|
Name |
Accession |
Description |
Interval |
E-value |
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
1-323 |
5.52e-150 |
|
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: 427.92 E-value: 5.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 1 MLSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHA 80
Cdd:COG1171 5 MPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 81 QGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGL 160
Cdd:COG1171 85 QGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 161 EIIEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQT 240
Cdd:COG1171 165 EILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 241 FPVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTVCLLSGGNIDVQTIAQVVDRGLV 320
Cdd:COG1171 245 FEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEILERGLV 324
|
...
gi 499662032 321 AAG 323
Cdd:COG1171 325 GEG 327
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
21-399 |
2.38e-144 |
|
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: 415.68 E-value: 2.38e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVMPE 100
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 101 NTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLPDVDTLLAPVGGGG 180
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 181 LISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTFPVIEALVDELVTVNEEQIA 260
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 261 QAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTVCLLSGGNIDVQTIAQVVDRGLVAAGRYLKIRIELNDAPGALG 340
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPGALY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 499662032 341 RLALLLGECRANIYHVSHDRHRLGIPLGRAEVNLELETRGSEHVREILAALAGADYKVV 399
Cdd:TIGR01127 321 HLLESIAEARANIVKIDHDRLSKEIPPGFAMVEITLETRGKEHLDEILKILRDMGYNFY 379
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
7-307 |
3.16e-141 |
|
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: 404.95 E-value: 3.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 7 IRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALS 86
Cdd:cd01562 4 ILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGVAYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 87 AARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDL 166
Cdd:cd01562 84 AKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEILEQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 167 PDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTFPVIEA 246
Cdd:cd01562 164 PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEIIRK 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499662032 247 LVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTVCLLSGGNID 307
Cdd:cd01562 244 LVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
1-402 |
2.58e-127 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 373.07 E-value: 2.58e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 1 MLSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHA 80
Cdd:PRK07334 4 MVTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 81 QGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGL 160
Cdd:PRK07334 84 QGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 161 EIIEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIvgLSGAHSLADGIALKRIGEQT 240
Cdd:PRK07334 164 EMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKGVAL--PCGGSTIAEGIAVKQPGQLT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 241 FPVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLhAARPLARGRTVCL-LSGGNIDVQTIAQVVDRGL 319
Cdd:PRK07334 242 LEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALL-AYPERFRGRKVGLvLSGGNIDTRLLANVLLRGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 320 VAAGRYLKIRIELNDAPGALGRLALLLGECRANIYHVSHDRHRLGIPLGRAEVNLELETRGSEHVREILAALAGADYKVV 399
Cdd:PRK07334 321 VRAGRLARLRVDIRDRPGALARVTALIGEAGANIIEVSHQRLFTDLPAKGAELELVIETRDAAHLQEVIAALRAAGFEAR 400
|
...
gi 499662032 400 ALD 402
Cdd:PRK07334 401 LVE 403
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
2-321 |
7.92e-120 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 351.73 E-value: 7.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 2 LSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQ 81
Cdd:PRK08638 9 VAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 82 GVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLE 161
Cdd:PRK08638 89 GVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 162 IIEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTF 241
Cdd:PRK08638 169 ILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 242 PVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHA--ARPLARGRTVCLLSGGNIDVQTIAQVVDRGL 319
Cdd:PRK08638 249 EIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGklDQYIQNKKVVAIISGGNVDLSRVSQITGHVV 328
|
..
gi 499662032 320 VA 321
Cdd:PRK08638 329 AA 330
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
19-306 |
1.37e-97 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 300.52 E-value: 1.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 19 RRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVM 98
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 99 PENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLPD-VDTLLAPVG 177
Cdd:PRK09224 99 PVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAVFVPVG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 178 GGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTFPVIEALVDELVTVNEE 257
Cdd:PRK09224 179 GGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDTD 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499662032 258 QIAQAIVALMEKTRLVVEGAGAVGLAALL-HAARPLARGRT-VCLLSGGNI 306
Cdd:PRK09224 259 EICAAIKDVFEDTRSIAEPAGALALAGLKkYVAQHGIEGETlVAILSGANM 309
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
2-321 |
2.09e-96 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 291.48 E-value: 2.09e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 2 LSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQ 81
Cdd:PRK07476 1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 82 GVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLE 161
Cdd:PRK07476 81 ALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 162 IIEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLAD----GIALKriG 237
Cdd:PRK07476 161 ILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslggGIGLD--N 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 238 EQTFPVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTVCLLSGGNIDVQTIAQVVDR 317
Cdd:PRK07476 239 RYTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELHRRIING 318
|
....
