|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
1-422 |
0e+00 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 790.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 1 MTVRTKVSTKDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCAS 80
Cdd:PRK08639 1 MTVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 81 AGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGDSNVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTI 160
Cdd:PRK08639 81 AGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 161 AGQGTLAKEILNQAEKEDkTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKF 240
Cdd:PRK08639 161 AGQGTVAVEILEQLEKEG-SPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGK-PVTLEKIDKF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 241 VDGASVARVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNND 320
Cdd:PRK08639 239 VDGAAVARVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKTVVCVISGGNND 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 321 INRMKEIEERSLLFEEMKHYFILNFPQRPGALREFVNDVLGPQDDITKFEYLKKTSQNTGTVIIGIQLKHHDDLIQLKDR 400
Cdd:PRK08639 319 IERMPEIKERSLIYEGLKHYFIVNFPQRPGALREFLDDVLGPNDDITRFEYLKKNNRETGPVLVGIELKDAEDYDGLIER 398
|
410 420
....*....|....*....|..
gi 487747924 401 VCQFDPSNIYINENKMLYSLLI 422
Cdd:PRK08639 399 MEAFGPSYIDINPNEPLYNLLI 420
|
|
| THD1 |
TIGR02079 |
threonine dehydratase; This model represents threonine dehydratase, the first step in the ... |
10-422 |
0e+00 |
|
threonine dehydratase; This model represents threonine dehydratase, the first step in the pathway converting threonine into isoleucine. At least two other clades of biosynthetic threonine dehydratases have been characterized by models (TIGR01124 and TIGR01127). Those sequences described by this model are exclusively found in species containg the rest of the isoleucine pathway and which are generally lacking in members of the those other two clades of threonine dehydratases. Members of this clade are also often gene clustered with other elements of the isoleucine pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 273957 [Multi-domain] Cd Length: 409 Bit Score: 611.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 10 KDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVA 89
Cdd:TIGR02079 1 QDIEAARKRLKEVVPHTPLQLNERLSEKYGANIYLKREDLQPVRSYKIRGAYNFLKQLSDAQLAKGVVCASAGNHAQGFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 90 YTAKKLNLKAVIFMPVTTPRQKINQVKFFGDSNVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKE 169
Cdd:TIGR02079 81 YACRHLGVHGTVFMPATTPKQKIDRVKIFGGEFIEIILVGDTFDQCAAAAREHVEDHGGTFIPPFDDPRIIEGQGTVAAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 170 ILNQAEKEdktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKFVDGASVARV 249
Cdd:TIGR02079 161 ILDQLPEK---PDYVVVPVGGGGLISGLTTYLAGTSPKTKIIGVEPEGAPSMKASLEAGE-VVTLDKIDNFVDGAAVKRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 250 GDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNNDINRMKEIEE 329
Cdd:TIGR02079 237 GDLNFKALKDVPDEVTLVPEGAVCTTILDLYNLEGIVAEPAGALSIAALERLGEEIKGKTVVCVVSGGNNDIERTEEIRE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 330 RSLLFEEMKHYFILNFPQRPGALREFVNDVLGPQDDITKFEYLKKTSQNTGTVIIGIQLKHHDDLIQLKDRVCQFDPSNI 409
Cdd:TIGR02079 317 RSLLYEGLKHYFIVRFPQRPGALREFLNDVLGPNDDITRFEYTKKSNRETGPALIGIELNDKEDFAGLLERMAAADIHYE 396
|
410
....*....|...
