|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
1-327 |
0e+00 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 612.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 1 MHITYDLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVA 80
Cdd:PRK08638 1 MHITYDLPVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 81 CSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIA 160
Cdd:PRK08638 81 CSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 161 GQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDV 240
Cdd:PRK08638 161 GQGTIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 241 SRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRV 320
Cdd:PRK08638 241 SRPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVDLSRV 320
|
....*..
gi 446470493 321 SQITGFV 327
Cdd:PRK08638 321 SQITGHV 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
11-316 |
2.33e-139 |
|
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: 396.47 E-value: 2.33e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 11 IDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGV 90
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 91 SLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIM 170
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 171 EDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEI 250
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470493 251 VRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDqyIQNRKTVSIISGGNID 316
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD--LKGKKVVVVLSGGNID 304
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
6-325 |
1.61e-131 |
|
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: 377.45 E-value: 1.61e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 6 DLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGN 85
Cdd:COG1171 3 ALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 86 HAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTI 165
Cdd:COG1171 83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 166 GLEIMEDLYDVDNVIVPiggggliagiaV-----------AIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTL 234
Cdd:COG1171 163 ALEILEQLPDLDAVFVP-----------VggggliagvaaALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 235 ADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEgagalacaallsgkLDQY---IQNRKTVSIIS 311
Cdd:COG1171 232 ADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEpagaa-----alaaLLAGkerLKGKRVVVVLS 306
|
330
....*....|....
gi 446470493 312 GGNIDLSRVSQITG 325
Cdd:COG1171 307 GGNIDPDRLAEILE 320
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
28-323 |
3.09e-104 |
|
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: 310.14 E-value: 3.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 28 TGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPK 107
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 108 GAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGG 187
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 188 LIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIR 267
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446470493 268 NSMIALIQRNKVVTEGAGALACAALLSGKLDQyiQNRKTVSIISGGNIDLSRVSQI 323
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDV--KGKKIAVVLSGGNIDLNLLNKI 294
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
6-316 |
1.35e-92 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 281.40 E-value: 1.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 6 DLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGN 85
Cdd:PRK07334 2 GLMVTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 86 HAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTI 165
Cdd:PRK07334 82 HAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 166 GLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSgeitTHRTTG--TLADGCDVSRP 243
Cdd:PRK07334 162 ALEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKG----VALPCGgsTIAEGIAVKQP 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446470493 244 GNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKldQYIQNRKTVSIISGGNID 316
Cdd:PRK07334 238 GQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYP--ERFRGRKVGLVLSGGNID 308
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
7-322 |
4.87e-85 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 259.18 E-value: 4.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 7 LPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNH 86
Cdd:PRK07048 4 LLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 87 AQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHgDNFNDTIAKVS-EIVEMEGRIFIPPYDDPKVIAGQGTI 165
Cdd:PRK07048 84 AQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTY-DRYTEDREEIGrRLAEERGLTLIPPYDHPHVIAGQGTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 166 GLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGN 245
Cdd:PRK07048 163 AKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGN 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446470493 246 LTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDqyIQNRKTVSIISGGNIDLSRVSQ 322
Cdd:PRK07048 243 YTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVP--LKGKRVGVIISGGNVDLARFAA 317
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
8-323 |
1.73e-81 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 253.19 E-value: 1.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 8 PVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHA 87
Cdd:PRK08639 6 TVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 88 QGVSLSCAMLGIDGKVVMPKGAPKSKVAAT----CDYsAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQG 163
Cdd:PRK08639 86 QGVAYACRHLGIPGVIFMPVTTPQQKIDQVrffgGEF-VEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 164 TIGLEIMEDL---YDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDV 240
Cdd:PRK08639 165 TVAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 241 SRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAAllsgkLDQY---IQNRKTVSIISGGNIDL 317
Cdd:PRK08639 245 ARVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAA-----LELYkdeIKGKTVVCVISGGNNDI 319
|
....*.
