|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02970 |
PLN02970 |
serine racemase |
2-329 |
0e+00 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 612.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 2 EANREKYAADILSIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVT 81
Cdd:PLN02970 1 EAASEKYAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 82 HSSGNHAAALSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIIS 161
Cdd:PLN02970 81 HSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 162 GQGTIALELLEQIQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRA 241
Cdd:PLN02970 161 GQGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 242 SLGDLTWPVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPSCRDCKNIGIVLSGGNVDLG 321
Cdd:PLN02970 241 SLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAWKGCKNVGIVLSGGNVDLG 320
|
....*...
gi 145340114 322 SLWDSFKS 329
Cdd:PLN02970 321 VLWESFSK 328
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
14-319 |
3.90e-136 |
|
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: 388.38 E-value: 3.90e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 14 SIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSL 93
Cdd:cd01562 3 DILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 94 AAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQ 173
Cdd:cd01562 83 AAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEILEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 174 IQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLR-ASLGDLTWPVVR 252
Cdd:cd01562 163 VPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAvKRPGELTFEIIR 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145340114 253 DLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPscrdcKNIGIVLSGGNVD 319
Cdd:cd01562 243 KLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKG-----KKVVVVLSGGNID 304
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
15-323 |
1.27e-132 |
|
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: 380.54 E-value: 1.27e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 15 IKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLA 94
Cdd:COG1171 11 IEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQGVAYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 95 AKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQI 174
Cdd:COG1171 91 ARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 175 QEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRA-SLGDLTWPVVRD 253
Cdd:COG1171 171 PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVgRPGELTFEILRD 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 254 LVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRnnpsCRDcKNIGIVLSGGNVDLGSL 323
Cdd:COG1171 251 LVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER----LKG-KRVVVVLSGGNIDPDRL 315
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
15-320 |
1.38e-110 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 324.28 E-value: 1.38e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 15 IKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLA 94
Cdd:PRK07048 11 VAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQAIALS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 95 AKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQI 174
Cdd:PRK07048 91 ARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 175 QEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRA-SLGDLTWPVVRD 253
Cdd:PRK07048 171 GPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTqHLGNYTFPIIRR 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145340114 254 LVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLsnsfRNNPSCRDcKNIGIVLSGGNVDL 320
Cdd:PRK07048 251 LVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAAL----RGKVPLKG-KRVGVIISGGNVDL 312
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
12-324 |
1.16e-83 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 256.24 E-value: 1.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 12 ILSIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSL-DAEQAAKGVVTHSSGNHAAA 90
Cdd:PRK06608 7 PQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELkEQGKLPDKIVAYSTGNHGQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 91 LSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSeatmSSREEIASKVL--QETGSVLIHPYNDGRIISGQGTIAL 168
Cdd:PRK06608 87 VAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILT----NTRQEAEEKAKedEEQGFYYIHPSDSDSTIAGAGTLCY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 169 ELLEQI-QEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVT-NTIADGLRA-SLGD 245
Cdd:PRK06608 163 EALQQLgFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTlSVSA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 246 LTWPVVRDLVDDVVtLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPScrdcKNIGIVLSGGNVDLGS--- 322
Cdd:PRK06608 243 RTFEYLKKLDDFYL-VEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKP----QKLLVILSGGNIDPILyne 317
|
..
