|
Name |
Accession |
Description |
Interval |
E-value |
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
1-323 |
1.07e-168 |
|
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: 474.91 E-value: 1.07e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 1 MIVFQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHA 80
Cdd:COG1171 5 MPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 81 QGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGL 160
Cdd:COG1171 85 QGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 161 EILQQLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLT 240
Cdd:COG1171 165 EILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 241 FELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKEKKVVSVLSGGNVDVNFISRIIEHGMV 320
Cdd:COG1171 245 FEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEILERGLV 324
|
...
gi 446557391 321 EAG 323
Cdd:COG1171 325 GEG 327
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
21-400 |
3.72e-166 |
|
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: 470.77 E-value: 3.72e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPK 100
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 101 GAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQQLEDVEAVICPIGGGG 180
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 181 LIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELVQRYVDDVFCVDEMEIA 260
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 261 RTMLMLLERNKLLVEGSGASSLASLLYHKVPIKEKKVVSVLSGGNVDVNFISRIIEHGMVEAGRFIHIATMIKDKPGYLH 340
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPGALY 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 341 HLLEIVTNFEANVLNIHLERIGTKVFPGYAQLHLSLETKDRNHIEEILSGLKKKGYVVEV 400
Cdd:TIGR01127 321 HLLESIAEARANIVKIDHDRLSKEIPPGFAMVEITLETRGKEHLDEILKILRDMGYNFYV 380
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
4-307 |
3.59e-163 |
|
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: 460.03 E-value: 3.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 4 FQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGV 83
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 84 AYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEIL 163
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 164 QQLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFEL 243
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557391 244 VQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKEKKVVSVLSGGNVD 307
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
1-402 |
1.24e-141 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 409.28 E-value: 1.24e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 1 MIVFQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHA 80
Cdd:PRK07334 4 MVTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 81 QGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGL 160
Cdd:PRK07334 84 QGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 161 EILQQLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLeeKKVITVESTPTMADGIAVKRPGDLT 240
Cdd:PRK07334 164 EMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAI--KGVALPCGGSTIAEGIAVKQPGQLT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 241 FELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKEKKVVSVLSGGNVDVNFISRIIEHGMV 320
Cdd:PRK07334 242 LEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNIDTRLLANVLLRGLV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 321 EAGRFIHIATMIKDKPGYLHHLLEIVTNFEANVLNIHLERIGTKVFPGYAQLHLSLETKDRNHIEEILSGLKKKGYVVEV 400
Cdd:PRK07334 322 RAGRLARLRVDIRDRPGALARVTALIGEAGANIIEVSHQRLFTDLPAKGAELELVIETRDAAHLQEVIAALRAAGFEARL 401
|
..
gi 446557391 401 ID 402
Cdd:PRK07334 402 VE 403
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
6-320 |
1.03e-131 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 381.39 E-value: 1.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 6 DIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAY 85
Cdd:PRK08638 13 DIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 86 SSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQQ 165
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILED 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 166 LEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELVQ 245
Cdd:PRK08638 173 LWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVR 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557391 246 RYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVP--IKEKKVVSVLSGGNVDVNFISRIIEHGMV 320
Cdd:PRK08638 253 ELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDqyIQNKKVVAIISGGNVDLSRVSQITGHVVA 329
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
1-326 |
4.73e-114 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 339.48 E-value: 4.73e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 1 MIVFQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHA 80
Cdd:PRK08639 6 TVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 81 QGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGA-HVE--LQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGT 157
Cdd:PRK08639 86 QGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGeFVEivLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 158 VGLEILQQLE---DVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVK 234
Cdd:PRK08639 166 VAVEILEQLEkegSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 235 RPGDLTFELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKEKKVVSVLSGGNVDVNFISRI 314
Cdd:PRK08639 246 RVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKTVVCVISGGNNDIERMPEI 325
|
330
....*....|....*
gi 446557391 315 IEHGMVEAGR---FI 326
Cdd:PRK08639 326 KERSLIYEGLkhyFI 340
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
21-310 |
2.23e-102 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 312.46 E-value: 2.23e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPK 100
Cdd:PRK09224 21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMPV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 101 GAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQQLED-VEAVICPIGGG 179
Cdd:PRK09224 101 TTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAVFVPVGGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 180 GLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELVQRYVDDVFCVDEMEI 259
Cdd:PRK09224 181 GLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDTDEI 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446557391 260 ARTMLMLLERNKLLVEGSGASSLASLL-Y---HKvpIKEKKVVSVLSGGNvdVNF 310
Cdd:PRK09224 261 CAAIKDVFEDTRSIAEPAGALALAGLKkYvaqHG--IEGETLVAILSGAN--MNF 311
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
21-399 |
2.91e-98 |
|
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: 301.65 E-value: 2.91e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPK 100
Cdd:TIGR01124 18 TPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGLKALIVMPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 101 GAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQQL-EDVEAVICPIGGG 179