gi 446470493 318 SRVSQI 323
Cdd:PRK08639 320 ERMPEI 325
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
37-266 |
1.28e-77 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 245.82 E-value: 1.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 37 SERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAA 116
Cdd:PRK09224 30 SARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 117 TCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYD-VDNVIVPIGGGGLIAGIAVA 195
Cdd:PRK09224 110 VRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAVFVPVGGGGLIAGVAAY 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446470493 196 IKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEI 266
Cdd:PRK09224 190 IKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDTDEI 260
|
|
| PLN02970 |
PLN02970 |
serine racemase |
11-319 |
6.18e-77 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 238.81 E-value: 6.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 11 IDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGV 90
Cdd:PLN02970 11 LSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 91 SLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIM 170
Cdd:PLN02970 91 ALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 171 EDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRpGNLTYEI 250
Cdd:PLN02970 171 EQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRASL-GDLTWPV 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446470493 251 VRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVS---IISGGNIDLSR 319
Cdd:PLN02970 250 VRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAWKGCKNvgiVLSGGNVDLGV 321
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
21-324 |
5.50e-76 |
|
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: 241.56 E-value: 5.50e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 21 LAGRIY----KTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAM 96
Cdd:TIGR01124 7 LTARVYeaaqETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 97 LGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIM-EDLYD 175
Cdd:TIGR01124 87 LGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILrQVANP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 176 VDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELV 255
Cdd:TIGR01124 167 LDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYL 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446470493 256 DDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRVSQIT 324
Cdd:TIGR01124 247 DDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTLVAILSGANMNFHRLRYVS 315
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
9-317 |
6.65e-76 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 235.63 E-value: 6.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 9 VAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQ 88
Cdd:PRK07476 1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 89 GVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLE 168
Cdd:PRK07476 81 ALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 169 IMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLAD--GCDVSRPGNL 246
Cdd:PRK07476 161 ILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslGGGIGLDNRY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446470493 247 TYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDqyIQNRKTVSIISGGNIDL 317
Cdd:PRK07476 241 TFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIA--ARDGPIVVVVSGANIDM 309
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
12-320 |
1.88e-73 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 229.58 E-value: 1.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 12 DDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVS 91
Cdd:PRK06815 5 DAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 92 LSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIME 171
Cdd:PRK06815 85 LAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 172 DLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVS-RPGNLTYEI 250
Cdd:PRK06815 165 QQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGvEPGAITFPL 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 251 VRELVDDIVLVSEDEIRNSMIALIQRNKVVTEgaGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRV 320
Cdd:PRK06815 245 CQQLIDQKVLVSEEEIKEAMRLIAETDRWLIE--GAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKY 312
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
17-320 |
2.89e-70 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 227.37 E-value: 2.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 17 AKQRLAGRIY----KTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSL 92
Cdd:PRK12483 23 LRKILAARVYdvarETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 93 SCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIM-E 171
Cdd:PRK12483 103 AAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILrQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 172 DLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIV 251
Cdd:PRK12483 183 HPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELC 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446470493 252 RELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRV 320
Cdd:PRK12483 263 RHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANVNFDRL 331
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
25-282 |
3.85e-70 |
|
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: 220.26 E-value: 3.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 25 IYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVV 104
Cdd:pfam00291 5 IGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 105 MPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIV-EMEGRIFIPPYDDPKVIAGQGTIGLEIMEDL-YDVDNVIVP 182
Cdd:pfam00291 85 VPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEGYGTIGLEILEQLgGDPDAVVVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 183 IGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSR-PGNLTYEIVRELVDDIVLV 261
Cdd:pfam00291 165 VGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDePGALALDLLDEYVGEVVTV 244
|
250 260
....*....|....*....|.