gi 145340114 323 LW 324
Cdd:PRK06608 318 LW 319
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
29-323 |
5.01e-80 |
|
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130197 [Multi-domain] Cd Length: 380 Bit Score: 248.51 E-value: 5.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 29 TPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVPK 108
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 109 GAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQIQEIDAIVVPISGGG 188
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 189 LISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRAS-LGDLTWPVVRDLVDDVVTLEECEII 267
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKkPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 145340114 268 EAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPscrdcKNIGIVLSGGNVDLGSL 323
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKG-----KKIAVVLSGGNIDLNLL 291
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
11-320 |
1.04e-79 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 246.19 E-value: 1.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 11 DILSIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAA 90
Cdd:PRK08638 10 AIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 91 LSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALEL 170
Cdd:PRK08638 90 VALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 171 LEQIQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRASL-GDLTWP 249
Cdd:PRK08638 170 LEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRpGNLTYE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145340114 250 VVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFrnNPSCRDCKNIGIVlSGGNVDL 320
Cdd:PRK08638 250 IVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKL--DQYIQNKKVVAII-SGGNVDL 317
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
22-315 |
1.54e-78 |
|
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: 241.83 E-value: 1.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 22 IKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIP 101
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 102 AYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQE-TGSVLIHPYNDGRIISGQGTIALELLEQIQE-IDA 179
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLGGdPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 180 IVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRA--SLGDLTWPVVRDLVDD 257
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgdEPGALALDLLDEYVGE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 145340114 258 VVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLsnsFRNNPSCRDCKNIGIVLSG 315
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALK---LALAGELKGGDRVVVVLTG 295
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
15-319 |
3.00e-75 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 236.71 E-value: 3.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 15 IKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLA 94
Cdd:PRK07334 10 IRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 95 AKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQI 174
Cdd:PRK07334 90 AQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLEDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 175 QEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQsKVAGKiiTLPV-TNTIADGLRA-SLGDLTWPVVR 252
Cdd:PRK07334 170 PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYA-AIKGV--ALPCgGSTIAEGIAVkQPGQLTLEIVR 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145340114 253 DLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNS--FRNnpscrdcKNIGIVLSGGNVD 319
Cdd:PRK07334 247 RLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPerFRG-------RKVGLVLSGGNID 308
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
14-323 |
6.52e-74 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 230.73 E-value: 6.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 14 SIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSL 93
Cdd:PRK06815 6 AILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 94 AAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQ 173
Cdd:PRK06815 86 AAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 174 IQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRASL--GDLTWPVV 251
Cdd:PRK06815 166 QPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGVepGAITFPLC 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145340114 252 RDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLsnsfRNNPSCRDcKNIGIVLSGGNVDLGSL 323
Cdd:PRK06815 246 QQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAAL----KLAPRYQG-KKVAVVLCGKNIVLEKY 312
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
14-321 |
2.95e-70 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 221.38 E-value: 2.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 14 SIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSL 93
Cdd:PRK07476 5 DIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 94 AAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQ 173
Cdd:PRK07476 85 AARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 174 IQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAE-PKGADDAAqSKVAGKIITLPVTNTIADGLRASLG---DLTWP 249
Cdd:PRK07476 165 LPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSmERGAAMHA-SLAAGRPVQVEEVPTLADSLGGGIGldnRYTFA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145340114 250 VVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPscrdcKNIGIVLSGGNVDLG 321
Cdd:PRK07476 244 MCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARD-----GPIVVVVSGANIDME 310
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
15-323 |
6.08e-68 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 215.20 E-value: 6.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 15 IKEAHDRIKPYIHRTPVLTSESlNSISGRSLFFKCECLQKGGAFKFRGACNAVLSldAEQAAKGVVTHSSGNHAAALSLA 94
