|
Name |
Accession |
Description |
Interval |
E-value |
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
26-407 |
2.77e-146 |
|
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: 420.31 E-value: 2.77e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 26 PLVKRTELVRaagiETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAASRSGTKSTIF 105
Cdd:TIGR01127 2 PLIYSTTLSD----ITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 106 LPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQLMDAEAVVVPVG 185
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 186 GGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFDMVEEYVDELVTVTDD 265
Cdd:TIGR01127 158 GGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 266 ETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNIDVNILSRVITRGLMKTGRKASLTLELLDKPG 345
Cdd:TIGR01127 238 EIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPG 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545666352 346 QLEEVSRIIAEKGANVTRVDHNSTAEDSDINGCYLTMQMETRDFRHVEEIRREFSERGFRLV 407
Cdd:TIGR01127 318 ALYHLLESIAEARANIVKIDHDRLSKEIPPGFAMVEITLETRGKEHLDEILKILRDMGYNFY 379
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
10-331 |
3.07e-146 |
|
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: 418.29 E-value: 3.07e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 10 MELTLDRVYQAAHVLKPLVKRTELVRAAGI--ETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNH 87
Cdd:COG1171 4 LMPTLADIEAAAARIAGVVRRTPLLRSPTLseRLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 88 AQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIG 167
Cdd:COG1171 84 AQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 168 MEICEQLMDAEAvvvpvggggLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSV 247
Cdd:COG1171 164 LEILEQLPDLDAvfvpvggggLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 248 TFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNIDVNILSRVITRGL 327
Cdd:COG1171 244 TFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEILERGL 323
|
....
gi 545666352 328 MKTG 331
Cdd:COG1171 324 VGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
14-315 |
1.38e-137 |
|
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: 395.32 E-value: 1.38e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 14 LDRVYQAAHVLKPLVKRTELVRAAGI--ETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGV 91
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLseLLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 92 ALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEIC 171
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 172 EQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFDM 251
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545666352 252 VEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNID 315
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
10-404 |
1.84e-111 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 332.63 E-value: 1.84e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 10 MELTLDRVYQAAHVLKPLVKRTELV--RAAGIETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNH 87
Cdd:PRK07334 3 LMVTLADIRAAAARLAGQVLRTPCVhsRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 88 AQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIG 167
Cdd:PRK07334 83 AQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 168 MEICEQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEvhTFADGIAVKKPGSV 247
Cdd:PRK07334 163 LEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKGVALPCGGS--TIAEGIAVKQPGQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 248 TFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNIDVNILSRVITRGL 327
Cdd:PRK07334 241 TLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNIDTRLLANVLLRGL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545666352 328 MKTGRKASLTLELLDKPGQLEEVSRIIAEKGANVTRVDHNSTAEDSDINGCYLTMQMETRDFRHVEEIRREFSERGF 404
Cdd:PRK07334 321 VRAGRLARLRVDIRDRPGALARVTALIGEAGANIIEVSHQRLFTDLPAKGAELELVIETRDAAHLQEVIAALRAAGF 397
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
12-322 |
4.74e-106 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 316.29 E-value: 4.74e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 12 LTLDRVYQAAHVLKPLVKRTELVRAAGIETDC--ELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQ 89
Cdd:PRK08638 9 VAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCkgEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 90 GVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGME 169
Cdd:PRK08638 89 GVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 170 ICEQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTF 249
Cdd:PRK08638 169 ILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTY 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545666352 250 DMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVP--VEGKKTVCIISGGNIDvniLSRV 322
Cdd:PRK08638 249 EIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDqyIQNKKVVAIISGGNVD---LSRV 320
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
7-349 |
6.13e-101 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 306.35 E-value: 6.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 7 GEKMELTLDRVYQAAHVLKPLVKRTELVRAAGI--ETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSA 84
Cdd:PRK08639 2 TVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLseKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 85 GNHAQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGA---EVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIA 161
Cdd:PRK08639 82 GNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 162 GQGTIGMEICEQLmDAEAVVVPVGGGG----LISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFAD 237
Cdd:PRK08639 162 GQGTVAVEILEQL-EKEGSPDYVFVPVggggLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 238 GIAVKKPGSVTFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNIDVN 317
Cdd:PRK08639 241 GAAVARVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKTVVCVISGGNNDIE 320
|
330 340 350
....*....|....*....|....*....|..