gi 487747924 410 YINENKMLYSLLI 422
Cdd:TIGR02079 397 DINENDILYNLLI 409
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
10-320 |
8.87e-161 |
|
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: 454.64 E-value: 8.87e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 10 KDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVA 89
Cdd:cd01562 2 EDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 90 YTAKKLNLKAVIFMPVTTPRQKINQVKFFGDsnvEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKE 169
Cdd:cd01562 82 YAAKLLGIPATIVMPETAPAAKVDATRAYGA---EVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 170 ILNQAEKedktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKFVDGASVARV 249
Cdd:cd01562 159 ILEQVPD----LDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGK-PVTLPEVDTIADGLAVKRP 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487747924 250 GDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNND 320
Cdd:cd01562 234 GELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
1-335 |
2.44e-156 |
|
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: 444.48 E-value: 2.44e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 1 MTVRTkVSTKDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCAS 80
Cdd:COG1171 1 MTALM-PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 81 AGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTI 160
Cdd:COG1171 80 AGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYG---AEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 161 AGQGTLAKEILNQAEKedktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKF 240
Cdd:COG1171 157 AGQGTIALEILEQLPD----LDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGE-PVTLPGVDTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 241 VDGASVARVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNND 320
Cdd:COG1171 232 ADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNID 311
|
330
....*....|....*
gi 487747924 321 INRMKEIEERSLLFE 335
Cdd:COG1171 312 PDRLAEILERGLVGE 326
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
24-393 |
1.21e-129 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 382.95 E-value: 1.21e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 24 KETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFM 103
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 104 PVTTPRQKINQVKFFGDsnvEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKEILNQAEKEdktFDY 183
Cdd:PRK09224 99 PVTTPDIKVDAVRAFGG---EVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHP---LDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 184 VFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKFVDGASVARVGDITFDIAKDKVDD 263
Cdd:PRK09224 173 VFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGE-RVDLPQVGLFADGVAVKRIGEETFRLCQEYVDD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 264 YVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQY--KKQIENKTIVCIVSGGNNDINRMKEIEERSLLFEEMKHYF 341
Cdd:PRK09224 252 VITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLKKYvaQHGIEGETLVAILSGANMNFDRLRYVAERAELGEQREALL 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 487747924 342 ILNFPQRPGALREFVNdVLGPQdDITKFEYlKKTSQNTGTVIIGIQLKHHDD 393
Cdd:PRK09224 332 AVTIPEEPGSFLKFCE-LLGGR-NVTEFNY-RYADAKEAHIFVGVQLSRGQE 380
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
25-416 |
9.80e-116 |
|
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: 347.49 E-value: 9.80e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 25 ETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMP 104
Cdd:TIGR01124 17 ETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGLKALIVMP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 105 VTTPRQKINQVKFFGDsnvEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKEILNQAEKEDktfDYV 184
Cdd:TIGR01124 97 ETTPDIKVDAVRGFGG---EVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANPL---DAV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 185 FAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKFVDGASVARVGDITFDIAKDKVDDY 264
Cdd:TIGR01124 171 FVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGE-PVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 265 VQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQY--KKQIENKTIVCIVSGGNNDINRMKEIEERSLLFEEMKHYFI 342
Cdd:TIGR01124 250 VTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYvaLHGIRGQTLVAILSGANMNFHRLRYVSERCELGEQREALLA 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747924 343 LNFPQRPGALREFVNdVLGPQdDITKFEYlKKTSQNTGTVIIGIQLKHHDDLIQLKDRVCQFDPSNIYINENKM 416
Cdd:TIGR01124 330 VTIPEQPGSFLKFCE-LLGNR-NITEFNY-RYADRKDAHIFVGVQLSNPQERQEILARLNDGGYSVVDLTDDEL 400
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
18-393 |
3.73e-102 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 313.27 E-value: 3.73e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 18 RLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVAYTAKKLNL 97
Cdd:PRK12483 30 RVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 98 KAVIFMPVTTPRQKINQVKFFGDsnvEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKEILNQaekE 177
Cdd:PRK12483 110 KAVIVMPRTTPQLKVDGVRAHGG---EVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQ---H 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 178 DKTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHSiVTLENIDKFVDGASVARVGDITFDIA 257
Cdd:PRK12483 184 PGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGER-VVLGQVGLFADGVAVAQIGEHTFELC 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 258 KDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQ--IENKTIVCIVSGGNNDINRMKEIEERSLLFE 335
Cdd:PRK12483 263 RHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAERegIEGQTLVAIDSGANVNFDRLRHVAERAELGE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 487747924 336 EMKHYFILNFPQRPGALREFVnDVLGPQdDITKFEYlKKTSQNTGTVIIGIQLKHHDD 393
Cdd:PRK12483 343 QREAIIAVTIPEQPGSFKAFC-AALGKR-QITEFNY-RYADAREAHLFVGVQTHPRHD 397
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
26-403 |
2.43e-93 |
|
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: 285.87 E-value: 2.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMPV 105
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 106 TTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKEILNQAekedKTFDYVF 185
Cdd:TIGR01127 81 SAPPSKVKATKSYG---AEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDI----PDVDTVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 186 AAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVViNHSIVTLENIDKFVDGASVARVGDITFDIAKDKVDDYV 265
Cdd:TIGR01127 154 VPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLR-EGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 266 QVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNNDINRMKEIEERSlLFEEMKHYFILNF 345
Cdd:TIGR01127 233 TVDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKIIEKG-LVKSGRKVRIETV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747924 346 -PQRPGALREFVNDVLGPQDDITKFEY---LKKTSQNTGTVIIGIQLKHHDDLIQLKDRVCQ 403
Cdd:TIGR01127 312 lPDRPGALYHLLESIAEARANIVKIDHdrlSKEIPPGFAMVEITLETRGKEHLDEILKILRD 373
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
21-401 |
2.24e-90 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 284.89 E-value: 2.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 21 NIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAV 100
Cdd:PLN02550 105 DVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 101 IFMPVTTPRQKINQVKFFGDSnveIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKEILNQAEkedKT 180
Cdd:PLN02550 185 IAMPVTTPEIKWQSVERLGAT---VVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQ---GP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 181 FDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSvvINHSI-VTLENIDKFVDGASVARVGDITFDIAKD 259
Cdd:PLN02550 259 LHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALS--LHHGErVMLDQVGGFADGVAVKEVGEETFRLCRE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 260 KVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKK--QIENKTIVCIVSGGNNDINRMKEIEERSLLFEEM 337
Cdd:PLN02550 337 LVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKyyGLKDENVVAITSGANMNFDRLRIVTELADVGRQQ 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747924 338 KHYFILNFPQRPGALREFVNDVlGPQdDITKFEYlKKTSQNTGTVIIGIQLKHHDDLIQLKDRV 401
Cdd:PLN02550 417 EAVLATFMPEEPGSFKRFCELV-GPM-NITEFKY-RYSSEKEALVLYSVGVHTEQELQALKKRM 477
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
7-327 |
1.04e-83 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 259.67 E-value: 1.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 7 VSTKDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQ 86
Cdd:PRK08638 9 VAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 87 GVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTL 166
Cdd:PRK08638 89 GVALSCALLGIDGKVVMPKGAPKSKVAATCGYG---AEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 167 AKEILNQAEKedktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTG----ASSMYQSVVINHSIV-TLenidkfV 241
Cdd:PRK08638 166 GLEILEDLWD----VDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENvhgmAASFYAGEITTHRTTgTL------A 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 242 DGASVARVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYK--KQIENKTIVCIVSGGNN 319
Cdd:PRK08638 236 DGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKldQYIQNKKVVAIISGGNV 315
|
....*...