Cdd:PRK08246 10 VRAAAQRIAPHIRRTPVLEADG-AGFGPAPVWLKLEHLQHTGSFKARGAFNRLLA--APVPAAGVVAASGGNAGLAVAYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 95 AKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQI 174
Cdd:PRK08246 87 AAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 175 QEIDAIVVPISGGGLISGVALAAksiKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRAS-LGDLTWPVVRD 253
Cdd:PRK08246 167 PGVDTVLVAVGGGGLIAGIAAWF---EGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARrVGEIAFALARA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 254 LVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPSCRdcknIGIVLSGGNVDLGSL 323
Cdd:PRK08246 244 HVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGER----VAVVLCGANTDPATL 309
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
29-323 |
2.75e-66 |
|
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: 216.52 E-value: 2.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 29 TPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVPK 108
Cdd:TIGR01124 18 TPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGLKALIVMPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 109 GAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQIQE-IDAIVVPISGG 187
Cdd:TIGR01124 98 TTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANpLDAVFVPVGGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 188 GLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRAS-LGDLTWPVVRDLVDDVVTLEECEI 266
Cdd:TIGR01124 178 GLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKrVGDETFRLCQQYLDDIVTVDTDEV 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 145340114 267 IEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNpsCRDcKNIGIVLSGGNVDLGSL 323
Cdd:TIGR01124 258 CAAIKDLFEDTRAVAEPAGALALAGLKKYVALHG--IRG-QTLVAILSGANMNFHRL 311
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
29-316 |
6.19e-62 |
|
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: 197.35 E-value: 6.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 29 TPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKG--VVTHSSGNHAAALSLAAKIQGIPAYIVV 106
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 107 PKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQET-GSVLIHPYNDGRIISGQGTIALELLEQI--QEIDAIVVP 183
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQLggQKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 184 ISGGGLISGVALAAKSIKPSIRIIAAEPKgaddaaqskvagkiitlpvtntiadglraslgdltwpvvrdlvddVVTLEE 263
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEPE---------------------------------------------VVTVSD 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 145340114 264 CEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPScrdcKNIGIVLSGG 316
Cdd:cd00640 196 EEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKG----KTVVVILTGG 244
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
35-318 |
1.75e-58 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 196.13 E-value: 1.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 35 ESLNSISGR---SLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVPKGAP 111
Cdd:PRK09224 24 EKAPKLSARlgnQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMPVTTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 112 KCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQIQE-IDAIVVPISGGGLI 190
Cdd:PRK09224 104 DIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAVFVPVGGGGLI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 191 SGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLR-ASLGDLTWPVVRDLVDDVVTLEECEIIEA 269
Cdd:PRK09224 184 AGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAvKRIGEETFRLCQEYVDDVITVDTDEICAA 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 145340114 270 MKMCYEILKVSVEPSGAIGLAAVLSNSFRNNpsCRDcKNIGIVLSGGNV 318
Cdd:PRK09224 264 IKDVFEDTRSIAEPAGALALAGLKKYVAQHG--IEG-ETLVAILSGANM 309
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
15-319 |
3.71e-58 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 193.10 E-value: 3.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 15 IKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLA 94
Cdd:PRK08639 12 IDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAYA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 95 AKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIwseatmssreEI-------------ASKVLQETGSVLIHPYNDGRIIS 161
Cdd:PRK08639 92 CRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFV----------EIvlvgdtfddsaaaAQEYAEETGATFIPPFDDPDVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 162 GQGTIALELLEQIQE---IDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADG 238
Cdd:PRK08639 162 GQGTVAVEILEQLEKegsPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 239 LR-ASLGDLTWPVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVlsnsfrnnPSCRD---CKNIGIVLS 314
Cdd:PRK08639 242 AAvARVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAAL--------ELYKDeikGKTVVCVIS 313
|
....*
gi 145340114 315 GGNVD 319
Cdd:PRK08639 314 GGNND 318
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
29-292 |
5.30e-55 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 187.31 E-value: 5.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 29 TPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVPK 108
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVMPR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 109 GAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQIQ-EIDAIVVPISGG 187
Cdd:PRK12483 118 TTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPgPLDAIFVPVGGG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 188 GLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLR-ASLGDLTWPVVRDLVDDVVTLEECEI 266
Cdd:PRK12483 198 GLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAvAQIGEHTFELCRHYVDEVVTVSTDEL 277
|
250 260
....*....|....*....|....*.
