|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
5-323 |
0e+00 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 538.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 5 SPPSLPTYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSS 84
Cdd:PRK07048 1 SDLLLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 85 GNHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQG 164
Cdd:PRK07048 81 GNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 165 TAAKELFEEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSI 244
Cdd:PRK07048 161 TAAKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648281068 245 GDITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALSGARVGILISGGNVDLARYARFL 323
Cdd:PRK07048 241 GNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALL 319
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
6-323 |
2.73e-147 |
|
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: 417.52 E-value: 2.73e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 6 PPSLPTYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSG 85
Cdd:COG1171 2 TALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 86 NHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGT 165
Cdd:COG1171 82 NHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 166 AAKELFEEVPDLDYLFVClggggllsgsLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIG 245
Cdd:COG1171 162 IALEILEQLPDLDAVFVPvggggliagvAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648281068 246 DITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALSGARVGILISGGNVDLARYARFL 323
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEIL 319
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
12-315 |
5.00e-144 |
|
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: 408.41 E-value: 5.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 12 YDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAV 91
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 92 ALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELF 171
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 172 EEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIGDITFAI 251
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648281068 252 IREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALSGARVGILISGGNVD 315
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| PLN02970 |
PLN02970 |
serine racemase |
2-319 |
2.94e-125 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 361.69 E-value: 2.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 2 TTNSPPSLPTYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALA 81
Cdd:PLN02970 1 EAASEKYAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 82 FSSGNHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIA 161
Cdd:PLN02970 81 HSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 162 GQGTAAKELFEEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQT 241
Cdd:PLN02970 161 GQGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 242 qSIGDITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGAL-----HGGVALSGARVGILISGGNVDL 316
Cdd:PLN02970 241 -SLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALsdsfrSNPAWKGCKNVGIVLSGGNVDL 319
|
...
gi 648281068 317 ARY 319
Cdd:PLN02970 320 GVL 322
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
29-316 |
1.39e-89 |
|
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: 272.77 E-value: 1.39e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAVALAAQMLDMPALIVMPE 108
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 109 DAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELFEEVPDLDYLFVCLGGGG 188
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 189 LLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIGDITFAIIREHVEDILAVADEHLV 268
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 648281068 269 QAMRFYAERKKIVVEPTGALSLAGALHGGVALSGARVGILISGGNVDL 316
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDL 288
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
1-318 |
1.88e-84 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 258.13 E-value: 1.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 1 MTTNSPPSLptyDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGAL 80
Cdd:PRK08638 3 ITYDLPVAI---DDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 81 AFSSGNHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTY-DRFTEDREAISrRLADERGMTLIPPFNHRDV 159
Cdd:PRK08638 80 ACSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHgDNFNDTIAKVE-EIVEEEGRTFIPPYDDPKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 160 IAGQGTAAKELFEEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGA 239
Cdd:PRK08638 159 IAGQGTIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 240 QTQSIGDITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVA--LSGARVGILISGGNVDLA 317
Cdd:PRK08638 239 DVSRPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDqyIQNKKVVAIISGGNVDLS 318
|
.