gi 487747924 320 DINRMKEI 327
Cdd:PRK08638 316 DLSRVSQI 323
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
26-316 |
1.51e-83 |
|
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: 257.62 E-value: 1.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMPV 105
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 106 TTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQ-HKMNFIDPFNNVYTIAGQGTLAKEILNQAEKEdktFDYV 184
Cdd:pfam00291 88 DAPPGKLLLMRALG---AEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLGGD---PDAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 185 FAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKFVDGASVARV-GDITFDIAKDKVDD 263
Cdd:pfam00291 162 VVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGR-PVPVPVADTIADGLGVGDEpGALALDLLDEYVGE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 487747924 264 YVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQI--ENKTIVCIVSG 316
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGElkGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
26-317 |
2.67e-81 |
|
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: 250.12 E-value: 2.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKG--ITCASAGNHAQGVAYTAKKLNLKAVIFM 103
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 104 PVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQ-HKMNFIDPFNNVYTIAGQGTLAKEILNQAekEDKTFD 182
Cdd:cd00640 81 PEGASPEKVAQMRALG---AEVVLVPGDFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQGTIGLEILEQL--GGQKPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 183 YVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPtgassmyqsvvinhsivtlenidkfvdgasvarvgditfdiakdkvd 262
Cdd:cd00640 156 AVVVPVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------- 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 487747924 263 DYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQI-ENKTIVCIVSGG 317
Cdd:cd00640 189 EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLgKGKTVVVILTGG 244
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
10-318 |
5.32e-79 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 246.91 E-value: 5.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 10 KDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVA 89
Cdd:PRK06815 5 DAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 90 YTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKE 169
Cdd:PRK06815 85 LAAKLAGIPVTVYAPEQASAIKLDAIRALG---AEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGME 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 170 ILNQAEKedktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKFVDG-ASVAR 248
Cdd:PRK06815 162 LVEQQPD----LDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGE-IVEVAEQPTLSDGtAGGVE 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 249 VGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGN 318
Cdd:PRK06815 237 PGAITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKN 306
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
7-352 |
7.79e-79 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 249.43 E-value: 7.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 7 VSTKDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQ 86
Cdd:PRK07334 5 VTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 87 GVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTL 166
Cdd:PRK07334 85 GVAYHAQRLGIPATIVMPRFTPTVKVERTRGFG---AEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 167 AKEILnqaekEDK-TFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQsvVINHSIVTLENiDKFVDGAS 245
Cdd:PRK07334 162 ALEML-----EDApDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYA--AIKGVALPCGG-STIAEGIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 246 VARVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNNDINRMK 325
Cdd:PRK07334 234 VKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNIDTRLLA 313
|
330 340
....*....|....*....|....*..
gi 487747924 326 EIEERSLLFEEMKHYFILNFPQRPGAL 352
Cdd:PRK07334 314 NVLLRGLVRAGRLARLRVDIRDRPGAL 340
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
7-323 |
1.09e-63 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 207.56 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 7 VSTKDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQ 86
Cdd:PRK07048 6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 87 GVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTL 166
Cdd:PRK07048 86 AIALSARLLGIPATIVMPQDAPAAKVAATRGYG---GEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 167 AKEILnqaeKEDKTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVViNHSIVTLENIDKFVDGASV 246
Cdd:PRK07048 163 AKELF----EEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFR-SGEIVHIDTPRTIADGAQT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747924 247 ARVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNNDINR 323
Cdd:PRK07048 238 QHLGNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLAR 314
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
7-327 |
5.75e-61 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 200.58 E-value: 5.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 7 VSTKDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQ 86
Cdd:PRK07476 1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 87 GVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTL 166
Cdd:PRK07476 81 ALAYAARALGIRATICMSRLVPANKVDAIRALG---AEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 167 AKEILNQAEKedktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHSiVTLENIDKFVD--GA 244
Cdd:PRK07476 158 GLEILEALPD----VATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRP-VQVEEVPTLADslGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 245 SVARVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNNDINRM 324
Cdd:PRK07476 233 GIGLDNRYTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELH 312
|
...