gi 145340114 267 IEAMKMCYEILKVSVEPSGAIGLAAV 292
Cdd:PRK12483 278 CAAIKDIYDDTRSITEPAGALAVAGI 303
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
15-320 |
3.15e-54 |
|
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: 180.05 E-value: 3.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 15 IKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAAALSLA 94
Cdd:TIGR02991 6 IERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRALAYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 95 AKIQGIPAYIVVPKGAPKCKVDNVIRYGGKV-IWSEATMSSREEIaSKVLQETGSVLIHPYNDGRIISGQGTIALELLEQ 173
Cdd:TIGR02991 86 AAEEGVRATICMSELVPQNKVDEIRRLGAEVrIVGRSQDDAQEEV-ERLVADRGLTMLPPFDHPDIVAGQGTLGLEVVEQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 174 IQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRASLG---DLTWPV 250
Cdd:TIGR02991 165 MPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLGGGIGldnRVTFAM 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 251 VRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLSNSFRNNPSCrdckniGIVLSGGNVDL 320
Cdd:TIGR02991 245 CKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPGPC------AVIVSGRNIDM 308
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
10-323 |
9.85e-40 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 142.84 E-value: 9.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 10 ADILSikeAHDRIKPYIHRTPVLTSESLnsisgrSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTHSSGNHAA 89
Cdd:PRK08813 24 ADVLA---AQARLRRYLSPTPLHYAERF------GVWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 90 ALSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALE 169
Cdd:PRK08813 95 GVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 170 LleQIQEIDAIVVPISGGGLISGVALAAKSikPSIRIIAAEPKGADDAAQSkVAGKIITLPVTNTIADGLRASL-GDLTW 248
Cdd:PRK08813 175 L--AAHAPDVVIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARA-IRGDLREIAPVATLADGVKVKIpGFLTR 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145340114 249 PVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAvlsnsFRNNPSCRDCKnigiVLSGGNVDLGSL 323
Cdd:PRK08813 250 RLCSSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAA-----GRRVSGKRKCA----VVSGGNIDATVL 315
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
3-323 |
1.13e-38 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 144.29 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 3 ANREKYAADILSIKEAHDRIKPYIHRTPVLtSESLnsisGRSLFFKCECLQKGGAFKFRGACNAVLSLDAEQAAKGVVTH 82
Cdd:PLN02550 89 PEAMEYLTNILSAKVYDVAIESPLQLAKKL-SERL----GVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 83 SSGNHAAALSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISG 162
Cdd:PLN02550 164 SAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 163 QGTIALELLEQIQ-EIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRA 241
Cdd:PLN02550 244 QGTVGMEIVRQHQgPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 242 SL-GDLTWPVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAvlSNSFRNNPSCRDcKNIGIVLSGGNVDL 320
Cdd:PLN02550 324 KEvGEETFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAG--AEAYCKYYGLKD-ENVVAITSGANMNF 400
|
...
gi 145340114 321 GSL 323
Cdd:PLN02550 401 DRL 403
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
29-294 |
2.02e-33 |
|
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: 125.49 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 29 TPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLSLdAEQAAKG---VVTHSSGNHAAALSLAAKIQGIPAYIV 105
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKS-AKQGLNEcvhVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 106 VPKGAPKCKVDNVIRYGGKVI-----WSEATMSSREEIASKvlqETGSVLIHPYNDGRIISGQGTIALELLEQIQE---I 177
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVvhgkvWWEADNYLREELAEN---DPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 178 DAIVVPISGGGLISGVALAAKSIKPS-IRIIAAEPKGADDAAQSKVAGKIITLPVTNTIADGLRAS-LGDLTWPVVRDLV 255
Cdd:cd06448 158 DAIVCSVGGGGLLNGIVQGLERNGWGdIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKtVSSQALEYAQEHN 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 145340114 256 DDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVLS 294
Cdd:cd06448 238 IKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYS 276
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
56-323 |
1.15e-31 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 120.87 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 56 GAFKFRGACNAVLSLDAEQ-AAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVPKGAPKCKvDNVIR-YGGKVI-WSEATM 132
Cdd:PRK06110 49 GAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEK-NAAMRaLGAELIeHGEDFQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 133 SSREEiASKVLQETGSVLIHPYNDgRIISGQGTIALELLEQIQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPK 212
Cdd:PRK06110 128 AAREE-AARLAAERGLHMVPSFHP-DLVRGVATYALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 213 GADDAAQSKVAGKIITLPVTNTIADGLRASLGDLT-WPVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAA 291
Cdd:PRK06110 206 HAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEaLEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAA 285
|
250 260 270
....*....|....*....|....*....|..
