSKVAATCGYGAEVVL--HGDNFNDTIAKVEEIVEEE 145
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
31-112 |
5.91e-04 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 41.13 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 31 KVESRNPSFSVKCRIGANMIWDAEKRGVLKKGVqiVEPTSGNTGIALAFVAAARGYKLTLTMPESMSLERRKLLKALGAN 110
Cdd:PRK06110 41 KHENHTPTGAFKVRGGLVYFDRLARRGPRVRGV--ISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAE 118
|
..
gi 827402719 111 LV 112
Cdd:PRK06110 119 LI 120
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
243-302 |
9.26e-04 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 40.62 E-value: 9.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827402719 243 IDRVE--KITNEEAISTARRLMEEEGILAGISSGAAVAAALKLI-ELPEfaDKNIVVILpsSG 302
Cdd:PRK13028 326 IGRVEyvTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLApELSK--DETILVNL--SG 384
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
14-217 |
1.86e-03 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 39.74 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 14 HTPLVRLN----RIGNgRILAKVESRNPSFSVKCRiGA-NMIW----DAEKRGVlkkgvqiVEPTSGN--TGIALAfvAA 82
Cdd:PRK09224 20 ETPLEKAPklsaRLGN-QVLLKREDLQPVFSFKLR-GAyNKMAqlteEQLARGV-------ITASAGNhaQGVALS--AA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 83 ARGYKLTLTMPESMSLERRKLLKALGANLVL-----TEAAkgmkgaiAKAEEIVAadpQRNLLLqqfnnpanpeIH---- 153
Cdd:PRK09224 89 RLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLhgdsfDEAY-------AHAIELAE---EEGLTF----------IHpfdd 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827402719 154 ------EKTTGPEIWQDTDGEID-VF-----------IAGvgtggtltgvsrYIKNTKGK-KIIsvAVEPTDSPVISQAL 214
Cdd:PRK09224 149 pdviagQGTIAMEILQQHPHPLDaVFvpvggggliagVAA------------YIKQLRPEiKVI--GVEPEDSACLKAAL 214
|
....
gi 827402719 215 -AGE 217
Cdd:PRK09224 215 eAGE 218
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
243-302 |
2.80e-03 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 39.28 E-value: 2.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827402719 243 IDRVE--KITNEEAISTARRLMEEEGILAGISSGAAVAAALKLI-ELPEfaDKNIVVILpsSG 302
Cdd:PRK04346 322 IGRAEyvSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLApTLGK--DQIIVVNL--SG 380
|
|
|