|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
1-398 |
5.24e-133 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 387.33 E-value: 5.24e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 1 MPVTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNH 80
Cdd:PRK07334 3 LMVTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 81 ALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIG 160
Cdd:PRK07334 83 AQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 161 LEILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKaGKPtLQPRQHTLADGLATLTVGAE 240
Cdd:PRK07334 163 LEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIK-GVA-LPCGGSTIAEGIAVKQPGQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 241 AFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGllPKL-RGRKVALVVGGGNIDPAVLSRVIEI 319
Cdd:PRK07334 241 TLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAY--PERfRGRKVGLVLSGGNIDTRLLANVLLR 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501342152 320 GLVHDGRLTRFAAVISDRPGGLAELSRVIASAGASIKDIAHDRAFSGPDVSAVRAVCTVETRDRAHITTLHRALRKHGF 398
Cdd:PRK07334 319 GLVRAGRLARLRVDIRDRPGALARVTALIGEAGANIIEVSHQRLFTDLPAKGAELELVIETRDAAHLQEVIAALRAAGF 397
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
1-325 |
2.62e-124 |
|
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: 362.43 E-value: 2.62e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 1 MPVTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNH 80
Cdd:COG1171 4 LMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 81 ALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIG 160
Cdd:COG1171 84 AQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 161 LEILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAE 240
Cdd:COG1171 164 LEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 241 AFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLpKLRGRKVALVVGGGNIDPAVLSRVIEIG 320
Cdd:COG1171 244 TFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKE-RLKGKRVVVVLSGGNIDPDRLAEILERG 322
|
....*
gi 501342152 321 LVHDG 325
Cdd:COG1171 323 LVGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
5-309 |
4.46e-121 |
|
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: 353.33 E-value: 4.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 5 LTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHALGL 84
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 85 AYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEIL 164
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 165 RQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEAFAL 244
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501342152 245 ARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLpKLRGRKVALVVGGGNID 309
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKL-DLKGKKVVVVLSGGNID 304
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
22-402 |
8.84e-118 |
|
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: 347.89 E-value: 8.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 22 SPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHALGLAYHGRLLGIPVTVVMPD 101
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 102 YAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEILRQVPDVEAILCPVGGGG 181
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 182 LIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEAFALARDRVDEVVQVKEEWIA 261
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 262 LAILRMIELEKTVVEGAGAVPLAAMMAGLLpKLRGRKVALVVGGGNIDPAVLSRVIEIGLVHDGRLTRFAAVISDRPGGL 341
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKV-DVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPGAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501342152 342 AELSRVIASAGASIKDIAHDRAFSGPDVSAVRAVCTVETRDRAHITTLHRALRKHGFSLEI 402
Cdd:TIGR01127 320 YHLLESIAEARANIVKIDHDRLSKEIPPGFAMVEITLETRGKEHLDEILKILRDMGYNFYV 380
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
1-324 |
5.10e-95 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 287.79 E-value: 5.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 1 MPVTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNH 80
Cdd:PRK08638 7 LPVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 81 ALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIG 160
Cdd:PRK08638 87 AQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 161 LEILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAE 240
Cdd:PRK08638 167 LEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 241 AFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPK-LRGRKVALVVGGGNIDPAVLSRVIEI 319
Cdd:PRK08638 247 TYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQyIQNKKVVAIISGGNVDLSRVSQITGH 326
|
....*
gi 501342152 320 GLVHD 324
Cdd:PRK08638 327 VVAAD 331
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
3-317 |
3.48e-83 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 257.20 E-value: 3.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 3 VTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHAL 82
Cdd:PRK07476 1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 83 GLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLE 162
Cdd:PRK07476 81 ALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 163 ILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATlTVGAE-- 240
Cdd:PRK07476 161 ILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADSLGG-GIGLDnr 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501342152 241 -AFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPKLRGRkVALVVGGGNIDPAVLSRVI 317
Cdd:PRK07476 240 yTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGP-IVVVVSGANIDMELHRRII 316
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
8-319 |
2.70e-79 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 246.91 E-value: 2.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 8 IRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHALGLAYH 87
Cdd:PRK06815 7 ILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 88 GRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEILRQV 167
Cdd:PRK06815 87 AKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 168 PDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLA-TLTVGAEAFALAR 246
Cdd:PRK06815 167 PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAgGVEPGAITFPLCQ 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501342152 247 DRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAgLLPKLRGRKVALVVGGGNIdpaVLSRVIEI 319
Cdd:PRK06815 247 QLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALK-LAPRYQGKKVAVVLCGKNI---VLEKYLEA 315
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
8-350 |
7.61e-72 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 233.47 E-value: 7.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 8 IRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHALGLAYH 87
Cdd:TIGR01124 4 RAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 88 GRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEILRQV 167
Cdd:TIGR01124 84 AARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 168 P-DVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEAFALAR 246
Cdd:TIGR01124 164 AnPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 247 DRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPK-LRGRKVALVVGGGNIDPAVLSRVIEIGLVHDG 325
Cdd:TIGR01124 244 QYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHgIRGQTLVAILSGANMNFHRLRYVSERCELGEQ 323
|
330 340
....*....|....*....|....*
gi 501342152 326 RLTRFAAVISDRPGGLAELSRVIAS 350
Cdd:TIGR01124 324 REALLAVTIPEQPGSFLKFCELLGN 348
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
1-343 |
2.27e-70 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 227.38 E-value: 2.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 1 MPVTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNH 80
Cdd:PRK08639 5 MTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 81 ALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGAR----VLIrGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQ 156
Cdd:PRK08639 85 AQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEfveiVLV-GDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 157 GTIGLEILRQV---PDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLA 233
Cdd:PRK08639 164 GTVAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 234 TLTVGAEAFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAmMAGLLPKLRGRKVALVVGGGNIDPAVL 313
Cdd:PRK08639 244 VARVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAA-LELYKDEIKGKTVVCVISGGNNDIERM 322
|
330 340 350
....*....|....*....|....*....|....