Cdd:TIGR01124 98 TTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVaNPLDAVFVPVGGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 180 GLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELVQRYVDDVFCVDEMEI 259
Cdd:TIGR01124 178 GLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDIVTVDTDEV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 260 ARTMLMLLERNKLLVEGSGASSLASLLYH--KVPIKEKKVVSVLSGGNVDVNFISRIIEHGMVEAGRFIHIATMIKDKPG 337
Cdd:TIGR01124 258 CAAIKDLFEDTRAVAEPAGALALAGLKKYvaLHGIRGQTLVAILSGANMNFHRLRYVSERCELGEQREALLAVTIPEQPG 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557391 338 YLHHLLEIVTNFEANVLNIHL-ERIGTKVFPGyaqlhlsLETKDRNHIEEILSGLKKKGYVVE 399
Cdd:TIGR01124 338 SFLKFCELLGNRNITEFNYRYaDRKDAHIFVG-------VQLSNPQERQEILARLNDGGYSVV 393
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
5-315 |
4.14e-97 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 292.64 E-value: 4.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 5 QDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVA 84
Cdd:PRK07476 4 ADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 85 YSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQ 164
Cdd:PRK07476 84 YAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 165 QLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMAD----GIAVKrpGDLT 240
Cdd:PRK07476 164 ALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslggGIGLD--NRYT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557391 241 FELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKEKKVVSVLSGGNVDVNFISRII 315
Cdd:PRK07476 242 FAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELHRRII 316
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
2-309 |
1.29e-96 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 291.54 E-value: 1.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 2 IVFQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQ 81
Cdd:PRK07048 6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 82 GVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLE 161
Cdd:PRK07048 86 AIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 162 ILQQLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTF 241
Cdd:PRK07048 166 LFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTF 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557391 242 ELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKEKKVVSVLSGGNVDVN 309
Cdd:PRK07048 246 PIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLA 313
|
|
| COG2061 |
COG2061 |
Uncharacterized conserved protein, contains ACT domain [General function prediction only]; |
6-402 |
2.27e-96 |
|
Uncharacterized conserved protein, contains ACT domain [General function prediction only];
Pssm-ID: 441664 [Multi-domain] Cd Length: 401 Bit Score: 293.49 E-value: 2.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 6 DIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAY 85
Cdd:COG2061 5 LDEEAAAAALAVVVVTTPLLLSSSSSLSVGLVVLLKEENLQTTGSFKRRGAYKLIALLLEEEEKGGVAAAAAGNAAQAAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 86 SSNMLSIPCTIVMPKGAPLSKVLATKKYG-AHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQ 164
Cdd:COG2061 85 AAAALGGISAIVVMPPPPPLPKVAATRGGgAVVVVVGGDDDAAAAAAAALQEEEGGFFHHPDDDDDVIAGGGGGGLEILE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 165 QLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELV 244
Cdd:COG2061 165 LLPDVVVVVVGGGGGGGGGGAAAAAKAKRPPIVIVGVQAEAAAAAPSSLAAGIEVVPGGGTTIADGIAVVKPGGLTFIII 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 245 QRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLyHKVPIKEKKVVSVLSGGNVDVNFISRIIEHGMVEAGR 324
Cdd:COG2061 245 RKVVDDVVVVVEEEIAAALLLLLERKKKVVEGAAAAAAAAAL-KKKPLRGKKVVVVLSGGNIDDLLLLRIIIKGLLAAGR 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557391 325 FIHIATMIKDKPGYLHHLLEIVTNFEANVLNIHLERIGTKVFPGYAQLHLSLETKDRNHIEEILSGLKKKGYVVEVID 402
Cdd:COG2061 324 RLVLLVVLPDRPGQLLRVLQPIAELGANIISVVHERENSKTPRGEVEVEVVLETRGEEHLEEIIAALREAGYNVRRVG 401
|
|
| PLN02970 |
PLN02970 |
serine racemase |
4-307 |
2.02e-95 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 288.50 E-value: 2.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 4 FQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGV 83
Cdd:PLN02970 11 LSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 84 AYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEIL 163
Cdd:PLN02970 91 ALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 164 QQLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRpGDLTFEL 243
Cdd:PLN02970 171 EQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRASL-GDLTWPV 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557391 244 VQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKE-----KKVVSVLSGGNVD 307
Cdd:PLN02970 250 VRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPawkgcKNVGIVLSGGNVD 318
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
4-306 |
4.14e-94 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 285.05 E-value: 4.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 4 FQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGV 83
Cdd:PRK06815 4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 84 AYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEIL 163
Cdd:PRK06815 84 ALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 164 QQLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIA--VKrPGDLTF 241
Cdd:PRK06815 164 EQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAggVE-PGAITF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557391 242 ELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKEKKVVSVLSGGNV 306
Cdd:PRK06815 243 PLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNI 307
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
21-303 |
3.25e-91 |
|
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: 276.88 E-value: 3.25e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPK 100
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 101 GAPLSKVLATKKYGAHVELQGDVFDDALAYALDL-KEKTGAKFVHPFDDEAVIAGQGTVGLEILQQL-EDVEAVICPIGG 178
Cdd:pfam00291 88 DAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELaAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLgGDPDAVVVPVGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 179 GGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKR-PGDLTFELVQRYVDDVFCVDEM 257
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDePGALALDLLDEYVGEVVTVSDE 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446557391 258 EIARTMLMLLERNKLLVEGSGASSLASLLYHKVP-IKEKK-VVSVLSG 303
Cdd:pfam00291 248 EALEAMRLLARREGIVVEPSSAAALAALKLALAGeLKGGDrVVVVLTG 295
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
21-398 |
1.71e-84 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 267.05 E-value: 1.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPK 100
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVMPR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 101 GAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEIL-QQLEDVEAVICPIGGG 179
