|
Name |
Accession |
Description |
Interval |
E-value |
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
8-312 |
2.56e-173 |
|
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273465 Cd Length: 298 Bit Score: 482.25 E-value: 2.56e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 8 NSLTIGHTPLVRLNRI--GNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARG 85
Cdd:TIGR01139 1 ISELIGNTPLVRLNRIegCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 86 YKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPAKYLLLQQFSNPANPEIHEKTTGPEIWEDT 165
Cdd:TIGR01139 81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 166 DGQVDVFISGVGTGGTLTGVSRYIKGTKGkkDLITVAVEPTDSPVIAQAlageeiKPGPHKIQGIGAGFIPGNLDLKLID 245
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKP--NIKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVID 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864743 246 KVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETfTNKNIVVILPSSGERYLSTALF 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 |
9.87e-159 |
|
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: 445.19 E-value: 9.87e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 8 NSLTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAAR 84
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLApgcDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 85 GYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPaKYLLLQQFSNPANPEIHEKTTGPEIWED 164
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETN-KYVMLDQFENPANPEAHYKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 165 TDGQVDVFISGVGTGGTLTGVSRYIKGTKGkkDLITVAVEPTDSPVIAQAlageeiKPGPHKIQGIGAGFIPGNLDLKLI 244
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLKEQNP--NIQIVAVEPAESPVLSGG------EPGPHKIQGIGAGFIPKILDLSLI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864743 245 DKVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETFTNKNIVVILPSSGERYLSTALF 312
Cdd:TIGR01136 232 DEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
2-323 |
9.43e-158 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 443.92 E-value: 9.43e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 2 SKIYEDNSLTIGHTPLVRLNRIGN---GRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALA 78
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEatgCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 79 YVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGA------KGMKGAIQKAEEIVASDPAKYLLLQQFSNPANPEI 152
Cdd:PRK10717 81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 153 HEKTTGPEIWEDTDGQVDVFISGVGTGGTLTGVSRYIKGTKGkkDLITVAVEPTDSPVIAQALAGEEIKPGPHKIQGIGA 232
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNP--KVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 233 GFIPGNLDLKLIDKVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDEtFTNKNIVVILPSSGERYLSTALF 312
Cdd:PRK10717 239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAREL-GPGHTIVTILCDSGERYQSKLFN 317
|
330
....*....|.
gi 493864743 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 |
8.29e-150 |
|
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: 422.53 E-value: 8.29e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 3 KIYEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAY 79
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGpgaEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 80 VAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPaKYLLLQQFSNPANPEIHEKTTGP 159
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETP-GAFWPNQFENPANPEAHYETTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 160 EIWEDTDGQVDVFISgvgtggtltgvSRYIKgtKGKKDLITVAVEPTDSPVIAQAlageeiKPGPHKIQGIGAGFIPGNL 239
Cdd:COG0031 161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLK--ERNPDIKIVAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKIL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 240 DLKLIDKVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETfTNKNIVVILPSSGERYLST 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 |
6.14e-130 |
|
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: 371.85 E-value: 6.14e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 13 GHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKLT 89
Cdd:cd01561 1 GNTPLVRLNRLSPGtgaEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 90 LTMPETMSIERRKLLKALGANLVLTEGAK--GMKGAIQKAEEIVASDPaKYLLLQQFSNPANPEIHEKTTGPEIWEDTDG 167
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETP-NAFWLNQFENPANPEAHYETTAPEIWEQLDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 168 QVDVFISGVGTGGTLTGVSRYIKgtKGKKDLITVAVEPTDSPVIaqalagEEIKPGPHKIQGIGAGFIPGNLDLKLIDKV 247
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLK--EKNPNVRIVGVDPVGSVLF------SGGPPGPHKIEGIGAGFIPENLDRSLIDEV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864743 248 VAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETfTNKNIVVILPSSGERYLS 308
Cdd:cd01561 232 VRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
2-320 |
2.72e-112 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 328.42 E-value: 2.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 2 SKIYEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVE-LVEPTSGNTGIAL 77
Cdd:PLN02565 3 SSIAKDVTELIGKTPLVYLNNVVDGcvaRIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 78 AYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPAKYLLlQQFSNPANPEIHEKTT 157
Cdd:PLN02565 83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYIL-QQFENPANPKIHYETT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 158 GPEIWEDTDGQVDVFISGVGTGGTLTGVSRYIKgtKGKKDLITVAVEPTDSPVIAQAlageeiKPGPHKIQGIGAGFIPG 237
Cdd:PLN02565 162 GPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLK--EQNPDIKLYGVEPVESAVLSGG------KPGPHKIQGIGAGFIPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 238 NLDLKLIDKVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETFTNKNIVVILPSSGERYLSTALFADLFT 317
Cdd:PLN02565 234 VLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKK 313
|
...