gi 446470493 262 SEDEIRNSMIALIQRNKVVTE 282
Cdd:pfam00291 245 SDEEALEAMRLLARREGIVVE 265
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
6-316 |
1.48e-61 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 199.85 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 6 DLPVAIDDIIEAKQRLagRIYKtgMPRSNYFSERCKgeIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGN 85
Cdd:PRK08813 18 DVAVSVADVLAAQARL--RRYL--SPTPLHYAERFG--VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 86 HAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTI 165
Cdd:PRK08813 92 HAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 166 GLEIMEDLYDVdnVIVPIGGGGLIAGIAVAIKSinPTIRVIGVQSENVHGMAASFHsGEITTHRTTGTLADGCDVSRPGN 245
Cdd:PRK08813 172 GIELAAHAPDV--VIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGF 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446470493 246 LTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAAllsgklDQYIQNRKTVSIISGGNID 316
Cdd:PRK08813 247 LTRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAA------GRRVSGKRKCAVVSGGNID 311
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
9-317 |
4.05e-61 |
|
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: 197.77 E-value: 4.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 9 VAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQ 88
Cdd:TIGR02991 1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 89 GVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLE 168
Cdd:TIGR02991 81 ALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 169 IMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLAD--GCDVSRPGNL 246
Cdd:TIGR02991 161 VVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446470493 247 TYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDqyiQNRKTVSIISGGNIDL 317
Cdd:TIGR02991 241 TFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIK---NPGPCAVIVSGRNIDM 308
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
37-328 |
3.80e-56 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 191.67 E-value: 3.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 37 SERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAA 116
Cdd:PLN02550 119 SERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 117 TCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYD-VDNVIVPIGGGGLIAGIAVA 195
Cdd:PLN02550 199 VERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGpLHAIFVPVGGGGLIAGIAAY 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 196 IKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQ 275
Cdd:PLN02550 279 VKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSRDAICASIKDMFE 358
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446470493 276 RNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRVSQITGFVD 328
Cdd:PLN02550 359 EKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMNFDRLRIVTELAD 411
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
28-282 |
1.44e-51 |
|
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: 170.77 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 28 TGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKG--VVACSAGNHAQGVSLSCAMLGIDGKVVM 105
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 106 PKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIV-EMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYD--VDNVIVP 182
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAeEDPGAYYVNQFDNPANIAGQGTIGLEILEQLGGqkPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 183 iggggliagiaV-----------AIKSINPTIRVIGVQSEnvhgmaasfhsgeitthrttgtladgcdvsrpgnltyeiv 251
Cdd:cd00640 161 -----------VggggniagiarALKELLPNVKVIGVEPE---------------------------------------- 189
|
250 260 270
....*....|....*....|....*....|.
gi 446470493 252 relvddIVLVSEDEIRNSMIALIQRNKVVTE 282
Cdd:cd00640 190 ------VVTVSDEEALEAIRLLAREEGILVE 214
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
6-323 |
8.62e-50 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 168.80 E-value: 8.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 6 DLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKR-KGVVACSAG 84
Cdd:PRK06608 2 LLLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLpDKIVAYSTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 85 NHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLhgdnfNDTIAKVSEIV---EMEGRIFIPPYDDPKVIAG 161
Cdd:PRK06608 82 NHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVIL-----TNTRQEAEEKAkedEEQGFYYIHPSDSDSTIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 162 QGTIGLEIMEDL-YDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTT-GTLADGCD 239
Cdd:PRK06608 157 AGTLCYEALQQLgFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 240 VSRPGNLTYEIVRELvDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYiQNRKTVSIISGGNIDLSR 319
Cdd:PRK06608 237 TLSVSARTFEYLKKL-DDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQS-KPQKLLVILSGGNIDPIL 314
|
....
gi 446470493 320 VSQI 323
Cdd:PRK06608 315 YNEL 318
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
12-282 |
1.48e-48 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 164.74 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 12 DDIIEAKQRLAGRIYKTGMPRSNYFSERcKGEIFLKFENMQRTGSFKIRGAFNKLssLTDAEKRKGVVACSAGNHAQGVS 91
Cdd:PRK08246 8 SDVRAAAQRIAPHIRRTPVLEADGAGFG-PAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 92 LSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIME 171
Cdd:PRK08246 85 YAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 172 DLYDVDNVIVPIGGGGLIAGIAVAIKsinPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIV 251
Cdd:PRK08246 165 QAPGVDTVLVAVGGGGLIAGIAAWFE---GRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALA 241
|
250 260 270
....*....|....*....|....*....|.