Cdd:PRK12483 118 TTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILrQHPGPLDAIFVPVGGG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 180 GLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELVQRYVDDVFCVDEMEI 259
Cdd:PRK12483 198 GLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVDEVVTVSTDEL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 260 ARTMLMLLERNKLLVEGSGASSLASLLYH--KVPIKEKKVVSVLSGGNVDVNFISRIIEHGMVEAGRFIHIATMIKDKPG 337
Cdd:PRK12483 278 CAAIKDIYDDTRSITEPAGALAVAGIKKYaeREGIEGQTLVAIDSGANVNFDRLRHVAERAELGEQREAIIAVTIPEQPG 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557391 338 YLHHLLEIVTNFEANVLNIhlerigtKVFPG-YAQLHLSLETKDRNH-IEEILSGLKKKGYVV 398
Cdd:PRK12483 358 SFKAFCAALGKRQITEFNY-------RYADArEAHLFVGVQTHPRHDpRAQLLASLRAQGFPV 413
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
6-315 |
7.86e-79 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 246.85 E-value: 7.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 6 DIIAAYEKMKGIVHMTPLDYSSTFSelsqneVYLKLENLQKTGSFKVRGSYNKM-VSLEKGDlENGVVAASAGNHAQGVA 84
Cdd:PRK08813 25 DVLAAQARLRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALlAGLERGD-ERPVICASAGNHAQGVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 85 YSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQ 164
Cdd:PRK08813 98 WSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 165 QLEDVeaVICPIGGGGLIAGVAMAIKEQkpSVKIYGVQTLACPGMKQSLeEKKVITVESTPTMADGIAVKRPGDLTFELV 244
Cdd:PRK08813 178 HAPDV--VIVPIGGGGLASGVALALKSQ--GVRVVGAQVEGVDSMARAI-RGDLREIAPVATLADGVKVKIPGFLTRRLC 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446557391 245 QRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASllYHKVPIKEKkvVSVLSGGNVDVNFISRII 315
Cdd:PRK08813 253 SSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAA--GRRVSGKRK--CAVVSGGNIDATVLATLL 319
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
1-307 |
1.40e-75 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 237.16 E-value: 1.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 1 MIVFQDIIAAYEKMKGIVHMTPLDYSSTFSeLSQNEVYLKLENLQKTGSFKVRGSYNKMvsLEKGDLENGVVAASAGNHA 80
Cdd:PRK08246 4 MITRSDVRAAAQRIAPHIRRTPVLEADGAG-FGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 81 QGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGL 160
Cdd:PRK08246 81 LAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 161 EILQQLEDVEAVICPIGGGGLIAGVAMAIkeqKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLT 240
Cdd:PRK08246 161 EIEEQAPGVDTVLVAVGGGGLIAGIAAWF---EGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557391 241 FELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLY-HKVPIKEKKVVSVLSGGNVD 307
Cdd:PRK08246 238 FALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSgAYVPAPGERVAVVLCGANTD 305
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
21-304 |
3.25e-75 |
|
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: 233.95 E-value: 3.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEK-GDLENG-VVAASAGNHAQGVAYSSNMLSIPCTIVM 98
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEeGKLPKGvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 99 PKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDL-KEKTGAKFVHPFDDEAVIAGQGTVGLEILQQLEDVE--AVICP 175
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELaEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLGGQKpdAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 176 IGGGGLIAGVAMAIKEQKPSVKIYGVQTlacpgmkqsleekkvitvestptmadgiavkrpgdltfelvqryvdDVFCVD 255
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446557391 256 EMEIARTMLMLLERNKLLVEGSGASSLASLL-YHKVPIKEKKVVSVLSGG 304
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALkLAKKLGKGKTVVVILTGG 244
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
4-316 |
4.24e-75 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 236.98 E-value: 4.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 4 FQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSL-EKGDLENGVVAASAGNHAQG 82
Cdd:PRK06608 7 PQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELkEQGKLPDKIVAYSTGNHGQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 83 VAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQgDVFDDALAYALdLKEKTGAKFVHPFDDEAVIAGQGTVGLEI 162
Cdd:PRK06608 87 VAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILT-NTRQEAEEKAK-EDEEQGFYYIHPSDSDSTIAGAGTLCYEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 163 LQQL-EDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTP-TMADGIAVKRPGDLT 240
Cdd:PRK06608 165 LQQLgFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSPnTIADGLKTLSVSART 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557391 241 FELVQRyVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLL-YHKVPIKEKKVVSVLSGGNVDVNFISRIIE 316
Cdd:PRK06608 245 FEYLKK-LDDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVnWLKTQSKPQKLLVILSGGNIDPILYNELWK 320
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
2-315 |
6.90e-72 |
|
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: 227.81 E-value: 6.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 2 IVFQDIIAAYEKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQ 81
Cdd:TIGR02991 1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 82 GVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLE 161
Cdd:TIGR02991 81 ALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 162 ILQQLEDVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMAD--GIAVKRPGDL 239
Cdd:TIGR02991 161 VVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557391 240 TFELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLLYHKVPIKeKKVVSVLSGGNVDVNFISRII 315
Cdd:TIGR02991 241 TFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNP-GPCAVIVSGRNIDMDLHKRII 315
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
21-346 |
2.20e-69 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 229.42 E-value: 2.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPK 100
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMPV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 101 GAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQQLED-VEAVICPIGGG 179
Cdd:PLN02550 190 TTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGpLHAIFVPVGGG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 180 GLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELVQRYVDDVFCVDEMEI 259
Cdd:PLN02550 270 GLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSRDAI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 260 ARTMLMLLERNKLLVEGSGASSLA-SLLYHK-VPIKEKKVVSVLSGGNVDVNFISRIIEHGMVEAGRFIHIATMIKDKPG 337
Cdd:PLN02550 350 CASIKDMFEEKRSILEPAGALALAgAEAYCKyYGLKDENVVAITSGANMNFDRLRIVTELADVGRQQEAVLATFMPEEPG 429
|
....*....
gi 446557391 338 YLHHLLEIV 346
Cdd:PLN02550 430 SFKRFCELV 438
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
36-315 |
1.97e-52 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 177.49 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 36 EVYLKLENLQKTGSFKVRGSYNKMVSL-EKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYG 114