gi 493864743 318 EKE 320
Cdd:PLN02565 314 EAE 316
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
4-323 |
4.22e-102 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 306.32 E-value: 4.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 4 IYEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVE-LVEPTSGNTGIALAY 79
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGcvaNIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSvLVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 80 VAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPAKYlLLQQFSNPANPEIHEKTTGP 159
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAY-MLQQFDNPANPKIHYETTGP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 160 EIWEDTDGQVDVFISGVGTGGTLTGVSRYIKGTKGKKDLItvAVEPTDSPVIAQAlageeiKPGPHKIQGIGAGFIPGNL 239
Cdd:PLN03013 272 EIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVI--GVEPTESDILSGG------KPGPHKIQGIGAGFIPKNL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 240 DLKLIDKVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETFTNKNIVVILPSSGeRYLSTALFADLFTEK 319
Cdd:PLN03013 344 DQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKR 422
|
....
gi 493864743 320 ELQQ 323
Cdd:PLN03013 423 WRKC 426
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
4-320 |
7.47e-101 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 299.23 E-value: 7.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 4 IYEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVE-LVEPTSGNTGIALAY 79
Cdd:PLN00011 7 IKNDVTELIGNTPMVYLNNIVDGcvaRIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKStLIEATAGNTGIGLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 80 VAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPAKYLLlQQFSNPANPEIHEKTTGP 159
Cdd:PLN00011 87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIP-QQFENPANPEIHYRTTGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 160 EIWEDTDGQVDVFISGVGTGGTLTGVSRYIKgtKGKKDLITVAVEPTDSPVIAQAlageeiKPGPHKIQGIGAGFIPGNL 239
Cdd:PLN00011 166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLK--EKNKDIKVCVVEPVESAVLSGG------QPGPHLIQGIGSGIIPFNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 240 DLKLIDKVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETFTNKNIVVILPSSGERYLSTALFADLFTEK 319
Cdd:PLN00011 238 DLTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEA 317
|
.
gi 493864743 320 E 320
Cdd:PLN00011 318 E 318
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
2-323 |
1.14e-92 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 280.31 E-value: 1.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 2 SKIYEDNSLTIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPG-VELVEPTSGNTGIAL 77
Cdd:PLN02556 47 TKIKTDASQLIGKTPLVYLNKVTEGcgaYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGNMGISL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 78 AYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPAKYLLlQQFSNPANPEIHEKTT 157
Cdd:PLN02556 127 AFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFML-QQFSNPANTQVHFETT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 158 GPEIWEDTDGQVDVFISGVGTGGTLTGVSRYIKGTKgkKDLITVAVEPTDSPVIAQAlageeiKPGPHKIQGIGAGFIPG 237
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKN--PNVKIYGVEPAESNVLNGG------KPGPHHITGNGVGFKPD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 238 NLDLKLIDKVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETFTNKNIVVILPSSGERYLSTALFADLFT 317
Cdd:PLN02556 278 ILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRK 357
|
....*.
