|
Name |
Accession |
Description |
Interval |
E-value |
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
8-312 |
0e+00 |
|
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: 504.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 8 NSLTIGHTPLVRLNRI--GNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARG 85
Cdd:TIGR01139 1 ISELIGNTPLVRLNRIegCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 86 YKLTLTMPETMSVERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPSKYLLLQQFSNPANPEIHEKTTGPEIWEDT 165
Cdd:TIGR01139 81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 166 DGQVDVFIAGVGTGGTLTGVSRYIKNTKGKteLITVAVEPTDSPVIAQAiagqelKPGPHKIQGIGAGFIPGNLDLKLID 245
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN--IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVID 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490520370 246 KVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETfTNKNIVVILPSSGERYLSTALF 312
Cdd:TIGR01139 233 EVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
8-312 |
2.23e-167 |
|
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: 467.14 E-value: 2.23e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 8 NSLTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAAR 84
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLApgcDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 85 GYKLTLTMPETMSVERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPsKYLLLQQFSNPANPEIHEKTTGPEIWED 164
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETN-KYVMLDQFENPANPEAHYKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 165 TDGQVDVFIAGVGTGGTLTGVSRYIKNTKGKteLITVAVEPTDSPVIAQAiagqelKPGPHKIQGIGAGFIPGNLDLKLI 244
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLKEQNPN--IQIVAVEPAESPVLSGG------EPGPHKIQGIGAGFIPKILDLSLI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490520370 245 DKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETFTNKNIVVILPSSGERYLSTALF 312
Cdd:TIGR01136 232 DEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
2-323 |
1.01e-164 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 461.64 E-value: 1.01e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 2 SKIFEDNSLTIGHTPLVRLNRIGN---GRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALA 78
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEatgCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 79 YVAAARGYKLTLTMPETMSVERRKLLKALGANLVLTEGA------KGMKGAIQKAEEIVASDPSKYLLLQQFSNPANPEI 152
Cdd:PRK10717 81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 153 HEKTTGPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKNTKGKteLITVAVEPTDSPVIAQAIAGQELKPGPHKIQGIGA 232
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPK--VKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 233 GFIPGNLDLKLIDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDEtFTNKNIVVILPSSGERYLSTALF 312
Cdd:PRK10717 239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAREL-GPGHTIVTILCDSGERYQSKLFN 317
|
330
....*....|.
gi 490520370 313 ADLFTEKELQQ 323
Cdd:PRK10717 318 PDFLREKGLPV 328
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
3-309 |
4.08e-159 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 446.42 E-value: 4.08e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 3 KIFEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAY 79
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGpgaEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 80 VAAARGYKLTLTMPETMSVERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPsKYLLLQQFSNPANPEIHEKTTGP 159
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETP-GAFWPNQFENPANPEAHYETTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 160 EIWEDTDGQVDVFIAgvgtggtltgvSRYIKNTKGKTELitVAVEPTDSPVIAQAiagqelKPGPHKIQGIGAGFIPGNL 239
Cdd:COG0031 161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLKERNPDIKI--VAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKIL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 240 DLKLIDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETfTNKNIVVILPSSGERYLST 309
Cdd:COG0031 233 DPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLG-PGKTIVTILPDSGERYLST 301
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
13-308 |
4.36e-140 |
|
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: 397.65 E-value: 4.36e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 13 GHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKLT 89
Cdd:cd01561 1 GNTPLVRLNRLSPGtgaEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 90 LTMPETMSVERRKLLKALGANLVLTEGAK--GMKGAIQKAEEIVASDPsKYLLLQQFSNPANPEIHEKTTGPEIWEDTDG 167
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETP-NAFWLNQFENPANPEAHYETTAPEIWEQLDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 168 QVDVFIAGVGTGGTLTGVSRYIKNTKGKTEliTVAVEPTDSPVIaqaiagQELKPGPHKIQGIGAGFIPGNLDLKLIDKV 247
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVR--IVGVDPVGSVLF------SGGPPGPHKIEGIGAGFIPENLDRSLIDEV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490520370 248 IGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETfTNKNIVVILPSSGERYLS 308
Cdd:cd01561 232 VRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
2-320 |
4.67e-117 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 340.75 E-value: 4.67e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 2 SKIFEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVE-LVEPTSGNTGIAL 77
Cdd:PLN02565 3 SSIAKDVTELIGKTPLVYLNNVVDGcvaRIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 78 AYVAAARGYKLTLTMPETMSVERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPSKYLLlQQFSNPANPEIHEKTT 157
Cdd:PLN02565 83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYIL-QQFENPANPKIHYETT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 158 GPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKNTKGKTELItvAVEPTDSPVIAQAiagqelKPGPHKIQGIGAGFIPG 237
Cdd:PLN02565 162 GPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLY--GVEPVESAVLSGG------KPGPHKIQGIGAGFIPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 238 NLDLKLIDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETFTNKNIVVILPSSGERYLSTALFADLFT 317
Cdd:PLN02565 234 VLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKK 313
|
...