gi 648281068 318 R 318
Cdd:PRK08638 319 R 319
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
11-315 |
1.25e-83 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 258.28 E-value: 1.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 11 TYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQA 90
Cdd:PRK07334 6 TLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 91 VALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTY-DRFTEDReAISRRLADERGMTLIPPFNHRDVIAGQGTAAKE 169
Cdd:PRK07334 86 VAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHgETLDEAR-AHARELAEEEGLTFVHPYDDPAVIAGQGTVALE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 170 LFEEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAgriVQIPTPH-TIADGAQTQSIGDIT 248
Cdd:PRK07334 165 MLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKG---VALPCGGsTIAEGIAVKQPGQLT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648281068 249 FAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALSGARVGILISGGNVD 315
Cdd:PRK07334 242 LEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNID 308
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
12-319 |
1.13e-76 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 237.67 E-value: 1.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 12 YDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAV 91
Cdd:PRK06815 4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 92 ALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELF 171
Cdd:PRK06815 84 ALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 172 EEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADG-AQTQSIGDITFA 250
Cdd:PRK06815 164 EQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGtAGGVEPGAITFP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648281068 251 IIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALSGARVGILISGGNVDLARY 319
Cdd:PRK06815 244 LCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKY 312
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
28-311 |
3.19e-73 |
|
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: 227.96 E-value: 3.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 28 RTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAVALAAQMLDMPALIVMP 107
Cdd:pfam00291 7 PTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 108 EDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLA-DERGMTLIPPFNHRDVIAGQGTAAKELFEEV-PDLDYLFVCLG 185
Cdd:pfam00291 87 EDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEGYGTIGLEILEQLgGDPDAVVVPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 186 GGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQ-SIGDITFAIIREHVEDILAVAD 264
Cdd:pfam00291 167 GGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVGEVVTVSD 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 648281068 265 EHLVQAMRFYAERKKIVVEPTGALSLAGA---LHGGVAlSGARVGILISG 311
Cdd:pfam00291 247 EEALEAMRLLARREGIVVEPSSAAALAALklaLAGELK-GGDRVVVVLTG 295
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
21-318 |
5.59e-73 |
|
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: 233.47 E-value: 5.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 21 RLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAVALAAQMLDM 100
Cdd:TIGR01124 10 RVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 101 PALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELFEEVP-DLDY 179
Cdd:TIGR01124 90 KALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVAnPLDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 180 LFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIGDITFAIIREHVEDI 259
Cdd:TIGR01124 170 VFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDI 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648281068 260 LAVADEHLVQAMRFYAERKKIVVEPTGALSLAG-----ALHGgvaLSGARVGILISGGNVDLAR 318
Cdd:TIGR01124 250 VTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGlkkyvALHG---IRGQTLVAILSGANMNFHR 310
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
8-325 |
1.18e-71 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 225.42 E-value: 1.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 8 SLPTYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTpEQRKR--GALAFSSG 85
Cdd:PRK06608 3 LLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELK-EQGKLpdKIVAYSTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 86 NHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAIsrRLADERGMTLIPPFNHRDVIAGQGT 165
Cdd:PRK06608 82 NHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKA--KEDEEQGFYYIHPSDSDSTIAGAGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 166 AAKELFEEV-PDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIP-TPHTIADGAQTQS 243
Cdd:PRK06608 160 LCYEALQQLgFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNySPNTIADGLKTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 244 IGDITFAIIREHveDILAVADE-----------HLVqamrfyaerkKIVVEPTGALSLAGALHGGVALSGA-RVGILISG 311
Cdd:PRK06608 240 VSARTFEYLKKL--DDFYLVEEyeiyywtawltHLL----------KVICEPSSAINMVAVVNWLKTQSKPqKLLVILSG 307
|
330
....*....|....
gi 648281068 312 GNVDLARYARFLHD 325
Cdd:PRK06608 308 GNIDPILYNELWKE 321
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
5-320 |
7.74e-69 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 220.45 E-value: 7.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 5 SPPSLPTYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSS 84
Cdd:PRK08639 2 TVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 85 GNHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVV-------TYDrfteDREAISRRLADERGMTLIPPFNHR 157
Cdd:PRK08639 82 GNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFVeivlvgdTFD----DSAAAAQEYAEETGATFIPPFDDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 158 DVIAGQGTAAKELFE---EVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHT 234
Cdd:PRK08639 158 DVIAGQGTVAVEILEqleKEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 235 IADGAQTQSIGDITFAIIREHVEDILAVaDEHLV-QAM-RFYAErKKIVVEPTGALSLAGALHGGVALSGARVGILISGG 312
Cdd:PRK08639 238 FVDGAAVARVGDLTFEILKDVVDDVVLV-PEGAVcTTIlELYNK-EGIVAEPAGALSIAALELYKDEIKGKTVVCVISGG 315
|
....*...
