|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
17-326 |
1.34e-138 |
|
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: 395.13 E-value: 1.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 17 VTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKG---CRHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 94 LPESTSLQVVQRLQGEGAEVQLTGKVW-DEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRT--PPGAL 169
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 170 VLAVGGGGLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHS 249
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756761764 250 EVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgCLPPSLTSVVVIVCGGNNINSRELQALKTHL 326
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
13-325 |
3.71e-51 |
|
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: 172.14 E-value: 3.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 13 PFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSggnagiaaayaaRKLGI 88
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaynaLASLSEEERARG---VVAASagnhaqgvayaaRLLGI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 89 PATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASL-------VQELKAV 161
Cdd:COG1171 97 PATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIaleileqLPDLDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 162 LrTPpgalvlavggggllagvvaglleVG------------WQHVP---IIAMETHGAHCFNAAITAGKLVTLPDITSVA 226
Cdd:COG1171 177 F-VP-----------------------VGgggliagvaaalKALSPdirVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 227 KSLGAKTVAARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGllrRLQAEGclppslTSVVV 306
Cdd:COG1171 233 DGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKG------KRVVV 303
|
330
....*....|....*....
gi 756761764 307 IVCGGnNINSRELQALKTH 325
Cdd:COG1171 304 VLSGG-NIDPDRLAEILER 321
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
18-310 |
5.09e-45 |
|
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: 155.16 E-value: 5.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEmAKKGC--RHLVCSSGGNAGIAAAYAARKLGIPATIVLP 95
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEggKTVVEASSGNHGRALAAAAARLGLKVTIVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 96 ESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLAvg 174
Cdd:pfam00291 87 EDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGpGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVP-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 175 gggllagvvaglleVG---------------WQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAK-TVAARA 238
Cdd:pfam00291 165 --------------VGgggliagiarglkelGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756761764 239 LECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEGclppsltSVVVIVCG 310
Cdd:pfam00291 231 LDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGD-------RVVVVLTG 295
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
16-312 |
5.36e-30 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 119.07 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 16 VVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPAT 91
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGaynkMAQLSPEQKARG---VIAASAGNHAQGVAFSAARLGLKAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 92 IVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVL 171
Cdd:TIGR01124 93 IVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 172 AVGGGGLLAGVVAGLLEVGWQhVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE-CMQVckIHSE 250
Cdd:TIGR01124 173 PVGGGGLAAGVAALIKQLMPE-IKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRlCQQY--LDDI 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 756761764 251 VVEDTEAV-SAVQQLLDDERMLVEPACGAALAaiysGLLRRLQAEGCLPPSLtsvVVIVCGGN 312
Cdd:TIGR01124 250 VTVDTDEVcAAIKDLFEDTRAVAEPAGALALA----GLKKYVALHGIRGQTL---VAILSGAN 305
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
13-312 |
1.68e-26 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 106.58 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 13 PFHVVTPLLESwALSQVAGMPVFLKCENVQPSGSFKIRGIGHFcQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATI 92
Cdd:PRK08246 19 PHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGAFNR-LLAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 93 VLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLa 172
Cdd:PRK08246 97 FVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVA- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 173 vggggllagvvaglleVG----------W--QHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE 240
Cdd:PRK08246 176 ----------------VGgggliagiaaWfeGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756761764 241 CMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgclppsltSVVVIVCGGN 312
Cdd:PRK08246 240 LARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGAN 303
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
17-326 |
1.34e-138 |
|
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: 395.13 E-value: 1.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 17 VTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKG---CRHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 94 LPESTSLQVVQRLQGEGAEVQLTGKVW-DEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRT--PPGAL 169
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 170 VLAVGGGGLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHS 249
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756761764 250 EVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgCLPPSLTSVVVIVCGGNNINSRELQALKTHL 326
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
13-325 |
3.71e-51 |
|
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: 172.14 E-value: 3.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 13 PFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSggnagiaaayaaRKLGI 88
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaynaLASLSEEERARG---VVAASagnhaqgvayaaRLLGI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 89 PATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASL-------VQELKAV 161
Cdd:COG1171 97 PATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIaleileqLPDLDAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 162 LrTPpgalvlavggggllagvvaglleVG------------WQHVP---IIAMETHGAHCFNAAITAGKLVTLPDITSVA 226
Cdd:COG1171 177 F-VP-----------------------VGgggliagvaaalKALSPdirVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 227 KSLGAKTVAARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGllrRLQAEGclppslTSVVV 306
Cdd:COG1171 233 DGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKG------KRVVV 303
|
330
....*....|....*....