gi 490520370 318 EKE 320
Cdd:PLN02565 314 EAE 316
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
4-323 |
2.42e-108 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 322.11 E-value: 2.42e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 4 IFEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVE-LVEPTSGNTGIALAY 79
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGcvaNIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSvLVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 80 VAAARGYKLTLTMPETMSVERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPSKYlLLQQFSNPANPEIHEKTTGP 159
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAY-MLQQFDNPANPKIHYETTGP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 160 EIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKNTKGKTELItvAVEPTDSPVIAQAiagqelKPGPHKIQGIGAGFIPGNL 239
Cdd:PLN03013 272 EIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVI--GVEPTESDILSGG------KPGPHKIQGIGAGFIPKNL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 240 DLKLIDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETFTNKNIVVILPSSGeRYLSTALFADLFTEK 319
Cdd:PLN03013 344 DQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKR 422
|
....
gi 490520370 320 ELQQ 323
Cdd:PLN03013 423 WRKC 426
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
4-320 |
2.86e-105 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 310.78 E-value: 2.86e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 4 IFEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVE-LVEPTSGNTGIALAY 79
Cdd:PLN00011 7 IKNDVTELIGNTPMVYLNNIVDGcvaRIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKStLIEATAGNTGIGLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 80 VAAARGYKLTLTMPETMSVERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPSKYLLlQQFSNPANPEIHEKTTGP 159
Cdd:PLN00011 87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIP-QQFENPANPEIHYRTTGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 160 EIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKNtKGKtELITVAVEPTDSPVIAQAiagqelKPGPHKIQGIGAGFIPGNL 239
Cdd:PLN00011 166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLKE-KNK-DIKVCVVEPVESAVLSGG------QPGPHLIQGIGSGIIPFNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 240 DLKLIDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETFTNKNIVVILPSSGERYLSTALFADLFTEK 319
Cdd:PLN00011 238 DLTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEA 317
|
.
gi 490520370 320 E 320
Cdd:PLN00011 318 E 318
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
2-323 |
6.43e-98 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 293.40 E-value: 6.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 2 SKIFEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPG-VELVEPTSGNTGIAL 77
Cdd:PLN02556 47 TKIKTDASQLIGKTPLVYLNKVTEGcgaYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGNMGISL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 78 AYVAAARGYKLTLTMPETMSVERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPSKYLLlQQFSNPANPEIHEKTT 157
Cdd:PLN02556 127 AFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFML-QQFSNPANTQVHFETT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 158 GPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKNTKGKTELitVAVEPTDSPVIAQAiagqelKPGPHKIQGIGAGFIPG 237
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKI--YGVEPAESNVLNGG------KPGPHHITGNGVGFKPD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 238 NLDLKLIDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETFTNKNIVVILPSSGERYLSTALFADLFT 317
Cdd:PLN02556 278 ILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRK 357
|
....*.