gi 487747924 325 KEI 327
Cdd:PRK07476 313 RRI 315
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
7-336 |
2.74e-60 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 199.23 E-value: 2.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 7 VSTKDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKN-KGITCASAGNHA 85
Cdd:PRK06608 5 QNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLpDKIVAYSTGNHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 86 QGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIgDTFDhclaQALNYTKQHKMN---FIDPFNNVYTIAG 162
Cdd:PRK06608 85 QAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYG---GEVILT-NTRQ----EAEEKAKEDEEQgfyYIHPSDSDSTIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 163 QGTLAKEILNQAekeDKTFDYVFAAIGGGGLISGvsTYFKAH--SPHTKIIGVEPTGASSMYQSVVINhSIVTLENI-DK 239
Cdd:PRK06608 157 AGTLCYEALQQL---GFSPDAIFASCGGGGLISG--TYLAKEliSPTSLLIGSEPLNANDAYLSLKNN-KIYRLNYSpNT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 240 FVDGASVARVGDITFDIAKdKVDDYVQVDEgavcstiLDMYSKQA-------IVAEPAGALSVSALEQY-KKQIENKTIV 311
Cdd:PRK06608 231 IADGLKTLSVSARTFEYLK-KLDDFYLVEE-------YEIYYWTAwlthllkVICEPSSAINMVAVVNWlKTQSKPQKLL 302
|
330 340
....*....|....*....|....*
gi 487747924 312 CIVSGGNNDINRMKEIEERSLLFEE 336
Cdd:PRK06608 303 VILSGGNIDPILYNELWKEDYLTIP 327
|
|
| PLN02970 |
PLN02970 |
serine racemase |
7-326 |
1.80e-59 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 196.82 E-value: 1.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 7 VSTKDIDEAYLRLKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQ 86
Cdd:PLN02970 9 ADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 87 GVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGDsnvEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTL 166
Cdd:PLN02970 89 ALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGG---IITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 167 AKEILNQAekedKTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKFVDGASv 246
Cdd:PLN02970 166 ALEFLEQV----PELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGE-IITLPVTNTIADGLR- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 247 ARVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSAL--EQYKKQI---ENKTIVCIVSGGNNDI 321
Cdd:PLN02970 240 ASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAAlsDSFRSNPawkGCKNVGIVLSGGNVDL 319
|
....*
gi 487747924 322 NRMKE 326
Cdd:PLN02970 320 GVLWE 324
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
7-320 |
8.41e-49 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 168.21 E-value: 8.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 7 VSTKDIDEAYLRLKNIVKETPLqFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAIsvLSNEEKNKGITCASAGNHAQ 86
Cdd:PRK08246 5 ITRSDVRAAAQRIAPHIRRTPV-LEADGAGFGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 87 GVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTL 166
Cdd:PRK08246 82 AVAYAAAALGVPATVFVPETAPPAKVARLRALG---AEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 167 AKEILNQAEKedktFDYVFAAIGGGGLISGVSTYFKahsPHTKIIGVEPTGASSMYQSvvinhsivtLEN---IDkfVDG 243
Cdd:PRK08246 159 GLEIEEQAPG----VDTVLVAVGGGGLIAGIAAWFE---GRARVVAVEPEGAPTLHAA---------LAAgepVD--VPV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 244 ASVA-------RVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALE--QYKKQiENKTIVCIV 314
Cdd:PRK08246 221 SGIAadslgarRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLsgAYVPA-PGERVAVVL 299
|
....*.