gi 756761764 307 IVCGGnNINSRELQALKTH 325
Cdd:COG1171 304 VLSGG-NIDPDRLAEILER 321
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
6-313 |
1.94e-47 |
|
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: 161.89 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 6 AEHAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAY 81
Cdd:cd01562 6 AAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 82 AARKLGIPATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASL------- 154
Cdd:cd01562 83 AAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIgleileq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 155 VQELKAVL------------------RTPpgalvlavggggllagvvagllevgwqHVPIIAMETHGAHCFNAAITAGKL 216
Cdd:cd01562 163 VPDLDAVFvpvggggliagiatavkaLSP---------------------------NTKVIGVEPEGAPAMAQSLAAGKP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 217 VTLPDITSVAKSLGAKTVAARALEcmqVCKIH-SEV--VEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQA 293
Cdd:cd01562 216 VTLPEVDTIADGLAVKRPGELTFE---IIRKLvDDVvtVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGK 292
|
330 340
....*....|....*....|
gi 756761764 294 egclppsltSVVVIVCGGNN 313
Cdd:cd01562 293 ---------KVVVVLSGGNI 303
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
18-310 |
5.09e-45 |
|
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: 155.16 E-value: 5.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEmAKKGC--RHLVCSSGGNAGIAAAYAARKLGIPATIVLP 95
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEggKTVVEASSGNHGRALAAAAARLGLKVTIVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 96 ESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLAvg 174
Cdd:pfam00291 87 EDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGpGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVP-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 175 gggllagvvaglleVG---------------WQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAK-TVAARA 238
Cdd:pfam00291 165 --------------VGgggliagiarglkelGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756761764 239 LECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEGclppsltSVVVIVCG 310
Cdd:pfam00291 231 LDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGD-------RVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
18-311 |
1.04e-38 |
|
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: 137.26 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQ---EMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVL 94
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILlaeEEGKLPKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 95 PESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAvlrtppgalvlav 173
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILE------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 174 ggggllagvvagllEVGWQHVPII--AMETHGAHcfnAAITAGKLVTLPDItsvakslgaKTVAARAlecmqvckiHSEV 251
Cdd:cd00640 148 --------------QLGGQKPDAVvvPVGGGGNI---AGIARALKELLPNV---------KVIGVEP---------EVVT 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 252 VEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSglLRRLQAEGclppslTSVVVIVCGG 311
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALK--LAKKLGKG------KTVVVILTGG 244
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
16-312 |
5.36e-30 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 119.07 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 16 VVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPAT 91
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGaynkMAQLSPEQKARG---VIAASAGNHAQGVAFSAARLGLKAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 92 IVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVL 171
Cdd:TIGR01124 93 IVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 172 AVGGGGLLAGVVAGLLEVGWQhVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE-CMQVckIHSE 250
Cdd:TIGR01124 173 PVGGGGLAAGVAALIKQLMPE-IKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRlCQQY--LDDI 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 756761764 251 VVEDTEAV-SAVQQLLDDERMLVEPACGAALAaiysGLLRRLQAEGCLPPSLtsvVVIVCGGN 312
Cdd:TIGR01124 250 VTVDTDEVcAAIKDLFEDTRAVAEPAGALALA----GLKKYVALHGIRGQTL---VAILSGAN 305
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
13-312 |
1.68e-26 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 106.58 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 13 PFHVVTPLLESwALSQVAGMPVFLKCENVQPSGSFKIRGIGHFcQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATI 92
Cdd:PRK08246 19 PHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGAFNR-LLAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 93 VLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLa 172
Cdd:PRK08246 97 FVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVA- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 173 vggggllagvvaglleVG----------W--QHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE 240