gi 499662032 318 GLVA 321
Cdd:PRK07476 319 EVAD 322
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
3-317 |
7.95e-95 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 287.30 E-value: 7.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 3 SLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQG 82
Cdd:PRK07048 7 TYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 83 VALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEI 162
Cdd:PRK07048 87 IALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 163 IEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTFP 242
Cdd:PRK07048 167 FEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFP 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499662032 243 VIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTVCLLSGGNIDVQTIAQVVDR 317
Cdd:PRK07048 247 IIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLSG 321
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
1-323 |
3.89e-94 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 289.01 E-value: 3.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 1 MLSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHA 80
Cdd:PRK08639 6 TVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 81 QGVALSAARLGVAATVVMPENTPLAKMQATRGYGA---EVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGT 157
Cdd:PRK08639 86 QGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 158 IGLEIIEDL---PDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALK 234
Cdd:PRK08639 166 VAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 235 RIGEQTFPVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLaRGRT-VCLLSGGNIDVQTIAQ 313
Cdd:PRK08639 246 RVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEI-KGKTvVCVISGGNNDIERMPE 324
|
330
....*....|
gi 499662032 314 VVDRGLVAAG 323
Cdd:PRK08639 325 IKERSLIYEG 334
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
21-324 |
8.77e-91 |
|
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: 282.78 E-value: 8.77e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVMPE 100
Cdd:TIGR01124 18 TPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGLKALIVMPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 101 NTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLP-DVDTLLAPVGGG 179
Cdd:TIGR01124 98 TTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVAnPLDAVFVPVGGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 180 GLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTFPVIEALVDELVTVNEEQI 259
Cdd:TIGR01124 178 GLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDIVTVDTDEV 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499662032 260 AQAIVALMEKTRLVVEGAGAVGLAAL-LHAARPLARGRT-VCLLSGGNIDVQTIAQVVDRGLVAAGR 324
Cdd:TIGR01124 258 CAAIKDLFEDTRAVAEPAGALALAGLkKYVALHGIRGQTlVAILSGANMNFHRLRYVSERCELGEQR 324
|
|
| PLN02970 |
PLN02970 |
serine racemase |
2-314 |
5.86e-86 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 265.00 E-value: 5.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 2 LSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQ 81
Cdd:PLN02970 9 ADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 82 GVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLE 161
Cdd:PLN02970 89 ALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 162 IIEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIAlKRIGEQTF 241
Cdd:PLN02970 169 FLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLR-ASLGDLTW 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499662032 242 PVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLH---AARPLARGRTVC--LLSGGNIDVQTIAQV 314
Cdd:PLN02970 248 PVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSdsfRSNPAWKGCKNVgiVLSGGNVDLGVLWES 325
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
7-316 |
7.16e-82 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 253.85 E-value: 7.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 7 IRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALS 86
Cdd:PRK06815 7 ILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 87 AARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDL 166
Cdd:PRK06815 87 AKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 167 PDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALK-RIGEQTFPVIE 245
Cdd:PRK06815 167 PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGvEPGAITFPLCQ 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499662032 246 ALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAArPLARGRTVCL-LSGGNIDVQTIAQVVD 316
Cdd:PRK06815 247 QLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLA-PRYQGKKVAVvLCGKNIVLEKYLEAVS 317
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
19-303 |
1.42e-81 |
|
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: 252.62 E-value: 1.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 19 RRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVM 98
Cdd:pfam00291 6 GPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 99 PENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRL-QHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDL-PDVDTLLAPV 176
Cdd:pfam00291 86 PEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELaAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLgGDPDAVVVPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 177 GGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRI-GEQTFPVIEALVDELVTVN 255
Cdd:pfam00291 166 GGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVGEVVTVS 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499662032 256 EEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPL--ARGRTVCLLSG 303
Cdd:pfam00291 246 DEEALEAMRLLARREGIVVEPSSAAALAALKLALAGElkGGDRVVVVLTG 295
|
|
| COG2061 |
COG2061 |
Uncharacterized conserved protein, contains ACT domain [General function prediction only]; |
1-402 |
6.32e-80 |
|
Uncharacterized conserved protein, contains ACT domain [General function prediction only];
Pssm-ID: 441664 [Multi-domain] Cd Length: 401 Bit Score: 251.89 E-value: 6.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 1 MLSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHA 80
Cdd:COG2061 1 LLLLLDEEAAAAALAVVVVTTPLLLSSSSSLSVGLVVLLKEENLQTTGSFKRRGAYKLIALLLEEEEKGGVAAAAAGNAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 81 QGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGL 160
Cdd:COG2061 81 QAAAAAAALGGISAIVVMPPPPPLPKVAATRGGGAVVVVVGGDDDAAAAAAAALQEEEGGFFHHPDDDDDVIAGGGGGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 161 EIIEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQT 240
Cdd:COG2061 161 EILELLPDVVVVVVGGGGGGGGGGAAAAAKAKRPPIVIVGVQAEAAAAAPSSLAAGIEVVPGGGTTIADGIAVVKPGGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 241 FPVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAArPLARGRTVCLLSGGNIDVQTIAQVVDRGLV 320
Cdd:COG2061 241 FIIIRKVVDDVVVVVEEEIAAALLLLLERKKKVVEGAAAAAAAAALKKK-PLRGKKVVVVLSGGNIDDLLLLRIIIKGLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 321 AAGRYLKIRIELNDAPGALGRLALLLGECRANIYHVSHDRHRLGIPLGRAEVNLELETRGSEHVREILAALAGADYKVVA 400
Cdd:COG2061 320 AAGRRLVLLVVLPDRPGQLLRVLQPIAELGANIISVVHERENSKTPRGEVEVEVVLETRGEEHLEEIIAALREAGYNVRR 399
|
..