gi 446470493 252 RELVDDIVLVSEDEIRNSMIALIQRNKVVTE 282
Cdd:PRK08246 242 RAHVVTSVLVSDEAIIAARRALWEELRLAVE 272
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
37-325 |
9.21e-36 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 131.65 E-value: 9.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 37 SERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKR-KGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVA 115
Cdd:PRK06110 31 AERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRvRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 116 ATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDdPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAVA 195
Cdd:PRK06110 111 AMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSFH-PDLVRGVATYALELFRAVPDLDVVYVPIGMGSGICGAIAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 196 IKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQ 275
Cdd:PRK06110 190 RDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAYFT 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446470493 276 RNKVVTEGAGALACAALLSGKldQYIQNRKTVSIISGGNIDLSRVSQITG 325
Cdd:PRK06110 270 DTHNVAEGAGAAALAAALQER--ERLAGKRVGLVLSGGNIDRAVFARVLA 317
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
7-273 |
1.57e-21 |
|
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: 93.04 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 7 LPVAIDDIIEAKqrlAGRiykTGMPRSNYFSERCKG-EIFLKFENMQRTGSFKIRG---AFNKLSSLtdaeKRKGVVACS 82
Cdd:cd01563 8 LPVTEDDIVSLG---EGN---TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGmtvAVSKAKEL----GVKAVACAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 83 AGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEmEGRIFIPPYDDPKVIAGQ 162
Cdd:cd01563 78 TGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAE-ENWIYLSNSLNPYRLEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 163 GTIGLEIMEDL-YDV-DNVIVPIGGGGLIAGIAVAIK------SINPTIRVIGVQSENVHGMAASFHSGEITTHRTTG-- 232
Cdd:cd01563 157 KTIAFEIAEQLgWEVpDYVVVPVGNGGNITAIWKGFKelkelgLIDRLPRMVGVQAEGAAPIVRAFKEGKDDIEPVENpe 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446470493 233 TLADGCDVSRPGNLTY--EIVRELVDDIVLVSEDEIRNSMIAL 273
Cdd:cd01563 237 TIATAIRIGNPASGPKalRAVRESGGTAVAVSDEEILEAQKLL 279
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
32-282 |
3.25e-20 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 90.26 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 32 RSNYFSERCKGEIFLKFENMQRTGSFKIRGAFnKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKG-AP 110
Cdd:COG0498 71 KAPRLADELGKNLYVKEEGHNPTGSFKDRAMQ-VAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPEGkVS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 111 KSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGrIF----IPPYddpkVIAGQGTIGLEIMEDLYDV-DNVIVPIGG 185
Cdd:COG0498 150 PGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEG-LYavnsINPA----RLEGQKTYAFEIAEQLGRVpDWVVVPTGN 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 186 GGLIAGIAVAIK------SINPTIRVIGVQSENVHGMAASFHSGEITTHRTTG-TLADGCDVSRPGNLtYEIVRELVD-- 256
Cdd:COG0498 225 GGNILAGYKAFKelkelgLIDRLPRLIAVQATGCNPILTAFETGRDEYEPERPeTIAPSMDIGNPSNG-ERALFALREsg 303
|
250 260
....*....|....*....|....*..