gi 487747924 315 SGGNND 320
Cdd:PRK08246 300 CGANTD 305
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
7-320 |
3.86e-47 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 165.18 E-value: 3.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 7 VSTKDIDEAYLRLKNIVKETPLqfdHYlSQKYNcnVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQ 86
Cdd:PRK08813 21 VSVADVLAAQARLRRYLSPTPL---HY-AERFG--VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 87 GVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGDSnveIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTL 166
Cdd:PRK08813 95 GVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT---VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 167 AKEILNQAEkedktfDYVFAAIGGGGLISGVSTYFKAHSphTKIIGVEPTGASSMYQSvvINHSIVTLENIDKFVDGASV 246
Cdd:PRK08813 172 GIELAAHAP------DVVIVPIGGGGLASGVALALKSQG--VRVVGAQVEGVDSMARA--IRGDLREIAPVATLADGVKV 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747924 247 ARVGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSAleqyKKQIENKTIVCIVSGGNND 320
Cdd:PRK08813 242 KIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAA----GRRVSGKRKCAVVSGGNID 311
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
25-319 |
3.16e-32 |
|
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: 124.33 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 25 ETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNK--GITCASAGNHAQGVAYTAKKLNLKAVIF 102
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNEcvHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 103 MPVTTPRQKINQVKffgDSNVEIVLIGDTFDhclaQALNYTKQHKMN------FIDPFNNVYTIAGQGTLAKEILNQAEK 176
Cdd:cd06448 81 VPESTKPRVVEKLR---DEGATVVVHGKVWW----EADNYLREELAEndpgpvYVHPFDDPLIWEGHSSMVDEIAQQLQS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 177 EDKTfDYVFAAIGGGGLISG-VSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHSiVTLENIDKFVDGASVARVGDITFD 255
Cdd:cd06448 154 QEKV-DAIVCSVGGGGLLNGiVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKL-VTLPKITSVATSLGAKTVSSQALE 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747924 256 IAKDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSA--------LEQYKKQIENKTIVCIVSGGNN 319
Cdd:cd06448 232 YAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVvysgkildLQLEVLLTPLDNVVVVVCGGSN 303
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
26-314 |
5.86e-30 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 117.23 E-value: 5.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAIsvLSNEEKNK---GITC--ASAGNHAQGVAYTAKKLNLKAV 100
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMI--EDAEKRGLlkpGTTIiePTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 101 IFMPVTTPRQKINQVKFFGdsnVEIVLI----GDTFDHCLAQALNYTKQHKMNFI-DPFNNVY-TIAGQGTLAKEILNQa 174
Cdd:cd01561 81 IVMPETMSEEKRKLLRALG---AEVILTpeaeADGMKGAIAKARELAAETPNAFWlNQFENPAnPEAHYETTAPEIWEQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 175 ekEDKTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGassmyqSVVIN------HSIvtlENIdkfvdGASvaR 248
Cdd:cd01561 157 --LDGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVG------SVLFSggppgpHKI---EGI-----GAG--F 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487747924 249 VGDItFDIakDKVDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQI-ENKTIVCIV 314
Cdd:cd01561 219 IPEN-LDR--SLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLgPGKTIVTIL 282
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
26-316 |
2.70e-29 |
|
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: 116.15 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPL-QFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLsNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMP 104
Cdd:cd01563 23 TPLvRAPRLGERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKA-KELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 105 VTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHK---MNFIDPfnnvYTIAGQGTLAKEILNQAEKEdkTF 181
Cdd:cd01563 102 AGKALGKLAQALAYG---ATVLAVEGNFDDALRLVRELAEENWiylSNSLNP----YRLEGQKTIAFEIAEQLGWE--VP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 182 DYVFAAIGGGGLISGVSTYFKA--------HSPhtKIIGVEPTGASSMYQSVVINH-SIVTLENIDKFVDGasvARVGD- 251
Cdd:cd01563 173 DYVVVPVGNGGNITAIWKGFKElkelglidRLP--RMVGVQAEGAAPIVRAFKEGKdDIEPVENPETIATA---IRIGNp 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747924 252 ITFDIAKDKVDDY----VQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQ---IENKTIVCIVSG 316
Cdd:cd01563 248 ASGPKALRAVRESggtaVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgiiDKGERVVVVLTG 319
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
34-320 |
9.47e-28 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 112.01 E-value: 9.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 34 LSQKYNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKN-KGITCASAGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKI 112
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRvRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 113 NQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNnVYTIAGQGTLAKEILNQAekedKTFDYVFAAIGGGG 192
Cdd:PRK06110 110 AAMRALG---AELIEHGEDFQAAREEAARLAAERGLHMVPSFH-PDLVRGVATYALELFRAV----PDLDVVYVPIGMGS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 193 LISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHsIVTLENIDKFVDGASVaRVGDIT-FDIAKDKVDDYVQVDEGA 271
Cdd:PRK06110 182 GICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGR-VVTTPVATTLADGMAC-RTPDPEaLEVIRAGADRIVRVTDDE 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 487747924 272 VCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIVSGGNND 320
Cdd:PRK06110 260 VAAAMRAYFTDTHNVAEGAGAAALAAALQERERLAGKRVGLVLSGGNID 308
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
26-316 |
1.60e-26 |
|
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: 109.90 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNCNVYLKREdlqWV---RSFKLRGAYNAISvLSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIF 102
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEE---GHnptGSFKDRAMQVAVS-LALERGAKTIVCASSGNGSAALAAYAARAGIEVFVF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 103 MPVT-TPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFnNVYTIAGQGTLAKEILNQAekeDKTF 181
Cdd:COG0498 143 VPEGkVSPGQLAQMLTYG---AHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQL---GRVP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 182 DYVFAAIGGGGLISGVstyFKA-----------HSPhtKIIGVEPTGASSMYQSVVINHSIVTLENIDKFVDGASVAR-V 249
Cdd:COG0498 216 DWVVVPTGNGGNILAG---YKAfkelkelglidRLP--RLIAVQATGCNPILTAFETGRDEYEPERPETIAPSMDIGNpS 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747924 250 GDIT--FDIAKDKvDDYVQVDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIE---NKTIVCIVSG 316
Cdd:COG0498 291 NGERalFALRESG-GTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEidpDEPVVVLSTG 361
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
338-421 |
3.02e-24 |
|
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes the second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153179 [Multi-domain] Cd Length: 81 Bit Score: 95.31 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 338 KHYFILNFPQRPGALREFVNDvLGPQDDITKFEYLKKTSqNTGTVIIGIQLKHHdDLIQLKDRVCQFDPSNIYINENKML 417
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNE-LLPKWNITLFHYRNQGS-DYGRVLVGIQVPDA-DLDELKERLDALGYPYQEETDNPAY 77
|
....