gi 145340114 292 VLSNSFRNNPscrdcKNIGIVLSGGNVDLGSL 323
Cdd:PRK06110 286 ALQERERLAG-----KRVGLVLSGGNIDRAVF 312
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
10-293 |
1.44e-29 |
|
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: 115.00 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 10 ADILSIKEAhdrikpyihRTPVLTSESLNSISG-RSLFFKCECLQKGGAFKFRGACNAVlSLDAEQAAKGVVTHSSGNHA 88
Cdd:cd01563 13 DDIVSLGEG---------NTPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAV-SKAKELGVKAVACASTGNTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 89 AALSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRiISGQGTIAL 168
Cdd:cd01563 83 ASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSNSLNPYR-LEGQKTIAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 169 ELLEQI--QEIDAIVVPISGGGLISGVALAAK------SIKPSIRIIAAEPKGADDAAQSKVAGKIITLPVTN--TIADG 238
Cdd:cd01563 162 EIAEQLgwEVPDYVVVPVGNGGNITAIWKGFKelkelgLIDRLPRMVGVQAEGAAPIVRAFKEGKDDIEPVENpeTIATA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 145340114 239 LR----ASlGDLTWPVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVL 293
Cdd:cd01563 242 IRignpAS-GPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLK 299
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
29-293 |
1.08e-28 |
|
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: 114.14 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 29 TPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGAcnAVL-SLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVP 107
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAM--QVAvSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 108 KG-APKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIIsGQGTIALELLEQIQEI-DAIVVPIS 185
Cdd:COG0498 145 EGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINPARLE-GQKTYAFEIAEQLGRVpDWVVVPTG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 186 GGGLISGVALAAK--------SIKPsiRIIAAEPKGADDAAQSKVAGK-IITLPVTNTIADG---------------LRA 241
Cdd:COG0498 224 NGGNILAGYKAFKelkelgliDRLP--RLIAVQATGCNPILTAFETGRdEYEPERPETIAPSmdignpsngeralfaLRE 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 145340114 242 SLGDltwpvvrdlvddVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVL 293
Cdd:COG0498 302 SGGT------------AVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLR 341
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
28-213 |
6.87e-20 |
|
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: 87.95 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 28 RTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLslDAEqaAKGVVTH-------SSGNHAAALSLAAKIQGI 100
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIE--DAE--KRGLLKPgttiiepTSGNTGIGLAMVAAAKGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 101 PAYIVVPKGAPKCKVDnVIR-YGGKVIWSEAT----MSSREEIASKVLQET-GSVLIHPY-NDGRIISGQGTIALELLEQ 173
Cdd:cd01561 78 RFIIVMPETMSEEKRK-LLRaLGAEVILTPEAeadgMKGAIAKARELAAETpNAFWLNQFeNPANPEAHYETTAPEIWEQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 145340114 174 IQ-EIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKG 213
Cdd:cd01561 157 LDgKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVG 197
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
29-292 |
1.41e-17 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 82.74 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 29 TPVLTSESLNSISG-RSLFFKCECLQKGGAFKFRGACNAVlSLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVP 107
Cdd:PRK08197 80 TPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGV-SRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 108 KGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETG----SVLIHPYNdgriISGQGTIALELLEQI--QEIDAIV 181
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGwfdvSTLKEPYR----IEGKKTMGLELAEQLgwRLPDVIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 182 VPISGG-GLIsGVALAAKSIK-------PSIRIIAAEPKGADDAAQSKVAGKIITLPVTN--TIADGLR--ASLGD-LTW 248
Cdd:PRK08197 235 YPTGGGvGLI-GIWKAFDELEalgwiggKRPRLVAVQAEGCAPIVKAWEEGKEESEFWEDahTVAFGIRvpKALGDfLVL 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 145340114 249 PVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAV 292
Cdd:PRK08197 314 DAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAA 357
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
26-214 |
7.44e-17 |
|
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: 79.32 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 26 IHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRgacnAVLSL--DAEqaAKGVVTH-------SSGNHAAALSLAAK 96
Cdd:COG0031 11 IGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDR----IALSMieDAE--KRGLLKPggtiveaTSGNTGIGLAMVAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 97 IQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEAT--MSSREEIASKVLQET-GSVLIHPY-NDGRIISGQGTIALELLE 172
Cdd:COG0031 85 AKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAAETpGAFWPNQFeNPANPEAHYETTGPEIWE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 145340114 173 QIQ-EIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGA 214
Cdd:COG0031 165 QTDgKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGS 207
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
29-191 |
6.42e-15 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 75.23 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 29 TPVLTSESLNSIsGRSLFFKCECLQKGGAFKFRGACNAVlSLDAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVVPK 108
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAV-SYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 109 GAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQIQEIDAIVVPISGGG 188
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINPTHVIVPTGSGSY 224
|
...