gi 648281068 313 NVDLARYA 320
Cdd:PRK08639 316 NNDIERMP 323
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
11-321 |
1.44e-67 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 214.44 E-value: 1.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 11 TYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQA 90
Cdd:PRK07476 2 SLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 91 VALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKEL 170
Cdd:PRK07476 82 LAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 171 FEEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADgaqtqSIGD---- 246
Cdd:PRK07476 162 LEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLAD-----SLGGgigl 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648281068 247 ---ITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALSGARVGILISGGNVDLARYAR 321
Cdd:PRK07476 237 dnrYTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELHRR 314
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
25-318 |
5.25e-65 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 213.08 E-value: 5.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 25 VAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAVALAAQMLDMPALI 104
Cdd:PRK09224 17 VAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 105 VMPEDAPASKMAATRSYGAQVV----TYDrfteDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELFEEVPD-LDY 179
Cdd:PRK09224 97 VMPVTTPDIKVDAVRAFGGEVVlhgdSFD----EAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 180 LFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIGDITFAIIREHVEDI 259
Cdd:PRK09224 173 VFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDV 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648281068 260 LAVADEHLVQAMRFYAERKKIVVEPTGALSLAG-----ALHGgvaLSGARVGILISGGNVDLAR 318
Cdd:PRK09224 253 ITVDTDEICAAIKDVFEDTRSIAEPAGALALAGlkkyvAQHG---IEGETLVAILSGANMNFDR 313
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
11-323 |
3.63e-59 |
|
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: 192.37 E-value: 3.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 11 TYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQA 90
Cdd:TIGR02991 2 TLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 91 VALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKEL 170
Cdd:TIGR02991 82 LAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 171 FEEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIAD--GAQTQSIGDIT 248
Cdd:TIGR02991 162 VEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648281068 249 FAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALSGaRVGILISGGNVDLARYARFL 323
Cdd:TIGR02991 242 FAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPG-PCAVIVSGRNIDMDLHKRII 315
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
19-318 |
3.89e-59 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 198.10 E-value: 3.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 19 AGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAVALAAQML 98
Cdd:PRK12483 28 AARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 99 DMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELFEEVPD-L 177
Cdd:PRK12483 108 GVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGpL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 178 DYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIGDITFAIIREHVE 257
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVD 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648281068 258 DILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGAlHGGVALSGARVGILI---SGGNVDLAR 318
Cdd:PRK12483 268 EVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGI-KKYAEREGIEGQTLVaidSGANVNFDR 330
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
29-312 |
2.75e-57 |
|
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: 185.41 E-value: 2.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGA--LAFSSGNHAQAVALAAQMLDMPALIVM 106
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGviIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 107 PEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADER-GMTLIPPFNHRDVIAGQGTAAKELFEEVPD--LDYLFVC 183
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQLGGqkPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 184 LGGGGLLSGSLLAAGQLSPRCKVYGVEPqagddarqslragrivqiptphtiadgaqtqsigditfaiirehveDILAVA 263