gi 487747924 418 YSLL 421
Cdd:cd04907 78 KLFL 81
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
79-314 |
1.39e-20 |
|
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: 91.26 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 79 ASAGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLI--GDTFDHCLAQALNYTKQHKMNFI-DPFN 155
Cdd:COG0031 70 ATSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYG---AEVVLTpgAEGMKGAIDKAEELAAETPGAFWpNQFE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 156 NV------YTiagqgTLAKEILNQAekeDKTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGassmyqSVVIN- 228
Cdd:COG0031 147 NPanpeahYE-----TTGPEIWEQT---DGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEG------SPLLSg 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 229 -----HSIvtlENIdkfvdGASvaRVGDItFDiaKDKVDDYVQV-DEGAVcSTILDMYSKQAIVAEP-AGALSVSALEQY 301
Cdd:COG0031 213 gepgpHKI---EGI-----GAG--FVPKI-LD--PSLIDEVITVsDEEAF-AMARRLAREEGILVGIsSGAAVAAALRLA 278
|
250
....*....|...
gi 487747924 302 KKQIENKTIVCIV 314
Cdd:COG0031 279 KRLGPGKTIVTIL 291
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
329-421 |
2.14e-18 |
|
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all contain a carboxy terminal region. This region may have a regulatory role. Some members contain two copies of this region. This family is homologous to the pfam01842 domain.
Pssm-ID: 395467 [Multi-domain] Cd Length: 91 Bit Score: 79.63 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 329 ERSLLFEEMKHYFILNFPQRPGALREFVNDVLGPqDDITKFEYlKKTSQNTGTVIIGIQLKHHDDLIQLKDRVCQFDPSN 408
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGR-NNITLFEY-RKHGDKNGCVLVGIELSQAEDLDEFIERLNKLGYDY 78
|
90
....*....|...
gi 487747924 409 IYINENKMLYSLL 421
Cdd:pfam00585 79 EDLSDNEAAYEHL 91
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
54-269 |
6.11e-17 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 81.85 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 54 SFK-LRGAY-----------NAISVLSNE--------EKNKGIT--CASAGNHAQGVAYTAKKLNLKAVIFMPVTTPRQK 111
Cdd:PRK08206 75 AFKaLGGAYavarllaeklgLDISELSFEeltsgevrEKLGDITfaTATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 112 INQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHkmnfidpfNNV---------YT------IAGQGTLAKEILNQAEK 176
Cdd:PRK08206 155 VDAIRALG---AECIITDGNYDDSVRLAAQEAQEN--------GWVvvqdtawegYEeiptwiMQGYGTMADEAVEQLKE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 177 EDKTFDYVFAAIGGGGLISGVSTYF----KAHSPHTKIigVEPTGASSMYQSvvinhsivtlenidkFVDGASVARVGD- 251
Cdd:PRK08206 224 MGVPPTHVFLQAGVGSLAGAVLGYFaevyGEQRPHFVV--VEPDQADCLYQS---------------AVDGKPVAVTGDm 286
|
250 260 270
....*....|....*....|....*....|..