gi 493864743 318 EKELQQ 323
Cdd:PLN02556 358 EAENMQ 363
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
11-312 |
9.57e-89 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 267.51 E-value: 9.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 11 TIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYK 87
Cdd:PRK11761 9 TIGNTPLVKLQRLPpdrGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 88 LTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASdpAKYLLLQQFSNPANPEIHEKTTGPEIWEDTDG 167
Cdd:PRK11761 89 MKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAE--GEGKVLDQFANPDNPLAHYETTGPEIWRQTEG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 168 QVDVFISGVGTGGTLTGVSRYIKgtKGKKDLITVAVEPTDspviaqalaGEEIkPGphkIQGIGAGFIPGNLDLKLIDKV 247
Cdd:PRK11761 167 RITHFVSSMGTTGTIMGVSRYLK--EQNPAVQIVGLQPEE---------GSSI-PG---IRRWPEEYLPKIFDASRVDRV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864743 248 VAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEdetfTNKN--IVVILPSSGERYLSTALF 312
Cdd:PRK11761 232 LDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAR----ENPNavIVAIICDRGDRYLSTGVF 294
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
12-308 |
3.28e-74 |
|
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: 235.46 E-value: 3.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 12 IGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKL 88
Cdd:TIGR01137 9 IGNTPLVRLNKVSKGlkcELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 89 TLTMPETMSIERRKLLKALGANLVLTEGAKGM---KGAIQKAEEIVASDPAKYlLLQQFSNPANPEIHEKTTGPEIWEDT 165
Cdd:TIGR01137 89 IIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPGAH-ILDQYRNPSNPLAHYDTTGPEILEQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 166 DGQVDVFISGVGTGGTLTGVSRYIKGTKGKkdLITVAVEPTDSpVIAQALAGEEIKPGPHKIQGIGAGFIPGNLDLKLID 245
Cdd:TIGR01137 168 EGKLDMFVAGVGTGGTITGIARYLKESCPG--CRIVGADPEGS-ILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVD 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864743 246 KVVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETFTNKNIVVILPSSGERYLS 308
Cdd:TIGR01137 245 EWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMT 307
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-275 |
9.78e-63 |
|
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: 201.00 E-value: 9.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 9 SLTIGHTPLVRLNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRgvlKPGVELVEPTSGNTGIALAYVAAARG 85
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSkelGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 86 YKLTLTMPETMSIERRKLLKALGANLVLTEGakGMKGAIQKAEEIVASDPaKYLLLQQFSNPANPEIHeKTTGPEIWEDT 165
Cdd:pfam00291 79 LKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGP-GAYYINQYDNPLNIEGY-GTIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 166 DGQVDVFISGVGTGGTLTGVSRYIKGTKGKKDLItvAVEPTDSPVIAQALAG---EEIKPGPHKIQGIGAGFIPGNLDLK 242
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVI--GVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALD 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 493864743 243 LIDK----VVAITNEEAISTARRLMDEEGILAGISSG 275
Cdd:pfam00291 233 LLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSA 269
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
15-302 |
4.14e-60 |
|
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: 192.34 E-value: 4.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 15 TPLVRLNRI---GNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVeLVEPTSGNTGIALAYVAAARGYKLTLT 91
Cdd:cd00640 1 TPLVRLKRLsklGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGV-IIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 92 MPETMSIERRKLLKALGANLVLTEGakGMKGAIQKAEEIVASDPaKYLLLQQFSNPANPEIHeKTTGPEIWEDTDGQ-VD 170
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDP-GAYYVNQFDNPANIAGQ-GTIGLEILEQLGGQkPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 171 VFISGVgtggtltgvsryikGTKGkkdLITvaveptdspviaqalageeikpgphkiqGIGAGFIPGNLDLKLI---DKV 247