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 648281068 264 DEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALS-GARVGILISGG 312
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGkGKTVVVILTGG 244
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
9-323 |
3.35e-57 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 187.51 E-value: 3.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 9 LPTYDDVAAAAGRLEGVAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQ-RKRGALAFSSGNH 87
Cdd:PRK06110 2 MFTLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 88 AQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTY-DRFTEDREAiSRRLADERGMTLIPPFnHRDVIAGQGTA 166
Cdd:PRK06110 82 GQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHgEDFQAAREE-AARLAAERGLHMVPSF-HPDLVRGVATY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 167 AKELFEEVPDLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIGD 246
Cdd:PRK06110 160 ALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDP 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648281068 247 ITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHGGVALSGARVGILISGGNVDLARYARFL 323
Cdd:PRK06110 240 EALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVFARVL 316
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
7-320 |
2.71e-55 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 182.08 E-value: 2.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 7 PSLPTYDDVAAAAGRLEGVAHRTPILRSRTADeLLGAQLFFKCENLQRTGAFKIRGAYNALsqFTPEQRKRGALAFSSGN 86
Cdd:PRK08246 2 HAMITRSDVRAAAQRIAPHIRRTPVLEADGAG-FGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 87 HAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVV-TYDRFTEDREAiSRRLADERGMTLIPPFNHRDVIAGQGT 165
Cdd:PRK08246 79 AGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVvVGAEYADALEA-AQAFAAETGALLCHAYDQPEVLAGAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 166 AAKELFEEVPDLDYLFVCLGGGGLLSGSLLAagqLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIG 245
Cdd:PRK08246 158 LGLEIEEQAPGVDTVLVAVGGGGLIAGIAAW---FEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648281068 246 DITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAgALHGG--VALSGARVGILISGGNVDLARYA 320
Cdd:PRK08246 235 EIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALA-ALLSGayVPAPGERVAVVLCGANTDPATLA 310
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
25-318 |
1.44e-49 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 173.95 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 25 VAHRTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAVALAAQMLDMPALI 104
Cdd:PLN02550 106 VAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 105 VMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELFEEVPD-LDYLFVC 183
Cdd:PLN02550 186 AMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGpLHAIFVP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 184 LGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRAGRIVQIPTPHTIADGAQTQSIGDITFAIIREHVEDILAVA 263
Cdd:PLN02550 266 VGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 264 DEHLVQAMRFYAERKKIVVEPTGALSLAGA-----LHGgvaLSGARVGILISGGNVDLAR 318
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALAGAeayckYYG---LKDENVVAITSGANMNFDR 402
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
14-325 |
6.71e-40 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 143.23 E-value: 6.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 14 DVAAAAGRLEGVAHRTPILRSrtadELLGAQLffKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSSGNHAQAVAL 93
Cdd:PRK08813 25 DVLAAQARLRRYLSPTPLHYA----ERFGVWL--KLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 94 AAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELFEE 173
Cdd:PRK08813 99 SAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 174 VPDLdylfVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGDDARQSLRaGRIVQIPTPHTIADGAQTQSIGDITFAIIR 253
Cdd:PRK08813 179 APDV----VIVPIGGGGLASGVALALKSQGVRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCS 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648281068 254 EHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAgalhGGVALSGARVGILISGGNVDLARYARFLHD 325
Cdd:PRK08813 254 SLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALA----AGRRVSGKRKCAVVSGGNIDATVLATLLSE 321
