|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
4-322 |
0e+00 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 600.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 4 NLVLPTYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSG 83
Cdd:PRK07048 2 DLLLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 84 NHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGT 163
Cdd:PRK07048 82 NHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 164 AAKELFEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLG 243
Cdd:PRK07048 162 AAKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075215 244 NYTFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAHFLS 322
Cdd:PRK07048 242 NYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLS 320
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
10-313 |
3.01e-148 |
|
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: 418.81 E-value: 3.01e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 10 YDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAI 89
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 90 ALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELF 169
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 170 EEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSI 249
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075215 250 IKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVD 313
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
4-321 |
5.65e-141 |
|
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: 401.34 E-value: 5.65e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 4 NLVLPTYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSG 83
Cdd:COG1171 2 TALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 84 NHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGT 163
Cdd:COG1171 82 NHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 164 AAKELFEEVGPLDALFVClggggllsgsalaaRHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLG 243
Cdd:COG1171 162 IALEILEQLPDLDAVFVPvggggliagvaaalKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075215 244 NYTFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAHFL 321
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEIL 319
|
|
| PLN02970 |
PLN02970 |
serine racemase |
9-317 |
4.08e-126 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 363.61 E-value: 4.08e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 9 TYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQA 88
Cdd:PLN02970 10 DLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 89 IALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKEL 168
Cdd:PLN02970 90 LALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 169 FEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQhLGNYTFS 248
Cdd:PLN02970 170 LEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS-LGDLTWP 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075215 249 IIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAarAMKEKLKN-------KRIGIIISGGNVDIERY 317
Cdd:PLN02970 249 VVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAA--ALSDSFRSnpawkgcKNVGIVLSGGNVDLGVL 322
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
27-314 |
6.24e-86 |
|
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: 263.14 E-value: 6.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 27 TPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPL 106
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 107 DAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGPLDALFVCLGGGG 186
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 187 LLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDILTVSDEELI 266
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19075215 267 DCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDI 314
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDL 288
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
9-316 |
1.54e-85 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 260.82 E-value: 1.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 9 TYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQA 88
Cdd:PRK08638 10 AIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 89 IALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMY-DRYKDDREKMaKEISEREGLTIIPPYDHPHVLAGQGTAAKE 167
Cdd:PRK08638 90 VALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHgDNFNDTIAKV-EEIVEEEGRTFIPPYDDPKVIAGQGTIGLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 168 LFEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTF 247
Cdd:PRK08638 169 ILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTY 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075215 248 SIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEK--LKNKRIGIIISGGNVDIER 316
Cdd:PRK08638 249 EIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDqyIQNKKVVAIISGGNVDLSR 319
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
4-313 |
2.85e-80 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 247.38 E-value: 2.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 4 NLVLPTYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAG-VLTFSS 82
Cdd:PRK06608 1 NLLLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPDkIVAYST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 83 GNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRyKDDREKMAKEiSEREGLTIIPPYDHPHVLAGQG 162
Cdd:PRK06608 81 GNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNT-RQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 163 TAAKELFEEVGP-LDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVH-IDTPKTIADGAQTQ 240