gi 501342152 314 SRVIEIGLVHDGR----LTRFAavisDRPGGLAE 343
Cdd:PRK08639 323 PEIKERSLIYEGLkhyfIVNFP----QRPGALRE 352
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
30-348 |
5.60e-68 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 223.48 E-value: 5.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 30 LSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHALGLAYHGRLLGIPVTVVMPDYAPLIKVT 109
Cdd:PRK09224 29 LSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 110 TCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEILRQVPD-VEAILCPVGGGGLIAGLAT 188
Cdd:PRK09224 109 AVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAVFVPVGGGGLIAGVAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 189 AVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEAFALARDRVDEVVQVKEEWIALAILRMI 268
Cdd:PRK09224 189 YIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDTDEICAAIKDVF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 269 ELEKTVVEGAGAVPLAAMMAGLLP-KLRGRKVALVVGGGNIDPAVLSRVIEIGLVHDGRLTRFAAVISDRPGGLAELSRV 347
Cdd:PRK09224 269 EDTRSIAEPAGALALAGLKKYVAQhGIEGETLVAILSGANMNFDRLRYVAERAELGEQREALLAVTIPEEPGSFLKFCEL 348
|
.
gi 501342152 348 I 348
Cdd:PRK09224 349 L 349
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
15-303 |
1.09e-65 |
|
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: 211.40 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 15 IADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHALGLAYHGRLLGIP 94
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 95 VTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQ-EGLTYIHGFDAPAIIAGQGTIGLEILRQV-PDVEA 172
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLgGDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 173 ILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLAT-LTVGAEAFALARDRVDE 251
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgDEPGALALDLLDEYVGE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 501342152 252 VVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPKLRGRKVALVV 303
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVV 292
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
3-317 |
5.34e-65 |
|
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: 210.09 E-value: 5.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 3 VTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHAL 82
Cdd:TIGR02991 1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 83 GLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLE 162
Cdd:TIGR02991 81 ALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 163 ILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATlTVG---A 239
Cdd:TIGR02991 161 VVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLGG-GIGldnR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501342152 240 EAFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLpKLRGRkVALVVGGGNIDPAVLSRVI 317
Cdd:TIGR02991 240 VTFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKI-KNPGP-CAVIVSGRNIDMDLHKRII 315
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
2-318 |
7.45e-65 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 209.88 E-value: 7.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 2 PVTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHA 81
Cdd:PRK07048 5 LPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 82 LGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGL 161
Cdd:PRK07048 85 QAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 162 EILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEA 241
Cdd:PRK07048 165 ELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYT 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501342152 242 FALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPkLRGRKVALVVGGGNIDPAVLSRVIE 318
Cdd:PRK07048 245 FPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVP-LKGKRVGVIISGGNVDLARFAALLS 320
|
|
| PLN02970 |
PLN02970 |
serine racemase |
3-313 |
4.21e-64 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 208.38 E-value: 4.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 3 VTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHAL 82
Cdd:PLN02970 9 ADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 83 GLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVlIRGVDFAEARAAADDLVVQE-GLTYIHGFDAPAIIAGQGTIGL 161
Cdd:PLN02970 89 ALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGII-TWCEPTVESREAVAARVQQEtGAVLIHPYNDGRVISGQGTIAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 162 EILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATlTVGAEA 241