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
29-296 |
7.70e-24 |
|
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: 99.30 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAFSS--GNHAQAVALAAQMLDMPALIVM 106
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECVHVVCSsgGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 107 PEDAPASKMAATRSYGAQVVTY--DRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELFEEVPDldylfvcl 184
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHgkVWWEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQS-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 185 ggggllsgsllaagQLSPR---CKV----------YGVEPQAGDDAR-------------QSLRAGRIVQIPTPHTIADG 238
Cdd:cd06448 154 --------------QEKVDaivCSVggggllngivQGLERNGWGDIPvvavetegahslnASLKAGKLVTLPKITSVATS 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 648281068 239 AQTQSIGDITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHG 296
Cdd:cd06448 220 LGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYSG 277
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
29-313 |
8.99e-24 |
|
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: 99.20 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRS-RTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAfSSGNHAQAVALAAQMLDMPALIVMP 107
Cdd:cd01563 23 TPLVRApRLGERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACA-STGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 108 EDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFN-HRdvIAGQGTAAKELFE----EVPdlDYLFV 182
Cdd:cd01563 102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSNSLNpYR--LEGQKTIAFEIAEqlgwEVP--DYVVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 183 CLGGGGLLSGSLLAAGQL------SPRCKVYGVEPQAGDDARQSLRAGR--IVQIPTPHTIADGAQtqsIGD-----ITF 249
Cdd:cd01563 178 PVGNGGNITAIWKGFKELkelgliDRLPRMVGVQAEGAAPIVRAFKEGKddIEPVENPETIATAIR---IGNpasgpKAL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648281068 250 AIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGALHG---GVALSGARVgILISGGN 313
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLreeGIIDKGERV-VVVLTGH 320
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
9-294 |
1.81e-20 |
|
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: 91.03 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 9 LPtYDDVAAAAGRLEGVahrTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFtpeqRKRGALAF---SSG 85
Cdd:COG0498 51 LP-FDDEEKAVSLGEGG---TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLA----LERGAKTIvcaSSG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 86 NHAQAVALAAQMLDMPALIVMPED-APASKMAATRSYGAQVV----TYDrfteDREAISRRLADERGMTLIPPFN-HRdv 159
Cdd:COG0498 123 NGSAALAAYAARAGIEVFVFVPEGkVSPGQLAQMLTYGAHVIavdgNFD----DAQRLVKELAADEGLYAVNSINpAR-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 160 IAGQGTAAKELFE---EVPD--------------LDYLFVCLGGGGLLSGSllaagqlsPRckVYGVEPQAGDDARQSLR 222
Cdd:COG0498 197 LEGQKTYAFEIAEqlgRVPDwvvvptgnggnilaGYKAFKELKELGLIDRL--------PR--LIAVQATGCNPILTAFE 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648281068 223 AGR-IVQIPTPHTIADGAQTQ--SIGDITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGAL 294
Cdd:COG0498 267 TGRdEYEPERPETIAPSMDIGnpSNGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLR 341
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
28-294 |
1.66e-14 |
|
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: 72.55 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 28 RTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSqftpEQRKRGALAF-------SSGNHAQAVALAAQMLDM 100
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIE----DAEKRGLLKPgttiiepTSGNTGIGLAMVAAAKGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 101 PALIVMPEDAPASKMAATRSYGAQVVTYD----RFTEDREAISRRLADERGMTLIP-----PFN---HRDviagqgTAAK 168
Cdd:cd01561 78 RFIIVMPETMSEEKRKLLRALGAEVILTPeaeaDGMKGAIAKARELAAETPNAFWLnqfenPANpeaHYE------TTAP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 169 ELFEEVPD-LDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPqagddarqslrAGRIV---QIPTPHTIadgaqtQSI 244
Cdd:cd01561 152 EIWEQLDGkVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDP-----------VGSVLfsgGPPGPHKI------EGI 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 648281068 245 G-DITFAII-REHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGAL 294