gi 499662032 401 LD 402
Cdd:COG2061 400 VG 401
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
19-336 |
1.02e-79 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 255.11 E-value: 1.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 19 RRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVM 98
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 99 PENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLPD-VDTLLAPVG 177
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGpLDAIFVPVG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 178 GGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTFPVIEALVDELVTVNEE 257
Cdd:PRK12483 196 GGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVDEVVTVSTD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 258 QIAQAIVALMEKTRLVVEGAGAVGLAAL-LHAARPLARGRT-VCLLSGGNIDVQTIAQVVDRGLVAAGRYLKIRIELNDA 335
Cdd:PRK12483 276 ELCAAIKDIYDDTRSITEPAGALAVAGIkKYAEREGIEGQTlVAIDSGANVNFDRLRHVAERAELGEQREAIIAVTIPEQ 355
|
.
gi 499662032 336 P 336
Cdd:PRK12483 356 P 356
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
21-304 |
4.84e-72 |
|
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: 226.24 E-value: 4.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFM--ARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVM 98
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLIllAEEEGKLPKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 99 PENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRL-QHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLPD--VDTLLAP 175
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELaEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLGGqkPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 176 VGGGGLISEVATAIKALRPTVRVIGVEAaaapaallsrrqghivglsgahsladgialkrigeqtfpviealvdELVTVN 255
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499662032 256 EEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRT-VCLLSGG 304
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTvVVILTGG 244
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
1-312 |
7.15e-72 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 227.92 E-value: 7.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 1 MLSLTQIRAAADALQGQFRRTELIHSHFFSEQIGlPLYFKCENLQRSGSFKVRGAFHFM--ARQPAqrlaAGVVTASAGN 78
Cdd:PRK08246 4 MITRSDVRAAAQRIAPHIRRTPVLEADGAGFGPA-PVWLKLEHLQHTGSFKARGAFNRLlaAPVPA----AGVVAASGGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 79 HAQGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTI 158
Cdd:PRK08246 79 AGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 159 GLEIIEDLPDVDTLLAPVGGGGLISEVATaikALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGE 238
Cdd:PRK08246 159 GLEIEEQAPGVDTVLVAVGGGGLIAGIAA---WFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGE 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499662032 239 QTFPVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTVC-LLSGGNIDVQTIA 312
Cdd:PRK08246 236 IAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGERVAvVLCGANTDPATLA 310
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
2-316 |
1.06e-71 |
|
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.
Pssm-ID: 132036 [Multi-domain] Cd Length: 317 Bit Score: 227.81 E-value: 1.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 2 LSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQ 81
Cdd:TIGR02991 1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 82 GVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLE 161
Cdd:TIGR02991 81 ALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 162 IIEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLAD----GIALKriG 237
Cdd:TIGR02991 161 VVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslggGIGLD--N 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499662032 238 EQTFPVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLhAARPLARGRTVCLLSGGNIDVQTIAQVVD 316
Cdd:TIGR02991 239 RVTFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALL-AGKIKNPGPCAVIVSGRNIDMDLHKRIID 316
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
30-283 |
1.53e-68 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 227.50 E-value: 1.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 30 SEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVMPENTPLAKMQA 109
Cdd:PLN02550 119 SERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 110 TRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLPD-VDTLLAPVGGGGLISEVATA 188
Cdd:PLN02550 199 VERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGpLHAIFVPVGGGGLIAGIAAY 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 189 IKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTFPVIEALVDELVTVNEEQIAQAIVALME 268
Cdd:PLN02550 279 VKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSRDAICASIKDMFE 358
|
250
....*....|....*
gi 499662032 269 KTRLVVEGAGAVGLA 283
Cdd:PLN02550 359 EKRSILEPAGALALA 373
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
1-314 |
6.28e-68 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 218.87 E-value: 6.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 1 MLSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMAR-QPAQRLAAGVVTASAGNH 79