gi 545666352 318 ILSRVITRGLMKTGRKASLTLELLDKPGQLEE 349
Cdd:PRK08639 321 RMPEIKERSLIYEGLKHYFIVNFPQRPGALRE 352
|
|
| COG2061 |
COG2061 |
Uncharacterized conserved protein, contains ACT domain [General function prediction only]; |
10-408 |
2.03e-90 |
|
Uncharacterized conserved protein, contains ACT domain [General function prediction only];
Pssm-ID: 441664 [Multi-domain] Cd Length: 401 Bit Score: 278.47 E-value: 2.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 10 MELTLDRVYQAAHVLKPLVKRTELVRAAGIETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQ 89
Cdd:COG2061 2 LLLLDEEAAAAALAVVVVTTPLLLSSSSSLSVGLVVLLKEENLQTTGSFKRRGAYKLIALLLEEEEKGGVAAAAAGNAAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 90 GVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGME 169
Cdd:COG2061 82 AAAAAAALGGISAIVVMPPPPPLPKVAATRGGGAVVVVVGGDDDAAAAAAAALQEEEGGFFHHPDDDDDVIAGGGGGGLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 170 ICEQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTF 249
Cdd:COG2061 162 ILELLPDVVVVVVGGGGGGGGGGAAAAAKAKRPPIVIVGVQAEAAAAAPSSLAAGIEVVPGGGTTIADGIAVVKPGGLTF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 250 DMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAvLFHKVPVEGKKTVCIISGGNIDVNILSRVITRGLMK 329
Cdd:COG2061 242 IIIRKVVDDVVVVVEEEIAAALLLLLERKKKVVEGAAAAAAAA-ALKKKPLRGKKVVVVLSGGNIDDLLLLRIIIKGLLA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545666352 330 TGRKASLTLELLDKPGQLEEVSRIIAEKGANVTRVDHNSTAEDSDINGCYLTMQMETRDFRHVEEIRREFSERGFRLVQ 408
Cdd:COG2061 321 AGRRLVLLVVLPDRPGQLLRVLQPIAELGANIISVVHERENSKTPRGEVEVEVVLETRGEEHLEEIIAALREAGYNVRR 399
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
14-314 |
9.00e-84 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 258.85 E-value: 9.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 14 LDRVYQAAHVLKPLVKRTELVRAAGIE--TDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGV 91
Cdd:PRK06815 4 FDAILEAHQRLRPQVRVTPLEHSPLLSqhTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 92 ALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEIC 171
Cdd:PRK06815 84 ALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 172 EQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVK-KPGSVTFD 250
Cdd:PRK06815 164 EQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGvEPGAITFP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545666352 251 MVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNI 314
Cdd:PRK06815 244 LCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNI 307
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
16-362 |
8.95e-83 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 262.00 E-value: 8.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 16 RVYQAAHVlKPLVKRTELVRAAGietdCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAA 95
Cdd:PRK09224 13 RVYDVAQE-TPLEKAPKLSARLG----NQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 96 SRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQLM 175
Cdd:PRK09224 88 ARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 176 DA-EAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFDMVEE 254
Cdd:PRK09224 168 HPlDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 255 YVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAA----VLFHKvpVEGKKTVCIISGGNIDVNILSRVITRGLMKT 330
Cdd:PRK09224 248 YVDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAGlkkyVAQHG--IEGETLVAILSGANMNFDRLRYVAERAELGE 325
|
330 340 350
....*....|....*....|....*....|..
gi 545666352 331 GRKASLTLELLDKPGQLEEVSRIIAEKgaNVT 362
Cdd:PRK09224 326 QREALLAVTIPEEPGSFLKFCELLGGR--NVT 355
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
12-328 |
4.87e-81 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 251.81 E-value: 4.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 12 LTLDRVYQAAHVLKPLVKRTELVRAAGIE--TDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQ 89
Cdd:PRK07476 1 VSLADIYRARRRIAGRVRRTPLVASASLSarAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 90 GVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGME 169
Cdd:PRK07476 81 ALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 170 ICEQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFAD----GIAVKKpg 245
Cdd:PRK07476 161 ILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslggGIGLDN-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 246 SVTFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNIDVNILSRVITR 325
Cdd:PRK07476 239 RYTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELHRRIING 318
|
...
gi 545666352 326 GLM 328
Cdd:PRK07476 319 EVA 321
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
16-362 |
2.37e-78 |
|
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: 250.42 E-value: 2.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 16 RVYQAAhVLKPLvkrtELVRAAGIETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAA 95
Cdd:TIGR01124 10 RVYEAA-QETPL----QKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 96 SRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQL- 174
Cdd:TIGR01124 85 ARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 175 MDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFDMVEE 254
Cdd:TIGR01124 165 NPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 255 YVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAV--LFHKVPVEGKKTVCIISGGNIDVNILSRVITRGLMKTGR 332
Cdd:TIGR01124 245 YLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLkkYVALHGIRGQTLVAILSGANMNFHRLRYVSERCELGEQR 324
|
330 340 350
....*....|....*....|....*....|
gi 545666352 333 KASLTLELLDKPGQLEEVSRIIAEKgaNVT 362
Cdd:TIGR01124 325 EALLAVTIPEQPGSFLKFCELLGNR--NIT 352
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
24-311 |
2.14e-76 |
|
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: 239.13 E-value: 2.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 24 LKPLVKRTELVRAAGI--ETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAASRSGTK 101
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLskELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 102 STIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRY-QKESGAVFIHPFNDIDVIAGQGTIGMEICEQL-MDAEA 179
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELaAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLgGDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 180 VVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKK-PGSVTFDMVEEYVDE 258
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDePGALALDLLDEYVGE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 545666352 259 LVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPV--EGKKTVCIISG 311
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGElkGGDRVVVVLTG 295
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
16-407 |
1.47e-75 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 243.94 E-value: 1.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 16 RVYQAAhVLKPLvkrtELVRAAGIETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAA 95
Cdd:PRK12483 30 RVYDVA-RETPL----QRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 96 SRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQLM 175
Cdd:PRK12483 105 ARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 176 DA-EAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFDMVEE 254
Cdd:PRK12483 185 GPlDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRH 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 255 YVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAV--LFHKVPVEGKKTVCIISGGNIDVNILSRVITRGLMKTGR 332
Cdd:PRK12483 265 YVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIkkYAEREGIEGQTLVAIDSGANVNFDRLRHVAERAELGEQR 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545666352 333 KASLTLELLDKPGQLEEVSRIIAEKgaNVTrvDHNSTAEDSDINGCYLTMQMETRDFRHvEEIRREFSERGFRLV 407
Cdd:PRK12483 345 EAIIAVTIPEQPGSFKAFCAALGKR--QIT--EFNYRYADAREAHLFVGVQTHPRHDPR-AQLLASLRAQGFPVL 414
|
|
| PLN02970 |
PLN02970 |
serine racemase |
4-319 |
2.47e-74 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 234.96 E-value: 2.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 4 GAGGEKMELTLDRVYQAAHVLKPLVKRTELVRAAGIETDC--ELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVA 81
Cdd:PLN02970 1 EAASEKYAADLSSIREARKRIAPFIHRTPVLTSSSLDALAgrSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 82 CSAGNHAQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIA 161
Cdd:PLN02970 81 HSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 162 GQGTIGMEICEQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAV 241
Cdd:PLN02970 161 GQGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 242 KKpGSVTFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVL---FHKVPV--EGKKTVCIISGGNIDV 316
Cdd:PLN02970 241 SL-GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALsdsFRSNPAwkGCKNVGIVLSGGNVDL 319
|
...