gi 145340114 189 LIS 191
Cdd:PRK05638 225 LYS 227
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
27-239 |
4.86e-13 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 69.08 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 27 HRTPVLTSESLNSISgrsLFFKCECLQKGGAFKFRGACNAVLSLdAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVV 106
Cdd:PRK08329 59 HLTPPITPTVKRSIK---VYFKLDYLQPTGSFKDRGTYVTVAKL-KEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 107 PKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQGTIALELLEQIQEIDAIVVPISG 186
Cdd:PRK08329 135 SYNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGS 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 145340114 187 GGLISGVALAAK------SIKPSIRIIAAEPKGADDAAQSKVAgkiitlpvTNTIADGL 239
Cdd:PRK08329 215 GTLFLGIWKGFKelhemgEISKMPKLVAVQAEGYESLCKRSKS--------ENKLADGI 265
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
10-294 |
7.92e-13 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 68.75 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 10 ADILSIKEAHDRIK-----PYIHRTPVLTSESLNSISG-RSLFFKCECLQKG-GAFKFRGACNAVLSLDAEQAAKG---- 78
Cdd:PRK08206 21 LPLLSQEEAKKARAfhqsfPGYAPTPLVALPDLAAELGvGSILVKDESYRFGlNAFKALGGAYAVARLLAEKLGLDisel 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 79 ------------------VVTHSSGNHAAALSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIAS 140
Cdd:PRK08206 101 sfeeltsgevreklgditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 141 KVLQETGSVLIHP-----YND--GRIISGQGTIALELLEQIQEIDAIV--VPISG--GGLISGVA--LAAKSIKPSIRII 207
Cdd:PRK08206 181 QEAQENGWVVVQDtawegYEEipTWIMQGYGTMADEAVEQLKEMGVPPthVFLQAgvGSLAGAVLgyFAEVYGEQRPHFV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 208 AAEPKGADDAAQSKVAGKIITlpVT---NTIADGLraSLGD---LTWPVVRDLVDDVVTLEECEIIEAMKMCYEILK--- 278
Cdd:PRK08206 261 VVEPDQADCLYQSAVDGKPVA--VTgdmDTIMAGL--ACGEpnpLAWEILRNCADAFISCPDEVAALGMRILANPLGgdp 336
|
330
....*....|....*...
gi 145340114 279 --VSVEpSGAIGLAAVLS 294
Cdd:PRK08206 337 piVSGE-SGAVGLGALAA 353
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
28-293 |
1.04e-12 |
|
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: 67.79 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 28 RTPVLTSESLNS-ISGRSLFFKCECLQKGGAFKFRGACNAVLSLdAEQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIVV 106
Cdd:TIGR00260 22 VTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKA-LELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 107 PKGA-PKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQET-----GSVLIHPYNdgriISGQGTIALELLEQI--QEID 178
Cdd:TIGR00260 101 PAGKiSLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKpalglNSANSIPYR----LEGQKTYAFEAVEQLgwEAPD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 179 AIVVPISGGGLISGVALAAKSIK-------PSIRIIAAEpkGADDAAQSKVAGKIITLPVT-NTIA---DGLRASLGDLT 247
Cdd:TIGR00260 177 KVVVPVPNSGNFGAIWKGFKEKKmlgldslPVKRGIQAE--GAADIVRAFLEGGQWEPIETpETLStamDIGNPANWPRA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 145340114 248 WPVVRDLVDDVVTLEECEIIEAMKMCYEILKVSVEPSGAIGLAAVL 293