Cdd:PRK06608 4 LQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLElKEQGKLPDKIVAYSTGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 80 AQGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTvfDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIG 159
Cdd:PRK06608 84 GQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNT--RQEAEEKAKEDEEQGFYYIHPSDSDSTIAGAGTLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 160 LEIIEDL-PDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGA-HSLADGIALKRIG 237
Cdd:PRK06608 162 YEALQQLgFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVS 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499662032 238 EQTFPVIEALvDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLH-AARPLARGRTVCLLSGGNIDVQTIAQV 314
Cdd:PRK06608 242 ARTFEYLKKL-DDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNwLKTQSKPQKLLVILSGGNIDPILYNEL 318
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
1-315 |
1.61e-59 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 196.37 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 1 MLSLTQIRAAADALQGQFRRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGA---FHFMARQpaQRLAAGVVTASAG 77
Cdd:PRK06110 2 MFTLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGlvyFDRLARR--GPRVRGVISATRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 78 NHAQGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFdHPLIMAGQGT 157
Cdd:PRK06110 80 NHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 158 IGLEIIEDLPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIG 237
Cdd:PRK06110 159 YALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPD 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499662032 238 EQTFPVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHaARPLARGRTVCL-LSGGNIDVQTIAQVV 315
Cdd:PRK06110 239 PEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQ-ERERLAGKRVGLvLSGGNIDRAVFARVL 316
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
13-315 |
1.69e-53 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 181.75 E-value: 1.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 13 ALQGQFRRTELIHSHFFSEQIGLplYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAGVVTASAGNHAQGVALSAARLGV 92
Cdd:PRK08813 28 AAQARLRRYLSPTPLHYAERFGV--WLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 93 AATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLPDVdtL 172
Cdd:PRK08813 106 QAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAHAPDV--V 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 173 LAPVGGGGLISEVATAIKAlrPTVRVIGVEAAAAPAALLSRRqGHIVGLSGAHSLADGIALKRIGEQTFPVIEALVDELV 252
Cdd:PRK08813 184 IVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499662032 253 TVNEEQIAQAIVALMEKTRLVVEGAGAVGLAallhAARPLARGRTVCLLSGGNIDVQTIAQVV 315
Cdd:PRK08813 261 IVREAELRETLVRLALEEHVIAEGAGALALA----AGRRVSGKRKCAVVSGGNIDATVLATLL 319
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
21-287 |
3.04e-43 |
|
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: 153.61 E-value: 3.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHF--MARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVM 98
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLcqKSAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 99 PENTPLAKMQATRGYGAEVVLHGTVFDDAqEEALRLQHTHDL---LYVPPFDHPLIMAGQGTIGLEIIEDLPD---VDTL 172
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVWWEA-DNYLREELAENDpgpVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 173 LAPVGGGGLISEVATAI-KALRPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIALKRIGEQTF------PVIE 245
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLeRNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALeyaqehNIKS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499662032 246 ALVDELvtvneeQIAQAIVALMEKTRLVVEGAGAVGLAALLH 287
Cdd:cd06448 241 EVVSDR------DAVQACLRFADDERILVEPACGAALAVVYS 276
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
21-303 |
2.32e-32 |
|
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: 124.63 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLP-LYFKCENLQRSGSFKVRGAFHFMARqpAQRLAA-GVVTASAGNHAQGVALSAARLGVAATVVM 98
Cdd:cd01563 23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTVAVSK--AKELGVkAVACASTGNTSASLAAYAARAGIKCVVFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 99 PENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHdLLYVPPFDHPLIMAGQGTIGLEIIEDL----PDVdtLLA 174
Cdd:cd01563 101 PAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN-WIYLSNSLNPYRLEGQKTIAFEIAEQLgwevPDY--VVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 175 PVGGGGLISEVATAIKALRPT------VRVIGVEAAAAPAALLSRRQG--HIVGLSGAHSLADGIalkRIG-----EQTF 241
Cdd:cd01563 178 PVGNGGNITAIWKGFKELKELglidrlPRMVGVQAEGAAPIVRAFKEGkdDIEPVENPETIATAI---RIGnpasgPKAL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499662032 242 PVIEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARP--LARG-RTVCLLSG 303
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgiIDKGeRVVVVLTG 319
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
21-303 |
5.78e-29 |
|
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: 116.84 E-value: 5.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFhFMARQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVMPE 100
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQ-VAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 101 N-TPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFdHPLIMAGQGTIGLEIIEDLPDV-DTLLAPVGG 178