Cdd:PRK08246 176 ----------------VGgggliagiaaWfeGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756761764 241 CMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgclppsltSVVVIVCGGN 312
Cdd:PRK08246 240 LARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGAN 303
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
16-312 |
2.60e-25 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 105.61 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 16 VVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPAT 91
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARG---VITASAGNHAQGVALSAARLGIKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 92 IVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVL 171
Cdd:PRK09224 96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVFV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 172 AVGGGGLLAGVVAGLLEVgWQHVPIIAMETHGAHCFNAAITAGKLVTLPDItsvakSLGAKTVAARAL--ECMQVCKIH- 248
Cdd:PRK09224 176 PVGGGGLIAGVAAYIKQL-RPEIKVIGVEPEDSACLKAALEAGERVDLPQV-----GLFADGVAVKRIgeETFRLCQEYv 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756761764 249 SEVVE-DTEAV-SAVQQLLDDERMLVEPAcGA-ALAaiysGLLRRLQAEGCLPPSLtsvVVIVCGGN 312
Cdd:PRK09224 250 DDVITvDTDEIcAAIKDVFEDTRSIAEPA-GAlALA----GLKKYVAQHGIEGETL---VAILSGAN 308
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
18-283 |
3.66e-23 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 99.87 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGaynkMARLPAEQLARG---VITASAGNHAQGVALAAARLGVKAVIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLAV 173
Cdd:PRK12483 115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGPLDAIFVPV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 174 GGGGLLAGVVAGLLEVGwQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAAralECMQVCKIH-SEVV 252
Cdd:PRK12483 195 GGGGLIAGIAAYVKYVR-PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGE---HTFELCRHYvDEVV 270
|
250 260 270
....*....|....*....|....*....|...
gi 756761764 253 E-DTEAV-SAVQQLLDDERMLVEPACGAALAAI 283
Cdd:PRK12483 271 TvSTDELcAAIKDIYDDTRSITEPAGALAVAGI 303
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
16-158 |
5.55e-23 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 96.96 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 16 VVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGC-RHLVCSSGGNAGIAAAYAARKLGIPATIVL 94
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERaRGVVTASTGNHGRALAYAARALGIRATICM 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756761764 95 PESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQEL 158
Cdd:PRK07476 98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEI 161
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
15-313 |
6.20e-22 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 95.26 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 15 HVV--TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGI 88
Cdd:PRK08639 21 DVVpeTPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGaynaISQLSDEELAAG---VVCASAGNHAQGVAYACRHLGI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 89 PATIVLPESTSLQVVQRLQ---GEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTP 165
Cdd:PRK08639 98 PGVIFMPVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 166 PGALVLAVGgggllagvvaglleVGW------------QHVP---IIAMETHGAHCFNAAITAGKLVTLPDI------TS 224
Cdd:PRK08639 178 GSPDYVFVP--------------VGGgglisgvttylkERSPktkIIGVEPAGAASMKAALEAGKPVTLEKIdkfvdgAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 225 VAKsLGAKTVAaralecmqVCKihsEVVEDTEAV------SAVQQLLDDERMLVEPACGAALAAiysglLRRLQAEgcLP 298
Cdd:PRK08639 244 VAR-VGDLTFE--------ILK---DVVDDVVLVpegavcTTILELYNKEGIVAEPAGALSIAA-----LELYKDE--IK 304
|
330
....*....|....*
gi 756761764 299 PSltSVVVIVCGGNN 313
Cdd:PRK08639 305 GK--TVVCVISGGNN 317
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
8-323 |
5.33e-20 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 88.60 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 8 HAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAA 83
Cdd:PRK06815 11 HQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 84 RKLGIPATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELkaVLR 163
Cdd:PRK06815 88 KLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMEL--VEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 164 TPPGALVLAVGGGGLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLV------TLPDITSVAKSLGAKTVAAr 237
Cdd:PRK06815 166 QPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVevaeqpTLSDGTAGGVEPGAITFPL- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 238 aleCMQVCKiHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAiYSGLLRRLQAEgclppsltSVVVIVCGGNNINSR 317
Cdd:PRK06815 245 ---CQQLID-QKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAA-ALKLAPRYQGK--------KVAVVLCGKNIVLEK 311
|
....*.