gi 545666352 317 NIL 319
Cdd:PLN02970 320 GVL 322
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
13-325 |
3.62e-73 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 231.45 E-value: 3.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 13 TLDRVYQAAHVLKPLVKRTELV--RAAGIETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQG 90
Cdd:PRK07048 7 TYDDVAAAAARLAGVAHRTPVLtsRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 91 VALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEI 170
Cdd:PRK07048 87 IALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 171 CEQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFD 250
Cdd:PRK07048 167 FEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFP 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545666352 251 MVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNIDVNILSRVITR 325
Cdd:PRK07048 247 IIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLSG 321
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
31-312 |
1.53e-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: 201.59 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 31 TELVRAAGI--ETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRG--VVACSAGNHAQGVALAASRSGTKSTIFL 106
Cdd:cd00640 1 TPLVRLKRLskLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 107 PAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKES-GAVFIHPFNDIDVIAGQGTIGMEICEQLMDAEavvvpvg 185
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQLGGQK------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 186 GGG---------LISGVSFVVKKLNPACKVYGVQAsgaasmlksrrdhaleslsevhtfadgiavkkpgsvtfdmveeyv 256
Cdd:cd00640 154 PDAvvvpvggggNIAGIARALKELLPNVKVIGVEP--------------------------------------------- 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 545666352 257 dELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKV-PVEGKKTVCIISGG 312
Cdd:cd00640 189 -EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKkLGKGKTVVVILTGG 244
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
10-315 |
2.74e-62 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 202.88 E-value: 2.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 10 MELTLDRVYQAAHVLKPLVKRTELVRAAGIETDC-ELYLKTENLQNTGSFKIRGACYRIstLTEEERRRGVVACSAGNHA 88
Cdd:PRK08246 3 AMITRSDVRAAAQRIAPHIRRTPVLEADGAGFGPaPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 89 QGVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGM 168
Cdd:PRK08246 81 LAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 169 EICEQLMDAEAVVVPVGGGGLISGVSFVVKklnPACKVYGVQASGAASMlksrrDHALESLSEVHTFADGIAV-----KK 243
Cdd:PRK08246 161 EIEEQAPGVDTVLVAVGGGGLIAGIAAWFE---GRARVVAVEPEGAPTL-----HAALAAGEPVDVPVSGIAAdslgaRR 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545666352 244 PGSVTFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLF-HKVPVEGKKTVCIISGGNID 315
Cdd:PRK08246 233 VGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSgAYVPAPGERVAVVLCGANTD 305
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
12-323 |
3.03e-62 |
|
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: 203.16 E-value: 3.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 12 LTLDRVYQAAHVLKPLVKRTELVRAAGIETDC--ELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQ 89
Cdd:TIGR02991 1 VTLQDIERAAARISGRVEETPLVESPSLSELCgvPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 90 GVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGME 169
Cdd:TIGR02991 81 ALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 170 ICEQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFAD--GIAVKKPGSV 247
Cdd:TIGR02991 161 VVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545666352 248 TFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGkKTVCIISGGNIDVNILSRVI 323
Cdd:TIGR02991 241 TFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPG-PCAVIVSGRNIDMDLHKRII 315
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
16-371 |
6.65e-57 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 196.30 E-value: 6.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 16 RVYQAAhVLKPLVKRTELVRAAGIEtdceLYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAA 95
Cdd:PLN02550 102 KVYDVA-IESPLQLAKKLSERLGVK----VLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 96 SRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQLM 175
Cdd:PLN02550 177 QRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQ 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 176 DA-EAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFDMVEE 254
Cdd:PLN02550 257 GPlHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 255 YVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVA-AVLFHK-VPVEGKKTVCIISGGNIDVNILsRVITRgLMKTGR 332
Cdd:PLN02550 337 LVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAgAEAYCKyYGLKDENVVAITSGANMNFDRL-RIVTE-LADVGR 414
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 545666352 333 K--ASLTLELLDKPGQLEEVSRIIAEkgANVTRVDHNSTAE 371
Cdd:PLN02550 415 QqeAVLATFMPEEPGSFKRFCELVGP--MNITEFKYRYSSE 453
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
45-333 |
4.22e-52 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 177.90 E-value: 4.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 45 LYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGAE 124