Cdd:COG0498 146 GkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLGRVpDWVVVPTGN 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 179 GGLISEVATAIKALR--------PtvRVIGVEAAAAPAALLSRRQGH-IVGLSGAHSLADGIalkRIGEqtfPV-IEALV 248
Cdd:COG0498 225 GGNILAGYKAFKELKelglidrlP--RLIAVQATGCNPILTAFETGRdEYEPERPETIAPSM---DIGN---PSnGERAL 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499662032 249 DEL-------VTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARP--LARG-RTVCLLSG 303
Cdd:COG0498 297 FALresggtaVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDePVVVLSTG 361
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
20-298 |
1.09e-25 |
|
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: 105.29 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 20 RTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHfMARQPAQR--LAAG--VVTASAGNHAQGVALSAARLGVAAT 95
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALY-MIEDAEKRglLKPGttIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 96 VVMPENTPLAKMQATRGYGAEVVLHGTVFDD----AQEEALRLQHTHDLLYVP-PFDHPL-IMAGQGTIGLEIIEDLPD- 168
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLnQFENPAnPEAHYETTAPEIWEQLDGk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 169 VDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAaaapaallsrrQGHIV---GLSGAHSLAdGIALKRIGEQtfpVIE 245
Cdd:cd01561 161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDP-----------VGSVLfsgGPPGPHKIE-GIGAGFIPEN---LDR 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499662032 246 ALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTV 298
Cdd:cd01561 226 SLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTI 278
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
20-301 |
1.71e-21 |
|
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: 93.96 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 20 RTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHfMARQpAQR---LAAG--VVTASAGNHAQGVALSAARLGVAA 94
Cdd:COG0031 13 NTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALS-MIED-AEKrglLKPGgtIVEATSGNTGIGLAMVAAAKGYRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 95 TVVMPENTPLAKMQATRGYGAEVVL----HGTvfDDAQEEALRLQHTHDLLYVP-PFDHPL-IMAGQGTIGLEIIEDLP- 167
Cdd:COG0031 91 ILVMPETMSKERRALLRAYGAEVVLtpgaEGM--KGAIDKAEELAAETPGAFWPnQFENPAnPEAHYETTGPEIWEQTDg 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 168 DVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEaaAAPAALLSRrqghivGLSGAHsladgiALKRIGEQTFP--VIE 245
Cdd:COG0031 169 KVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVE--PEGSPLLSG------GEPGPH------KIEGIGAGFVPkiLDP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499662032 246 ALVDELVTVNEEQIAQAIVALMEKTRLVVEG-AGAVGLAALLHAARPLARGRTVCLL 301
Cdd:COG0031 235 SLIDEVITVSDEEAFAMARRLAREEGILVGIsSGAAVAAALRLAKRLGPGKTIVTIL 291
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
21-304 |
9.48e-17 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 81.20 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLP-LYFKCENLQRSGSFKVRGAFhfMARQPAQRLAA-GVVTASAGNHAQGVALSAARLGVAATVVM 98
Cdd:PRK08197 80 TPLLPLPRLGKALGIGrLWVKDEGLNPTGSFKARGLA--VGVSRAKELGVkHLAMPTNGNAGAAWAAYAARAGIRATIFM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 99 PENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIE----DLPDVdtLLA 174
Cdd:PRK08197 158 PADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEqlgwRLPDV--ILY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 175 PVGGG-GLISeVATAIKAL---------RPTVRVIGVEAAAAPAALLSRRQGHIVGLSGAHSLADGIAL-KRIGEqtFPV 243
Cdd:PRK08197 236 PTGGGvGLIG-IWKAFDELealgwiggkRPRLVAVQAEGCAPIVKAWEEGKEESEFWEDAHTVAFGIRVpKALGD--FLV 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499662032 244 IEALVDE---LVTVNEEQI--AQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTVCLLSGG 304
Cdd:PRK08197 313 LDAVRETggcAIAVSDDAIlaAQRELAREEGLFACPEGAATFAAARQLRESGWLKGDERVVLFNTG 378
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
1-290 |
1.15e-16 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 81.08 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 1 MLSLTQIRAAADALQG--QFRRTELIHSHFFSEQIGL-PLYFKCENlQRSG--SFKVRGAFHFMARQPAQRL-------- 67
Cdd:PRK08206 23 LLSQEEAKKARAFHQSfpGYAPTPLVALPDLAAELGVgSILVKDES-YRFGlnAFKALGGAYAVARLLAEKLgldisels 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 68 -----------AAG---VVTASAGNHAQGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGTVFDDAQEEALR 133
Cdd:PRK08206 102 feeltsgevreKLGditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 134 LQHTHDLLYV----------PPFDhplIMAGQGTIGLEIIEDLPDVDT------LLAPVGG--GGLISEVATAIKALRPT 195
Cdd:PRK08206 182 EAQENGWVVVqdtawegyeeIPTW---IMQGYGTMADEAVEQLKEMGVppthvfLQAGVGSlaGAVLGYFAEVYGEQRPH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 196 VRVigVEAAAAPAALLSRRQGHIVGLSGA-HSLADGIAlkrIGE---QTFPVIEALVDELVTVNEEQIAQAIVALMEK-- 269
Cdd:PRK08206 259 FVV--VEPDQADCLYQSAVDGKPVAVTGDmDTIMAGLA---CGEpnpLAWEILRNCADAFISCPDEVAALGMRILANPlg 333
|
330 340
....*....|....*....|...
gi 499662032 270 --TRLVVEGAGAVGLAALLHAAR 290
Cdd:PRK08206 334 gdPPIVSGESGAVGLGALAALMT 356
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
32-285 |