gi 490520370 318 EKELQQ 323
Cdd:PLN02556 358 EAENMQ 363
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
1-312 |
7.73e-96 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 285.61 E-value: 7.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 1 MSKIFEDnslTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIAL 77
Cdd:PRK11761 2 AYPTLED---TIGNTPLVKLQRLPpdrGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 78 AYVAAARGYKLTLTMPETMSVERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASdpSKYLLLQQFSNPANPEIHEKTT 157
Cdd:PRK11761 79 AMIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAE--GEGKVLDQFANPDNPLAHYETT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 158 GPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKNTKGKTELitVAVEPTDSPVIaqaiagqelkPGphkIQGIGAGFIPG 237
Cdd:PRK11761 157 GPEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQI--VGLQPEEGSSI----------PG---IRRWPEEYLPK 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490520370 238 NLDLKLIDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKL-QEDEtftNKNIVVILPSSGERYLSTALF 312
Cdd:PRK11761 222 IFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIaRENP---NAVIVAIICDRGDRYLSTGVF 294
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
12-308 |
1.65e-80 |
|
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: 251.64 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 12 IGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKL 88
Cdd:TIGR01137 9 IGNTPLVRLNKVSKGlkcELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 89 TLTMPETMSVERRKLLKALGANLVLTEGAKGM---KGAIQKAEEIVASDPSKYlLLQQFSNPANPEIHEKTTGPEIWEDT 165
Cdd:TIGR01137 89 IIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPGAH-ILDQYRNPSNPLAHYDTTGPEILEQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 166 DGQVDVFIAGVGTGGTLTGVSRYIKNTKGKteLITVAVEPTDSpVIAQAIAGQELKPGPHKIQGIGAGFIPGNLDLKLID 245
Cdd:TIGR01137 168 EGKLDMFVAGVGTGGTITGIARYLKESCPG--CRIVGADPEGS-ILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVD 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490520370 246 KVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETFTNKNIVVILPSSGERYLS 308
Cdd:TIGR01137 245 EWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMT 307
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-300 |
3.50e-70 |
|
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: 219.87 E-value: 3.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 9 SLTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRgvlKPGVELVEPTSGNTGIALAYVAAARG 85
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSkelGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 86 YKLTLTMPETMSVERRKLLKALGANLVLTEGakGMKGAIQKAEEIvASDPSKYLLLQQFSNPANPEIHeKTTGPEIWEDT 165
Cdd:pfam00291 79 LKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAAREL-AAEGPGAYYINQYDNPLNIEGY-GTIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 166 DGQVDVFIAGVGTGGTLTGVSRYIKNTKGKTELItvAVEPTDSPVIAQAIAG---QELKPGPHKIQGIGAGFIPGNLDLK 242
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVI--GVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490520370 243 LIDK----VIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETFTNKNIVVILP 300
Cdd:pfam00291 233 LLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLT 294
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
15-302 |
1.64e-67 |
|
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: 211.22 E-value: 1.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 15 TPLVRLNRI---GNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVeLVEPTSGNTGIALAYVAAARGYKLTLT 91
Cdd:cd00640 1 TPLVRLKRLsklGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGV-IIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 92 MPETMSVERRKLLKALGANLVLTEGakGMKGAIQKAEEIVASDPsKYLLLQQFSNPANPEIHeKTTGPEIWEDTDGQ-VD 170
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDP-GAYYVNQFDNPANIAGQ-GTIGLEILEQLGGQkPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 171 VFIAgvgtggtltgvsryikntkgktelitvaveptdsPV-----IAqaiagqelkpgphkiqGIGAGFIPGNLDLKLI- 244
Cdd:cd00640 156 AVVV----------------------------------PVggggnIA----------------GIARALKELLPNVKVIg 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 245 --DKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETfTNKNIVVILPSS 302
Cdd:cd00640 186 vePEVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTGG 244
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
12-308 |
1.23e-30 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 119.71 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 12 IGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKL 88
Cdd:PLN02356 51 IGNTPLIRINSLSEAtgcEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKC 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 89 TLTMPETMSVERRKLLKALGAN--------------------------------LVLTEGAKG-----MKGAIQKAEE-- 129
Cdd:PLN02356 131 HVVIPDDVAIEKSQILEALGATvervrpvsithkdhyvniarrraleanelaskRRKGSETDGihlekTNGCISEEEKen 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 130 -IVASDPSKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYI--KNTKGKTELItvavEPT 206
Cdd:PLN02356 211 sLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLqeKNPNIKCFLI----DPP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 207 DSPVIAQAI----------AGQELK-PGPHKIQGIGAGFIPGNLDLKLIDKVIGITNEEAISTARRLMEEEGILAGISSG 275
Cdd:PLN02356 287 GSGLFNKVTrgvmytreeaEGRRLKnPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSA 366
|
330 340 350
....*....|....*....|....*....|...