Cdd:TIGR00260 255 LEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALL 300
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
16-291 |
3.39e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 63.22 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 16 KEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGAcNAVLSLDAEQAAKGVVTHSSGNHAAALSLAA 95
Cdd:PRK06450 38 KNLERKNFPYIKHFISLGEGRTPLIKKGNIWFKLDFLNPTGSYKDRGS-VTLISYLAEKGIKQISEDSSGNAGASIAAYG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 96 KIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEAtmsSREEIaSKVLQETG----SVLIHP-YNDG-RiisgqgTIALE 169
Cdd:PRK06450 117 AAAGIEVKIFVPETASGGKLKQIESYGAEVVRVRG---SREDV-AKAAENSGyyyaSHVLQPqFRDGiR------TLAYE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 170 LLEQI--QEIDAIVVPISGGGLISGV------ALAAKSIKPSIRIIAAEPKgaddaAQSKVAGKIITLPVT-----NTIA 236
Cdd:PRK06450 187 IAKDLdwKIPNYVFIPVSAGTLLLGVysgfkhLLDSGVISEMPKIVAVQTE-----QVSPLCAKFKGISYTppdkvTSIA 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 237 DGL---RASLGDLTWpVVRDLVDDVVTLEECEIIEAMKmcyEILK--VSVEPSGAIGLAA 291
Cdd:PRK06450 262 DALvstRPFLLDYMV-KALSEYGECIVVSDNEIVEAWK---ELAKkgLLVEYSSATVYAA 317
|
|
| diampropi_NH3ly |
TIGR01747 |
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ... |
80-295 |
3.92e-09 |
|
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]
Pssm-ID: 130808 Cd Length: 376 Bit Score: 57.21 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 80 VTHSSGNHAAALSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYN-DGR 158
Cdd:TIGR01747 98 ATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQMAQQHGWVVVQDTAwEGY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 159 ------IISGQGTIALELLEQIQEIDAI----VVPISGGGLISGVALA--AKSIKPSI-RIIAAEPKGADDAAQSKVAGK 225
Cdd:TIGR01747 178 ekiptwIMQGYATLADEAVEQLREMGSVtpthVLLQAGVGSMAGGVLGyfVDVYSENNpHSIVVEPDKADCLYQSAVKKD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 226 IITLPVTN---TIADGLraSLGD---LTWPVVRDLVDDVVTLEECEIIEAMKMCYEILK-----VSVEpSGAIG---LAA 291
Cdd:TIGR01747 258 GDIVNVGGdmaTIMAGL--ACGEpnpISWEILRNCTSQFISAQDSVAAKGMRVLGAPYGgdpriISGE-SGAVGlglLAA 334
|
....
gi 145340114 292 VLSN 295
Cdd:TIGR01747 335 VMYH 338
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
28-193 |
6.88e-09 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 56.25 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 28 RTPVLTSESLNSISG-RSLFFKCECLQKGGAFKFRGACNAVLslDA-EQAAKGVVTHSSGNHAAALSLAAKIQGIPAYIV 105
Cdd:PRK06381 15 GTPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVR--RAmRLGYSGITVGTCGNYGASIAYFARLYGLKAVIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 106 VPKGAPKCKVDNVIRYGGKVI-----WSEATMSSREEIASKVLQET--GSVliHPYNDgriISGQGTIALELLEQIQEI- 177
Cdd:PRK06381 93 IPRSYSNSRVKEMEKYGAEIIyvdgkYEEAVERSRKFAKENGIYDAnpGSV--NSVVD---IEAYSAIAYEIYEALGDVp 167
|
170
....*....|....*.