Cdd:PRK06608 159 TLCYEALQQLGFsPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRlNYSPNTIADGLKTL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075215 241 HLGNYTFSIIKeKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARA-MKEKLKNKRIGIIISGGNVD 313
Cdd:PRK06608 239 SVSARTFEYLK-KLDDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNwLKTQSKPQKLLVILSGGNID 311
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
26-309 |
1.49e-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: 228.73 E-value: 1.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 26 KTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMP 105
Cdd:pfam00291 7 PTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 106 LDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEI-SEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGP-LDALFVCLG 183
Cdd:pfam00291 87 EDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELaAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGdPDAVVVPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 184 GGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQ-HLGNYTFSIIKEKVDDILTVSD 262
Cdd:pfam00291 167 GGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVGEVVTVSD 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19075215 263 EELIDCLKFYAARMKIVVEPTGCLSFAAAR-AMKEKLKNK-RIGIIISG 309
Cdd:pfam00291 247 EEALEAMRLLARREGIVVEPSSAAALAALKlALAGELKGGdRVVVVLTG 295
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
9-313 |
1.29e-72 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 229.78 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 9 TYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQA 88
Cdd:PRK07334 6 TLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 89 IALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKEL 168
Cdd:PRK07334 86 VAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 169 FEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAgNDGQQSFRKGSIVHIDTpKTIADGAQTQHLGNYTFS 248
Cdd:PRK07334 166 LEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTEL-YPSMYAAIKGVALPCGG-STIAEGIAVKQPGQLTLE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075215 249 IIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVD 313
Cdd:PRK07334 244 IVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNID 308
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
10-317 |
1.04e-68 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 216.87 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 10 YDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAI 89
Cdd:PRK06815 4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 90 ALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELF 169
Cdd:PRK06815 84 ALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 170 EEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADG-AQTQHLGNYTFS 248
Cdd:PRK06815 164 EQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGtAGGVEPGAITFP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075215 249 IIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERY 317
Cdd:PRK06815 244 LCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKY 312
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
19-319 |
2.15e-68 |
|
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: 221.53 E-value: 2.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 19 RIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGI 98
Cdd:TIGR01124 10 RVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 99 PAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVG-PLDA 177
Cdd:TIGR01124 90 KALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVAnPLDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 178 LFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDI 257
Cdd:TIGR01124 170 VFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDI 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075215 258 LTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAAR--AMKEKLKNKRIGIIISGGNVDIERYAH 319
Cdd:TIGR01124 250 VTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKkyVALHGIRGQTLVAILSGANMNFHRLRY 313
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
11-318 |
7.27e-66 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 212.74 E-value: 7.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 11 DDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIA 90
Cdd:PRK08639 10 KDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 91 LSAKILGIPAKIIMPLDAPEAKVAATKGYGGQ---VIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKE 167
Cdd:PRK08639 90 YACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEfveIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 168 LFE---EVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGN 244
Cdd:PRK08639 170 ILEqleKEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGD 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075215 245 YTFSIIKEKVDDILTVSD----EELIDCLKFYAarmkIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYA 318
Cdd:PRK08639 250 LTFEILKDVVDDVVLVPEgavcTTILELYNKEG----IVAEPAGALSIAALELYKDEIKGKTVVCVISGGNNDIERMP 323
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
42-316 |
1.61e-63 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 208.84 E-value: 1.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 42 EVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGG 121
Cdd:PRK09224 36 QVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 122 QVIMY-DRYkDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEV-GPLDALFVCLGGGGLLSGSALAARHFA 199