gi 446470493 257 -DIVLVSEDEIRNSMIALIQRNKVVTE 282
Cdd:COG0498 304 gTAVAVSDEEILEAIRLLARREGIFVE 330
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
27-276 |
8.23e-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: 82.18 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 27 KTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAfnkLSSLTDAEKR----KG--VVACSAGNHAQGVSLSCAMLGID 100
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIA---LYMIEDAEKRgllkPGttIIEPTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 101 GKVVMPKGAPKSKVAATCDYSAEVVL----HGDNFNDTIAKVSEIVEMEGRIFIP-PYDDP-KVIAGQGTIGLEIMEDL- 173
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILtpeaEADGMKGAIAKARELAAETPNAFWLnQFENPaNPEAHYETTAPEIWEQLd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 174 YDVDNVIVPiggggliagiaV-----------AIKSINPTIRVIGVQSENvhgmAASFHSGEITTHRTTGTLADgcdvSR 242
Cdd:cd01561 159 GKVDAFVAG-----------VgtggtitgvarYLKEKNPNVRIVGVDPVG----SVLFSGGPPGPHKIEGIGAG----FI 219
|
250 260 270
....*....|....*....|....*....|....
gi 446470493 243 PGNLTyeivRELVDDIVLVSEDEIRNSMIALIQR 276
Cdd:cd01561 220 PENLD----RSLIDEVVRVSDEEAFAMARRLARE 249
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
27-179 |
1.66e-17 |
|
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: 81.58 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 27 KTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRK--GVVACSAGNHAQGVSLSCAMLGIDGKVV 104
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNEcvHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446470493 105 MPKGAPKSKVAATCDYSAEVVLHGDNFNDT-IAKVSEIVEME-GRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNV 179
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWWEAdNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSQEKV 157
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
1-266 |
6.13e-17 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 81.01 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 1 MHITYDLPVAidDIIEAKQRLAGR-IYKTGMPRSNY---------------FSERCKGEIFLKFENMQRTGSFKIRGAFN 64
Cdd:PRK05638 25 LEIIYDYSSV--DVRKWKNRDPGVwRYKELLPQVKKiislgeggtplirarISEKLGENVYIKDETRNPTGSFRDRLATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 65 KLS-SLTDAEKrkGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVE 143
Cdd:PRK05638 103 AVSyGLPYAAN--GFIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELAR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 144 MEGRIFIPPYDDPKVIAGQGTIGLEIMEDlYDVDNVIVPIGGGGLIA------GIAVAIKSINPTIRVIGVQSENVHGMA 217
Cdd:PRK05638 181 LNGLYNVTPEYNIIGLEGQKTIAFELWEE-INPTHVIVPTGSGSYLYsiykgfKELLEIGVIEEIPKLIAVQTERCNPIA 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446470493 218 ASFHSgeiTTHRTTGTLADGCDVSRP--GNLTYEIVRELVDDIVLVSEDEI 266
Cdd:PRK05638 260 SEILG---NKTKCNETKALGLYVKNPvmKEYVSEAIKESGGTAVVVNEEEI 307
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
12-265 |
3.76e-13 |
|
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: 68.92 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 12 DDIIEAkqrlagrIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAfnkLSSLTDAEKR----KG--VVACSAGN 85
Cdd:COG0031 5 DSILEL-------IGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIA---LSMIEDAEKRgllkPGgtIVEATSGN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 86 haQGVSLS--CAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVL--HGDNFNDTIAKVSEIVEMEGRIFIP-PYDDPK-VI 159
Cdd:COG0031 75 --TGIGLAmvAAAKGYRLILVMPETMSKERRALLRAYGAEVVLtpGAEGMKGAIDKAEELAAETPGAFWPnQFENPAnPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 160 AGQGTIGLEIMEDLY-DVDNVIVPiggggliagiaV-----------AIKSINPTIRVIGVQSENvhgmAASFHSGEITT 227