Cdd:PRK06110 37 EVWVKHENHTPTGAFKVRGGLVYFDRLaRRGPRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 115 AHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAViAGQGTVGLEILQQLEDVEAVICPIGGGGLIAGVAMAIKEQKP 194
Cdd:PRK06110 117 AELIEHGEDFQAAREEAARLAAERGLHMVPSFHPDLV-RGVATYALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 195 SVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELVQRYVDDVFCVDEMEIARTMLMLLERNKLLV 274
Cdd:PRK06110 196 KTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVA 275
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446557391 275 EGSGASSLASLLYHKVPIKEKKVVSVLSGGNVDVNFISRII 315
Cdd:PRK06110 276 EGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVFARVL 316
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
21-305 |
1.61e-47 |
|
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: 164.39 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRG--SYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVM 98
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGigHLCQKSAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 99 PKGAPLSKVLATKKYGAHVELQGDV-FDDALAYALDLKEK-TGAKFVHPFDDEAVIAGQGTVGLEILQQLED---VEAVI 173
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVwWEADNYLREELAENdPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekVDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 174 CPIGGGGLIAGVAMAIKE-QKPSVKIYGVQTLACPGMKQSLEEKKVITVESTPTMADGIAVKRPGDLTFELVQRYVDDVF 252
Cdd:cd06448 162 CSVGGGGLLNGIVQGLERnGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557391 253 CVDEMEIARTMLMLLERNKLLVEGSGASSLAsLLYHKV---------PIKEKKVVSVLSGGN 305
Cdd:cd06448 242 VVSDRDAVQACLRFADDERILVEPACGAALA-VVYSGKildlqlevlLTPLDNVVVVVCGGS 302
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
20-303 |
1.85e-35 |
|
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: 132.72 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 20 MTPLDYSSTFSE-LSQNEVYLKLENLQKTGSFKVRGSYNKM-VSLEKGdlENGVVAASAGNHAQGVAYSSNMLSIPCTIV 97
Cdd:cd01563 22 NTPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDRGMTVAVsKAKELG--VKAVACASTGNTSASLAAYAARAGIKCVVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 98 MPKGAPLSKVLATKKYGAHV-ELQGDvFDDALAYALDLKEKTGAKFVH---PFddeaVIAGQGTVGLEILQQL--EDVEA 171
Cdd:cd01563 100 LPAGKALGKLAQALAYGATVlAVEGN-FDDALRLVRELAEENWIYLSNslnPY----RLEGQKTIAFEIAEQLgwEVPDY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 172 VICPIGGGGLIAGVAMAIKEQKPS------VKIYGVQTLACPGMKQSLEEKK--VITVESTPTMADGIAVKRP--GDLTF 241
Cdd:cd01563 175 VVVPVGNGGNITAIWKGFKELKELglidrlPRMVGVQAEGAAPIVRAFKEGKddIEPVENPETIATAIRIGNPasGPKAL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557391 242 ELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASL--LYHKVPIKEK-KVVSVLSG 303
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLkkLREEGIIDKGeRVVVVLTG 319
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
20-303 |
1.28e-33 |
|
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: 129.16 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 20 MTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYnKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMP 99
Cdd:COG0498 66 GTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQ-VAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 100 KG-APLSKVLATKKYGAHV-ELQGDvFDDALAYALDLKEKTGAKFVH---PFddeaVIAGQGTVGLEILQQLEDV-EAVI 173
Cdd:COG0498 145 EGkVSPGQLAQMLTYGAHViAVDGN-FDDAQRLVKELAADEGLYAVNsinPA----RLEGQKTYAFEIAEQLGRVpDWVV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 174 CPIGGGGLIAGVAMAIKEQK--------PsvKIYGVQTLACPGMKQSLEE-KKVITVESTPTMADGIAVKRPGDltFELV 244
Cdd:COG0498 220 VPTGNGGNILAGYKAFKELKelglidrlP--RLIAVQATGCNPILTAFETgRDEYEPERPETIAPSMDIGNPSN--GERA 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557391 245 QRYVD----DVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASL--LYHKVPIKEK-KVVSVLSG 303
Cdd:COG0498 296 LFALResggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLrkLREEGEIDPDePVVVLSTG 361
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
21-301 |
3.76e-30 |
|
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: 117.61 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNkMVS--LEKGDLENG--VVAASAGNHAQGVAYSSNMLSIPCTI 96
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALY-MIEdaEKRGLLKPGttIIEPTSGNTGIGLAMVAAAKGYRFII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 97 VMPKGAPLSKVLATKKYGAHVEL----QGDVFDDALAYALDLKEKT-GAKFVHPFDDEA-VIAGQGTVGLEILQQLED-V 169
Cdd:cd01561 82 VMPETMSEEKRKLLRALGAEVILtpeaEADGMKGAIAKARELAAETpNAFWLNQFENPAnPEAHYETTAPEIWEQLDGkV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 170 EAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQsleekkvitVESTPTMADGI-AVKRPGDLTFELvqryV 248
Cdd:cd01561 162 DAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSG---------GPPGPHKIEGIgAGFIPENLDRSL----I 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446557391 249 DDVFCVDEMEIARTMLMLLERNKLLVEGS-GASSLASLLYHKVPIKEKKVVSVL 301
Cdd:cd01561 229 DEVVRVSDEEAFAMARRLAREEGLLVGGSsGAAVAAALKLAKRLGPGKTIVTIL 282
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
1-301 |
1.03e-24 |
|
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: 102.82 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 1 MIVFQDIIAAyekmkgiVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNkMVS--LEKGDLENG--VVAASA 76
Cdd:COG0031 1 MRIYDSILEL-------IGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALS-MIEdaEKRGLLKPGgtIVEATS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 77 GNHAQGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVEL--QGDVFDDALAYALDLKEKT-GAKFVHPFDDEA-VI 152
Cdd:COG0031 73 GNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLtpGAEGMKGAIDKAEELAAETpGAFWPNQFENPAnPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 153 AGQGTVGLEILQQLE-DVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSLEEKKVItvestptmaDGI 231
Cdd:COG0031 153 AHYETTGPEIWEQTDgKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKI---------EGI 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557391 232 AVKR-PGDLTFELvqryVDDVFCVDEMEIARTMLMLLERNKLLVEGS-GASSLASLLYHKVPIKEKKVVSVL 301
Cdd:COG0031 224 GAGFvPKILDPSL----IDEVITVSDEEAFAMARRLAREEGILVGISsGAAVAAALRLAKRLGPGKTIVTIL 291
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
21-303 |
2.09e-19 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 89.49 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNeVYLKLENLQKTGSFKVRGSyNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPK 100
Cdd:PRK05638 67 TPLIRARISEKLGEN-VYIKDETRNPTGSFRDRLA-TVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 101 GAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQQLeDVEAVICPIGGGG 180
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEI-NPTHVIVPTGSGS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 181 LIAGVAMAIKE--------QKPsvKIYGVQTLACPGMKQSLEEkkvITVESTPTMADGIAVKRPgdLTFELVQRYVDD-- 250