gi 487747924 252 --------------ITFDIAKDKVDDYVQVDE 269
Cdd:PRK08206 287 dtimaglacgepnpLAWEILRNCADAFISCPD 318
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
341-400 |
4.31e-16 |
|
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes each of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153157 [Multi-domain] Cd Length: 68 Bit Score: 72.54 E-value: 4.31e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 341 FILNFPQRPGALREFVNdVLGPQDDITKFEYLKKTSqNTGTVIIGIQLKHHDDLIQLKDR 400
Cdd:cd04885 1 FAVTFPERPGALKKFLE-LLGPPRNITEFHYRNQGG-DEARVLVGIQVPDREDLAELKER 58
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
18-213 |
3.61e-15 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 75.99 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 18 RLKNIVKETPLQFDHYLSQKYNCNVYLKREDL--------QWvrsFKLRgaYNAIsvlsnEEKNKG----ITCASAG-NH 84
Cdd:COG2515 4 RLPLAFLPTPLQPLPRLSAALGVELWIKRDDLtgpaiggnKT---RKLE--YLLA-----DALAQGadtlVTFGGAQsNH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 85 AQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGDSNVEIVLIGDTFDHCLAQALNYTKQHkmnFIDPFNNVYTIAGQG 164
Cdd:COG2515 74 ARATAAAAAKLGLKCVLVLRGEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRDEAMEAVAAE---LRARGGKPYVIPEGG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487747924 165 T----------LAKEILNQAEKEDKTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGV 213
Cdd:COG2515 151 SnplgalgyveAAAELAAQLAELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGI 209
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
34-225 |
3.62e-13 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 70.61 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 34 LSQKYNCNVYLKREDLQWVRSFKLRGAYNAISvLSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKIN 113
Cdd:PRK05638 74 ISEKLGENVYIKDETRNPTGSFRDRLATVAVS-YGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 114 QVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKEILNQAEKEdktfdYVFAAIGGGGL 193
Cdd:PRK05638 153 QMIAFG---AKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINPT-----HVIVPTGSGSY 224
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 487747924 194 ISGVSTYFKA--------HSPhtKIIGVEPTGASSMYQSV 225
Cdd:PRK05638 225 LYSIYKGFKElleigvieEIP--KLIAVQTERCNPIASEI 262
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
26-235 |
1.60e-12 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 67.83 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNC--NVYLKREDLQWVRSF---KLRgaynAISVLSNEEKNKGI-TCASAG----NHAQGVAYTAKKL 95
Cdd:cd06449 1 TPIQYLPRLSEHLGGkvEIYAKRDDCNSGLAFggnKIR----KLEYLLPDALAKGAdTLVTVGgiqsNHTRQVAAVAAKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 96 NLKAVIFM--PVTTPRQKINQV------KFFGdsnVEIVLIGDTFDHCLAQALNYTKQ------HKMNFIDPFNNVYTIA 161
Cdd:cd06449 77 GLKCVLVQenWVPYSDAVYDRVgnillsRIMG---ADVRLVSAGFDIGIRKSFEEAAEeveakgGKPYVIPAGGSEHPLG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487747924 162 GQGTL--AKEILNQAEKEDKTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSMYQSVVINHSIVTLE 235
Cdd:cd06449 154 GLGYVgfVLEIAQQEEELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLA 229
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
26-317 |
2.86e-12 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 67.04 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNCN-VYLKREDLQWVRSFKLRGAYNAISVlSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMp 104
Cdd:PRK06381 16 TPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRR-AMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFI- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 105 vttPRQKIN-QVKFFGDSNVEIVLIGDTFDHCLAQALNYTKqhKMNFIDP----FNNVYTIAGQGTLAKEILNQAEKEDk 179
Cdd:PRK06381 94 ---PRSYSNsRVKEMEKYGAEIIYVDGKYEEAVERSRKFAK--ENGIYDAnpgsVNSVVDIEAYSAIAYEIYEALGDVP- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 180 tfDYVFAAIGGGGLISGVSTYFKA--------HSPHtkIIGVEPTGASSMYQSVVINHSIVTLENIDKFVDGA-SVARVG 250
Cdd:PRK06381 168 --DAVAVPVGNGTTLAGIYHGFRRlydrgktsRMPR--MIGVSTSGGNQIVESFKRGSSEVVDLEVDEIRETAvNEPLVS 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487747924 251 DITFDI--AKDKVDD------YVQVDEGAVCSTIldMYSKQAIVAEPAGALSVSALEQY-KKQIENKTIVCIVSGG 317
Cdd:PRK06381 244 YRSFDGdnALEAIYDshgyafGFSDDEMVKYAEL--LRRMEGLNALPASASALAALVKYlKKNGVNDNVVAVITGR 317
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
41-202 |
8.61e-12 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 66.00 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 41 NVYLKREDLQWVRSFKLRGAYNAISVLSnEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGd 120
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTVAKLK-EEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLG- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 121 SNVEIVLiGDTFD-HclAQALNYTKQHKMNFIDPFNNVYTIAGQGTLAKEILNQAekedKTFDYVFAAIGGGGLISGVST 199
Cdd:PRK08329 151 AELHFVE-GDRMEvH--EEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQI----GVPDYAFVPVGSGTLFLGIWK 223
|
...