5.42e-16 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 78.71 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 32 QIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAAgVVTASAGNHAQGVALSAARLGVAATVVMPENTPLAKMQATR 111
Cdd:PRK08329 69 KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINE-VVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 112 GYGAEvvLHGTVFD--DAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLPDVDTLLAPVGGGGLISEVATAI 189
Cdd:PRK08329 148 RLGAE--LHFVEGDrmEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIWKGF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 190 KALR------PTVRVIGVEAAAAPAalLSRRQghivglSGAHSLADGIAL---KRIgEQTFPVIEALVDELVTVNEEQIA 260
Cdd:PRK08329 226 KELHemgeisKMPKLVAVQAEGYES--LCKRS------KSENKLADGIAIpepPRK-EEMLRALEESNGFCISVGEEETR 296
|
250 260
....*....|....*....|....*
gi 499662032 261 QAIVALMeKTRLVVEGAGAVGLAAL 285
Cdd:PRK08329 297 AALHWLR-RMGFLVEPTSAVALAAY 320
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
21-286 |
6.14e-16 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 79.09 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFfSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRlAAGVVTASAGNHAQGVALSAARLGVAATVVMPE 100
Cdd:PRK05638 67 TPLIRARI-SEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYA-ANGFIVASDGNAAASVAAYSARAGKEAFVVVPR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 101 NTPLAKMQATRGYGAEVVLHGTVFDDAQEEALRLQHTHDLLYVPPFDHPLIMAGQGTIGLEIIEDLpDVDTLLAPVGGGG 180
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEI-NPTHVIVPTGSGS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 181 LI-------SEVATaIKALRPTVRVIGVEAAAApaallSRRQGHIVGLSGA--HSLADGIALKRigeqtfPVIEALVDE- 250
Cdd:PRK05638 224 YLysiykgfKELLE-IGVIEEIPKLIAVQTERC-----NPIASEILGNKTKcnETKALGLYVKN------PVMKEYVSEa 291
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499662032 251 -------LVTVNEEQIAQAIVALMEKTrLVVEGAGAVGLAALL 286
Cdd:PRK05638 292 ikesggtAVVVNEEEIMAGEKLLAKEG-IFAELSSAVVMPALL 333
|
|
| ACT_ThrD-II-like |
cd04886 |
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and ... |
328-399 |
8.94e-15 |
|
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains; This CD includes the C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains. The Escherichia coli tdcB gene product, ThrD-II, anaerobically catalyzes the pyridoxal phosphate-dependent dehydration of L-threonine and L-serine to ammonia and to alpha-ketobutyrate and pyruvate, respectively. Tetrameric ThrD-II is subject to allosteric activation by AMP, inhibition by alpha-keto acids, and catabolite inactivation by several metabolites of glycolysis and the citric acid cycle. Also included in this CD are N-terminal ACT domains present in smaller (~170 a.a.) archaeal proteins of unknown function. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153158 [Multi-domain] Cd Length: 73 Bit Score: 68.72 E-value: 8.94e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499662032 328 IRIELNDAPGALGRLALLLGECRANIYHVSHDRHRLGIPLGRAEVNLELETRGSEHVREILAALAGADYKVV 399
Cdd:cd04886 1 LRVELPDRPGQLAKLLAVIAEAGANIIEVSHDRAFKTLPLGEVEVELTLETRGAEHIEEIIAALREAGYDVR 72
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
21-298 |
5.32e-13 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 69.50 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFhFMARQPAQR--LAAG--VVTASAGNHAQGVALSAARLGVAATV 96
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAAL-NIIWDAEKRglLKPGgtIVEGTAGNTGIGLALVAAARGYKTVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 97 VMPENTPLAKMQATRGYGAEVVL----------HGTVFDDAQEEALRLQHTHDLLYVPPFDHPL-IMAGQGTIGLEIIED 165
Cdd:PRK10717 93 VMPETQSQEKKDLLRALGAELVLvpaapyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNPAnREAHYETTGPEIWEQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 166 LP-DVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEaaAAPAALLSR-RQGHIVglSGAHSLADGIALKRIgeqTFPV 243
Cdd:PRK10717 173 TDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLAD--PTGSALYSYyKTGELK--AEGSSITEGIGQGRI---TANL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499662032 244 IEALVDELVTVNEEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTV 298
Cdd:PRK10717 246 EGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTI 300
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
71-301 |
5.58e-11 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 64.03 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 71 VVTASAGNHAQGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHGT---VFDDAQEEALRLQHTHDLLYVPPFD 147
Cdd:PLN03013 178 LVEPTSGNTGIGLAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPakgMTGAVQKAEEILKNTPDAYMLQQFD 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 148 HPL-IMAGQGTIGLEIIEDLP-DVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEaaAAPAALLSRrqghivGLSGAH 225
Cdd:PLN03013 258 NPAnPKIHYETTGPEIWDDTKgKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVE--PTESDILSG------GKPGPH 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499662032 226 SladgiaLKRIGEQTFP--VIEALVDELVTVNEEQIAQAIVALMEKTRLVVE-GAGAVGLAALLHAARPLARGRTVCLL 301
Cdd:PLN03013 330 K------IQGIGAGFIPknLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGiSSGAAAAAAIKVAKRPENAGKLIAVS 402
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
5-202 |
6.69e-11 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 63.44 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 5 TQIRAAADALQGqfrRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFMARQPAQRLAA----GVVTASAGNHA 80