Cdd:PRK05638 224 YLYSIYKGFKElleigvieEIP--KLIAVQTERCNPIASEILG---NKTKCNETKALGLYVKNP--VMKEYVSEAIKEsg 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557391 251 --VFCVDEMEIARTMlMLLERNKLLVEGSGASSLASLL-YHKVPIKEK--KVVSVLSG 303
Cdd:PRK05638 297 gtAVVVNEEEIMAGE-KLLAKEGIFAELSSAVVMPALLkLGEEGYIEKgdKVVLVVTG 353
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
1-277 |
3.03e-17 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 81.83 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 1 MIVFQDIIAAyekmkgIVHmTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNkMV--SLEKGDLENG--VVAASA 76
Cdd:PRK10717 1 MKIFEDVSDT------IGN-TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALN-IIwdAEKRGLLKPGgtIVEGTA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 77 GNHAQGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAH-VELQGDVFDD---------ALAYALDLKEKTGAKFVHPF 146
Cdd:PRK10717 73 GNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAElVLVPAAPYANpnnyvkgagRLAEELVASEPNGAIWANQF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 147 DD----EAVIAgqgTVGLEILQQLE-DVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYgvqtLACPgMKQSL-------E 214
Cdd:PRK10717 153 DNpanrEAHYE---TTGPEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIV----LADP-TGSALysyyktgE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557391 215 EKKvitveSTPTMADGIAVKRpgdLTFELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGS 277
Cdd:PRK10717 225 LKA-----EGSSITEGIGQGR---ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGS 279
|
|
| ACT_ThrD-II-like |
cd04886 |
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and ... |
328-400 |
4.36e-17 |
|
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: 75.27 E-value: 4.36e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557391 328 IATMIKDKPGYLHHLLEIVTNFEANVLNIHLERIGTKVFPGYAQLHLSLETKDRNHIEEILSGLKKKGYVVEV 400
Cdd:cd04886 1 LRVELPDRPGQLAKLLAVIAEAGANIIEVSHDRAFKTLPLGEVEVELTLETRGAEHIEEIIAALREAGYDVRR 73
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
20-285 |
2.25e-16 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 80.04 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 20 MTPL-DYSSTFSELSQNEVYLKLENLQKTGSFKVRGSyNKMVSLEKGDLENGVVAASAGNHAQGVA-YSSNMlSIPCTIV 97
Cdd:PRK08197 79 MTPLlPLPRLGKALGIGRLWVKDEGLNPTGSFKARGL-AVGVSRAKELGVKHLAMPTNGNAGAAWAaYAARA-GIRATIF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 98 MPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHPFDDEAVIAGQGTVGLEILQQL--EDVEAVICP 175
Cdd:PRK08197 157 MPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLgwRLPDVILYP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 176 IGGG-GLIaGVAMAIKEQKPSVKIYG-------VQTLACPGMKQSLEEKKvitVESTP-----TMADGIAVKRP-GD-LT 240
Cdd:PRK08197 237 TGGGvGLI-GIWKAFDELEALGWIGGkrprlvaVQAEGCAPIVKAWEEGK---EESEFwedahTVAFGIRVPKAlGDfLV 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446557391 241 FELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASL 285
Cdd:PRK08197 313 LDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAA 357
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
48-286 |
3.18e-16 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 79.54 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 48 GSFKVRG--------------------SYNKMVSLEKGDLENGVVAASA--GNHAQGVAYSSNMLSIPCTIVMPKGAPLS 105
Cdd:PRK08206 74 NAFKALGgayavarllaeklgldiselSFEELTSGEVREKLGDITFATAtdGNHGRGVAWAAQQLGQKAVIYMPKGSSEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 106 KVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHpfdDEA----------VIAGQGTVGLEILQQLEDVEA---- 171
Cdd:PRK08206 154 RVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVQ---DTAwegyeeiptwIMQGYGTMADEAVEQLKEMGVppth 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 172 VICPIGGGGLIAGV----AMAIKEQKPSVKIYGVQTLACpgMKQSLEEKKVITVE-STPTMADGIAVKRPGDLTFELVQR 246
Cdd:PRK08206 231 VFLQAGVGSLAGAVlgyfAEVYGEQRPHFVVVEPDQADC--LYQSAVDGKPVAVTgDMDTIMAGLACGEPNPLAWEILRN 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446557391 247 YVDDVFCVDEMEIARTMLML---LERNKLLVEG-SGASSLASLL 286
Cdd:PRK08206 309 CADAFISCPDEVAALGMRILanpLGGDPPIVSGeSGAVGLGALA 352
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
36-305 |
2.22e-14 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 73.71 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 36 EVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLeNGVVAASAGNHAQGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGA 115
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI-NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 116 HV-ELQGD---VFDDALAYAldlkEKTGAKFVHPFDDEAVIAGQGTVGLEILQQLEDVEAVICPIGGGGLIAGVAMAIKE 191
Cdd:PRK08329 152 ELhFVEGDrmeVHEEAVKFS----KRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIWKGFKE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 192 QKPSVKIYGVQTLACPGMK--QSLEEKKVitveSTPTMADGIAVKRPGDLTFELVQRYVDDVFC--VDEMEIaRTMLMLL 267
Cdd:PRK08329 228 LHEMGEISKMPKLVAVQAEgyESLCKRSK----SENKLADGIAIPEPPRKEEMLRALEESNGFCisVGEEET-RAALHWL 302
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446557391 268 ERNKLLVEGSGASSLASL--LYHKVPIKE-KKVVSVLSGGN 305
Cdd:PRK08329 303 RRMGFLVEPTSAVALAAYwkLLEEGLIEGgSKVLLPLSGSG 343
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
21-301 |
1.05e-11 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 65.75 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDL----ENGVVAASAGNHAQGVAYSSNMLSIPCTI 96
Cdd:PLN02556 60 TPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLitpgKTTLIEPTSGNMGISLAFMAAMKGYKMIL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 97 VMPKGAPLSKVLATKKYGAHVELQGDV--FDDALAYALDLKEKTGAKFV-HPFDDEA-VIAGQGTVGLEILQQ-LEDVEA 171
Cdd:PLN02556 140 TMPSYTSLERRVTMRAFGAELVLTDPTkgMGGTVKKAYELLESTPDAFMlQQFSNPAnTQVHFETTGPEIWEDtLGQVDI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 172 VICPIGGGGLIAGVAMAIKEQKPSVKIYGVQtlacPGMKQSLEEKKvitveSTPTMADGIAVK-RPGDLTFELVQRyVDD 250
Cdd:PLN02556 220 FVMGIGSGGTVSGVGKYLKSKNPNVKIYGVE----PAESNVLNGGK-----PGPHHITGNGVGfKPDILDMDVMEK-VLE 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446557391 251 VFCVDEMEIARTmlMLLERNKLLVEGSGASSLASLLYHKVPI-KEKKVVSVL 301
Cdd:PLN02556 290 VSSEDAVNMARE--LALKEGLMVGISSGANTVAALRLAKMPEnKGKLIVTVH 339
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
31-191 |
5.12e-11 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 63.19 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 31 ELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLeNGVVAASAGNHAQGVAYSSNMLSIPCTIVMPKGAPLSKVLAT 110
Cdd:PRK06381 27 ELGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY-SGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 111 KKYGAHV-ELQGDvFDDALAYALDLKEKTGAKFVHPFDDEAVIA--GQGTVGLEILQQLEDV-EAVICPIGGGGLIAGVA 186
Cdd:PRK06381 106 EKYGAEIiYVDGK-YEEAVERSRKFAKENGIYDANPGSVNSVVDieAYSAIAYEIYEALGDVpDAVAVPVGNGTTLAGIY 184
|
....*
gi 446557391 187 MAIKE 191
Cdd:PRK06381 185 HGFRR 189
|
|
| 2_3_DAP_am_ly |
TIGR03528 |
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ... |
55-288 |
1.50e-10 |
|
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.