Cdd:cd00640 156 AVVVPV--------------GGGG---NIA----------------------------GIARALKELLPNVKVIgvePEV 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 493864743 248 VAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETfTNKNIVVILPSS 302
Cdd:cd00640 191 VTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTGG 244
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
1-308 |
4.37e-27 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 110.08 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 1 MSKIYEDNSL--TIGHTPLVRLNRIGNG---RILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGI 75
Cdd:PLN02356 38 LSKKKPRNGLidAIGNTPLIRINSLSEAtgcEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 76 ALAYVAAARGYKLTLTMPETMSIERRKLLKALGAN--------------------------------LVLTEGAKG---- 119
Cdd:PLN02356 118 SLATVAPAYGCKCHVVIPDDVAIEKSQILEALGATvervrpvsithkdhyvniarrraleanelaskRRKGSETDGihle 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 120 -MKGAIQKAEE---IVASDPAKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFISGVGTGGTLTGVSRYIKgtKGK 195
Cdd:PLN02356 198 kTNGCISEEEKensLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQ--EKN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 196 KDLITVAVEPTDSPVIAQALAG-----EEIK------PGPHKIQGIGAGFIPGNLDLKLIDKVVAITNEEAISTARRLMD 264
Cdd:PLN02356 276 PNIKCFLIDPPGSGLFNKVTRGvmytrEEAEgrrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLK 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 493864743 265 EEGILAGISSGAAVAAALKLLEdETFTNKNIVVILPSSGERYLS 308
Cdd:PLN02356 356 NDGLFVGSSSAMNCVGAVRVAQ-SLGPGHTIVTILCDSGMRHLS 398
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
14-303 |
1.48e-13 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 69.82 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCRiGA-NMIW----DAEKRGVlkpgvelVEPTSGNTGIALAYVAAARG 85
Cdd:cd01562 17 RTPLLTsptLSELLGAEVYLKCENLQKTGSFKIR-GAyNKLLslseEERAKGV-------VAASAGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 86 YKLTLTMPETMSIERRKLLKALGANLVLTEgaKGMKGAIQKAEEIVASDPAKYLllqqfsNPANpeiHEK------TTGP 159
Cdd:cd01562 89 IPATIVMPETAPAAKVDATRAYGAEVVLYG--EDFDEAEAKARELAEEEGLTFI------HPFD---DPDviagqgTIGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 160 EIWEDTDGQVDVF--------ISgvgtggtltGVSRYIKGTKGKkdlITV-AVEPTDSPVIAQAL-AGEEIK-PGPHKIQ 228
Cdd:cd01562 158 EILEQVPDLDAVFvpvgggglIA---------GIATAVKALSPN---TKViGVEPEGAPAMAQSLaAGKPVTlPEVDTIA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 229 GIGAGFIPGNLDL----KLIDKVVAITNEEAISTARRLMDEEGI---------LAGISSGAavaaalklledETFTNKNI 295
Cdd:cd01562 226 DGLAVKRPGELTFeiirKLVDDVVTVSEDEIAAAMLLLFEREKLvaepagalaLAALLSGK-----------LDLKGKKV 294
|
....*...
gi 493864743 296 VVILpsSG 303
Cdd:cd01562 295 VVVL--SG 300
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
14-303 |
2.86e-13 |
|
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: 69.29 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCRIGANMIW----DAEKRGVlkpgvelVEPTSGNTGIALAYVAAARGY 86
Cdd:COG1171 24 RTPLLRsptLSERLGAEVYLKLENLQPTGSFKLRGAYNALAslseEERARGV-------VAASAGNHAQGVAYAARLLGI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 87 KLTLTMPETMSIERRKLLKALGANLVLTEGAkgMKGAIQKAEEIVASDpaKYLLLQQFSNP------AnpeihekTTGPE 160
Cdd:COG1171 97 PATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAELAEEE--GATFVHPFDDPdviagqG-------TIALE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 161 IWEDTdGQVDV---------FISgvgtggtltGVSRYIKGTkgKKDLITVAVEPTDSPVIAQALAGEEIK--PGPHKI-Q 228
Cdd:COG1171 166 ILEQL-PDLDAvfvpvggggLIA---------GVAAALKAL--SPDIRVIGVEPEGAAAMYRSLAAGEPVtlPGVDTIaD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 229 GIGAGfIPGNLDLKLI----DKVVAITNEEAISTARRLMDEEGI---------LAGISSGAavaaalklledETFTNKNI 295
Cdd:COG1171 234 GLAVG-RPGELTFEILrdlvDDIVTVSEDEIAAAMRLLLERTKIvvepagaaaLAALLAGK-----------ERLKGKRV 301
|
....*...