Cdd:PRK09224 116 EVVLHgDSF-DEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHpHPLDAVFVPVGGGGLIAGVAAYIKQLR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 200 PNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDILTVSDEELidClkfyAARMKI- 278
Cdd:PRK09224 195 PEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDTDEI--C----AAIKDVf 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 19075215 279 -----VVEPTGCLSFAAAR--AMKEKLKNKRIGIIISGGNVDIER 316
Cdd:PRK09224 269 edtrsIAEPAGALALAGLKkyVAQHGIEGETLVAILSGANMNFDR 313
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
17-319 |
2.94e-60 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 200.79 E-value: 2.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 17 SERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKIL 96
Cdd:PRK12483 28 AARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 97 GIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKE-LFEEVGPL 175
Cdd:PRK12483 108 GVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEiLRQHPGPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 176 DALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVD 255
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVD 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075215 256 DILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAAR--AMKEKLKNKRIGIIISGGNVDIERYAH 319
Cdd:PRK12483 268 EVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKkyAEREGIEGQTLVAIDSGANVNFDRLRH 333
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
27-310 |
2.92e-59 |
|
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: 190.42 E-value: 2.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 27 TPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAG--VLTFSSGNHAQAIALSAKILGIPAKIIM 104
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 105 PLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISER-EGLTIIPPYDHPHVLAGQGTAAKELFEEVG--PLDALFVC 181
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQGTIGLEILEQLGgqKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 182 LGGGGLLSGSALAARHFAPNCEVYGVEPEagndgqqsfrkgsivhidtpktiadgaqtqhlgnytfsiikekvddILTVS 261
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------------------VVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19075215 262 DEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKL-KNKRIGIIISGG 310
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLgKGKTVVVILTGG 244
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
9-319 |
3.66e-57 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 187.48 E-value: 3.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 9 TYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQA 88
Cdd:PRK07476 2 SLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 89 IALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKEL 168
Cdd:PRK07476 82 LAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 169 FEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGaqtqhLGN---- 244
Cdd:PRK07476 162 LEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADS-----LGGgigl 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075215 245 ---YTFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAH 319
Cdd:PRK07476 237 dnrYTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELHRR 314
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
17-316 |
1.04e-49 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 174.34 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 17 SERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKIL 96
Cdd:PLN02550 100 SAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 97 GIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEV-GPL 175
Cdd:PLN02550 180 GCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHqGPL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 176 DALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVD 255
Cdd:PLN02550 260 HAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVD 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075215 256 DILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKE--KLKNKRIGIIISGGNVDIER 316
Cdd:PLN02550 340 GVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKyyGLKDENVVAITSGANMNFDR 402
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
9-315 |
2.46e-49 |
|
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: 166.95 E-value: 2.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 9 TYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQA 88
Cdd:TIGR02991 2 TLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 89 IALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKEL 168
Cdd:TIGR02991 82 LAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 169 FEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIAD--GAQTQHLGNYT 246
Cdd:TIGR02991 162 VEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075215 247 FSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNkRIGIIISGGNVDIE 315
Cdd:TIGR02991 242 FAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPG-PCAVIVSGRNIDMD 309
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
41-322 |
2.68e-47 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 161.70 E-value: 2.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 41 AEVFFKCENFQKMGAFKFRGALNALSQLNEAQ-RKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGY 119
Cdd:PRK06110 36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 120 GGQVIMY-DRYKDDREKmAKEISEREGLTIIPPYdHPHVLAGQGTAAKELFEEVGPLDALFVCLGGGGLLSGSALAARHF 198
Cdd:PRK06110 116 GAELIEHgEDFQAAREE-AARLAAERGLHMVPSF-HPDLVRGVATYALELFRAVPDLDVVYVPIGMGSGICGAIAARDAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 199 APNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDILTVSDEELIDCLKFYAARMKI 278