Cdd:PLN02970 168 EFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA-SLGDLT 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501342152 242 FALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMM-----AGLLPKlRGRKVALVVGGGNIDPAVL 313
Cdd:PLN02970 247 WPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALsdsfrSNPAWK-GCKNVGIVLSGGNVDLGVL 322
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
1-313 |
1.86e-62 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 203.26 E-value: 1.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 1 MPVTLTDIRAAQRRIADGVIVSPCPEsIPLSEITGARIVCKLDNFQRTGSFKERGARNALklLSPTARQRGVVAASAGNH 80
Cdd:PRK08246 3 AMITRSDVRAAAQRIAPHIRRTPVLE-ADGAGFGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 81 ALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIG 160
Cdd:PRK08246 80 GLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 161 LEILRQVPDVEAILCPVGGGGLIAGLATAVkslRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAE 240
Cdd:PRK08246 160 LEIEEQAPGVDTVLVAVGGGGLIAGIAAWF---EGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501342152 241 AFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPKLRGRKVALVVGGGNIDPAVL 313
Cdd:PRK08246 237 AFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGERVAVVLCGANTDPATL 309
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
14-339 |
2.20e-61 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 206.57 E-value: 2.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 14 RIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHALGLAYHGRLLGI 93
Cdd:PRK12483 30 RVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 94 PVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEILRQVPD-VEA 172
Cdd:PRK12483 110 KAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGpLDA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 173 ILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEAFALARDRVDEV 252
Cdd:PRK12483 190 IFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVDEV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 253 VQVKEEWIALAILRMIELEKTVVEGAGAVPLA-----AMMAGllpkLRGRKVALVVGGGNIDPAVLSRVIEIGLVHDGRL 327
Cdd:PRK12483 270 VTVSTDELCAAIKDIYDDTRSITEPAGALAVAgikkyAEREG----IEGQTLVAIDSGANVNFDRLRHVAERAELGEQRE 345
|
330
....*....|..
gi 501342152 328 TRFAAVISDRPG 339
Cdd:PRK12483 346 AIIAVTIPEQPG 357
|
|
| COG2061 |
COG2061 |
Uncharacterized conserved protein, contains ACT domain [General function prediction only]; |
2-404 |
8.40e-59 |
|
Uncharacterized conserved protein, contains ACT domain [General function prediction only];
Pssm-ID: 441664 [Multi-domain] Cd Length: 401 Bit Score: 196.80 E-value: 8.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 2 PVTLTDIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHA 81
Cdd:COG2061 1 LLLLLDEEAAAAALAVVVVTTPLLLSSSSSLSVGLVVLLKEENLQTTGSFKRRGAYKLIALLLEEEEKGGVAAAAAGNAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 82 LGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGL 161
Cdd:COG2061 81 QAAAAAAALGGISAIVVMPPPPPLPKVAATRGGGAVVVVVGGDDDAAAAAAAALQEEEGGFFHHPDDDDDVIAGGGGGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 162 EILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEA 241
Cdd:COG2061 161 EILELLPDVVVVVVGGGGGGGGGGAAAAAKAKRPPIVIVGVQAEAAAAAPSSLAAGIEVVPGGGTTIADGIAVVKPGGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 242 FALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMagLLPKLRGRKVALVVGGGNIDPAVLSRVIEIGL 321
Cdd:COG2061 241 FIIIRKVVDDVVVVVEEEIAAALLLLLERKKKVVEGAAAAAAAAAL--KKKPLRGKKVVVVLSGGNIDDLLLLRIIIKGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 322 VHDGRLTRFAAVISDRPGGLAELSRVIASAGASIKDIAHDRAFSGPDVSAVRAVCTVETRDRAHITTLHRALRKHGFSLE 401
Cdd:COG2061 319 LAAGRRLVLLVVLPDRPGQLLRVLQPIAELGANIISVVHERENSKTPRGEVEVEVVLETRGEEHLEEIIAALREAGYNVR 398
|
...
gi 501342152 402 ISR 404
Cdd:COG2061 399 RVG 401
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
5-350 |
7.39e-54 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 188.21 E-value: 7.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 5 LTDIRAAqrRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNHALGL 84
Cdd:PLN02550 95 LTNILSA--KVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 85 AYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEIL 164
Cdd:PLN02550 173 ALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 165 RQVPD-VEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEAFA 243
Cdd:PLN02550 253 RQHQGpLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 244 LARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGL-LPKLRGRKVALVVGGGNIDPAVLSRVIEIGLV 322
Cdd:PLN02550 333 LCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCkYYGLKDENVVAITSGANMNFDRLRIVTELADV 412
|
330 340
....*....|....*....|....*...