gi 490520370 276 AAVAAALKLQEdETFTNKNIVVILPSSGERYLS 308
Cdd:PLN02356 367 MNCVGAVRVAQ-SLGPGHTIVTILCDSGMRHLS 398
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
14-303 |
8.42e-20 |
|
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: 87.93 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCRiGA-NMIW----DAEKRGVlkpgvelVEPTSGNTGIALAYVAAARG 85
Cdd:cd01562 17 RTPLLTsptLSELLGAEVYLKCENLQKTGSFKIR-GAyNKLLslseEERAKGV-------VAASAGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 86 YKLTLTMPETMSVERRKLLKALGANLVLTEgaKGMKGAIQKAEEIVASdpSKYLLLqqfsNPANpeiHEK------TTGP 159
Cdd:cd01562 89 IPATIVMPETAPAAKVDATRAYGAEVVLYG--EDFDEAEAKARELAEE--EGLTFI----HPFD---DPDviagqgTIGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 160 EIWEDTDGQVDVF-----------IAGvgtggtltgvsrYIKNTKGKTELItvAVEPTDSPVIAQAI-AGQ--ELKPGPH 225
Cdd:cd01562 158 EILEQVPDLDAVFvpvggggliagIAT------------AVKALSPNTKVI--GVEPEGAPAMAQSLaAGKpvTLPEVDT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 226 KIQGIgAGFIPGNLDL----KLIDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDEtfTNKNIVVILps 301
Cdd:cd01562 224 IADGL-AVKRPGELTFeiirKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL--KGKKVVVVL-- 298
|
..
gi 490520370 302 SG 303
Cdd:cd01562 299 SG 300
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
14-303 |
1.76e-19 |
|
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: 87.01 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCRIGANMIW----DAEKRGVlkpgvelVEPTSGNTGIALAYVAAARGY 86
Cdd:COG1171 24 RTPLLRsptLSERLGAEVYLKLENLQPTGSFKLRGAYNALAslseEERARGV-------VAASAGNHAQGVAYAARLLGI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 87 KLTLTMPETMSVERRKLLKALGANLVLTEGAkgMKGAIQKAEEIVASdpSKYLLLQQFSNP------AnpeihekTTGPE 160
Cdd:COG1171 97 PATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAELAEE--EGATFVHPFDDPdviagqG-------TIALE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 161 IWEDTdGQVD-VF-----------IAGvgtggtltgvsrYIKNTKGKTELItvAVEPTDSPVIAQAIAGQELK--PGPHK 226
Cdd:COG1171 166 ILEQL-PDLDaVFvpvggggliagVAA------------ALKALSPDIRVI--GVEPEGAAAMYRSLAAGEPVtlPGVDT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 227 I-QGIGAGfIPGNLDLKLI----DKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDetFTNKNIVVILps 301
Cdd:COG1171 231 IaDGLAVG-RPGELTFEILrdlvDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER--LKGKRVVVVL-- 305
|
..
gi 490520370 302 SG 303
Cdd:COG1171 306 SG 307
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
6-299 |
3.25e-17 |
|
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: 81.40 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 6 EDNSLTIGH--TPLVRLNRIGN---GRILAKVESRNPSFSVKCR---IGANMiwdAEKRGVlkpgVELVEPTSGNTGIAL 77
Cdd:COG0498 56 EEKAVSLGEggTPLVKAPRLADelgKNLYVKEEGHNPTGSFKDRamqVAVSL---ALERGA----KTIVCASSGNGSAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 78 AYVAAARGYKLTLTMPET-MSVERRKLLKALGANLVLTEGAKGmkGAIQKAEEIvASDPSKYLLlqqfsNPANPEIHE-- 154
Cdd:COG0498 129 AAYAARAGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFD--DAQRLVKEL-AADEGLYAV-----NSINPARLEgq 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 155 KTTGPEIWEDTDGQVDVF----------IAGVgtggtltgvsryikntKGKTELIT----------VAVEPTDSPVIAQA 214
Cdd:COG0498 201 KTYAFEIAEQLGRVPDWVvvptgnggniLAGY----------------KAFKELKElglidrlprlIAVQATGCNPILTA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 215 IAGQELKPGPHKIQGIGAG---FIPGNLD--LKLIDK----VIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQ 285
Cdd:COG0498 265 FETGRDEYEPERPETIAPSmdiGNPSNGEraLFALREsggtAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLR 344
|
330
....*....|....