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 125 VRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQLMDaeAVVVPVGGGGLISGVSFVVKklNPAC 204
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAHAPD--VVIVPIGGGGLASGVALALK--SQGV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 205 KVYGVQASGAASMLKSRRDHaLESLSEVHTFADGIAVKKPGSVTFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEG 284
Cdd:PRK08813 206 RVVGAQVEGVDSMARAIRGD-LREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEG 284
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 545666352 285 AGAVSVAAvlfhKVPVEGKKTVCIISGGNIDVNILSRVITRGLMKTGRK 333
Cdd:PRK08813 285 AGALALAA----GRRVSGKRKCAVVSGGNIDATVLATLLSEVRPRPPRK 329
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
17-322 |
1.71e-51 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 175.73 E-value: 1.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 17 VYQAAHVLKPLVKRTELVRAAGIE--TDCELYLKTENLQNTGSFKIRGACYRISTLTEEERR-RGVVACSAGNHAQGVAL 93
Cdd:PRK06608 10 IAAAHNRIKQYLHLTPIVHSESLNemLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLpDKIVAYSTGNHGQAVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 94 AASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDgVYDDAYEAALRyQKESGAVFIHPFNDIDVIAGQGTIGMEICEQ 173
Cdd:PRK06608 90 ASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTN-TRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYEALQQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 174 L-MDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYG---VQASGAASMLKSRRDHALESLSEvhTFADGIAVKKPGSVTF 249
Cdd:PRK06608 168 LgFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGsepLNANDAYLSLKNNKIYRLNYSPN--TIADGLKTLSVSARTF 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545666352 250 DMVEEyVDELVTVtdDETAAAILT--LMERQKVVSEGAGAVSVAAVL-FHKVPVEGKKTVCIISGGNIDVNILSRV 322
Cdd:PRK06608 246 EYLKK-LDDFYLV--EEYEIYYWTawLTHLLKVICEPSSAINMVAVVnWLKTQSKPQKLLVILSGGNIDPILYNEL 318
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
43-326 |
2.04e-42 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 151.30 E-value: 2.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 43 CELYLKTENLQNTGSFKIRGACYRISTLTEEERR-RGVVACSAGNHAQGVALAASRSGTKSTIFLPAVAPISKVEATRAY 121
Cdd:PRK06110 36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRvRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 122 GAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDiDVIAGQGTIGMEICEQLMDAEAVVVPVGGGGLISGVSFVVKKLN 201
Cdd:PRK06110 116 GAELIEHGEDFQAAREEAARLAAERGLHMVPSFHP-DLVRGVATYALELFRAVPDLDVVYVPIGMGSGICGAIAARDALG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 202 PACKVYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFDMVEEYVDELVTVTDDETAAAILTLMERQKVV 281
Cdd:PRK06110 195 LKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNV 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 545666352 282 SEGAGAVSVAAVLFHKVPVEGKKTVCIISGGNIDVNILSRVITRG 326
Cdd:PRK06110 275 AEGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVFARVLAGA 319
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
26-311 |
6.12e-40 |
|
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: 144.66 E-value: 6.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 26 PLVKRTELVRAAGIEtdcELYLKTENLQNTGSFKIRGACYRISTLtEEERRRGVVACSAGNHAQGVALAASRSGTKSTIF 105
Cdd:cd01563 24 PLVRAPRLGERLGGK---NLYVKDEGLNPTGSFKDRGMTVAVSKA-KELGVKAVACASTGNTSASLAAYAARAGIKCVVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 106 LPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNdIDVIAGQGTIGMEICEQLmDAEAVVVPVG 185
Cdd:cd01563 100 LPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSNSLN-PYRLEGQKTIAFEIAEQL-GWEVPDYVVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 186 ---GGGLISGVSFVVKKL--------NPacKVYGVQASGAASML---KSRRDHAlESLSEVHTFADGIAVKKPGSV--TF 249
Cdd:cd01563 178 pvgNGGNITAIWKGFKELkelglidrLP--RMVGVQAEGAAPIVrafKEGKDDI-EPVENPETIATAIRIGNPASGpkAL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545666352 250 DMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHK---VPVEGKKTVCIISG 311
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLReegIIDKGERVVVVLTG 319
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
26-311 |
5.61e-31 |
|
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: 122.23 E-value: 5.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 26 PLVKRTELVRAAGietdCELYLKtENLQN-TGSFKIRG---ACYRIStlteeERRRGVVAC-SAGNHAQGVALAASRSGT 100
Cdd:COG0498 68 PLVKAPRLADELG----KNLYVK-EEGHNpTGSFKDRAmqvAVSLAL-----ERGAKTIVCaSSGNGSAALAAYAARAGI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 101 KSTIFLPA--VAPISKVEATrAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNdIDVIAGQGTIGMEICEQLMDAE 178
Cdd:COG0498 138 EVFVFVPEgkVSPGQLAQML-TYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSIN-PARLEGQKTYAFEIAEQLGRVP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 179 AVvvpvgggglisgvsFVV------------------------KKLnPacKVYGVQASGAASMLKS-RRDHALESLSEVH 233
Cdd:COG0498 216 DW--------------VVVptgnggnilagykafkelkelgliDRL-P--RLIAVQATGCNPILTAfETGRDEYEPERPE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 234 TFADGIAVKKPGSvtfdmVEEYVDEL-------VTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHK---VPVEGK 303
Cdd:COG0498 279 TIAPSMDIGNPSN-----GERALFALresggtaVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLReegEIDPDE 353
|
....*...