Cdd:PRK06110 194 GLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHN 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19075215 279 VVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAHFLS 322
Cdd:PRK06110 274 VAEGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVFARVLA 317
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
7-313 |
2.23e-46 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 158.96 E-value: 2.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 7 LPTYDDVASASERIKKFANKTPVLTSSTVNKEfVAEVFFKCENFQKMGAFKFRGALNALsqLNEAQRKAGVLTFSSGNHA 86
Cdd:PRK08246 4 MITRSDVRAAAQRIAPHIRRTPVLEADGAGFG-PAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 87 QAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMY-DRYKDDREKmAKEISEREGLTIIPPYDHPHVLAGQGTAA 165
Cdd:PRK08246 81 LAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVgAEYADALEA-AQAFAAETGALLCHAYDQPEVLAGAGTLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 166 KELFEEVGPLDALFVCLGGGGLLSGSALAarhFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNY 245
Cdd:PRK08246 160 LEIEEQAPGVDTVLVAVGGGGLIAGIAAW---FEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 246 TFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAA--ARAMKEKlKNKRIGIIISGGNVD 313
Cdd:PRK08246 237 AFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAAllSGAYVPA-PGERVAVVLCGANTD 305
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
12-323 |
8.11e-40 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 142.84 E-value: 8.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 12 DVASASERIKKFANKTPVLTSSTVNkefvaeVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIAL 91
Cdd:PRK08813 25 DVLAAQARLRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 92 SAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEE 171
Cdd:PRK08813 99 SAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 172 vGPlDALFVCLGGGGLLSGSALAARhfAPNCEVYGVEPEaGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIK 251
Cdd:PRK08813 179 -AP-DVVIVPIGGGGLASGVALALK--SQGVRVVGAQVE-GVDSMARAIRGDLREIAPVATLADGVKVKIPGFLTRRLCS 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075215 252 EKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARamkeKLKNKRIGIIISGGNVDIERYAHFLSQ 323
Cdd:PRK08813 254 SLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAAGR----RVSGKRKCAVVSGGNIDATVLATLLSE 321
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
26-323 |
3.44e-25 |
|
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: 102.76 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 26 KTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSS--GNHAQAIALSAKILGIPAKII 103
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECVHVVCSsgGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 104 MPLDAPEAKVAATKGYGGQVI-MYDRYKDDREKMAKEISERE-GLTIIPPYDHPHVLAGQGTAAKELFEEVG---PLDAL 178
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVvHGKVWWEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQsqeKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 179 fVCLG--GGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDD 256
Cdd:cd06448 161 -VCSVggGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075215 257 ILTVSDEELID-CLKFyAARMKIVVEPTGCLSFAAA-------RAMKEKLKNKRIGIII--SGGNVDIERYAHFLSQ 323
Cdd:cd06448 240 SEVVSDRDAVQaCLRF-ADDERILVEPACGAALAVVysgkildLQLEVLLTPLDNVVVVvcGGSNITLEQLKEYKKQ 315
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
27-297 |
4.46e-23 |
|
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: 97.28 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 27 TPVLTSSTVNKE-FVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAgVLTFSSGNHAQAIALSAKILGIPAKIIMP 105
Cdd:cd01563 23 TPLVRAPRLGERlGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKA-VACASTGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 106 LDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIpPYDHPHVLAGQGTAAKELFEEVG---PlDALFVCL 182
Cdd:cd01563 102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLS-NSLNPYRLEGQKTIAFEIAEQLGwevP-DYVVVPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 183 GGGGLLSGSALAARHFA--------PncEVYGVEPEAGNDGQQSFRKG--SIVHIDTPKTIADGAQtqhLGN-----YTF 247
Cdd:cd01563 180 GNGGNITAIWKGFKELKelglidrlP--RMVGVQAEGAAPIVRAFKEGkdDIEPVENPETIATAIR---IGNpasgpKAL 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19075215 248 SIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEK 297
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREE 304
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
26-317 |
1.18e-18 |
|
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: 84.49 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 26 KTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRgalNALSQLNEAQRKaGVLTF-------SSGNHAQAIALSAKILGI 98
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDR---IALYMIEDAEKR-GLLKPgttiiepTSGNTGIGLAMVAAAKGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 99 PAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDD----REKMAKEISEREGLTIIP-PYDHP-HVLAGQGTAAKELFEEV 172
Cdd:cd01561 78 RFIIVMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLnQFENPaNPEAHYETTAPEIWEQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 173 -GPLDALFV----------ClggggllsgsalaARHF---APNCEVYGVEPEagndgqqsfrkGSIVHIDTPKTiadGAQ 238
Cdd:cd01561 158 dGKVDAFVAgvgtggtitgV-------------ARYLkekNPNVRIVGVDPV-----------GSVLFSGGPPG---PHK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 239 TQHLGNytfSII-----KEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKL-KNKRIGIII-SGGn 311
Cdd:cd01561 211 IEGIGA---GFIpenldRSLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLgPGKTIVTILpDSG- 286
|
....*.