Cdd:COG0031 153 AHYETTGPEIWEQTDgKVDAFVAG-----------VgtggtitgvgrYLKERNPDIKIVAVEPEG----SPLLSGGEPGP 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 446470493 228 HRTTGtLADGCdvsRPGNLtyeiVRELVDDIVLVSEDE 265
Cdd:COG0031 218 HKIEG-IGAGF---VPKIL----DPSLIDEVITVSDEE 247
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
42-267 |
7.32e-10 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 59.63 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 42 GEIFLKFENMQRTGSFKIRGAFNKLSSLTDAeKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYS 121
Cdd:PRK08197 95 GRLWVKDEGLNPTGSFKARGLAVGVSRAKEL-GVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 122 AEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDL-YDVDNVIV-PIGGGGLIAGIAVAIKSI 199
Cdd:PRK08197 174 AELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLgWRLPDVILyPTGGGVGLIGIWKAFDEL 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446470493 200 -------NPTIRVIGVQSENVHGMAASFHSGEITTHRTTG--TLADGCDVSRP-GN-LTYEIVRELVDDIVLVSEDEIR 267
Cdd:PRK08197 254 ealgwigGKRPRLVAVQAEGCAPIVKAWEEGKEESEFWEDahTVAFGIRVPKAlGDfLVLDAVRETGGCAIAVSDDAIL 332
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
43-282 |
1.32e-08 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 55.60 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 43 EIFLKFENMQRTGSFKIRGAFNKLSSLTDaEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSA 122
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTVAKLKE-EGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 123 EV-VLHGDNFnDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIK---- 197
Cdd:PRK08329 152 ELhFVEGDRM-EVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIWKGFKelhe 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 198 --SINPTIRVIGVQSENVHGMAASFHSgeitthrtTGTLADGCDVSRPGNL--TYEIVRELVDDIVLVSEDEIRNSMIAL 273
Cdd:PRK08329 231 mgEISKMPKLVAVQAEGYESLCKRSKS--------ENKLADGIAIPEPPRKeeMLRALEESNGFCISVGEEETRAALHWL 302
|
....*....
gi 446470493 274 IQRNKVVTE 282
Cdd:PRK08329 303 RRMGFLVEP 311
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
41-269 |
3.66e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 50.89 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 41 KGEIFLKFENMQRTGSFKIRGAFNKLSSLTDaEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDY 120
Cdd:PRK06450 64 KGNIWFKLDFLNPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 121 SAEVVLHGDNFNDtiakVSEIVEMEG-----RIFIPPYDDpkviaGQGTIGLEIMEDLYD--VDNVIVPIGGGGLIAGIA 193
Cdd:PRK06450 143 GAEVVRVRGSRED----VAKAAENSGyyyasHVLQPQFRD-----GIRTLAYEIAKDLDWkiPNYVFIPVSAGTLLLGVY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 194 VAIK------SINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPG--NLTYEIVRELVDDIVlVSEDE 265
Cdd:PRK06450 214 SGFKhlldsgVISEMPKIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADALVSTRPFllDYMVKALSEYGECIV-VSDNE 292
|
....
gi 446470493 266 IRNS 269
Cdd:PRK06450 293 IVEA 296
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
42-173 |
1.42e-06 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 49.49 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 42 GEIFLKFENmQRTG--SFKIRGA---------------FNKLSS--LTDAEKRKG----VVAC-SAGNHAQGVSLSCAML 97
Cdd:PRK08206 60 GSILVKDES-YRFGlnAFKALGGayavarllaeklgldISELSFeeLTSGEVREKlgdiTFATaTDGNHGRGVAWAAQQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 98 GIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFI-----PPYDD-PK-VIAGQGTIGLEIM 170
Cdd:PRK08206 139 GQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVqdtawEGYEEiPTwIMQGYGTMADEAV 218
|
...