Pssm-ID: 274631 Cd Length: 396 Bit Score: 62.43 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 55 SYNKMVSLEKGDLENGVVAASA--GNHAQGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYAL 132
Cdd:TIGR03528 98 SFEKLKSNEIREKLGDITFVTAtdGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGAECTITDLNYDDAVRLAW 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 133 DLKEKTGAKFVHpfdDEA----------VIAGQGTVGLEILQQLEDVEA-----VICPIGGGGLIAGV----AMAIKEQK 193
Cdd:TIGR03528 178 KMAQENGWVMVQ---DTAwegyekiptwIMQGYGTLALEALEQLKEQGVekpthVFLQAGVGSFAGAVqgyfASVYGEER 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 194 PSVKIYGVQTLACPGMKQSLEEKKVITVE-STPTMADGIAVKRPGDLTFELVQRYVDD-VFCVDEMEiARTMLML---LE 268
Cdd:TIGR03528 255 PITVIVEPDKADCIYRSAIADDGKPHFVTgDMATIMAGLACGEPNTIGWEILRDYASQfISCPDWVA-AKGMRILgnpLK 333
|
250 260
....*....|....*....|....
gi 446557391 269 RNKLLVEG-SGASS---LASLLYH 288
Cdd:TIGR03528 334 GDPRVISGeSGAVGtglLAAVMTH 357
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
12-301 |
3.70e-10 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 61.33 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 12 EKMKGIVHMTPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLE-KGDLENG---VVAASAGNHAQGVAYSS 87
Cdd:PLN03013 115 DNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEqKGFISPGksvLVEPTSGNTGIGLAFIA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 88 NMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDV--FDDALAYALD-LKEKTGAKFVHPFDDEAVIAGQ-GTVGLEIL 163
Cdd:PLN03013 195 ASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAkgMTGAVQKAEEiLKNTPDAYMLQQFDNPANPKIHyETTGPEIW 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 164 QQLE-DVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQtlacpgmkqsleekkvitvestPTMADGIAVKRPGDLTFE 242
Cdd:PLN03013 275 DDTKgKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVE----------------------PTESDILSGGKPGPHKIQ 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 243 ----------LVQRYVDDVFCVDEMEIARTMLMLLERNKLLVE-GSGASSLASLLYHKVPIKEKKVVSVL 301
Cdd:PLN03013 333 gigagfipknLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGiSSGAAAAAAIKVAKRPENAGKLIAVS 402
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
21-301 |
6.47e-10 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 59.94 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDL----ENGVVAASAGNHAQGVAYSSNMLSIPCTI 96
Cdd:PLN02565 16 TPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLikpgESVLIEPTSGNTGIGLAFMAAAKGYKLII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 97 VMPKGAPLSKVLATKKYGAHVELQGDV--FDDALAYALDLKEKTGAKFV-HPFDDEAVIAGQ-GTVGLEILQQLE-DVEA 171
Cdd:PLN02565 96 TMPASMSLERRIILLAFGAELVLTDPAkgMKGAVQKAEEILAKTPNSYIlQQFENPANPKIHyETTGPEIWKGTGgKVDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 172 VICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSleekkvitvESTPTMADGI-AVKRPGDLTFELvqryVDD 250
Cdd:PLN02565 176 FVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGG---------KPGPHKIQGIgAGFIPGVLDVDL----LDE 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446557391 251 VFCVDEMEIARTMLMLLERNKLLVE-GSGASSLASLLYHKVPIKEKKVVSVL 301
Cdd:PLN02565 243 VVQVSSDEAIETAKLLALKEGLLVGiSSGAAAAAAIKIAKRPENAGKLIVVI 294
|
|
| diampropi_NH3ly |
TIGR01747 |
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ... |
72-315 |
2.64e-09 |
|
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]
Pssm-ID: 130808 Cd Length: 376 Bit Score: 58.37 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 72 VAASAGNHAQGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYGAHVELQGDVFDDALAYALDLKEKTGAKFVHpfdDEA- 150
Cdd:TIGR01747 98 ATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQMAQQHGWVVVQ---DTAw 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 151 ---------VIAGQGTVGLEILQQLEDVEA-----VICPIGGGGLIAGV----AMAIKEQKPSVKIYGVQTLACPGMKQS 212
Cdd:TIGR01747 175 egyekiptwIMQGYATLADEAVEQLREMGSvtpthVLLQAGVGSMAGGVlgyfVDVYSENNPHSIVVEPDKADCLYQSAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 213 LEEKKVITVE-STPTMADGIAVKRPGDLTFELVQRYVDDVFCVDEMEIARTMLML---LERNKLLVEG-SGASS---LAS 284
Cdd:TIGR01747 255 KKDGDIVNVGgDMATIMAGLACGEPNPISWEILRNCTSQFISAQDSVAAKGMRVLgapYGGDPRIISGeSGAVGlglLAA 334
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446557391 285 LLYH--------KVPIKEKKVVSVLSG-GNVDVNFISRII 315
Cdd:TIGR01747 335 VMYHpqyqslmeKLQLDKDAVVLVISTeGDTDPDHYREIV 374
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
21-304 |
4.17e-09 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 57.32 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLE-KGDLENG---VVAASAGNHAQGVAYSSNMLSIPCTI 96
Cdd:PLN00011 18 TPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEdKGLITPGkstLIEATAGNTGIGLACIGAARGYKVIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 97 VMPKGAPLSKVLATKKYGAHVEL--QGDVFDDALAYALDLKEKTGA-----KFVHPFDDEAviaGQGTVGLEILQQLE-D 168
Cdd:PLN00011 98 VMPSTMSLERRIILRALGAEVHLtdQSIGLKGMLEKAEEILSKTPGgyipqQFENPANPEI---HYRTTGPEIWRDSAgK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 169 VEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQTLACPGMKQSleekkvitvESTPTMADGIAvkrPGDLTFELVQRYV 248
Cdd:PLN00011 175 VDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGG---------QPGPHLIQGIG---SGIIPFNLDLTIV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446557391 249 DDVFCVDEMEIARTMLMLLERNKLLVE-GSGASSLASLLYHKVPIKEKKVVSVL--SGG 304