gi 19075215 312 vdiERY 317
Cdd:cd01561 287 ---ERY 289
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
27-297 |
1.52e-17 |
|
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: 82.56 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 27 TPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAgVLTFSSGNHAQAIALSAKILGIPAKIIMPL 106
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKT-IVCASSGNGSAALAAYAARAGIEVFVFVPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 107 D-APEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYdHPHVLAGQGTAAKELFEEVGPL-DALFVclgg 184
Cdd:COG0498 146 GkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLGRVpDWVVV---- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 185 ggllsgsalaarhfaP-------------NCE------------VYGVEPEAGNDGQQSFRKG-SIVHIDTPKTIADGAQ 238
Cdd:COG0498 221 ---------------PtgnggnilagykaFKElkelglidrlprLIAVQATGCNPILTAFETGrDEYEPERPETIAPSMD 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075215 239 TQHLGNYT--FSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEK 297
Cdd:COG0498 286 IGNPSNGEraLFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREE 346
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
42-180 |
1.93e-13 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 69.86 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 42 EVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTfSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGG 121
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVID-SSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGA 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075215 122 QV--IMYDRYKDDREkmAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGPLDALFV 180
Cdd:PRK08329 152 ELhfVEGDRMEVHEE--AVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFV 210
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
18-297 |
1.56e-12 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 67.02 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 18 ERIKKF--ANKTPVLTSSTVNKEFVA-----------EVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAgVLTFSSGN 84
Cdd:TIGR00260 2 WRYREFlpVTEKDLVDLGEGVTPLFRapalaanvgikNLYVKELGHNPTLSFKDRGMAVALTKALELGNDT-VLCASTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 85 HAQAIALSAKILGIPAKIIMPLDAPEA-KVAATKGYGGQVIMYDRYKDDREKMAKEISE-REGLTIIPPYDHPHVLAGQG 162
Cdd:TIGR00260 81 TGAAAAAYAGKAGLKVVVLYPAGKISLgKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEdKPALGLNSANSIPYRLEGQK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 163 TAAKELFEEVG-----------PLDALFVCLGGGGLLSGSALAARhfAPncEVYGVEPEAGNDGQQSFRK-GSIVHIDTP 230
Cdd:TIGR00260 161 TYAFEAVEQLGweapdkvvvpvPNSGNFGAIWKGFKEKKMLGLDS--LP--VKRGIQAEGAADIVRAFLEgGQWEPIETP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075215 231 KTIADGAQTQHLGNYTFS--IIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEK 297
Cdd:TIGR00260 237 ETLSTAMDIGNPANWPRAleAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEK 305
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
27-174 |
8.49e-12 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 65.60 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 27 TPVLTSSTVNKEFVAeVFFKCENFQKMGAFKFRGALNALSQ-LNEAQRkaGVLTFSSGNHAQAIALSAKILGIPAKIIMP 105
Cdd:PRK05638 67 TPLIRARISEKLGEN-VYIKDETRNPTGSFRDRLATVAVSYgLPYAAN--GFIVASDGNAAASVAAYSARAGKEAFVVVP 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075215 106 LDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGP 174
Cdd:PRK05638 144 RKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINP 212
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
27-173 |
5.05e-11 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 63.10 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 27 TPVLTSSTVNKEF-VAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTfSSGNHAQAIALSAKILGIPAKIIMP 105
Cdd:PRK08197 80 TPLLPLPRLGKALgIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMP-TNGNAGAAWAAYAARAGIRATIFMP 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075215 106 LDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVG 173
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLG 226
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
42-300 |
5.16e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 62.83 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 42 EVFFKCENFQKMGAFKFRGALNALSQLNEaQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGG 121
Cdd:PRK06450 66 NIWFKLDFLNPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 122 QVImydRYKDDREKMAKEiSEREGLTIIPPYDHPHVLAGQGTAAKELFEEVG--PLDALFVCLGGGGLLSGSALAARHFA 199
Cdd:PRK06450 145 EVV---RVRGSREDVAKA-AENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDwkIPNYVFIPVSAGTLLLGVYSGFKHLL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 200 PNCE------VYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQH--LGNYTFSIIKEkVDDILTVSDEELIDCLKf 271
Cdd:PRK06450 221 DSGVisempkIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADALVSTRpfLLDYMVKALSE-YGECIVVSDNEIVEAWK- 298
|
250 260
....*....|....*....|....*....