gi 545666352 304 KTVCIISG 311
Cdd:COG0498 354 PVVVLSTG 361
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
26-313 |
2.30e-27 |
|
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: 110.47 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 26 PLVKRTELVRAAGietdCELYLKTENLQNTGSFKIRGACYRISTLTEEERR--RGVVACSAGNHAQGVALAASRSGTKST 103
Cdd:cd06448 3 PLIESTALSKTAG----CNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNecVHVVCSSGGNAGLAAAYAARKLGVPCT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 104 IFLPAVAPISKVEATRAYGAEVRMIDGVYDDAyEAALRYQ---KESGAVFIHPFNDIDVIAGQGTIGMEICEQLMDAE-- 178
Cdd:cd06448 79 IVVPESTKPRVVEKLRDEGATVVVHGKVWWEA-DNYLREElaeNDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSQEkv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 179 -AVVVPVGGGGLISGVSFVVKKlNPACK--VYGVQASGAASMLKSRRDHALESLSEVHTFADGIAVKKPGSVTFDMVEEY 255
Cdd:cd06448 158 dAIVCSVGGGGLLNGIVQGLER-NGWGDipVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEH 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545666352 256 VDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAV--------LFHKVPVEGKKTVCIISGGN 313
Cdd:cd06448 237 NIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVysgkildlQLEVLLTPLDNVVVVVCGGS 302
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
30-309 |
6.29e-22 |
|
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: 94.89 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 30 RTELVRAAGI--ETDCELYLKTENLQNTGSFKIRGACYRISTLteEER---RRG--VVACSAGNHAQGVALAASRSGTKS 102
Cdd:cd01561 2 NTPLVRLNRLspGTGAEIYAKLEFFNPGGSVKDRIALYMIEDA--EKRgllKPGttIIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 103 TIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKE-----SGAVFIHPF-NDIDVIAGQGTIGMEICEQL-- 174
Cdd:cd01561 80 IIVMPETMSEEKRKLLRALGAEVILTPEAEADGMKGAIAKARElaaetPNAFWLNQFeNPANPEAHYETTAPEIWEQLdg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 175 -MDAeavvvpvggggL---------ISGVSFVVKKLNPACKVYGVQASGAASML-KSRRDHALEslsevhtfadGI-AVK 242
Cdd:cd01561 160 kVDA-----------FvagvgtggtITGVARYLKEKNPNVRIVGVDPVGSVLFSgGPPGPHKIE----------GIgAGF 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545666352 243 KPGsvTFDMveEYVDELVTVTDDETAAAILTLMERqkvvsEG------AGAVSVAAVLFHKVPVEGKKTVCII 309
Cdd:cd01561 219 IPE--NLDR--SLIDEVVRVSDEEAFAMARRLARE-----EGllvggsSGAAVAAALKLAKRLGPGKTIVTIL 282
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
26-291 |
1.36e-21 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 95.45 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 26 PLVKRTELVRAAGIEtdcELYLKTENLQNTGSFKIRGACYRIStLTEEERRRGVVACSAGNHAQGVALAASRSGTKSTIF 105
Cdd:PRK08197 81 PLLPLPRLGKALGIG---RLWVKDEGLNPTGSFKARGLAVGVS-RAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 106 LPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQLM----DAeavv 181
Cdd:PRK08197 157 MPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLGwrlpDV---- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 182 vpvgggglI-----SGVSFV--VKKLN----------PACKVYGVQASGAASMLKSRRDHALES--LSEVHTFADGIAVK 242
Cdd:PRK08197 233 --------IlyptgGGVGLIgiWKAFDelealgwiggKRPRLVAVQAEGCAPIVKAWEEGKEESefWEDAHTVAFGIRVP 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 545666352 243 KP-GS-VTFDMVEEYVDELVTVTDDETAAAILTLMERQK--VVSEGAGAVSVA 291
Cdd:PRK08197 305 KAlGDfLVLDAVRETGGCAIAVSDDAILAAQRELAREEGlfACPEGAATFAAA 357
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
25-311 |
2.69e-21 |
|
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: 93.60 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 25 KPLVKRTELVRAAGIEtdcELYLKTENLQNTGSFKIRGACYRISTLTEeeRRRGVVAC-SAGNHAQGVALAASRSGTKST 103
Cdd:TIGR00260 23 TPLFRAPALAANVGIK---NLYVKELGHNPTLSFKDRGMAVALTKALE--LGNDTVLCaSTGNTGAAAAAYAGKAGLKVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 104 IFLPAvAPIS--KVEATRAYGAEVRMIDGVYDDAYEAALRYQKESgavFIHPFNDIDV----IAGQGTIGMEICEQL--M 175
Cdd:TIGR00260 98 VLYPA-GKISlgKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDK---PALGLNSANSipyrLEGQKTYAFEAVEQLgwE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 176 DAEAVVVPVGGGGLISGV--SFVVKK---LNPACKVYGVQASGAASM----LKSRRDHALESLSevhTFADGIAVKKPGS 246
Cdd:TIGR00260 174 APDKVVVPVPNSGNFGAIwkGFKEKKmlgLDSLPVKRGIQAEGAADIvrafLEGGQWEPIETPE---TLSTAMDIGNPAN 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 247 VTF--DMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVE---GKKTVCIISG 311
Cdd:TIGR00260 251 WPRalEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTadpAERVVCALTG 320
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
44-292 |
9.99e-20 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 89.50 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 44 ELYLKTENLQNTGSFKIRGACYRISTLTEEERRRgVVACSAGNHAQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGA 123
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINE-VVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 124 EVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQLMDAEAVVVPVGGGGLISGVSFVVKKL--- 200
Cdd:PRK08329 152 ELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIWKGFKELhem 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 201 ---NPACKVYGVQASGAASMLKsrRDHaleslsEVHTFADGIAVKKPGSV--TFDMVEEYVDELVTVTDDETAAAiLTLM 275
Cdd:PRK08329 232 geiSKMPKLVAVQAEGYESLCK--RSK------SENKLADGIAIPEPPRKeeMLRALEESNGFCISVGEEETRAA-LHWL 302
|
250
....*....|....*..