gi 490520370 286 EDETFTNKNIVVIL 299
Cdd:COG0498 345 EEGEIDPDEPVVVL 358
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
9-303 |
3.04e-15 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 74.94 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 9 SLTIGHTPLVRLNRI----GNGRILAKVESRNPSFSVKCRiGANM-IWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAA 83
Cdd:cd01563 17 SLGEGNTPLVRAPRLgerlGGKNLYVKDEGLNPTGSFKDR-GMTVaVSKAKELGV----KAVACASTGNTSASLAAYAAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 84 RGYKLTLTMPETMSVErrKLLKAL--GANLVLTEGakGMKGAIQKAEEIVASDPSkYLllqqfSNPANPEIHE--KTTGP 159
Cdd:cd01563 92 AGIKCVVFLPAGKALG--KLAQALayGATVLAVEG--NFDDALRLVRELAEENWI-YL-----SNSLNPYRLEgqKTIAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 160 EIWEDTDGQV-DVFIAGVGTGgtltgvSRYIKNTKGKTELIT----------VAVEPTDSPVIAQAI-AGQELK---PGP 224
Cdd:cd01563 162 EIAEQLGWEVpDYVVVPVGNG------GNITAIWKGFKELKElglidrlprmVGVQAEGAAPIVRAFkEGKDDIepvENP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 225 HKI-QGIGAGFiPGNLD--LKLIDK----VIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETF-TNKNIV 296
Cdd:cd01563 236 ETIaTAIRIGN-PASGPkaLRAVREsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIdKGERVV 314
|
....*..
gi 490520370 297 VILPSSG 303
Cdd:cd01563 315 VVLTGHG 321
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
15-299 |
9.99e-13 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 67.80 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 15 TPL---VRLNRIGNGRILAKVESRNPSFSVKCRIGANMI--WDAEKRgvlKPGVelVEPTSGNTGIALAYVAAARGYKLT 89
Cdd:PRK06815 21 TPLehsPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLrlLNEAQR---QQGV--ITASSGNHGQGVALAAKLAGIPVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 90 LTMPETMSVERRKLLKALGANLVLTeGAKGMKGAIqkAEEIVASDPSKylllqQFSNPAN-PEI--HEKTTGPEIWEDTD 166
Cdd:PRK06815 96 VYAPEQASAIKLDAIRALGAEVRLY-GGDALNAEL--AARRAAEQQGK-----VYISPYNdPQViaGQGTIGMELVEQQP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 167 GQVDVFIAGVGTGGTLTGVSrYIKNTKGKTELItvAVEPTDSPVIAQAI-AGQ--ELKPGPHKIQGIGAGFIPGNLDLKL 243
Cdd:PRK06815 168 DLDAVFVAVGGGGLISGIAT-YLKTLSPKTEII--GCWPANSPSLYTSLeAGEivEVAEQPTLSDGTAGGVEPGAITFPL 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490520370 244 IDKVIGIT---NEEAISTARRLM--EEEGILAGiSSGAAVAAALKLQEDetFTNKNIVVIL 299
Cdd:PRK06815 245 CQQLIDQKvlvSEEEIKEAMRLIaeTDRWLIEG-AAGVALAAALKLAPR--YQGKKVAVVL 302
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
9-303 |
2.14e-12 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 67.53 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 9 SLTIGHTPLVRlNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKpgveLVEPTSGNTGIALAYVAAARG 85