Cdd:PLN00011 243 DEIIQVTGEEAIETAKLLALKEGLLVGiSSGAAAAAALKVAKRPENAGKLIVVIfpSGG 301
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
21-202 |
1.18e-07 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 52.95 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNkMV--SLEKGDLENG--VVAASAGNHAQGVAYSSNMLSIPCTI 96
Cdd:PRK11761 13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALS-MIvqAEKRGEIKPGdtLIEATSGNTGIALAMIAAIKGYRMKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 97 VMPKGAPLSKVLATKKYGAHVELQGDvfDDALAYALDLKEKTGAK--------FVHPfdDEAVIAGQGTvGLEILQQLE- 167
Cdd:PRK11761 92 IMPENMSQERRAAMRAYGAELILVPK--EQGMEGARDLALQMQAEgegkvldqFANP--DNPLAHYETT-GPEIWRQTEg 166
|
170 180 190
....*....|....*....|....*....|....*
gi 446557391 168 DVEAVICPIGGGGLIAGVAMAIKEQKPSVKIYGVQ 202
Cdd:PRK11761 167 RITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQ 201
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
35-307 |
2.59e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 52.04 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 35 NEVYLKLENLQKTGSFKVRGSyNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMPKGAPLSKVLATKKYG 114
Cdd:PRK06450 65 GNIWFKLDFLNPTGSYKDRGS-VTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 115 AHV-ELQGDVfDDALAYAldlkEKTGAKFV----HP-FDDeaviaGQGTVGLEILQQLED--VEAVICPIGGGGLIAGVA 186
Cdd:PRK06450 144 AEVvRVRGSR-EDVAKAA----ENSGYYYAshvlQPqFRD-----GIRTLAYEIAKDLDWkiPNYVFIPVSAGTLLLGVY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 187 MAIK--------EQKPsvKIYGVQTLA----CPGMKQ-SLEEKKVITvestpTMADGIAVKRPGDLTFEL-VQRYVDDVF 252
Cdd:PRK06450 214 SGFKhlldsgviSEMP--KIVAVQTEQvsplCAKFKGiSYTPPDKVT-----SIADALVSTRPFLLDYMVkALSEYGECI 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446557391 253 CVDEMEI--ARTMlmlLERNKLLVEGSGASSLASllYHKVPIKEKKVVSVLSGGNVD 307
Cdd:PRK06450 287 VVSDNEIveAWKE---LAKKGLLVEYSSATVYAA--YKKYSVNDSVLVLTGSGLKVL 338
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
21-207 |
6.16e-06 |
|
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: 47.92 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSE-LSQNEVYLKLENLQKTGSFKVRGS-----YNKMVSLEKGDLENGvvaasAGNHAQGVAYSSNMLSIPC 94
Cdd:cd06446 35 TPLYRAKRLSEyLGGAKIYLKREDLNHTGAHKINNAlgqalLAKRMGKKRVIAETG-----AGQHGVATATACALFGLEC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 95 TIVMpkGA------PLSKVLaTKKYGAHV-----ELQ--GDVFDDALAYALDLKEKTgaKFV-------HPFDDeAVIAG 154
Cdd:cd06446 110 EIYM--GAvdverqPLNVFR-MELLGAEVvpvpsGSGtlKDAISEAIRDWVTNVEDT--HYLlgsvvgpHPYPN-MVRDF 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446557391 155 QGTVGLEILQQLEDVE-----AVICPIGGGGLIAGVAMAIKEQKpSVKIYGVQTLACP 207
Cdd:cd06446 184 QSVIGEEAKKQILEKEgelpdVVIACVGGGSNAAGLFYPFINDK-DVKLIGVEAGGCG 240
|
|
| ACT_4 |
pfam13291 |
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ... |
334-400 |
1.52e-05 |
|
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.
Pssm-ID: 463831 [Multi-domain] Cd Length: 79 Bit Score: 42.93 E-value: 1.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446557391 334 DKPGYLHHLLEIVTNFEANVLNIHLErigTKVFPGYAQLHLSLETKDRNHIEEILSGLKKKGYVVEV 400
Cdd:pfam13291 14 DRPGLLADITQVISEEKANIVSVNAK---TRKKDGTAEIKITLEVKDVEHLERLMAKLRRIPGVIDV 77
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
21-202 |
3.43e-05 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 46.18 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNE------VYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPC 94
Cdd:PRK13802 327 SPLTEAPRFAERVKEKtgldarVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKC 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 95 TIVMPKGAPLSKVLATKKY---GA---HVELQGDVFDDALAYAL-----DLKEK-----TGAKfVHPFdDEAVIAGQGTV 158
Cdd:PRK13802 407 RIYMGQIDARRQALNVARMrmlGAevvEVTLGDRILKDAINEALrdwvtNVKDThyllgTVAG-PHPF-PAMVRDFQKII 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446557391 159 GLEILQQLED------VEAVICPIGGGGLIAGVAMAIKEQkPSVKIYGVQ 202
Cdd:PRK13802 485 GEEAKQQLQDwygidhPDAICACVGGGSNAIGVMNAFLDD-ERVNLYGYE 533
|
|
| ACT_RelA-SpoT |
cd04876 |
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ... |
326-400 |
8.87e-05 |
|
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153148 [Multi-domain] Cd Length: 71 Bit Score: 40.51 E-value: 8.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557391 326 IHIatMIKDKPGYLHHLLEIVTNFEANVLNIHLERIGTkvfpGYAQLHLSLETKDRNHIEEILSGLKKKGYVVEV 400
Cdd:cd04876 1 IRV--EAIDRPGLLADITTVIAEEKINILSVNTRTDDD----GLATIRLTLEVRDLEHLARIMRKLRQIPGVIDV 69
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
6-236 |
9.12e-05 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 44.42 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 6 DIIAAYEKMkgivhmTPLDYSSTFSE--LSQNEVYLKLENLQKTGSFKVRGsynkMVSL--------EKGDLENGVVAAS 75
Cdd:PLN02569 125 DIVSLFEGN------SNLFWAERLGKefLGMNDLWVKHCGISHTGSFKDLG----MTVLvsqvnrlrKMAKPVVGVGCAS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 76 AGNHAQGV-AYSSNMlSIPCTIVMPKGAP-LSKVLATKKYGAHV-ELQGDvFDDALAYALDLKEKTG---AKFVHPFDDE 149
Cdd:PLN02569 195 TGDTSAALsAYCAAA-GIPSIVFLPADKIsIAQLVQPIANGALVlSIDTD-FDGCMRLIREVTAELPiylANSLNSLRLE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 150 aviaGQGTVGLEILQQLE-DV-EAVICPIGGGGLIAGVAMAIKEQK--------PsvKIYGVQTLACPGMKQSLE--EKK 217
Cdd:PLN02569 273 ----GQKTAAIEILQQFDwEVpDWVIVPGGNLGNIYAFYKGFKMCKelglvdrlP--RLVCAQAANANPLYRAYKsgWEE 346
|
250
....*....|....*....