gi 501342152 323 HDGRLTRFAAVISDRPGGLAELSRVIAS 350
Cdd:PLN02550 413 GRQQEAVLATFMPEEPGSFKRFCELVGP 440
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
7-318 |
1.54e-51 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 175.73 E-value: 1.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 7 DIRAAQRRIADGVIVSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNAL-KLLSPTARQRGVVAASAGNHALGLA 85
Cdd:PRK06608 9 NIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLlELKEQGKLPDKIVAYSTGNHGQAVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 86 YHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARV-LIRGVDFAEARAAADDlvvQEGLTYIHGFDAPAIIAGQGTIGLEIL 164
Cdd:PRK06608 89 YASKLFGIKTRIYLPLNTSKVKQQAALYYGGEViLTNTRQEAEEKAKEDE---EQGFYYIHPSDSDSTIAGAGTLCYEAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 165 RQV-PDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGK-PTLQPRQHTLADGLATLTVGAEAF 242
Cdd:PRK06608 166 QQLgFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKiYRLNYSPNTIADGLKTLSVSARTF 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501342152 243 ALARdRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPKLRGRKVALVVGGGNIDPAVLSRVIE 318
Cdd:PRK06608 246 EYLK-KLDDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKPQKLLVILSGGNIDPILYNELWK 320
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
22-306 |
1.80e-48 |
|
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: 165.00 E-value: 1.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 22 SPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRG--VVAASAGNHALGLAYHGRLLGIPVTVVM 99
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 100 PDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQ-EGLTYIHGFDAPAIIAGQGTIGLEILRQVPDVE--AILCP 176
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQGTIGLEILEQLGGQKpdAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 177 VGGGGLIAGLATAVKSLRPRVKIVGVESvstrnlsaalkagkptlqprqhtladglatltvgaeafalardrvdEVVQVK 256
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 501342152 257 EEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPKLRGRKVALVVGGG 306
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
1-317 |
2.73e-46 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 161.70 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 1 MPVTLTDIRAAQRRIadGVIVSPCPE-SIPL-SEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQ-RGVVAASA 77
Cdd:PRK06110 1 MMFTLAELEAAAAVV--YAAMPPTPQyRWPLlAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRvRGVISATR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 78 GNHALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDaPAIIAGQG 157
Cdd:PRK06110 79 GNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSFH-PDLVRGVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 158 TIGLEILRQVPDVEAILCPVGGGGLIAGLATAVKSLRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTV 237
Cdd:PRK06110 158 TYALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 238 GAEAFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAgLLPKLRGRKVALVVGGGNIDPAVLSRVI 317
Cdd:PRK06110 238 DPEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQ-ERERLAGKRVGLVLSGGNIDRAVFARVL 316
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
1-317 |
6.12e-44 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 156.32 E-value: 6.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 1 MPVTLTDIRAAQRRIADgvIVSPCPesIPLSEITGarIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAASAGNH 80
Cdd:PRK08813 19 VAVSVADVLAAQARLRR--YLSPTP--LHYAERFG--VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 81 ALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIG 160
Cdd:PRK08813 93 AQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 161 LEILRQVPDVeaILCPVGGGGLIAGLATAVKSlrPRVKIVGVESVSTRNLSAALKAGKPTLQPRQhTLADGLATLTVGAE 240
Cdd:PRK08813 173 IELAAHAPDV--VIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARAIRGDLREIAPVA-TLADGVKVKIPGFL 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501342152 241 AFALARDRVDEVVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMagllpKLRGRKVALVVGGGNIDPAVLSRVI 317
Cdd:PRK08813 248 TRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAAGR-----RVSGKRKCAVVSGGNIDATVLATLL 319
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
21-307 |
5.20e-37 |
|