gi 545666352 276 ERQKVVSEGAGAVSVAA 292
Cdd:PRK08329 303 RRMGFLVEPTSAVALAA 319
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
26-294 |
5.41e-19 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 88.01 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 26 PLVKRTELVRAAGIEtdcELYLKTE----NLqntGSFKIRGACY------------RISTLTEEERRRG---------VV 80
Cdd:PRK08206 46 PLVALPDLAAELGVG---SILVKDEsyrfGL---NAFKALGGAYavarllaeklglDISELSFEELTSGevreklgdiTF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 81 AC-SAGNHAQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHP-----F 154
Cdd:PRK08206 120 ATaTDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVQDtawegY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 155 NDI--DVIAGQGTIGMEICEQLmdaEAVVVPVGGGGLISGV--------SFVVKKLNPAC-KVYGVQASGAASMLKSRRD 223
Cdd:PRK08206 200 EEIptWIMQGYGTMADEAVEQL---KEMGVPPTHVFLQAGVgslagavlGYFAEVYGEQRpHFVVVEPDQADCLYQSAVD 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545666352 224 ---HALEslSEVHTFADGIAVKKPGSVTFDMVEEYVDELVTVTDDETAAAILTLME----RQKVVSEGAGAVSVAAVL 294
Cdd:PRK08206 277 gkpVAVT--GDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDEVAALGMRILANplggDPPIVSGESGAVGLGALA 352
|
|
| ACT_ThrD-II-like |
cd04886 |
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and ... |
336-408 |
1.36e-15 |
|
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains; This CD includes the C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains. The Escherichia coli tdcB gene product, ThrD-II, anaerobically catalyzes the pyridoxal phosphate-dependent dehydration of L-threonine and L-serine to ammonia and to alpha-ketobutyrate and pyruvate, respectively. Tetrameric ThrD-II is subject to allosteric activation by AMP, inhibition by alpha-keto acids, and catabolite inactivation by several metabolites of glycolysis and the citric acid cycle. Also included in this CD are N-terminal ACT domains present in smaller (~170 a.a.) archaeal proteins of unknown function. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153158 [Multi-domain] Cd Length: 73 Bit Score: 71.04 E-value: 1.36e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545666352 336 LTLELLDKPGQLEEVSRIIAEKGANVTRVDHNSTAEDSDINGCYLTMQMETRDFRHVEEIRREFSERGFRLVQ 408
Cdd:cd04886 1 LRVELPDRPGQLAKLLAVIAEAGANIIEVSHDRAFKTLPLGEVEVELTLETRGAEHIEEIIAALREAGYDVRR 73
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
27-309 |
2.01e-15 |
|
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: 76.24 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 27 LVKRTELVRAAGI--ETDCELYLKTENLQNTGSFKIRGACYRIstltEEERRRG-------VVACSAGNHAQGVALAASR 97
Cdd:COG0031 10 LIGNTPLVRLNRLspGPGAEIYAKLESFNPGGSVKDRIALSMI----EDAEKRGllkpggtIVEATSGNTGIGLAMVAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 98 SGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGV--YDDAYEAALRYQKE-SGAVFIHPFNDID-VIAGQGTIGMEICEQ 173
Cdd:COG0031 86 KGYRLILVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAAEtPGAFWPNQFENPAnPEAHYETTGPEIWEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 174 L---MDAeavvvpvggggL---------ISGVSFVVKKLNPACKVYGVQASGAASML-KSRRDHALEslsevhtfadGIA 240
Cdd:COG0031 166 TdgkVDA-----------FvagvgtggtITGVGRYLKERNPDIKIVAVEPEGSPLLSgGEPGPHKIE----------GIG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545666352 241 vkkPGSVT--FDMveEYVDELVTVTDDETAAAILTLMERqkvvsEG------AGAVSVAAV-LFHKVPvEGKKTVCII 309
Cdd:COG0031 225 ---AGFVPkiLDP--SLIDEVITVSDEEAFAMARRLARE-----EGilvgisSGAAVAAALrLAKRLG-PGKTIVTIL 291
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
31-294 |
2.70e-11 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 64.83 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 31 TELVRAA-GIETDCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVAcSAGNHAQGVALAASRSGTKSTIFLPAV 109
Cdd:PRK05638 67 TPLIRARiSEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVA-SDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 110 APISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIAGQGTIGMEICEQLMDAEAVVVPVGGGGL 189
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINPTHVIVPTGSGSYL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 190 IS---GVSFVVKK--LNPACKVYGVQASGAASMLKSRrdHALESLSEvHTFADGIAVKKPgsVTFDMVEEYVDE----LV 260
Cdd:PRK05638 226 YSiykGFKELLEIgvIEEIPKLIAVQTERCNPIASEI--LGNKTKCN-ETKALGLYVKNP--VMKEYVSEAIKEsggtAV 300
|
250 260 270
....*....|....*....|....*....|....
gi 545666352 261 TVTDDETAAAILTLMErQKVVSEGAGAVSVAAVL 294
Cdd:PRK05638 301 VVNEEEIMAGEKLLAK-EGIFAELSSAVVMPALL 333
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
27-294 |
4.29e-11 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 63.73 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 27 LVKRTELVR--AAGIETDCELYLKTENLQNTGSFKIRGACYRIstltEEERRRG-------VVACSAGNHAQGVALAASR 97
Cdd:PRK10717 10 TIGNTPLIRlnRASEATGCEILGKAEFLNPGGSVKDRAALNII----WDAEKRGllkpggtIVEGTAGNTGIGLALVAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 98 SGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGV-YDD---------AYEAALRYQKESGAVFIHPFNDID-VIAGQGTI 166
Cdd:PRK10717 86 RGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApYANpnnyvkgagRLAEELVASEPNGAIWANQFDNPAnREAHYETT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 167 GMEICEQlMDAE--AVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAA--SMLKSRrdhalESLSEVHTFADGIAVk 242