gi 145340114 178 DAIVVPISGGGLISGV 193
Cdd:PRK06381 168 DAVAVPVGNGTTLAGI 183
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
26-214 |
7.76e-08 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 52.94 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 26 IHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLslDAEqaAKG-------VVTHSSGNHAAALSLAAKIQ 98
Cdd:PRK10717 11 IGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIW--DAE--KRGllkpggtIVEGTAGNTGIGLALVAAAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 99 GIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEATMSSREEIASKVLQETGSVLIHPYNDGRIISGQ-----------GTIA 167
Cdd:PRK10717 87 GYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNNYVKGAGRLAEELVASEPNGAIWANQfdnpanreahyETTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 145340114 168 LELLEQIQ-EIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEPKGA 214
Cdd:PRK10717 167 PEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGS 214
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
2-213 |
1.12e-04 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 43.29 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 2 EANREKYAADILsiKEAHDRIKPYIHR-TPVLTSESLNS-ISGRSLFFKCECLQKGGAFKFRGACNAVLsLDAEQAAKGV 79
Cdd:cd06446 9 EFSKERYDPDFP--EELRELYKDYVGRpTPLYRAKRLSEyLGGAKIYLKREDLNHTGAHKINNALGQAL-LAKRMGKKRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 80 VTHS-SGNHAAALSLAAKIQGIPAyiVVPKGApkckVD------NVIR---YGGKVIWSEA-------TMSSREEIASKV 142
Cdd:cd06446 86 IAETgAGQHGVATATACALFGLEC--EIYMGA----VDverqplNVFRmelLGAEVVPVPSgsgtlkdAISEAIRDWVTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 143 LQET----GSVL-IHPYNDgRIISGQGTIALELLEQIQEI-----DAIVVPISGGGLISGVALAAKSIKpSIRIIAAEPK 212
Cdd:cd06446 160 VEDThyllGSVVgPHPYPN-MVRDFQSVIGEEAKKQILEKegelpDVVIACVGGGSNAAGLFYPFINDK-DVKLIGVEAG 237
|
.
gi 145340114 213 G 213
Cdd:cd06446 238 G 238
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
78-192 |
2.51e-04 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 42.49 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 78 GVVTHSSGNHAAALSLAAKIQGIPAYIVVPkgAPKCKVDNVIR--YGGKVIWSEAT-MSSREEIASKVLQETGSVLIHPY 154
Cdd:PLN02569 189 GVGCASTGDTSAALSAYCAAAGIPSIVFLP--ADKISIAQLVQpiANGALVLSIDTdFDGCMRLIREVTAELPIYLANSL 266
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 145340114 155 NDGRiISGQGTIALELLEQI--QEIDAIVVPISGGGLISG 192
Cdd:PLN02569 267 NSLR-LEGQKTAAIEILQQFdwEVPDWVIVPGGNLGNIYA 305
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
4-107 |
1.37e-03 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 40.36 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 4 NREKYAADILSIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVL-SLDAEQ-AAKGVVT 81
Cdd:PLN02356 29 SRKRKTKKPLSKKKPRNGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEeALESGQlFPGGVVT 108
|
90 100
....*....|....*....|....*..
gi 145340114 82 H-SSGNHAAALSLAAKIQGIPAYIVVP 107
Cdd:PLN02356 109 EgSAGSTAISLATVAPAYGCKCHVVIP 135
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
3-211 |
6.77e-03 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 38.02 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 3 ANREKYAADILSIKEAHDRIKPYIHRTPVLTSESLNSISGRSLFFKCECLQKGGAFKFRGACNAVLslDAEQaaKGVVTH 82
Cdd:PLN02556 34 AQRLRDLPKDLPGTKIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIE--DAEK--KNLITP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145340114 83 --------SSGNHAAALSLAAKIQGIPAYIVVPKGAPKCKVDNVIRYGGKVIWSEAT--MSSREEIASKVLQETGSVLI- 151
Cdd:PLN02556 110 gkttliepTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTkgMGGTVKKAYELLESTPDAFMl 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145340114 152 ----HPYNDGRIISGQGTIALEllEQIQEIDAIVVPISGGGLISGVALAAKSIKPSIRIIAAEP 211
Cdd:PLN02556 190 qqfsNPANTQVHFETTGPEIWE--DTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP 251
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
167-208 |
8.12e-03 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 37.50 E-value: 8.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 145340114 167 ALELLEQIQE----IDAIVVPISGGGLISGVALAAKSIKPSIRIIA 208
Cdd:PRK03910 170 ALEIAQQLAEggvdFDAVVVASGSGGTHAGLAAGLAALGPDIPVIG 215
|
|
| |