gi 493864743 296 VVILpsSG 303
Cdd:COG1171 302 VVVL--SG 307
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
6-299 |
1.05e-11 |
|
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: 65.22 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 6 EDNSLTIGH--TPLVRLNRIGN---GRILAKVESRNPSFSVKCR---IGANMiwdAEKRGVlkpgVELVEPTSGNTGIAL 77
Cdd:COG0498 56 EEKAVSLGEggTPLVKAPRLADelgKNLYVKEEGHNPTGSFKDRamqVAVSL---ALERGA----KTIVCASSGNGSAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 78 AYVAAARGYKLTLTMPET-MSIERRKLLKALGANLVLTEGAKGmkGAIQKAEEIvASDPAKYLLlqqfsNPANPEIHE-- 154
Cdd:COG0498 129 AAYAARAGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFD--DAQRLVKEL-AADEGLYAV-----NSINPARLEgq 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 155 KTTGPEIWEDTDGQVDVFIsgvgtggtltgvsrY--------IKGTKGKKDLIT----------VAVEPTDSPVIAQALA 216
Cdd:COG0498 201 KTYAFEIAEQLGRVPDWVV--------------VptgnggniLAGYKAFKELKElglidrlprlIAVQATGCNPILTAFE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 217 GEEIKPGPHKIQ------GIGagfIPGNLD--LKLIDK----VVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKL 284
Cdd:COG0498 267 TGRDEYEPERPEtiapsmDIG---NPSNGEraLFALREsggtAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKL 343
|
330
....*....|....*
gi 493864743 285 LEDETFTNKNIVVIL 299
Cdd:COG0498 344 REEGEIDPDEPVVVL 358
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
9-303 |
4.38e-10 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 59.91 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 9 SLTIGHTPLVRLNRI----GNGRILAKVESRNPSFSVKCRiGANM-IWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAA 83
Cdd:cd01563 17 SLGEGNTPLVRAPRLgerlGGKNLYVKDEGLNPTGSFKDR-GMTVaVSKAKELGV----KAVACASTGNTSASLAAYAAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 84 RGYKLTLTMPETMSIErrKLLKAL--GANLVLTEGakGMKGAIQKAEEIVASDPAkYLllqqfSNPANPEIHE--KTTGP 159
Cdd:cd01563 92 AGIKCVVFLPAGKALG--KLAQALayGATVLAVEG--NFDDALRLVRELAEENWI-YL-----SNSLNPYRLEgqKTIAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 160 EIWEDTDGQV-DVFIsgvGTGGTLTGVSRYIKGTK--GKKDLIT-----VAVEPTDSPVIAQAL--AGEEIKPG--PHKI 227
Cdd:cd01563 162 EIAEQLGWEVpDYVV---VPVGNGGNITAIWKGFKelKELGLIDrlprmVGVQAEGAAPIVRAFkeGKDDIEPVenPETI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 228 -QGIGAGFiPGNLD--LKLIDK----VVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETF-TNKNIVVIL 299
Cdd:cd01563 239 aTAIRIGN-PASGPkaLRAVREsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIdKGERVVVVL 317
|
....
gi 493864743 300 PSSG 303
Cdd:cd01563 318 TGHG 321
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
9-138 |
3.11e-09 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 57.70 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 9 SLTIGHTPLVRLNR----IGNGRILAKVESRNPSFSVKCRiGANM-IWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAA 83
Cdd:PRK08197 74 SLGEGMTPLLPLPRlgkaLGIGRLWVKDEGLNPTGSFKAR-GLAVgVSRAKELGV----KHLAMPTNGNAGAAWAAYAAR 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 493864743 84 RGYKLTLTMPETMSIERRKLLKALGANLVLTEgakgmkGAIQKAEEIVASDPAKY 138
Cdd:PRK08197 149 AGIRATIFMPADAPEITRLECALAGAELYLVD------GLISDAGKIVAEAVAEY 197
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
14-136 |
8.36e-08 |
|
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: 52.69 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCR-IGaNMIWDAEKRGVLKPgVELVEPTSGNTGIALAYVAAARGYKLT 89
Cdd:cd06448 1 KTPLIEstaLSKTAGCNVFLKLENLQPSGSFKIRgIG-HLCQKSAKQGLNEC-VHVVCSSGGNAGLAAAYAARKLGVPCT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 493864743 90 LTMPET---MSIERrklLKALGANLVLtEGAKGMKGAIQKAEEIVASDPA 136
Cdd:cd06448 79 IVVPEStkpRVVEK---LRDEGATVVV-HGKVWWEADNYLREELAENDPG 124
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
12-114 |
1.98e-07 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 51.70 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 12 IGHTPLVR---LNRIGNGRILAKVESRNPSFSVKCRIGAN-MIWDAEKRgvlKPGVELVEPTSGNTGIALAYVAAARGYK 87
Cdd:PRK06608 21 LHLTPIVHsesLNEMLGHEIFFKVESLQKTGAFKVRGVLNhLLELKEQG---KLPDKIVAYSTGNHGQAVAYASKLFGIK 97
|
90 100
....*....|....*....|....*..