Cdd:PRK10717 166 GPEIWEQ-TDGKvdGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAlySYYKTG-----ELKAEGSSITEGIGQ- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 545666352 243 kpGSVTFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVL 294
Cdd:PRK10717 239 --GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAAL 288
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
44-174 |
6.61e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 63.22 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 44 ELYLKTENLQNTGSFKIRGACYRISTLTEEERRRgVVACSAGNHAQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGA 123
Cdd:PRK06450 66 NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQ-ISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGA 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 545666352 124 EVRMIDGVYDDAYEAAlryqKESGAVF----IHP-FNDidviaGQGTIGMEICEQL 174
Cdd:PRK06450 145 EVVRVRGSREDVAKAA----ENSGYYYashvLQPqFRD-----GIRTLAYEIAKDL 191
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
26-179 |
5.34e-10 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 60.10 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 26 PLVKRTELVRAAGIEtdcELYLKTENLQNTGSFKIRGACYRIstltEEERRRG---VVACSAGNHAQGVALAASRSGTKS 102
Cdd:PRK06381 17 PLLRARKLEEELGLR---KIYLKFEGANPTGTQKDRIAEAHV----RRAMRLGysgITVGTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545666352 103 TIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRYQKESGAVFIHPFNDIDVIA--GQGTIGMEICEQLMDAEA 179
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDieAYSAIAYEIYEALGDVPD 168
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
27-308 |
6.41e-08 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 54.20 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 27 LVKRTELVRAAGIETDCELYL--KTENLQNTGSFKIRGAcyrISTLTEEERRR-------GVVACSAGNHAQGVALAASR 97
Cdd:PLN02556 56 LIGKTPLVYLNKVTEGCGAYIaaKQEMFQPTSSIKDRPA---LAMIEDAEKKNlitpgktTLIEPTSGNMGISLAFMAAM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 98 SGTKSTIFLPAVAPISKVEATRAYGAEVRMID------GVYDDAYEAalrYQKESGAVFIHPF-NDIDVIAGQGTIGMEI 170
Cdd:PLN02556 133 KGYKMILTMPSYTSLERRVTMRAFGAELVLTDptkgmgGTVKKAYEL---LESTPDAFMLQQFsNPANTQVHFETTGPEI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 171 CEQ-LMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASgAASMLKSRRDhaleslSEVHTFADGIAVkKPGSVTF 249
Cdd:PLN02556 210 WEDtLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPA-ESNVLNGGKP------GPHHITGNGVGF-KPDILDM 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 250 DMVEEYVDelVTVTDDETAAAILTLMErQKVVSEGAGAVSVAAVLFHKVPV-EGKKTVCI 308
Cdd:PLN02556 282 DVMEKVLE--VSSEDAVNMARELALKE-GLMVGISSGANTVAALRLAKMPEnKGKLIVTV 338
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
45-324 |
8.63e-08 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 54.05 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 45 LYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAASRSGTKSTIFLPAV---APISKVEATRAY 121
Cdd:PRK13803 288 IYLKREDLNHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEdikRQALNVERMKLL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 122 GAEVRMI---DGVYDDAYEAALRYQKES---------GAVFIHPFNDIdVIAGQGTIGMEICEQLMDAEAVVVPVGGGGL 189
Cdd:PRK13803 368 GANVIPVlsgSKTLKDAVNEAIRDWVASvpdthyligSAVGPHPYPEM-VAYFQSVIGEEAKEQLKEQTGKLPDAIIACV 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 190 ISGV----SFVVKKLNPACKVYGVQASG--------AASMLKSRRDHALESLS-----------EVHTFADGIAVKKPGS 246
Cdd:PRK13803 447 GGGSnaigIFYHFLDDPSVKLIGVEAGGkgvntgehAATIKKGRKGVLHGSMTylmqdengqilEPHSISAGLDYPGIGP 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 247 VTFDMVEEYVDELVTVTDDETAAAILTLMERQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCI-ISG-GNIDVNILSRVIT 324
Cdd:PRK13803 527 MHANLFETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKDIVIVnLSGrGDKDIPTLKEYFE 606
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
22-178 |
3.91e-07 |
|
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: 51.77 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 22 HVLKPLVKR-TELVRAAGIE---TDCELYLKTENLQNTGSFKIR---GACYristLTEEERRRGVVA-CSAGNHAQGVAL 93
Cdd:cd06446 25 ELYKDYVGRpTPLYRAKRLSeylGGAKIYLKREDLNHTGAHKINnalGQAL----LAKRMGKKRVIAeTGAGQHGVATAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 94 AASRSGTKSTIFLPAVAPISK---VEATRAYGAEVRMI---DGVYDDAYEAALRYQKESG---------AVFIHPFNDId 158
Cdd:cd06446 101 ACALFGLECEIYMGAVDVERQplnVFRMELLGAEVVPVpsgSGTLKDAISEAIRDWVTNVedthyllgsVVGPHPYPNM- 179
|
170 180
....*....|....*....|
gi 545666352 159 VIAGQGTIGMEICEQLMDAE 178
Cdd:cd06446 180 VRDFQSVIGEEAKKQILEKE 199
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
44-173 |
1.21e-05 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 47.12 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 44 ELYLKTENLQNTGSFKIRGACYRISTLTEEERRR----GVVACSAGNhaQGVALAA--SRSGTKSTIFLPAVAP-ISKVE 116
Cdd:PLN02569 151 DLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAkpvvGVGCASTGD--TSAALSAycAAAGIPSIVFLPADKIsIAQLV 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 117 ATRAYGAEVRMIDGVYDDayeaALRYQKESGAVF-IHPFNDIDV--IAGQGTIGMEICEQ 173
Cdd:PLN02569 229 QPIANGALVLSIDTDFDG----CMRLIREVTAELpIYLANSLNSlrLEGQKTAAIEILQQ 284
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
336-399 |
5.83e-05 |
|
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.
Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 40.74 E-value: 5.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545666352 336 LTLELLDKPGQLEEVSRIIAEKGANVTRVDHNSTAEDSDINgcyltMQMETRDFRHVEEIRREF 399
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEAD-----IFIVVDGDGDLEKLLEAL 59
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
42-213 |
1.20e-04 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 44.25 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 42 DCELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAASRSGTKSTIFLPAVAPISK---VEAT 118
Cdd:PRK13802 346 DARVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQalnVARM 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 119 RAYGAEVRMI---DGVYDDAYEAALR----YQKES----GAVF-IHPFNDIdVIAGQGTIGMEICEQLMDAEAVVVPVGG 186
Cdd:PRK13802 426 RMLGAEVVEVtlgDRILKDAINEALRdwvtNVKDThyllGTVAgPHPFPAM-VRDFQKIIGEEAKQQLQDWYGIDHPDAI 504
|
170 180 190
....*....|....*....|....*....|..
gi 545666352 187 GGLISGVSFVVKKLN-----PACKVYGVQASG 213
Cdd:PRK13802 505 CACVGGGSNAIGVMNaflddERVNLYGYEAGG 536
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
79-312 |
4.06e-04 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 41.91 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 79 VVACSAGNHAQGVALAASRSGTKSTIFLPAVAPISKVEATRAYGAEVRMID------GVYDDAYEAAlryQKESGAVFIH 152
Cdd:PLN00011 72 LIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDqsiglkGMLEKAEEIL---SKTPGGYIPQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 153 PF-NDIDVIAGQGTIGMEIC-EQLMDAEAVVVPVGGGGLISGVSFVVKKLNPACKVYGVQASGAASMLKSRRDHALesls 230
Cdd:PLN00011 149 QFeNPANPEIHYRTTGPEIWrDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHL---- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 231 evhtfADGIAvkkPGSVTFDMVEEYVDELVTVTDDET--AAAILTLMErQKVVSEGAGAVSVAAVLFHKVPVEGKKTVCI 308
Cdd:PLN00011 225 -----IQGIG---SGIIPFNLDLTIVDEIIQVTGEEAieTAKLLALKE-GLLVGISSGAAAAAALKVAKRPENAGKLIVV 295
|
....*.
gi 545666352 309 I--SGG 312
Cdd:PLN00011 296 IfpSGG 301
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
44-141 |
5.38e-04 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 42.05 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 44 ELYLKTENLQNTGSFKIRGACYRISTLTEEERRRGVVACSAGNHAQGVALAASRSGTKSTIFLPAV---APISKVEATRA 120
Cdd:PLN02618 88 EIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQdmeRQALNVFRMRL 167
|
90 100
....*....|....*....|....
gi 545666352 121 YGAEVRMI---DGVYDDAYEAALR 141
Cdd:PLN02618 168 LGAEVRPVhsgTATLKDATSEAIR 191
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
44-266 |
7.71e-04 |
|
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.
Pssm-ID: 107208 Cd Length: 404 Bit Score: 41.56 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 44 ELYLKTEN-LQNTGSFKIRGACYRI--------------------STLTEEERRR-----GVVACSAGNHAQGVALAASR 97
Cdd:cd06447 76 RLLLKADShLPISGSIKARGGIYEVlkhaeklalehglltleddySKLASEKFRKlfsqySIAVGSTGNLGLSIGIMAAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 98 SGTKSTIFLPAVAPISKVEATRAYGAEVRMIDGVYDDAYEAALRY-QKESGAVFIHPFNDIDVIAGQGTIGMEICEQLmd 176
Cdd:cd06447 156 LGFKVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQaAADPMCYFVDDENSRDLFLGYAVAASRLKAQL-- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 177 AEAVVVPVGGGGLI-----------SGVSFVVKKL-NPACKVYGVQASGAASML----------KSRRDHALESLsevhT 234
Cdd:cd06447 234 AELGIKVDAEHPLFvylpcgvggapGGVAFGLKLIfGDNVHCFFAEPTHSPCMLlgmatglhdkISVQDIGIDNR----T 309
|
250 260 270
....*....|....*....|....*....|..
gi 545666352 235 FADGIAVKKPGSVTFDMVEEYVDELVTVTDDE 266
Cdd:cd06447 310 AADGLAVGRPSGLVGKLMEPLLSGIYTVEDDE 341
|
|
| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
336-398 |
2.99e-03 |
|
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153198 Cd Length: 72 Bit Score: 36.17 E-value: 2.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545666352 336 LTLELL--DKPGQLEEVSRIIAEKGANVTRVDHnSTAEDSDINGCYLT-MQMETRDFRHVEEIRRE 398
Cdd:cd04926 2 VRLELRteDRVGLLSDVTRVFRENGLTVTRAEI-STQGDMAVNVFYVTdANGNPVDPKTIEAVRQE 66
|
|
| SpoT |
COG0317 |
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription]; |
334-395 |
3.93e-03 |
|
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
Pssm-ID: 440086 [Multi-domain] Cd Length: 722 Bit Score: 39.37 E-value: 3.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545666352 334 ASLTLELLDKPGQLEEVSRIIAEKGANVTRVdhNSTAEDSDIngCYLTMQMETRDFRHVEEI 395
Cdd:COG0317 647 VDIRIEALDRPGLLADITSVIAEEKINILSV--NTRSRDDGT--ATIRFTVEVRDLDHLARV 704
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
26-210 |
6.84e-03 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 38.32 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 26 PLVKrteLVRAAGiETDCELYLKTENLQNTGSFKIRGAcyrISTLTEEERR-------RGVVACSaGNhaQGVALA--AS 96
Cdd:PRK11761 14 PLVK---LQRLPP-DRGNTILAKLEGNNPAGSVKDRPA---LSMIVQAEKRgeikpgdTLIEATS-GN--TGIALAmiAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545666352 97 RSGTKSTIFLPAVAPISKVEATRAYGAEVRMI--DGVYDDAYEAALRYQKESGAVFIHPFNDID-VIAGQGTIGMEICEQ 173
Cdd:PRK11761 84 IKGYRMKLIMPENMSQERRAAMRAYGAELILVpkEQGMEGARDLALQMQAEGEGKVLDQFANPDnPLAHYETTGPEIWRQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545666352 174 L----------MDAEAVvvpvgggglISGVSFVVKKLNPACKVYGVQ 210
Cdd:PRK11761 164 TegrithfvssMGTTGT---------IMGVSRYLKEQNPAVQIVGLQ 201
|
|
| |