Cdd:PRK05638 61 SLGEGGTPLIR-ARISeklGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANG----FIVASDGNAAASVAAYSARAG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 86 YKLTLTMPETMSVERRKLLKALGANLVLTEgaKGMKGAIQKAEEIVAsdpskyllLQQFSNpANPEIH------EKTTGP 159
Cdd:PRK05638 136 KEAFVVVPRKVDKGKLIQMIAFGAKIIRYG--ESVDEAIEYAEELAR--------LNGLYN-VTPEYNiiglegQKTIAF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 160 EIWEDTdGQVDVFIAGVGTGGTLtgvSRYikntKGKTELIT----------VAVEPTDSPVIAQAIAGQELKPGPHKIQG 229
Cdd:PRK05638 205 ELWEEI-NPTHVIVPTGSGSYLY---SIY----KGFKELLEigvieeipklIAVQTERCNPIASEILGNKTKCNETKALG 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490520370 230 IGA-GFIPGNLDLKLIDKVIG---ITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDETF-TNKNIVVILPSSG 303
Cdd:PRK05638 277 LYVkNPVMKEYVSEAIKESGGtavVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIeKGDKVVLVVTGSG 355
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
9-287 |
2.58e-10 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 60.78 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 9 SLTIGHTPLVRLNR----IGNGRILAKVESRNPSFSVKCRiGANM-IWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAA 83
Cdd:PRK08197 74 SLGEGMTPLLPLPRlgkaLGIGRLWVKDEGLNPTGSFKAR-GLAVgVSRAKELGV----KHLAMPTNGNAGAAWAAYAAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 84 RGYKLTLTMPETMSVERRKLLKALGANLVLTEgakgmkGAIQKAEEIVASDPSKYLL--LQQFSNPANPEiHEKTTGPEI 161
Cdd:PRK08197 149 AGIRATIFMPADAPEITRLECALAGAELYLVD------GLISDAGKIVAEAVAEYGWfdVSTLKEPYRIE-GKKTMGLEL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 162 WEDTDGQV-DVFIagvgtggtltgvsrYikNTKGKTELI---------------------TVAVEPTDSPVIAQAI-AGQ 218
Cdd:PRK08197 222 AEQLGWRLpDVIL--------------Y--PTGGGVGLIgiwkafdelealgwiggkrprLVAVQAEGCAPIVKAWeEGK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 219 ELK---PGPHKIQ-GIGagfIPGNLDLKLIDKVIGITN-------EEAISTA-RRLMEEEGILAGISSGAAVAAALKLQE 286
Cdd:PRK08197 286 EESefwEDAHTVAfGIR---VPKALGDFLVLDAVRETGgcaiavsDDAILAAqRELAREEGLFACPEGAATFAAARQLRE 362
|
.
gi 490520370 287 D 287
Cdd:PRK08197 363 S 363
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
9-289 |
1.13e-09 |
|
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: 58.55 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 9 SLTIGHTPLVRLNR----IGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAAR 84
Cdd:TIGR00260 17 DLGEGVTPLFRAPAlaanVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 85 GYKLTLTMPETmSVERRKLLKALGANlVLTEGAKGMKGAIQKAEEIVASDPSKYLLLQQFSNPANPEiHEKTTGPEIWED 164
Cdd:TIGR00260 93 GLKVVVLYPAG-KISLGKLAQALGYN-AEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLE-GQKTYAFEAVEQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 165 TDGQVD---VFIAGVGTGGTLTGVSRYIKNTKGKTEL-ITVAVEPTDSPVIAQA-IAGQELKP--GPHKIQGIGAGFIPG 237