gi 493864743 88 LTLTMPETMSIERRKLLKALGANLVLT 114
Cdd:PRK06608 98 TRIYLPLNTSKVKQQAALYYGGEVILT 124
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
9-129 |
3.28e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 51.27 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 9 SLTIGHTPLVRlnrigNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAARGYKL 88
Cdd:PRK06450 53 SLGEGRTPLIK-----KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEV 123
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 493864743 89 TLTMPETMSIERRKLLKALGANLVLTEGAkgmKGAIQKAEE 129
Cdd:PRK06450 124 KIFVPETASGGKLKQIESYGAEVVRVRGS---REDVAKAAE 161
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
1-132 |
4.98e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 50.47 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 1 MSKIYEDNSLTIGHTPLVRLNRIGN----GRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkPGVELvePTSGNTGIA 76
Cdd:PRK06381 2 EEELSSSEEKPPGGTPLLRARKLEEelglRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY--SGITV--GTCGNYGAS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 493864743 77 LAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGakgmkgaiqKAEEIVA 132
Cdd:PRK06381 78 IAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDG---------KYEEAVE 124
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
9-303 |
6.30e-07 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 50.58 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 9 SLTIGHTPLVRlNRIG---NGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKpgveLVEPTSGNTGIALAYVAAARG 85
Cdd:PRK05638 61 SLGEGGTPLIR-ARISeklGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANG----FIVASDGNAAASVAAYSARAG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 86 YKLTLTMPETMSIERRKLLKALGANLVLTEgaKGMKGAIQKAEEIvasdpAKYLLLQQFSNPANPEIHE--KTTGPEIWE 163
Cdd:PRK05638 136 KEAFVVVPRKVDKGKLIQMIAFGAKIIRYG--ESVDEAIEYAEEL-----ARLNGLYNVTPEYNIIGLEgqKTIAFELWE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 164 DTdGQVDVFISGVGTGGTLtgvSRYikgtKGKKDLIT----------VAVEPTDSPVIAQALAGEEIKPGPHKIQGIGA- 232
Cdd:PRK05638 209 EI-NPTHVIVPTGSGSYLY---SIY----KGFKELLEigvieeipklIAVQTERCNPIASEILGNKTKCNETKALGLYVk 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864743 233 GFIPGNLDLKLIDK---VVAITNEEAISTARRLMDEEGILAGISSGAAVAAALKLLEDETF-TNKNIVVILPSSG 303
Cdd:PRK05638 281 NPVMKEYVSEAIKEsggTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIeKGDKVVLVVTGSG 355
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
12-129 |
1.42e-06 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 49.18 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 12 IGHTPLVRLNRIGNGR--ILAKVESRNPSFSVKCRiGA-NMIWDAEKrgvlkPGVELVEPTSGNTGIALAYVAAARGYKL 88
Cdd:PRK08246 21 IRRTPVLEADGAGFGPapVWLKLEHLQHTGSFKAR-GAfNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 493864743 89 TLTMPETMSIERRKLLKALGANLVLTEG--AKGMKGAIQKAEE 129
Cdd:PRK08246 95 TVFVPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAE 137
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
15-299 |
3.16e-06 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 48.15 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 15 TPL---VRLNRIGNGRILAKVESRNPSFSVKCRIGANMI--WDAEKRgvlKPGVelVEPTSGNTGIALAYVAAARGYKLT 89
Cdd:PRK06815 21 TPLehsPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLrlLNEAQR---QQGV--ITASSGNHGQGVALAAKLAGIPVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 90 LTMPETMSIERRKLLKALGANLVLTeGAKGMKGaiqkaeEIVASDPAKylllQQ---FSNPAN-PEI--HEKTTGPEIWE 163
Cdd:PRK06815 96 VYAPEQASAIKLDAIRALGAEVRLY-GGDALNA------ELAARRAAE----QQgkvYISPYNdPQViaGQGTIGMELVE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 164 DTDGQVDVFISGVGTGGTLTGVSrYIKGTKGKKDLItvAVEPTDSPVIAQAL-AGEEIKPG--PHKIQGIGAGFIPGNLD 240
Cdd:PRK06815 165 QQPDLDAVFVAVGGGGLISGIAT-YLKTLSPKTEII--GCWPANSPSLYTSLeAGEIVEVAeqPTLSDGTAGGVEPGAIT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864743 241 L----KLIDKVVAITnEEAISTARRLMDE------EGIlAGISsgaavaAALKLLEDETFTNKNIVVIL 299
Cdd:PRK06815 242 FplcqQLIDQKVLVS-EEEIKEAMRLIAEtdrwliEGA-AGVA------LAAALKLAPRYQGKKVAVVL 302
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