gi 446470493 171 EDL 173
Cdd:PRK08206 219 EQL 221
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
16-209 |
5.10e-06 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 47.65 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 16 EAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAfnkLSSLTDAEKRK-------GVVACSAGNHAQ 88
Cdd:PLN02556 48 KIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPA---LAMIEDAEKKNlitpgktTLIEPTSGNMGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 89 GVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVL--HGDNFNDTIAKVSEIVEMEGRIF-IPPYDDP-KVIAGQGT 164
Cdd:PLN02556 125 SLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLtdPTKGMGGTVKKAYELLESTPDAFmLQQFSNPaNTQVHFET 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446470493 165 IGLEIMED-LYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQ 209
Cdd:PLN02556 205 TGPEIWEDtLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVE 250
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
18-105 |
1.86e-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: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 18 KQRLAGRIYK-TGMPRsnyFSERCK------GEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGV 90
Cdd:PRK13802 319 NQRYVGRPSPlTEAPR---FAERVKektgldARVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVAT 395
|
90
....*....|....*
gi 446470493 91 SLSCAMLGIDGKVVM 105
Cdd:PRK13802 396 ATVCAMLGLKCRIYM 410
|
|
| diampropi_NH3ly |
TIGR01747 |
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ... |
62-173 |
7.75e-05 |
|
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: 44.11 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 62 AFNKLSSLTDAEKRKGVVACSA--GNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVS 139
Cdd:TIGR01747 79 SFEHLKNDAIGEKMGQATFATAtdGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAM 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446470493 140 EIVEMEGRIF-----------IPPYddpkVIAGQGTIGLEIMEDL 173
Cdd:TIGR01747 159 QMAQQHGWVVvqdtawegyekIPTW----IMQGYATLADEAVEQL 199
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
18-126 |
1.38e-04 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 42.93 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 18 KQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAfnkLSSLTDAEKR------KGVVACSAGNHAQGVS 91
Cdd:PRK10717 4 FEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAA---LNIIWDAEKRgllkpgGTIVEGTAGNTGIGLA 80
|
90 100 110
....*....|....*....|....*....|....*
gi 446470493 92 LSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVL 126
Cdd:PRK10717 81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVL 115
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
43-182 |
1.73e-03 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 39.80 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 43 EIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRK----GVVACSAGNHAQGVSLSCAMLGIDGKVVMPkgAPKSKVAATC 118
Cdd:PLN02569 151 DLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAkpvvGVGCASTGDTSAALSAYCAAAGIPSIVFLP--ADKISIAQLV 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446470493 119 DYSAE--VVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDL-YDV-DNVIVP 182
Cdd:PLN02569 229 QPIANgaLVLSIDTDFDGCMRLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFdWEVpDWVIVP 296
|
|
| 2_3_DAP_am_ly |
TIGR03528 |
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ... |
63-173 |
1.73e-03 |
|
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: 39.70 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 63 FNKLSSLTDAEKRKGVVACSA--GNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSE 140
Cdd:TIGR03528 99 FEKLKSNEIREKLGDITFVTAtdGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGAECTITDLNYDDAVRLAWK 178
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446470493 141 IVEMEGRIFIPP-----YDD-PKVI-AGQGTIGLEIMEDL 173
Cdd:TIGR03528 179 MAQENGWVMVQDtawegYEKiPTWImQGYGTLALEALEQL 218
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
37-105 |
3.93e-03 |
|
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: 38.67 E-value: 3.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470493 37 SERCKG-EIFLKFENMQRTGSFKIRGA-----FNKlssltdAEKRKGVVA-CSAGNHAQGVSLSCAMLGIDGKVVM 105
Cdd:cd06446 44 SEYLGGaKIYLKREDLNHTGAHKINNAlgqalLAK------RMGKKRVIAeTGAGQHGVATATACALFGLECEIYM 113
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
19-105 |
8.72e-03 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 37.87 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 19 QRLAGRiyKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLG 98
Cdd:PRK13803 265 QNYAGR--PTPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFG 342
|
....*..
gi 446470493 99 IDGKVVM 105
Cdd:PRK13803 343 LKCTIFM 349
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
16-105 |
8.81e-03 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 37.81 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470493 16 EAKQRLAGrIYKTGMPRSN--YFSER----------CKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSA 83
Cdd:PLN02618 50 EFQEELAG-ILKDYVGRETplYFAERltehykradgEGPEIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGA 128
|
90 100
....*....|....*....|..
gi 446470493 84 GNHAQGVSLSCAMLGIDGKVVM 105
Cdd:PLN02618 129 GQHGVATATVCARFGLECIVYM 150
|
|
| |