Cdd:TIGR00260 170 LGWEAPdkvVVPVPNSGNFGAIWKGFKEKKMLGLDSLpVKRGIQAEGAADIVRAfLEGGQWEPieTPETLSTAMDIGNPA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490520370 238 NLD--LKLIDKVIG----ITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDET 289
Cdd:TIGR00260 250 NWPraLEAFRRSNGyaedLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGT 307
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
14-298 |
2.18e-09 |
|
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: 57.69 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCR-IGaNMIWDAEKRGVLKPgVELVEPTSGNTGIALAYVAAARGYKLT 89
Cdd:cd06448 1 KTPLIEstaLSKTAGCNVFLKLENLQPSGSFKIRgIG-HLCQKSAKQGLNEC-VHVVCSSGGNAGLAAAYAARKLGVPCT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 90 LTMPETMSVERRKLLKALGANLVLtegakgmKGAIQKaeeivasDPSKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQV 169
Cdd:cd06448 79 IVVPESTKPRVVEKLRDEGATVVV-------HGKVWW-------EADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 170 DVFIAGVGTGGTLTGV-----------------SRYikntkGKTELITVAVEPTDSPVIAQAI-AGQ--ELKPGPHKIQG 229
Cdd:cd06448 145 DEIAQQLQSQEKVDAIvcsvggggllngivqglERN-----GWGDIPVVAVETEGAHSLNASLkAGKlvTLPKITSVATS 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490520370 230 IGAGFIpGNLDLKLID----KVIGITNEEAISTARRLMEEEGILAGISSGAAVAAA-----LKLQEDETFTNKNIVVI 298
Cdd:cd06448 220 LGAKTV-SSQALEYAQehniKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVysgkiLDLQLEVLLTPLDNVVV 296
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
9-303 |
6.69e-09 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 56.28 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 9 SLTIGHTPLVRlnrigNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAARGYKL 88
Cdd:PRK06450 53 SLGEGRTPLIK-----KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 89 TLTMPETMSVERRKLLKALGANLVLTEGAkgmKGAIQKAeeivASDPSKYLLlqqfSNPANPEIHE--KTTGPEIWEDTD 166
Cdd:PRK06450 124 KIFVPETASGGKLKQIESYGAEVVRVRGS---REDVAKA----AENSGYYYA----SHVLQPQFRDgiRTLAYEIAKDLD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 167 GQV--DVFIAGVGTGGTLTGVS--RYIKNTkGKTELI--TVAVEPTD-SPVIAQaIAGQELKPgPHKIQGIGAGFIPGNL 239
Cdd:PRK06450 193 WKIpnYVFIPVSAGTLLLGVYSgfKHLLDS-GVISEMpkIVAVQTEQvSPLCAK-FKGISYTP-PDKVTSIADALVSTRP 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490520370 240 DL--KLIDKVIG-----ITNEEAISTARRLMEEEGILAGISSgAAVAAALKLQEDEtftnkNIVVILPSSG 303
Cdd:PRK06450 270 FLldYMVKALSEygeciVVSDNEIVEAWKELAKKGLLVEYSS-ATVYAAYKKYSVN-----DSVLVLTGSG 334
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
12-114 |
2.23e-07 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 51.70 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 12 IGHTPLVR---LNRIGNGRILAKVESRNPSFSVKCRIGAN-MIWDAEKRgvlKPGVELVEPTSGNTGIALAYVAAARGYK 87
Cdd:PRK06608 21 LHLTPIVHsesLNEMLGHEIFFKVESLQKTGAFKVRGVLNhLLELKEQG---KLPDKIVAYSTGNHGQAVAYASKLFGIK 97
|
90 100
....*....|....*....|....*..