gi 19075215 272 YAARMKIVVEPTGCLSFAAARamKEKLKN 300
Cdd:PRK06450 299 ELAKKGLLVEYSSATVYAAYK--KYSVND 325
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
27-317 |
5.24e-09 |
|
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: 56.21 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 27 TPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRgalNALSQLNEAQRKaGVLT-------FSSGNHAQAIALSAKILGIP 99
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDR---IALSMIEDAEKR-GLLKpggtiveATSGNTGIGLAMVAAAKGYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 100 AKIIMPLDAPEAKVAATKGYGGQVIMYDRYK--DDREKMAKEISEREGLTIIP--------PYDHPHvlagqgTAAKELF 169
Cdd:COG0031 90 LILVMPETMSKERRALLRAYGAEVVLTPGAEgmKGAIDKAEELAAETPGAFWPnqfenpanPEAHYE------TTGPEIW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 170 EEV-GPLDALFVClggggllsgsalaaRHFAPNCEVYGVEPEagndgqqsfrkGSIVHidtPKTIADGAQTQHLG----- 243
Cdd:COG0031 164 EQTdGKVDAFVAGvgtggtitgvgrylKERNPDIKIVAVEPE-----------GSPLL---SGGEPGPHKIEGIGagfvp 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075215 244 -NYTFSIIkekvDDILTVSDEELIDCLKFYAARMKIVVEP-TGCLSFAAARAMKEKLKNKRIGIII--SGgnvdiERY 317
Cdd:COG0031 230 kILDPSLI----DEVITVSDEEAFAMARRLAREEGILVGIsSGAAVAAALRLAKRLGPGKTIVTILpdSG-----ERY 298
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
12-180 |
5.76e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 50.47 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 12 DVASASEriKKFANKTPVLTSSTVNKEF-VAEVFFKCENFQKMGAFKFRGALNALSQLNEaQRKAGVLTFSSGNHAQAIA 90
Cdd:PRK06381 3 EELSSSE--EKPPGGTPLLRARKLEEELgLRKIYLKFEGANPTGTQKDRIAEAHVRRAMR-LGYSGITVGTCGNYGASIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 91 LSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLtiippYD------HPHV-LAGQGT 163
Cdd:PRK06381 80 YFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGI-----YDanpgsvNSVVdIEAYSA 154
|
170
....*....|....*...
gi 19075215 164 AAKELFEEVGPL-DALFV 180
Cdd:PRK06381 155 IAYEIYEALGDVpDAVAV 172
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
6-173 |
8.98e-07 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 50.20 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 6 VLPTY--DDVASAserikkFANKTPVLTSSTVNKEF--VAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKA----GV 77
Cdd:PLN02569 117 VLPEIddDDIVSL------FEGNSNLFWAERLGKEFlgMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAkpvvGV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 78 LTFSSGNHAQAIALSAKILGIPAKIIMPLDAPE-AKVAATKGYGGQVIMYDRYKDDREKMAKEISERegltiIPPYD--- 153
Cdd:PLN02569 191 GCASTGDTSAALSAYCAAAGIPSIVFLPADKISiAQLVQPIANGALVLSIDTDFDGCMRLIREVTAE-----LPIYLans 265
|
170 180
....*....|....*....|.
gi 19075215 154 -HPHVLAGQGTAAKELFEEVG 173
Cdd:PLN02569 266 lNSLRLEGQKTAAIEILQQFD 286
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
20-124 |
4.42e-03 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 38.32 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075215 20 IKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQ------------LNEAqrkagvltfSSGNHAQ 87
Cdd:PRK11761 6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQaekrgeikpgdtLIEA---------TSGNTGI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 19075215 88 AIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVI 124
Cdd:PRK11761 77 ALAMIAAIKGYRMKLIMPENMSQERRAAMRAYGAELI 113
|
|
| |