gi 446557391 218 VITVESTPTMADGIAVKRP 236
Cdd:PLN02569 347 FKPVKANPTFASAIQIGDP 365
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
21-202 |
1.12e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 44.42 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSELSQNEVYLKLENLQKTGSFKVRGSYNKMVSLEKGDLENGVVAASAGNHAQGVAYSSNMLSIPCTIVMpk 100
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFM-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 101 GAPLSK-----VLATKKYGAHV-------ELQGDVFDDALAYALDLKEKT-----GAKFVHPFdDEAVIAGQGTVGLEIL 163
Cdd:PRK13803 350 GEEDIKrqalnVERMKLLGANVipvlsgsKTLKDAVNEAIRDWVASVPDThyligSAVGPHPY-PEMVAYFQSVIGEEAK 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446557391 164 QQLEDVE-----AVICPIGGGGLIAGVAMAIKEQkPSVKIYGVQ 202
Cdd:PRK13803 429 EQLKEQTgklpdAIIACVGGGSNAIGIFYHFLDD-PSVKLIGVE 471
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
36-286 |
1.28e-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: 43.87 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 36 EVYLKLEN-LQKTGSFKVRG------SYNKMVSLEKGDL-------------------ENGVVAASAGNHAQGVAYSSNM 89
Cdd:cd06447 76 RLLLKADShLPISGSIKARGgiyevlKHAEKLALEHGLLtleddysklasekfrklfsQYSIAVGSTGNLGLSIGIMAAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 90 LSIPCTIVMPKGAPLSKVLATKKYGAHV-ELQGDvFDDALAYALdlKEKTGAKFVHPFDDEA---VIAGQGTVGLEILQQ 165
Cdd:cd06447 156 LGFKVTVHMSADAKQWKKDKLRSKGVTVvEYETD-YSKAVEEGR--KQAAADPMCYFVDDENsrdLFLGYAVAASRLKAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 166 LED----VEA-----VICPIGGGGLIAGVAMAIKEQ-KPSVKIYGVQTLACP----GMKQSLEEKkvITVE----STPTM 227
Cdd:cd06447 233 LAElgikVDAehplfVYLPCGVGGAPGGVAFGLKLIfGDNVHCFFAEPTHSPcmllGMATGLHDK--ISVQdigiDNRTA 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446557391 228 ADGIAVKRPGDLTFELVQRYVDDVFCVDEMEIARTMLMLLERNKLLVEGSGASSLASLL 286
Cdd:cd06447 311 ADGLAVGRPSGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPA 369
|
|
| PRK04435 |
PRK04435 |
ACT domain-containing protein; |
320-401 |
1.29e-03 |
|
ACT domain-containing protein;
Pssm-ID: 179848 [Multi-domain] Cd Length: 147 Bit Score: 39.02 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 320 VEAGRFIHIATMIKDKPGYLHHLLEIVTNFEANVLNIH----LErigtkvfpGYAQLHLSLETKDRN-HIEEILSGLKKK 394
Cdd:PRK04435 64 MVKGKIITLSLLLEDRSGTLSKVLNVIAEAGGNILTINqsipLQ--------GRANVTISIDTSSMEgDIDELLEKLRNL 135
|
....*....
gi 446557391 395 GYV--VEVI 401
Cdd:PRK04435 136 DGVekVELI 144
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
21-201 |
1.30e-03 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 40.48 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 21 TPLDYSSTFSE--LSQNEVYLKLENLQKTGSFkvrgSYNKMVSLE-------KGDLENGV-VAASAGNHAQGVAYSSNML 90
Cdd:cd06449 1 TPIQYLPRLSEhlGGKVEIYAKRDDCNSGLAF----GGNKIRKLEyllpdalAKGADTLVtVGGIQSNHTRQVAAVAAKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 91 SIPCTIVMPKGAPLSKVLATKK--------YGAHVELQGDVFD----DALAYALDLKEKTGAK-FVHPFD-DEAVIAGQG 156
Cdd:cd06449 77 GLKCVLVQENWVPYSDAVYDRVgnillsriMGADVRLVSAGFDigirKSFEEAAEEVEAKGGKpYVIPAGgSEHPLGGLG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446557391 157 TVG--LEILQQLEDV----EAVICPIGGGGLIAGVAMAIKEQKPSVKIYGV 201
Cdd:cd06449 157 YVGfvLEIAQQEEELgfkfDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGI 207
|
|
| ACT_PheB-BS |
cd04888 |
C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway ... |
328-400 |
4.73e-03 |
|
C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and related domains; This CD includes the C-terminal ACT domain of a small (~147 a.a.) putative phenylalanine biosynthetic pathway protein described in Bacillus subtilis (BS) PheB (PheB-BS) and other related ACT domains. In B. subtilis, the upstream gene of pheB, pheA encodes prephenate dehydratase (PDT). The presumed product of the pheB gene is chorismate mutase (CM). The deduced product of the B. subtilis pheB gene, however, has no significant homology to the CM portion of the bifunctional CM-PDT of Escherichia coli. The presence of an ACT domain lends support to the prediction that these proteins function as a phenylalanine-binding regulatory protein. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153160 Cd Length: 76 Bit Score: 35.63 E-value: 4.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557391 328 IATMIKDKPGYLHHLLEIVTNFEANVLNIHLErigtkvFP--GYAQLHLSLETKDRN-HIEEILSGLKKKGYVVEV 400
Cdd:cd04888 3 LSLLLEHRPGVLSKVLNTIAQVRGNVLTINQN------IPihGRANVTISIDTSTMNgDIDELLEELREIDGVEKV 72
|
|
| PheB |
COG4492 |
ACT domain-containing protein, UPF0735 family [General function prediction only]; |
323-401 |
7.49e-03 |
|
ACT domain-containing protein, UPF0735 family [General function prediction only];
Pssm-ID: 443581 [Multi-domain] Cd Length: 147 Bit Score: 36.66 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557391 323 GRFIHIATMIKDKPGYLHHLLEIVTNFEANVLNIH----LErigtkvfpGYAQLHLSLETKD-RNHIEEILSGLKKKGYV 397
Cdd:COG4492 67 GKIITLSLLLEDEPGVLSSVLNIIAEAGGNILTINqsipIQ--------GIANVTISIETSDmTIDIEELLEELRELEGV 138
|
....*.
gi 446557391 398 --VEVI 401
Cdd:COG4492 139 rkVEIL 144
|
|
| |