Cdd:cd01561 215 GaGFIPENLdRSLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAAL 266
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
28-311 |
5.59e-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: 65.48 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 28 RTPILRS-RTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAfSSGNHAQAVALAAQMLDMPALIVM 106
Cdd:TIGR00260 22 VTPLFRApALAANVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCA-STGNTGAAAAAYAGKAGLKVVVLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 107 PEDAPA-SKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDV-IAGQGTAAKELFE----EVPDLDYL 180
Cdd:TIGR00260 101 PAGKISlGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYrLEGQKTYAFEAVEqlgwEAPDKVVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 181 FVCLG---GGGLLSGSLLAAGQLSPRCKVYGVEPQ-AGDDARQSLRAGRIVQIPTPHTIADGAQTQSIGDITFA--IIRE 254
Cdd:TIGR00260 181 PVPNSgnfGAIWKGFKEKKMLGLDSLPVKRGIQAEgAADIVRAFLEGGQWEPIETPETLSTAMDIGNPANWPRAleAFRR 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 255 HVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGAL---HGGVALSGARVGILISG 311
Cdd:TIGR00260 261 SNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLklvEKGTADPAERVVCALTG 320
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
29-174 |
5.96e-12 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 65.99 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELlGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAfSSGNHAQAVALAAQMLDMPALIVMPE 108
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVA-SDGNAAASVAAYSARAGKEAFVVVPR 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648281068 109 DAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIAGQGTAAKELFEEV 174
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEI 210
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
29-176 |
1.00e-11 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 65.02 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELLGA-QLFFKCENLQRTGAFKIRGAYNALSQftpeQRKRGALAF---SSGNHAQAVALAAQMLDMPALI 104
Cdd:PRK08197 80 TPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGLAVGVSR----AKELGVKHLampTNGNAGAAWAAYAARAGIRATI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 105 VMPEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGM----TLIPPFNhrdvIAGQGTAAKELFE----EVPD 176
Cdd:PRK08197 156 FMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWfdvsTLKEPYR----IEGKKTMGLELAEqlgwRLPD 231
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
29-316 |
4.68e-10 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 59.84 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRsrtadelLGAQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALAfSSGNHAQAVALAAQMLDMPALIVMPE 108
Cdd:PRK08329 65 TPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVID-SSGNAALSLALYSLSEGIKVHVFVSY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 109 DAPASKMAATRSYGAQV--VTYDRFTEDREAIsrRLADERGMTLIPPFNHRDVIAGQGTAAKELFEEVPDLDYLFVCLGG 186
Cdd:PRK08329 137 NASKEKISLLSRLGAELhfVEGDRMEVHEEAV--KFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 187 GGLLSGSLLAAGQL------SPRCKVYGVEPQAGDD-ARQSLRAGRI---VQIPTPHTIADgaqtqsigdiTFAIIREHV 256
Cdd:PRK08329 215 GTLFLGIWKGFKELhemgeiSKMPKLVAVQAEGYESlCKRSKSENKLadgIAIPEPPRKEE----------MLRALEESN 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648281068 257 EDILAVADEHLVQAMRfYAERKKIVVEPTGALSLAG---ALHGGVALSGARVGILISGGNVDL 316
Cdd:PRK08329 285 GFCISVGEEETRAALH-WLRRMGFLVEPTSAVALAAywkLLEEGLIEGGSKVLLPLSGSGLKN 346
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
12-294 |
4.87e-10 |
|
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: 59.68 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 12 YDDVAAAAGRlegvahrTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYN----ALsqftpeqrKRGAL------- 80
Cdd:COG0031 4 YDSILELIGN-------TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSmiedAE--------KRGLLkpggtiv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 81 -AfSSGNHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYDRFTEDREAI--SRRLADERGMTLIP----- 152
Cdd:COG0031 69 eA-TSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIdkAEELAAETPGAFWPnqfen 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 153 PFN---HRDviagqgTAAKELFEEVP-DLDYLFVClggggllsgsllaagQLSPRCKVYGVEPQAGddarqSLRAGrivQ 228