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: 136.66 E-value: 5.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 21 VSPCPESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLLS--PTARQRGVVAASAGNHALGLAYHGRLLGIPVTVV 98
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAkqGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 99 MPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVV--QEGLTYIHGFDAPAIIAGQGTIGLEILRQVPD---VEAI 173
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAenDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 174 LCPVGGGGLIAGLATAVKS-LRPRVKIVGVESVSTRNLSAALKAGKPTLQPRQHTLADGLATLTVGAEAFALARDRVDEV 252
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERnGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501342152 253 VQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMMAGLLPKLRGRK-------VALVVGGGN 307
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVlltpldnVVVVVCGGS 302
|
|
| ACT_ThrD-II-like |
cd04886 |
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and ... |
333-402 |
5.97e-18 |
|
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: 77.58 E-value: 5.97e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 333 VISDRPGGLAELSRVIASAGASIKDIAHDRAFSGPDVSAVRAVCTVETRDRAHITTLHRALRKHGFSLEI 402
Cdd:cd04886 4 ELPDRPGQLAKLLAVIAEAGANIIEVSHDRAFKTLPLGEVEVELTLETRGAEHIEEIIAALREAGYDVRR 73
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
26-319 |
1.65e-17 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 83.33 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 26 ESIPLSEITGARIVCKLDNFQRTGSFKERGARNALKLlsptARQRG---VVAASAGNHALGLAYHGRLLGIPVTVVMP-D 101
Cdd:COG0498 71 KAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSL----ALERGaktIVCASSGNGSAALAAYAARAGIEVFVFVPeG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 102 YAPLIKVTTCQRLGARVL-IRGvDFAEARAAADDLVVQEGLTYIHGFDaPAIIAGQGTIGLEILRQ---VPDveAILCPV 177
Cdd:COG0498 147 KVSPGQLAQMLTYGAHVIaVDG-NFDDAQRLVKELAADEGLYAVNSIN-PARLEGQKTYAFEIAEQlgrVPD--WVVVPT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 178 GGGGLIAGLATAVKSLR--------PRvkIVGVESVSTRNLSAALKAGKPTLQP-RQHTLADGLATLTvgAEAFALARDR 248
Cdd:COG0498 223 GNGGNILAGYKAFKELKelglidrlPR--LIAVQATGCNPILTAFETGRDEYEPeRPETIAPSMDIGN--PSNGERALFA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 249 VDE----VVQVKEEWIALAILRMIELEKTVVEGAGAVPLAAMM----AGLLPKlrGRKVALVV-GGGNIDPAVLSRVIEI 319
Cdd:COG0498 299 LREsggtAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRklreEGEIDP--DEPVVVLStGHGLKFPDAVREALGG 376
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
32-285 |
4.23e-13 |
|
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: 69.54 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 32 EITGARIVCKLDNFQRTGSFKERGARNALKLlsptARQRG---VVAASAGNHALGLAYHGRLLGIPVTVVMPDYAPLIKV 108
Cdd:cd01563 34 RLGGKNLYVKDEGLNPTGSFKDRGMTVAVSK----AKELGvkaVACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 109 TTCQRLGARVL-IRGvDF----AEARAAADDLVVqegltYIHGFDAPAIIAGQGTIGLEILRQ----VPDveAILCPVGG 179
Cdd:cd01563 110 AQALAYGATVLaVEG-NFddalRLVRELAEENWI-----YLSNSLNPYRLEGQKTIAFEIAEQlgweVPD--YVVVPVGN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 180 GGLIAGLATAVKSLR------PRVKIVGVESVSTRNLSAALKAGKPTLQP--RQHTLADGLAtltVGAEA-FALARDRVD 250
Cdd:cd01563 182 GGNITAIWKGFKELKelglidRLPRMVGVQAEGAAPIVRAFKEGKDDIEPveNPETIATAIR---IGNPAsGPKALRAVR 258
|
250 260 270
....*....|....*....|....*....|....*....
gi 501342152 251 E----VVQVKEEWIALAILRMIELEKTVVEGAGAVPLAA 285
Cdd:cd01563 259 EsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAG 297
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
22-286 |
7.65e-13 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 69.08 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 22 SPCPESIPLSEItGARIVCKLDNFQRTGSFKERGARNALKLLsptaRQRG---VVAASAGNHALGLAYHGRLLGIPVTVV 98
Cdd:PRK08329 59 HLTPPITPTVKR-SIKVYFKLDYLQPTGSFKDRGTYVTVAKL----KEEGineVVIDSSGNAALSLALYSLSEGIKVHVF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 99 MPDYAPLIKVTTCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEILRQVPDVEAILCPVG 178
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 179 GGGLIAGLATAVKSLRprvkIVGvESVSTRNLSAALKAGKPTLQPRQH---TLADGLATLTVG--AEAFALARDRVDEVV 253
Cdd:PRK08329 214 SGTLFLGIWKGFKELH----EMG-EISKMPKLVAVQAEGYESLCKRSKsenKLADGIAIPEPPrkEEMLRALEESNGFCI 288
|
250 260 270
....*....|....*....|....*....|...