9-169 |
1.38e-04 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 43.14 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 9 SLTIGHTPLVRLNR----IGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAAR 84
Cdd:TIGR00260 17 DLGEGVTPLFRAPAlaanVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 85 GYKLTLTMPETmSIERRKLLKALGANlVLTEGAKGMKGAIQKAEEIVASDPAKYLLLQQFSNPANPEiHEKTTGPEIWED 164
Cdd:TIGR00260 93 GLKVVVLYPAG-KISLGKLAQALGYN-AEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLE-GQKTYAFEAVEQ 169
|
....*
gi 493864743 165 TDGQV 169
Cdd:TIGR00260 170 LGWEA 174
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
22-220 |
2.00e-04 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 42.86 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 22 RIGNgRILAKVESRNPSFSVKCRIG----ANMIWDAEKRGVlkpgvelVEPTSGNTGIALAYVAAARGYKLTLTMPETMS 97
Cdd:PRK12483 49 RLGN-QVLLKREDLQPVFSFKIRGAynkmARLPAEQLARGV-------ITASAGNHAQGVALAAARLGVKAVIVMPRTTP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 98 IERRKLLKALGANLVLTegAKGMKGAIQKAEEIVASDPAKYllLQQFSNPaNPEIHEKTTGPEIWEDTDGQVDVFISGVG 177
Cdd:PRK12483 121 QLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEEGLTF--VPPFDDP-DVIAGQGTVAMEILRQHPGPLDAIFVPVG 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493864743 178 TGGTLTGVSRYIKGTkgKKDLITVAVEPTDSPVIAQAL-AGEEI 220
Cdd:PRK12483 196 GGGLIAGIAAYVKYV--RPEIKVIGVEPDDSNCLQAALaAGERV 237
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
31-112 |
1.06e-03 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 40.36 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 31 KVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVelVEPTSGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGAN 110
Cdd:PRK06110 41 KHENHTPTGAFKVRGGLVYFDRLARRGPRVRGV--ISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAE 118
|
..
gi 493864743 111 LV 112
Cdd:PRK06110 119 LI 120
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
9-121 |
1.94e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 39.42 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 9 SLTIGHTPLVRLNRigngRILAKVESRNPSFSVKCRIGANMIWDAEKRGVlkpgVELVEPTSGNTGIALAYVAAARGYKL 88
Cdd:PRK08329 59 HLTPPITPTVKRSI----KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKV 130
|
90 100 110
....*....|....*....|....*....|...
gi 493864743 89 TLTMPETMSIERRKLLKALGANLVLTEGAKgMK 121
Cdd:PRK08329 131 HVFVSYNASKEKISLLSRLGAELHFVEGDR-ME 162
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
14-113 |
2.68e-03 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 39.35 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 14 HTPLVRLN----RIGNgRILAKVESRNPSFSVKCRiGA-NMIW----DAEKRGVlkpgvelVEPTSGN--TGIALAyvAA 82
Cdd:PRK09224 20 ETPLEKAPklsaRLGN-QVLLKREDLQPVFSFKLR-GAyNKMAqlteEQLARGV-------ITASAGNhaQGVALS--AA 88
|
90 100 110
....*....|....*....|....*....|....
gi 493864743 83 ARGYKLTLTMPET---MSIERrklLKALGANLVL 113
Cdd:PRK09224 89 RLGIKAVIVMPVTtpdIKVDA---VRAFGGEVVL 119
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
14-114 |
2.84e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 38.79 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 14 HTPLVR---LNRIGNGRILAKVESRNPSFSVKCRIGANMIW----DAEKRGVlkpgvelVEPTSGNTGIALAYVAAARGY 86
Cdd:PRK07476 19 RTPLVAsasLSARAGVPVWLKLETLQPTGSFKLRGATNALLslsaQERARGV-------VTASTGNHGRALAYAARALGI 91
|
90 100
....*....|....*....|....*...
gi 493864743 87 KLTLTMPETMSIERRKLLKALGANLVLT 114
Cdd:PRK07476 92 RATICMSRLVPANKVDAIRALGAEVRIV 119
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
15-136 |
4.53e-03 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 38.32 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864743 15 TPLVRLN----RIGNGRILAKVES-RNP---------SFSVKC-----------RIGANMIWDAEKRGVLKpGVELVEPT 69
Cdd:PRK08206 45 TPLVALPdlaaELGVGSILVKDESyRFGlnafkalggAYAVARllaeklgldisELSFEELTSGEVREKLG-DITFATAT 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864743 70 SGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGA--KGMKGAIQKAEE---IVASDPA 136
Cdd:PRK08206 124 DGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNydDSVRLAAQEAQEngwVVVQDTA 195
|
|
|