gi 756761764 318 ELQALK 323
Cdd:PRK06815 312 YLEAVS 317
|
|
| PLN02970 |
PLN02970 |
serine racemase |
5-312 |
1.06e-19 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 88.20 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 5 VAEHAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAA 80
Cdd:PLN02970 15 REARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKG---VVTHSSGNHAAALA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 81 YAARKLGIPATIVLPESTSLQVVQRLQGEGAEVqltgkVWDEANLR-----AQELAKRDGWENVPPFDHPLIWKGHASL- 154
Cdd:PLN02970 92 LAAKLRGIPAYIVVPKNAPACKVDAVIRYGGII-----TWCEPTVEsreavAARVQQETGAVLIHPYNDGRVISGQGTIa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 155 ------VQELKAVLrtppgalvlavggggllagvvaglleVGWQ-----------------HVPIIAMETHGAHCFNAAI 211
Cdd:PLN02970 167 lefleqVPELDVII--------------------------VPISggglisgialaakaikpSIKIIAAEPKGADDAAQSK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 212 TAGKLVTLPDITSVAK----SLGAKTVA-ARALecmqVCKIhsEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSG 286
Cdd:PLN02970 221 AAGEIITLPVTNTIADglraSLGDLTWPvVRDL----VDDV--ITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSD 294
|
330 340
....*....|....*....|....*..
gi 756761764 287 LLR-RLQAEGClppslTSVVVIVCGGN 312
Cdd:PLN02970 295 SFRsNPAWKGC-----KNVGIVLSGGN 316
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
18-154 |
1.24e-19 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 87.87 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PRK08638 28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGIDGKVV 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756761764 94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASL 154
Cdd:PRK08638 105 MPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTI 165
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
18-281 |
9.52e-19 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 86.90 E-value: 9.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGaynmMAKLPKEQLDKG---VICSSAGNHAQGVALSAQRLGCDAVIA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 94 LPEST---SLQVVQRLqgeGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALV 170
Cdd:PLN02550 187 MPVTTpeiKWQSVERL---GATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIF 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 171 LAVGGGGLLAGVVAGLLEVGwQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAAralECMQVCK--IH 248
Cdd:PLN02550 264 VPVGGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGE---ETFRLCRelVD 339
|
250 260 270
....*....|....*....|....*....|....
gi 756761764 249 SEVVEDTEAVSA-VQQLLDDERMLVEPACGAALA 281
Cdd:PLN02550 340 GVVLVSRDAICAsIKDMFEEKRSILEPAGALALA 373
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
18-158 |
1.61e-18 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 85.33 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PRK07334 24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGalnkLLLLTEEERARG---VIAMSAGNHAQGVAYHAQRLGIPATIV 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756761764 94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQEL 158
Cdd:PRK07334 101 MPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEM 165
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
18-157 |
4.17e-17 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 80.59 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCR--HLVCSSGGNAGIAAAYAARKLGIPATIVLP 95
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLpdKIVAYSTGNHGQAVAYASKLFGIKTRIYLP 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756761764 96 ESTSLQVVQRLQGEGAEVQLTgKVWDEANLRAQElAKRDGWENVPPFDHPLIWKGHASLVQE 157
Cdd:PRK06608 104 LNTSKVKQQAALYYGGEVILT-NTRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYE 163
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
18-312 |
4.31e-17 |
|
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.