gi 501342152 254 QVKEEWIaLAILRMIELEKTVVEGAGAVPLAAM 286
Cdd:PRK08329 289 SVGEEET-RAALHWLRRMGFLVEPTSAVALAAY 320
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
30-286 |
4.99e-12 |
|
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: 66.23 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 30 LSEITGARIVCKLDNFQRTGSFKERGARN----ALK--LLSPTARqrgVVAASAGNHALGLAYHGRLLGIPVTVVMPDYA 103
Cdd:COG0031 22 LSPGPGAEIYAKLESFNPGGSVKDRIALSmiedAEKrgLLKPGGT---IVEATSGNTGIGLAMVAAAKGYRLILVMPETM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 104 PLIKVTTCQRLGARV-LIRGVD-FAEARAAADDLVVQ-EGLTYIHGFDAPA-IIAGQGTIGLEILRQVP-DVEAILCPVg 178
Cdd:COG0031 99 SKERRALLRAYGAEVvLTPGAEgMKGAIDKAEELAAEtPGAFWPNQFENPAnPEAHYETTGPEIWEQTDgKVDAFVAGV- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 179 gggliaglAT---------AVKSLRPRVKIVGVESVStrnlSAALKAGKptlqPRQHTLaDGLATLTVGAeafALARDRV 249
Cdd:COG0031 178 --------GTggtitgvgrYLKERNPDIKIVAVEPEG----SPLLSGGE----PGPHKI-EGIGAGFVPK---ILDPSLI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 501342152 250 DEVVQVKEEwiaLAILRMIELEKTvvEG------AGAVPLAAM 286
Cdd:COG0031 238 DEVITVSDE---EAFAMARRLARE--EGilvgisSGAAVAAAL 275
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
30-258 |
1.61e-11 |
|
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: 64.46 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 30 LSEITGARIVCKLDNFQRTGSFKERGARNALKllspTARQRG-------VVAASAGNHALGLAYHGRLLGIPVTVVMPDY 102
Cdd:cd01561 11 LSPGTGAEIYAKLEFFNPGGSVKDRIALYMIE----DAEKRGllkpgttIIEPTSGNTGIGLAMVAAAKGYRFIIVMPET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 103 APLIKVTTCQRLGARV-LIRGVDF---AEARAAADDLVvQEGLTYIH--GFDAPA-IIAGQGTIGLEILRQVPD-VEAIL 174
Cdd:cd01561 87 MSEEKRKLLRALGAEViLTPEAEAdgmKGAIAKARELA-AETPNAFWlnQFENPAnPEAHYETTAPEIWEQLDGkVDAFV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 175 CPVGGGGLIAGLATAVKSLRPRVKIVGVESVStrnlSAALKAGKPTlqprQHTLADglatltVGAEaFA---LARDRVDE 251
Cdd:cd01561 166 AGVGTGGTITGVARYLKEKNPNVRIVGVDPVG----SVLFSGGPPG----PHKIEG------IGAG-FIpenLDRSLIDE 230
|
....*..
gi 501342152 252 VVQVKEE 258
Cdd:cd01561 231 VVRVSDE 237
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
48-176 |
1.72e-09 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 59.24 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 48 TGSFKERGARNALKLlsptARQRGV---VAASAGNHALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARV-LIRGV 123
Cdd:PRK08197 107 TGSFKARGLAVGVSR----AKELGVkhlAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELyLVDGL 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501342152 124 --DFAEARAAAddlVVQEGLtyihgFDA-----PAIIAGQGTIGLEILRQ----VPDVeaILCP 176
Cdd:PRK08197 183 isDAGKIVAEA---VAEYGW-----FDVstlkePYRIEGKKTMGLELAEQlgwrLPDV--ILYP 236
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
30-302 |
3.85e-08 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 54.97 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 30 LSEITGARIVCKLDNFQRTGSFKERGARNAL------KLLSPTarQRGVVAASAGNHALGLAYHGRLLGIPVTVVMPDYA 103
Cdd:PLN02556 68 VTEGCGAYIAAKQEMFQPTSSIKDRPALAMIedaekkNLITPG--KTTLIEPTSGNMGISLAFMAAMKGYKMILTMPSYT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 104 PLIKVTTCQRLGARVLI----RGVDfAEARAAADDLVVQEGLTYIHGFDAPAIIAGQ-GTIGLEILRQ-VPDVEAILCPV 177
Cdd:PLN02556 146 SLERRVTMRAFGAELVLtdptKGMG-GTVKKAYELLESTPDAFMLQQFSNPANTQVHfETTGPEIWEDtLGQVDIFVMGI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 178 GGGGLIAGLATAVKSLRPRVKIVGVESVStrnlSAALKAGKPTlqpRQHTLADGlatltVGAEAFALARDRVDEVVQVKE 257
Cdd:PLN02556 225 GSGGTVSGVGKYLKSKNPNVKIYGVEPAE----SNVLNGGKPG---PHHITGNG-----VGFKPDILDMDVMEKVLEVSS 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 501342152 258 EwIALAILRMIELEKTVVEG--AGAVPLAAMMAGLLPKLRGRKVALV 302
Cdd:PLN02556 293 E-DAVNMARELALKEGLMVGisSGANTVAALRLAKMPENKGKLIVTV 338
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
23-168 |
2.38e-07 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 52.00 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 23 PCPEsiPLSEITGARIVCKLDNFQRTGSFKERGARNALKllspTARQRG---VVAASAGNHALGLAYHGRLLGIPVTVVM 99