Cdd:PLN02556 47 TKIKTDASQLIG---KTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITpgktTLIEPTSGNMG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 81 QGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLH-------GTVfddaQEEALRLQHTHDLLYVPPFDHPL-IM 152
Cdd:PLN02556 124 ISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTdptkgmgGTV----KKAYELLESTPDAFMLQQFSNPAnTQ 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499662032 153 AGQGTIGLEIIED-LPDVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVE 202
Cdd:PLN02556 200 VHFETTGPEIWEDtLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVE 250
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
40-304 |
8.89e-08 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 53.47 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 40 KCENLQRSGSFKVRGAFHFMARQPAQRL----AAGVVTASAGNHAQGVALSAARLGVAATVVMPENTPLAKMQATRGYGA 115
Cdd:PLN00011 37 KLEMMEPCSSVKDRIAYSMIKDAEDKGLitpgKSTLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIILRALGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 116 EVVLHGT------VFDDAQEealRLQHTHDLLYVPPFDHPL-IMAGQGTIGLEIIEDLP-DVDTLLAPVGGGGLISEVAT 187
Cdd:PLN00011 117 EVHLTDQsiglkgMLEKAEE---ILSKTPGGYIPQQFENPAnPEIHYRTTGPEIWRDSAgKVDILVAGVGTGGTATGVGK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 188 AIKALRPTVRVIGVEaaAAPAALLSRrqghivGLSGAHsLADGIAlkrIGEQTFPVIEALVDELVTV-NEEQIAQAIVAL 266
Cdd:PLN00011 194 FLKEKNKDIKVCVVE--PVESAVLSG------GQPGPH-LIQGIG---SGIIPFNLDLTIVDEIIQVtGEEAIETAKLLA 261
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499662032 267 MEKTRLVVEGAGAVGLAALLHAARPLARGRTVCLL--SGG 304
Cdd:PLN00011 262 LKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIfpSGG 301
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
37-182 |
1.19e-07 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 53.66 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 37 LYFKCENLQRSGSFKVRGAFhfMARQPAQRL------AAGVVTASAGNhaQGVALSA--ARLGVAATVVMPENTP-LAKM 107
Cdd:PLN02569 152 LWVKHCGISHTGSFKDLGMT--VLVSQVNRLrkmakpVVGVGCASTGD--TSAALSAycAAAGIPSIVFLPADKIsIAQL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 108 QATRGYGAEVVLHGTVFDDaqeeALRL--QHTHDLlyvPPFD----HPLIMAGQGTIGLEIIE----DLPDVdtLLAPVG 177
Cdd:PLN02569 228 VQPIANGALVLSIDTDFDG----CMRLirEVTAEL---PIYLanslNSLRLEGQKTAAIEILQqfdwEVPDW--VIVPGG 298
|
....*
gi 499662032 178 GGGLI 182
Cdd:PLN02569 299 NLGNI 303
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
19-316 |
2.85e-06 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 49.42 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 19 RRTELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAF--HFMARQPAQ-RLAAgvvTASAGNHAQGVALSAARLGVAAT 95
Cdd:PRK13803 270 RPTPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALgqALLAKRMGKtRIIA---ETGAGQHGVATATACALFGLKCT 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 96 VVMPENTplAKMQATRGY-----GAEV--VLHGT-VFDDAQEEALR-----LQHTHDLL--YVPPFDHPLIMAG-QGTIG 159
Cdd:PRK13803 347 IFMGEED--IKRQALNVErmkllGANVipVLSGSkTLKDAVNEAIRdwvasVPDTHYLIgsAVGPHPYPEMVAYfQSVIG 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 160 LEIIEDLPDV-----DTLLAPVGGGgliSEVATAIKAL--RPTVRVIGVEAA----------------------AAPAAL 210
Cdd:PRK13803 425 EEAKEQLKEQtgklpDAIIACVGGG---SNAIGIFYHFldDPSVKLIGVEAGgkgvntgehaatikkgrkgvlhGSMTYL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 211 LSRRQGHIVglsGAHSLADGIALKRIGEQTFPVIEALVDELVTVNEEqiaQAIVALMEKTRL-----VVEGAGAvgLAAL 285
Cdd:PRK13803 502 MQDENGQIL---EPHSISAGLDYPGIGPMHANLFETGRAIYTSVTDE---EALDAFKLLAKLegiipALESSHA--LAYL 573
|
330 340 350
....*....|....*....|....*....|...
gi 499662032 286 LHAARPLARGRTVCL-LSG-GNIDVQTIAQVVD 316
Cdd:PRK13803 574 KEGRKKFKKKDIVIVnLSGrGDKDIPTLKEYFE 606
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
71-298 |
3.17e-06 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 48.77 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 71 VVTASAGNHAQGVALSAARLGVAATVVMPENTPLAKMQATRGYGAEVVLHgtvfDDAQEEALRLQHTHDLLYVPP----- 145
Cdd:PLN02565 70 LIEPTSGNTGIGLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLT----DPAKGMKGAVQKAEEILAKTPnsyil 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 146 --FDHPL-IMAGQGTIGLEIIEDLP-DVDTLLAPVGGGGLISEVATAIKALRPTVRVIGVEAAAAPaaLLSRrqghivGL 221
Cdd:PLN02565 146 qqFENPAnPKIHYETTGPEIWKGTGgKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESA--VLSG------GK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 222 SGAHSLadgialKRIGEQTFP-VIEA-LVDELVTVN-EEQIAQAIVALMEKTRLVVEGAGAVGLAALLHAARPLARGRTV 298
Cdd:PLN02565 218 PGPHKI------QGIGAGFIPgVLDVdLLDEVVQVSsDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLI 291
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
20-182 |
1.76e-05 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 46.27 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 20 RTELIHSHFFseqiglplYFKCENLQRSGSFKVRGAFHFMArQPAQRLAAGVVTASAGNHAQGVALSAARLGVAATVVMP 99
Cdd:PRK06450 58 RTPLIKKGNI--------WFKLDFLNPTGSYKDRGSVTLIS-YLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 100 ENTPLAKMQATRGYGAEVV-LHGTVfDDAQEEALRLQHthdlLYVPPFDHPLIMAGQGTIGLEIIEDL----PdvDTLLA 174
Cdd:PRK06450 129 ETASGGKLKQIESYGAEVVrVRGSR-EDVAKAAENSGY----YYASHVLQPQFRDGIRTLAYEIAKDLdwkiP--NYVFI 201
|
....*...