Pssm-ID: 132036 [Multi-domain] Cd Length: 317 Bit Score: 80.28 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEM-AKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPE 96
Cdd:TIGR02991 20 TPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLsDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMSE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 97 STSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLvqELKAVLRTPPGALVLAVGGG 176
Cdd:TIGR02991 100 LVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTL--GLEVVEQMPDLATVLVPLSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 177 GLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHSEVVEDTE 256
Cdd:TIGR02991 178 GGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLGGGIGLDNRVTFAMCKALLDEIVLVSE 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 756761764 257 A--VSAVQQLLDDERMLVEPACGAALAAIYSGllrRLQAEGclppsltSVVVIVCGGN 312
Cdd:TIGR02991 258 AeiAAGIRHAYAEEREIVEGAGAVGIAALLAG---KIKNPG-------PCAVIVSGRN 305
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
18-158 |
5.04e-17 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 80.45 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAG---VVTFSSGNHAQAIALSARLLGIPATIV 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756761764 94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQEL 158
Cdd:PRK07048 102 MPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKEL 166
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
26-312 |
8.29e-14 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 70.79 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 26 LSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKG--CRHLVCSSGGNAGIAAAYAARKLGIPATIVLPESTSLQVV 103
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGprVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 104 QRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFdHPLIWKGHASLVQELkavLRTPPGALVLAVGGGGLLAGVV 183
Cdd:PRK06110 110 AAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALEL---FRAVPDLDVVYVPIGMGSGICG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 184 AGLLE--VGWQhVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHSEVVEDTEAVSAV 261
Cdd:PRK06110 186 AIAARdaLGLK-TRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAM 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 756761764 262 QQLLDDERMLVEPACGAALAAIysgLLRRLQAEGclppslTSVVVIVCGGN 312
Cdd:PRK06110 265 RAYFTDTHNVAEGAGAAALAAA---LQERERLAG------KRVGLVLSGGN 306
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
34-160 |
2.33e-11 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 63.88 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 34 VFLKCENVQPSGSFKIRG-IGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPESTSLQVVQRLQGEGAE 112
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGaLNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 756761764 113 VQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKA 160
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAA 177
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
18-310 |
5.99e-11 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 62.61 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMP-VFLKCENVQPSGSFKIRGIG---HFCQEMakkGCRHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd01563 23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTvavSKAKEL---GVKAVACASTGNTSASLAAYAARAGIKCVVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRD---------------------------GWEnVPpfDH-- 144
Cdd:cd01563 100 LPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENwiylsnslnpyrlegqktiafeiaeqlGWE-VP--DYvv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 145 -PL--------IWKGhaslVQELKavlrtppgalvlavggggllagvvagllEVGW-QHVP-IIAMETHGAHCFNAAITA 213
Cdd:cd01563 177 vPVgnggnitaIWKG----FKELK----------------------------ELGLiDRLPrMVGVQAEGAAPIVRAFKE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 214 GKLVTLP--DITSVAKSL--GAKTVAARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAiysglLR 289
Cdd:cd01563 225 GKDDIEPveNPETIATAIriGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAG-----LK 299
|
330 340
....*....|....*....|.
gi 756761764 290 RLQAEGCLPPSLTsVVVIVCG 310
Cdd:cd01563 300 KLREEGIIDKGER-VVVVLTG 319
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
17-307 |
2.24e-08 |
|
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: 54.82 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 17 VTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPE 96
Cdd:COG0498 66 GTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 97 S-TSLqvVQRLQ--GEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFdHPL--------------------------- 146
Cdd:COG0498 146 GkVSP--GQLAQmlTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPArlegqktyafeiaeqlgrvpdwvvvpt 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 147 --------IWKGhaslVQELKavlrtppgalvlavggggllagvvagllEVGW-QHVP-IIAMETHGAHCFNAAITAGKL 216
Cdd:COG0498 223 gnggnilaGYKA----FKELK----------------------------ELGLiDRLPrLIAVQATGCNPILTAFETGRD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 217 VTLPDitsvakslGAKTVA-----------ARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAiys 285
Cdd:COG0498 271 EYEPE--------RPETIApsmdignpsngERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAG--- 339
|
330 340
....*....|....*....|..