Cdd:TIGR00260 27 RAPA--LAANVGIKNLYVKELGHNPTLSFKDRGMAVALT----KALELGndtVLCASTGNTGAAAAAYAGKAGLKVVVLY 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501342152 100 P-DYAPLIKVTTCQRLGARVL-IRGvDFAEARAAADDLVvqeGLTYIHGFDA----PAIIAGQGTIGLEILRQVP 168
Cdd:TIGR00260 101 PaGKISLGKLAQALGYNAEVVaIDG-NFDDAQRLVKQLF---EDKPALGLNSansiPYRLEGQKTYAFEAVEQLG 171
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
30-167 |
6.20e-07 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 51.35 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 30 LSEITGARIVCKLDNFQRTGSFKERGARNALKLLSPTARQRGVVAaSAGNHALGLAYHGRLLGIPVTVVMPDYAPLIKVT 109
Cdd:PRK05638 74 ISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVA-SDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLI 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 501342152 110 TCQRLGARVLIRGVDFAEARAAADDLVVQEGLTYIHGFDAPAIIAGQGTIGLEILRQV 167
Cdd:PRK05638 153 QMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEI 210
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
36-306 |
2.07e-06 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 49.23 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 36 ARIVCKLDNFQRTGSFKERGARNALK------LLSPTarQRGVVAASAGNHALGLAYHGRLLGIPVTVVMPDYAPLIKVT 109
Cdd:PLN00011 32 ARIAAKLEMMEPCSSVKDRIAYSMIKdaedkgLITPG--KSTLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 110 TCQRLGARVLI--RGVDFAEARAAADDLVVQEGLTYI-HGFDAPAIIAGQ-GTIGLEILR-QVPDVEAILCPVGGGGLIA 184
Cdd:PLN00011 110 ILRALGAEVHLtdQSIGLKGMLEKAEEILSKTPGGYIpQQFENPANPEIHyRTTGPEIWRdSAGKVDILVAGVGTGGTAT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 185 GLATAVKSLRPRVKIVGVESVStrnlSAALKAGKPTLQprqhtLADGLATltvGAEAFALARDRVDEVVQVKEEWiALAI 264
Cdd:PLN00011 190 GVGKFLKEKNKDIKVCVVEPVE----SAVLSGGQPGPH-----LIQGIGS---GIIPFNLDLTIVDEIIQVTGEE-AIET 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 501342152 265 LRMIELEKTVVEG--AGAVPLAAMMAGLLPKLRGRKVALVVGGG 306
Cdd:PLN00011 257 AKLLALKEGLLVGisSGAAAAAALKVAKRPENAGKLIVVIFPSG 300
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
61-168 |
2.12e-04 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 43.33 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 61 KLLSPTARQRG----VVAASAGNHALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQRLGARVLIRGVDFAEA-RAAADD- 134
Cdd:PRK08206 104 ELTSGEVREKLgditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSvRLAAQEa 183
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 501342152 135 -----LVVQ----EGLTYIHGFdapaIIAGQGTIGLEILRQVP 168
Cdd:PRK08206 184 qengwVVVQdtawEGYEEIPTW----IMQGYGTMADEAVEQLK 222
|
|
| ACT_4 |
pfam13291 |
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ... |
328-395 |
2.57e-04 |
|
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: 39.46 E-value: 2.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501342152 328 TRFAAVISDRPGGLAELSRVIASAGASIKDI-AHDRAFSGPdvsaVRAVCTVETRDRAHITTLHRALRK 395
Cdd:pfam13291 6 VDLEVEAIDRPGLLADITQVISEEKANIVSVnAKTRKKDGT----AEIKITLEVKDVEHLERLMAKLRR 70
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
30-151 |
3.80e-04 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 42.16 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 30 LSEITGARIVCKLDNFQRTGSFKERGARNALKllspTARQRG-------VVAASAGNHALGLAYHGRLLGIPVTVVMPDY 102
Cdd:PRK10717 22 ASEATGCEILGKAEFLNPGGSVKDRAALNIIW----DAEKRGllkpggtIVEGTAGNTGIGLALVAAARGYKTVIVMPET 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 501342152 103 APLIKVTTCQRLGAR-VLIRGVDFAE-------ARAAADDLVVQEGLTYI--HGFDAPA 151
Cdd:PRK10717 98 QSQEKKDLLRALGAElVLVPAAPYANpnnyvkgAGRLAEELVASEPNGAIwaNQFDNPA 156
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
33-166 |
4.82e-04 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 42.03 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 33 ITGARIVCKLDNFQRTGSFKERGARNalkLLSPTARQR--GVVAASAGNHALGLAYHGRLLGIPVTVVMPDYAPLIKVTT 110