gi 499662032 175 PVGGGGLI 182
Cdd:PRK06450 202 PVSAGTLL 209
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
21-117 |
2.19e-05 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 46.52 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 21 TELIHSHFFSEQIGLPLYFKCENLQRSGSFKVRGAFHFM--ARQPAQRLAAGVVT-ASAGNHAQGVALSAARLGVAATVV 97
Cdd:PLN02356 54 TPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIeeALESGQLFPGGVVTeGSAGSTAISLATVAPAYGCKCHVV 133
|
90 100
....*....|....*....|
gi 499662032 98 MPENTPLAKMQATRGYGAEV 117
Cdd:PLN02356 134 IPDDVAIEKSQILEALGATV 153
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
20-179 |
2.35e-05 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 45.85 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 20 RTELIHSHFFSEQIGL-PLYFKCENLQRSGSFKVRGAFHFMARqpAQRLA-AGVVTASAGNHAQGVALSAARLGVAATVV 97
Cdd:PRK06381 15 GTPLLRARKLEEELGLrKIYLKFEGANPTGTQKDRIAEAHVRR--AMRLGySGITVGTCGNYGASIAYFARLYGLKAVIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 98 MPENTPLAKMQATRGYGAEVVLhgtvFDDAQEEALRLQH---THDLLY--VPPFDHPLI-MAGQGTIGLEIIEDLPDV-D 170
Cdd:PRK06381 93 IPRSYSNSRVKEMEKYGAEIIY----VDGKYEEAVERSRkfaKENGIYdaNPGSVNSVVdIEAYSAIAYEIYEALGDVpD 168
|
....*....
gi 499662032 171 TLLAPVGGG 179
Cdd:PRK06381 169 AVAVPVGNG 177
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
19-202 |
2.43e-05 |
|
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: 45.99 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 19 RRTELIHSHFFSEQI-GLPLYFKCENLQRSGSFKVRGAFhfmarqpAQRLAA---GV--VTAS--AGNHAQGVALSAARL 90
Cdd:cd06446 33 RPTPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKINNAL-------GQALLAkrmGKkrVIAEtgAGQHGVATATACALF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 91 GVAATVVMPENT----PL--AKMQAtrgYGAEVVL----HGTVfDDAQEEALR-----LQHTHDLL--YVPPFDHPLI-M 152
Cdd:cd06446 106 GLECEIYMGAVDverqPLnvFRMEL---LGAEVVPvpsgSGTL-KDAISEAIRdwvtnVEDTHYLLgsVVGPHPYPNMvR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499662032 153 AGQGTIGLEIIE-------DLPDVdtLLAPVGGG----GLISEVataIKalRPTVRVIGVE 202
Cdd:cd06446 182 DFQSVIGEEAKKqilekegELPDV--VIACVGGGsnaaGLFYPF---IN--DKDVKLIGVE 235
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
31-179 |
4.16e-05 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 45.79 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 31 EQIGLP--LYFKCENLQRSGSFKVRGAFH---FMARQPAQRLAAgvvTASAGNHAQGVALSAARLGVAATVVMPENTplA 105
Cdd:PRK13802 341 EKTGLDarVFLKREDLNHTGAHKINNALGqalLVKRMGKTRVIA---ETGAGQHGVATATVCAMLGLKCRIYMGQID--A 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 106 KMQA-----TRGYGAEVV---LHGTVFDDAQEEALR-----LQHTHDLLYVPPFDHP---LIMAGQGTIGLEIIEDLPD- 168
Cdd:PRK13802 416 RRQAlnvarMRMLGAEVVevtLGDRILKDAINEALRdwvtnVKDTHYLLGTVAGPHPfpaMVRDFQKIIGEEAKQQLQDw 495
|
170
....*....|....*.
gi 499662032 169 -----VDTLLAPVGGG 179
Cdd:PRK13802 496 ygidhPDAICACVGGG 511
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
37-119 |
1.40e-04 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 43.32 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 37 LYFKCENLQRSGSFKVRGAFHfMARQPAQR--LAAG--VVTASAGNHAQGVALSAARLGVAATVVMPENTPLAKMQATRG 112
Cdd:PRK11761 29 ILAKLEGNNPAGSVKDRPALS-MIVQAEKRgeIKPGdtLIEATSGNTGIALAMIAAIKGYRMKLIMPENMSQERRAAMRA 107
|
....*..
gi 499662032 113 YGAEVVL 119
Cdd:PRK11761 108 YGAELIL 114
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
37-202 |
2.36e-04 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 43.20 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 37 LYFKCENLQRSGSFKVRGAFhfmaRQP--AQRLAAGVVTASAGNHAQGVALSA--ARLGVAATVVMpeNTPLAKMQAT-- 110
Cdd:PLN02618 89 IYLKREDLNHTGAHKINNAV----AQAllAKRLGKKRIIAETGAGQHGVATATvcARFGLECIVYM--GAQDMERQALnv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499662032 111 ---RGYGAEV--VLHGT-VFDDAQEEALR-----LQHTHDLL--YVPPFDHPLIMAG-QGTIG-------LEIIEDLPDV 169
Cdd:PLN02618 163 frmRLLGAEVrpVHSGTaTLKDATSEAIRdwvtnVETTHYILgsVAGPHPYPMMVRDfHSVIGketrrqaMEKWGGKPDV 242
|
170 180 190
....*....|....*....|....*....|....*..
gi 499662032 170 dtLLAPVGGG----GLISEVATaikalRPTVRVIGVE 202
Cdd:PLN02618 243 --LVACVGGGsnamGLFHEFID-----DEDVRLIGVE 272
|
|
| |