gi 756761764 286 glLRRLQAEGCLPPSLTSVVVI 307
Cdd:COG0498 340 --LRKLREEGEIDPDEPVVVLS 359
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
11-136 |
8.43e-06 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 46.92 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 11 QEPFHVV------TPLLESWALSQVAGMP-VFLKCENVQPSGSFKIRGIGhFCQEMAKK-GCRHLVCSSGGNAGIAAAYA 82
Cdd:PRK08197 67 RDPEHIVslgegmTPLLPLPRLGKALGIGrLWVKDEGLNPTGSFKARGLA-VGVSRAKElGVKHLAMPTNGNAGAAWAAY 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 756761764 83 ARKLGIPATIVLPESTSLQVVQRLQGEGAEVQLT-GKVWDEANLRAQELAKRdGW 136
Cdd:PRK08197 146 AARAGIRATIFMPADAPEITRLECALAGAELYLVdGLISDAGKIVAEAVAEY-GW 199
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
17-318 |
8.71e-06 |
|
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: 46.61 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 17 VTPLLESWALSQ-VAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLP 95
Cdd:TIGR00260 22 VTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 96 E-STSL-QVVQRLqGEGAEV-QLTGKvWDEANLRAQELAKRD-GWE----NVPPFdHPLIWKGHA-SLVQELKAVLRTPP 166
Cdd:TIGR00260 102 AgKISLgKLAQAL-GYNAEVvAIDGN-FDDAQRLVKQLFEDKpALGlnsaNSIPY-RLEGQKTYAfEAVEQLGWEAPDKV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 167 GALVLAVGGGGLLAGVVAGLLEVGWQHVPI-IAMETHGAHCF-NAAITAGKLVTLPDITSVAKSL--GAKTVAARALECM 242
Cdd:TIGR00260 179 VVPVPNSGNFGAIWKGFKEKKMLGLDSLPVkRGIQAEGAADIvRAFLEGGQWEPIETPETLSTAMdiGNPANWPRALEAF 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 756761764 243 QVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAiysglLRRLQAEGCLPPSLTSVVVIVcgGNNINSRE 318
Cdd:TIGR00260 259 RRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAA-----LLKLVEKGTADPAERVVCALT--GNGLKDPE 327
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
18-158 |
1.54e-05 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 46.34 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESwALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPES 97
Cdd:PRK05638 67 TPLIRA-RISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756761764 98 TSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQEL 158
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFEL 206
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
18-151 |
1.60e-03 |
|
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: 39.80 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGC----RHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 756761764 94 LPESTSLQVVQRLQGEGAEVQLTGKVWDE----ANLRAQELAKR-DGWENVPPFDHPLIWKGH 151
Cdd:cd01561 83 MPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAEtPNAFWLNQFENPANPEAH 145
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
4-135 |
6.64e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 37.88 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 4 PVAEHAKQEPFHVVTPLLEswalsqvAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAA 83
Cdd:PRK08329 51 PVDEEFLPHLTPPITPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYS 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 756761764 84 RKLGIPATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDG 135
Cdd:PRK08329 124 LSEGIKVHVFVSYNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNN 175
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
18-166 |
7.91e-03 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 37.76 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756761764 18 TPLLESWALSQVAGM-PVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPE 96
Cdd:PRK06381 16 TPLLRARKLEEELGLrKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756761764 97 STSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFD-HPLI-WKGHASLVQELKAVLRTPP 166
Cdd:PRK06381 96 SYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSvNSVVdIEAYSAIAYEIYEALGDVP 167
|
|
|