Cdd:COG0031 148 PANpeaHYE------TTGPEIWEQTDgKVDAFVAGvgtggtitgvgrylkERNPDIKIVAVEPEGS-----PLLSG---G 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648281068 229 IPTPHTIadgaqtQSIGD--ITFAIIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGAL 294
Cdd:COG0031 214 EPGPHKI------EGIGAgfVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAAL 275
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
71-294 |
1.62e-08 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 55.27 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 71 TPEQRKR-GALAFSS---GNHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVV----TYDrfteD--REAIsr 140
Cdd:PRK08206 107 SGEVREKlGDITFATatdGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIitdgNYD----DsvRLAA-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 141 RLADERGMTL-----------IPpfnhRDVIAGQGTAAKELFEEVPDLD----YLFVclggggllsgsllaagQ------ 199
Cdd:PRK08206 181 QEAQENGWVVvqdtawegyeeIP----TWIMQGYGTMADEAVEQLKEMGvpptHVFL----------------Qagvgsl 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 200 ----LSPRCKVYG--------VEPQAGDDARQSLRAGRIVQIptphtiadGAQTQSI------GD---ITFAIIREHVED 258
Cdd:PRK08206 241 agavLGYFAEVYGeqrphfvvVEPDQADCLYQSAVDGKPVAV--------TGDMDTImaglacGEpnpLAWEILRNCADA 312
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 648281068 259 ILAVADEHLVQAMRFYAE----RKKIVVEPTGALSLAGAL 294
Cdd:PRK08206 313 FISCPDEVAALGMRILANplggDPPIVSGESGAVGLGALA 352
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
28-182 |
1.03e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 52.79 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 28 RTPILRSRTADELLG-AQLFFKCENLQRTGAFKIRGAYNALSQfTPEQRKRGALAFSSGNHAQAVALAAQMLDMPALIVM 106
Cdd:PRK06381 15 GTPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRR-AMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFI 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648281068 107 PEDAPASKMAATRSYGAQVVTYDRFTEDREAISRRLADERGMTLIPPFNHRDVIA--GQGTAAKELFEEVPDL-DYLFV 182
Cdd:PRK06381 94 PRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDieAYSAIAYEIYEALGDVpDAVAV 172
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
28-182 |
3.62e-06 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 47.81 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 28 RTPILRsrtadellGAQLFFKCENLQRTGAFKIRGAYNALSQFTpEQRKRGALAFSSGNHAQAVALAAQMLDMPALIVMP 107
Cdd:PRK06450 58 RTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLA-EKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 108 EDAPASKMAATRSYGAQVVtydRFTEDREAISRRlADERGM-----TLIPPFnhRDVIAgqgTAAKELFEE----VPdlD 178
Cdd:PRK06450 129 ETASGGKLKQIESYGAEVV---RVRGSREDVAKA-AENSGYyyashVLQPQF--RDGIR---TLAYEIAKDldwkIP--N 197
|
....
gi 648281068 179 YLFV 182
Cdd:PRK06450 198 YVFI 201
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
12-149 |
2.21e-05 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 45.62 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 12 YDDVAAAAGRlegvahrTPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSqftpEQRKRGALA-------FSS 84
Cdd:PRK10717 4 FEDVSDTIGN-------TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIW----DAEKRGLLKpggtiveGTA 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648281068 85 GNHAQAVALAAQMLDMPALIVMPEDAPASKMAATRSYGAQVVTYD----RFTEDREAISRRLADERGMT 149
Cdd:PRK10717 73 GNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPaapyANPNNYVKGAGRLAEELVAS 141
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
29-126 |
4.84e-05 |
|
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273463 Cd Length: 299 Bit Score: 44.19 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQftPEQR---KRGALAF--SSGNHAQAVALAAQMLDMPAL 103
Cdd:TIGR01136 8 TPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILD--AEKRgllKPGDTIIeaTSGNTGIALAMVAAARGYKLI 85
|
90 100
....*....|....*....|...
gi 648281068 104 IVMPEDAPASKMAATRSYGAQVV 126
Cdd:TIGR01136 86 LTMPETMSLERRKLLRAYGAELI 108
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
29-126 |
7.11e-05 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 43.71 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELLGAQLFFKCENLQRTGAFKIRGAYNALSQftPEQR---KRGALAF--SSGNHAQAVALAAQMLDMPAL 103
Cdd:PRK11761 13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQ--AEKRgeiKPGDTLIeaTSGNTGIALAMIAAIKGYRMK 90
|
90 100
....*....|....*....|...