Cdd:PRK06450 62 IKKGNIWFKLDFLNPTGSYKDRGSVT---LISYLAEKGikQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQ 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 501342152 111 CQRLGARVL-IRGVDFAEARAAAddlvvQEGLTYIHGFDAPAIIAGQGTIGLEILRQ 166
Cdd:PRK06450 139 IESYGAEVVrVRGSREDVAKAAE-----NSGYYYASHVLQPQFRDGIRTLAYEIAKD 190
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
36-302 |
7.05e-04 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 41.45 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 36 ARIVCKLDNFQRTGSFKERGARNALKllspTARQRGVVAA--------SAGNHALGLAYHGRLLGIPVTVVMPDYAPLIK 107
Cdd:PLN02565 30 ARIAAKLEMMEPCSSVKDRIGYSMIT----DAEEKGLIKPgesvliepTSGNTGIGLAFMAAAKGYKLIITMPASMSLER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 108 VTTCQRLGARVLI----RGVDFAEARAaaDDLVVQEGLTYI-HGFDAPAIIAGQ-GTIGLEILRQVP-DVEAILCPVGGG 180
Cdd:PLN02565 106 RIILLAFGAELVLtdpaKGMKGAVQKA--EEILAKTPNSYIlQQFENPANPKIHyETTGPEIWKGTGgKVDAFVSGIGTG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 181 GLIAGLATAVKSLRPRVKIVGVESVStrnlSAALKAGKPTLQPRQHTLAdglatltvGAEAFALARDRVDEVVQV-KEEW 259
Cdd:PLN02565 184 GTITGAGKYLKEQNPDIKLYGVEPVE----SAVLSGGKPGPHKIQGIGA--------GFIPGVLDVDLLDEVVQVsSDEA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 501342152 260 IALAilRMIELEKTVVEG--AGAVPLAAMMAGLLPKLRGRKVALV 302
Cdd:PLN02565 252 IETA--KLLALKEGLLVGisSGAAAAAAIKIAKRPENAGKLIVVI 294
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
37-177 |
7.12e-04 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 41.23 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 37 RIVCKLDNFQRTGSFKERGA----RNALKLlsptaRQRGVVAASAGNHALGLAYHGRLLGIPVTVVMPDYAPLIKVTTCQ 112
Cdd:PRK06381 32 KIYLKFEGANPTGTQKDRIAeahvRRAMRL-----GYSGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEME 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501342152 113 RLGARVLIRGVDFAEARAAADDLVVQEGLtyihgFDA------PAI-IAGQGTIGLEILRQVPDV-EAILCPV 177
Cdd:PRK06381 107 KYGAEIIYVDGKYEEAVERSRKFAKENGI-----YDAnpgsvnSVVdIEAYSAIAYEIYEALGDVpDAVAVPV 174
|
|
| ACT_MalLac-Enz |
cd04887 |
ACT_MalLac-Enz CD includes the N-terminal ACT domain of putative NAD-dependent malic enzyme 1, ... |
334-394 |
6.89e-03 |
|
ACT_MalLac-Enz CD includes the N-terminal ACT domain of putative NAD-dependent malic enzyme 1, Bacillus subtilis YqkI and related domains; The ACT_MalLac-Enz CD includes the N-terminal ACT domain of putative NAD-dependent malic enzyme 1, Bacillus subtilis YqkI, a malolactic enzyme (MalLac-Enz) which converts malate to lactate, and other related ACT domains. The yqkJ product is predicted to convert malate directly to lactate, as opposed to related malic enzymes that convert malate to pyruvate. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153159 Cd Length: 74 Bit Score: 35.34 E-value: 6.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501342152 334 ISDRPGGLAELSRVIASAGASIKDIahDRAFSGPDVsAVRAVcTVETRDRAHITTLHRALR 394
Cdd:cd04887 6 LPNRPGMLGRVTTAIGEAGGDIGAI--DLVEQGRDY-TVRDI-TVDAPSEEHAETIVAAVR 62
|
|
| SpoT |
COG0317 |
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription]; |
328-395 |
8.82e-03 |
|
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
Pssm-ID: 440086 [Multi-domain] Cd Length: 722 Bit Score: 38.21 E-value: 8.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501342152 328 TRFAAVI----SDRPGGLAELSRVIASAGASIKDIahdrAFSGPDVSAVRAVCTVETRDRAHITTLHRALRK 395
Cdd:COG0317 643 GVFPVDIrieaLDRPGLLADITSVIAEEKINILSV----NTRSRDDGTATIRFTVEVRDLDHLARVLRKLRK 710
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
48-170 |
9.01e-03 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 38.26 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342152 48 TGSFKERGArnaLKLLSPTARQR-------GVVAASAGNHALGLAYHGRLLGIPVTVVMP----DYAPLIKVTTCqrlGA 116
Cdd:PLN02569 162 TGSFKDLGM---TVLVSQVNRLRkmakpvvGVGCASTGDTSAALSAYCAAAGIPSIVFLPadkiSIAQLVQPIAN---GA 235
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501342152 117 RVLIRGVDFaearaaaDDL--VVQEGLTYIHGFDAPAI----IAGQGTIGLEILRQ----VPDV 170
Cdd:PLN02569 236 LVLSIDTDF-------DGCmrLIREVTAELPIYLANSLnslrLEGQKTAAIEILQQfdweVPDW 292
|
|
| |