gi 490520370 88 LTLTMPETMSVERRKLLKALGANLVLT 114
Cdd:PRK06608 98 TRIYLPLNTSKVKQQAALYYGGEVILT 124
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
13-132 |
7.98e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 49.70 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 13 GHTPLVRLNRIGN----GRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkPGVELvePTSGNTGIALAYVAAARGYKL 88
Cdd:PRK06381 14 GGTPLLRARKLEEelglRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY--SGITV--GTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 490520370 89 TLTMPETMSVERRKLLKALGANLVLTEGakgmkgaiqKAEEIVA 132
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYVDG---------KYEEAVE 124
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
61-129 |
2.01e-06 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 48.80 E-value: 2.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490520370 61 PGVELVEPTSGNTGIALAYVAAARGYKLTLTMPETMSVERRKLLKALGANLVLTEG--AKGMKGAIQKAEE 129
Cdd:PRK08246 67 PAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAE 137
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
22-219 |
4.05e-04 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 42.09 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 22 RIGNgRILAKVESRNPSFSVKCRIG----ANMIWDAEKRGVlkpgvelVEPTSGNTGIALAYVAAARGYKLTLTMPETMS 97
Cdd:PRK12483 49 RLGN-QVLLKREDLQPVFSFKIRGAynkmARLPAEQLARGV-------ITASAGNHAQGVALAAARLGVKAVIVMPRTTP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 98 VERRKLLKALGANLVLTegAKGMKGAIQKAEEIVASDPSKYllLQQFSNPaNPEIHEKTTGPEIWEDTDGQVDVFIAGVG 177
Cdd:PRK12483 121 QLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEEGLTF--VPPFDDP-DVIAGQGTVAMEILRQHPGPLDAIFVPVG 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490520370 178 TGGTLTGVSRYIKNTkgKTELITVAVEPTDSPVIAQAIAGQE 219
Cdd:PRK12483 196 GGGLIAGIAAYVKYV--RPEIKVIGVEPDDSNCLQAALAAGE 235
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
31-112 |
1.09e-03 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 40.36 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 31 KVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVelVEPTSGNTGIALAYVAAARGYKLTLTMPETMSVERRKLLKALGAN 110
Cdd:PRK06110 41 KHENHTPTGAFKVRGGLVYFDRLARRGPRVRGV--ISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAE 118
|
..
gi 490520370 111 LV 112
Cdd:PRK06110 119 LI 120
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
9-121 |
1.55e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 39.81 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 9 SLTIGHTPLVRLNRigngRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAARGYKL 88
Cdd:PRK08329 59 HLTPPITPTVKRSI----KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKV 130
|
90 100 110
....*....|....*....|....*....|...
gi 490520370 89 TLTMPETMSVERRKLLKALGANLVLTEGAKgMK 121
Cdd:PRK08329 131 HVFVSYNASKEKISLLSRLGAELHFVEGDR-ME 162
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
251-310 |
1.75e-03 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 40.01 E-value: 1.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490520370 251 TNEEAISTARRLMEEEGILAGISSGAAVAAALKLQED---ETFTNKNIVVILPSSGERYLSTA 310
Cdd:PRK13802 607 TDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAAADlkaKGYEHPVMIVNISGRGDKDMNTA 669
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
14-113 |
2.08e-03 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 39.74 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 14 HTPLVRLN----RIGNgRILAKVESRNPSFSVKCRiGA-NMIW----DAEKRGVlkpgvelVEPTSGN--TGIALAyvAA 82
Cdd:PRK09224 20 ETPLEKAPklsaRLGN-QVLLKREDLQPVFSFKLR-GAyNKMAqlteEQLARGV-------ITASAGNhaQGVALS--AA 88
|
90 100 110
....*....|....*....|....*....|....
gi 490520370 83 ARGYKLTLTMPET---MSVERrklLKALGANLVL 113
Cdd:PRK09224 89 RLGIKAVIVMPVTtpdIKVDA---VRAFGGEVVL 119
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
249-303 |
2.22e-03 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 39.46 E-value: 2.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490520370 249 GITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEdETFTNKNIVVILpsSG 303
Cdd:PRK13028 333 TATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAP-ELSKDETILVNL--SG 384
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
14-114 |
2.23e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 39.18 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520370 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCRIGANMIW----DAEKRGVlkpgvelVEPTSGNTGIALAYVAAARGY 86
Cdd:PRK07476 19 RTPLVAsasLSARAGVPVWLKLETLQPTGSFKLRGATNALLslsaQERARGV-------VTASTGNHGRALAYAARALGI 91
|
90 100
....*....|....*....|....*...
gi 490520370 87 KLTLTMPETMSVERRKLLKALGANLVLT 114
Cdd:PRK07476 92 RATICMSRLVPANKVDAIRALGAEVRIV 119
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
249-303 |
9.53e-03 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 37.35 E-value: 9.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490520370 249 GITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDetfTNKNIVVILPSSG 303
Cdd:PRK04346 329 SITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPT---LGKDQIIVVNLSG 380
|
|
| |