gi 648281068 104 IVMPEDAPASKMAATRSYGAQVV 126
Cdd:PRK11761 91 LIMPENMSQERRAAMRAYGAELI 113
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
32-144 |
3.75e-04 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 42.32 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 32 LRSRTAdelLGAQLFFKCENLQRTGAFKIRgayNALSQFTPEQR---KRGALAFSSGNHAQAVALAAQMLDMPALIVMPE 108
Cdd:PRK13802 339 VKEKTG---LDARVFLKREDLNHTGAHKIN---NALGQALLVKRmgkTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQ 412
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 648281068 109 -DA--PASKMAATRSYGAQVVTY---DRFTEDreAISRRLAD 144
Cdd:PRK13802 413 iDArrQALNVARMRMLGAEVVEVtlgDRILKD--AINEALRD 452
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
29-126 |
3.89e-04 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 41.75 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELL-GAQLFFKCENLQRTGAFKIRgayNALSQFTPEQR---KR-----GAlafssGNHAQAVALAAQMLD 99
Cdd:cd06446 35 TPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKIN---NALGQALLAKRmgkKRviaetGA-----GQHGVATATACALFG 106
|
90 100 110
....*....|....*....|....*....|
gi 648281068 100 MPALIVM-PEDAPASKMAATR--SYGAQVV 126
Cdd:cd06446 107 LECEIYMgAVDVERQPLNVFRmeLLGAEVV 136
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
28-294 |
7.13e-04 |
|
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273465 Cd Length: 298 Bit Score: 40.81 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 28 RTPILRSRTADELlGAQLFFKCENLQRTGAFKIRGAYNALSQftPEQR---KRGALAF--SSGNHAQAVALAAQMLDMPA 102
Cdd:TIGR01139 7 NTPLVRLNRIEGC-NANVFVKLEGRNPSGSVKDRIALNMIWD--AEKRgllKPGKTIVepTSGNTGIALAMVAAARGYKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 103 LIVMPEDAPASKMAATRSYGAQVVtydrFTEDRE----AISR--RLADERGMTLIPP--F-NHRDVIAGQGTAAKELFEE 173
Cdd:TIGR01139 84 ILTMPETMSIERRKLLKAYGAELV----LTPGAEgmkgAIAKaeEIAASTPNSYFMLqqFeNPANPEIHRKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 174 VP-DLDYLFVCLGGGGLLSGSLLAAGQLSPRCKVYGVEPQAGddarQSLRAGRivqiPTPHTIadgaqtQSIGD--ITFA 250
Cdd:TIGR01139 160 TDgKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAES----PVLSGGK----PGPHKI------QGIGAgfIPKN 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 648281068 251 IIREHVEDILAVADEHLVQAMRFYAERKKIVVEPTGALSLAGAL 294
Cdd:TIGR01139 226 LNRSVIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAAL 269
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
29-127 |
1.01e-03 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 40.56 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILRSRTADELLGAQLFFKCENLQRTGAFKIRgayNALSQ--FTPEQRKRGALAFS-SGNHAQAVALAAQMLDMPALIV 105
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKIN---NALGQalLAKRMGKTRIIAETgAGQHGVATATACALFGLKCTIF 348
|
90 100
....*....|....*....|....*
gi 648281068 106 MPED---APASKMAATRSYGAQVVT 127
Cdd:PRK13803 349 MGEEdikRQALNVERMKLLGANVIP 373
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
29-126 |
2.45e-03 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 39.46 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 29 TPILR-SRTADELLGAQLFFKCENLQRTGAFKIRgayNALSQFTPEQR---KR-----GAlafssGNHAQAVALAAQMLD 99
Cdd:PRK13028 63 TPLYHaKRLSEELGGAQIYLKREDLNHTGAHKIN---NCLGQALLAKRmgkKRliaetGA-----GQHGVATATAAALFG 134
|
90 100 110
....*....|....*....|....*....|
gi 648281068 100 MPALIVMPE-DAPASKMAATRS--YGAQVV 126
Cdd:PRK13028 135 LECEIYMGEvDIERQHPNVFRMklLGAEVV 164
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
35-176 |
3.70e-03 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 39.03 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648281068 35 RTADELLG-AQLFFKCENLQRTGAFKIRGAYNALSQFTPEQRKRGALA----FSSGNHAQAVALAAQMLDMPALIVMPED 109
Cdd:PLN02569 141 RLGKEFLGmNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAKPVVgvgcASTGDTSAALSAYCAAAGIPSIVFLPAD 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648281068 110 APAS----KMAATrsyGAQVVTYDRFTEDREAISRRLADERGMTLIPPFN-HRdvIAGQGTAAKELFE----EVPD 176
Cdd:PLN02569 221 KISIaqlvQPIAN---GALVLSIDTDFDGCMRLIREVTAELPIYLANSLNsLR--LEGQKTAAIEILQqfdwEVPD 291
|
|
| |