gi 487747924 200 YFK 202
Cdd:PRK08329 224 GFK 226
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
18-322 |
6.12e-11 |
|
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. the beta chain contains the functional domain for or the synthesis of tryptophan from indole and serine. The enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-P attachment site is contained within the conserved region [LIVM]-x-H-x-G-[STA]-H-K-x-N] [K is the pyridoxal-P attachment site] which is present between residues 90-100 of the model. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 272987 Cd Length: 385 Bit Score: 63.53 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 18 RLKNIV-KETPLQFDHYLSQKYN-CNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVAYTAKKL 95
Cdd:TIGR00263 42 LLRNYAgRPTPLTFAPNLTEALGgAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 96 NLKAVIFMPVT-TPRQKIN--QVKFFGdSNVEIVLIGDTfdhCLAQALNYTKQhkmNFIDPFNNVYTIAG---------- 162
Cdd:TIGR00263 122 GLDCEVYMGAEdVERQKPNvfRMELLG-AKVIPVTSGSG---TLKDAVNEALR---DWVTSVDDTHYVLGsavgphpfpt 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 163 -----QGTLAKEILNQ-AEKEDKTFDYVFAAIGGGGLISGVSTYFkAHSPHTKIIGVEP--TGASSMYQSVVINHSIV-- 232
Cdd:TIGR00263 195 mvrdfQSVIGEEAKEQiLEQEGRLPDAVIACVGGGSNAIGIFYAF-IDDPSVQLIGVEAggLGIDTHKHAATLSKGSPgv 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 233 -------TLENID-KFVDGASVAR------VGDITFDIAKDKVDDYVQVDEGAVCSTILDMYSKQAIVA--EPAGALsvS 296
Cdd:TIGR00263 274 lhgmktyLLQDEDgQILEAHSVSAgldypgVGPEHAYLHETGRATYEAITDDEALEAFKLLSRNEGIIPalESSHAL--A 351
|
330 340
....*....|....*....|....*...
gi 487747924 297 ALEQYKKQI-ENKTIVCIVSG-GNNDIN 322
Cdd:TIGR00263 352 HLEKIAPTLpKDQIVVVNLSGrGDKDIF 379
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
26-313 |
1.33e-10 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 62.19 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYNAIsvLSNEEKNK---GITC--ASAGNHAQGVAYTAKKLNLKAV 100
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNII--WDAEKRGLlkpGGTIveGTAGNTGIGLALVAAARGYKTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 101 IFMPVTTPRQKINQVKFFGdsnVEIVLI-------GDTFDHC---LAQALNYTKQHKMNFIDPFNNVYT-IAGQGTLAKE 169
Cdd:PRK10717 92 IVMPETQSQEKKDLLRALG---AELVLVpaapyanPNNYVKGagrLAEELVASEPNGAIWANQFDNPANrEAHYETTGPE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 170 ILNQAEKEdktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGaSSMYqSVVINHSIVTlenidkfvDGASVAR- 248
Cdd:PRK10717 169 IWEQTDGK---VDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTG-SALY-SYYKTGELKA--------EGSSITEg 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487747924 249 --VGDITFDIAKDKVDDYVQV-DEGAVcSTILDMYSKQAIVAEPAGALSVSALEQYKKQI-ENKTIVCI 313
Cdd:PRK10717 236 igQGRITANLEGAPIDDAIRIpDEEAL-STAYRLLEEEGLCLGGSSGINVAAALRLARELgPGHTIVTI 303
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
26-217 |
4.69e-10 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 61.37 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 26 TPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRgayNAI--SVLSNEEKNKGITCAS-AGNHAQGVAYTAKKLNLKAVIF 102
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKIN---NALgqALLAKRMGKTRIIAETgAGQHGVATATACALFGLKCTIF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 103 M-PVTTPRQKIN--QVKFFGdSNVEIVLIGD-TFDHCLAQALNYtkqHKMNFIDPFNNVYTIAG-----------QGTLA 167
Cdd:PRK13803 349 MgEEDIKRQALNveRMKLLG-ANVIPVLSGSkTLKDAVNEAIRD---WVASVPDTHYLIGSAVGphpypemvayfQSVIG 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487747924 168 KEILNQ-AEKEDKTFDYVFAAIGGGGLISGVSTYFkAHSPHTKIIGVEPTG 217
Cdd:PRK13803 425 EEAKEQlKEQTGKLPDAIIACVGGGSNAIGIFYHF-LDDPSVKLIGVEAGG 474
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
10-221 |
9.75e-10 |
|
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: 59.86 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 10 KDIDEAYLRLKN---IVKE------------TPLQFDHYLSQKY-NCNVYLKREDLQWVRSFKLRgayNAIS-VLSNEE- 71
Cdd:cd06446 4 EELEQEFSKERYdpdFPEElrelykdyvgrpTPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKIN---NALGqALLAKRm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 72 -KNKGITCASAGNHAQGVAYTAKKLNLKAVIFM-PVTTPRQKINQV--KFFGdSNVEIVLIGD-TFDHCLAQALNYTKQH 146
Cdd:cd06446 81 gKKRVIAETGAGQHGVATATACALFGLECEIYMgAVDVERQPLNVFrmELLG-AEVVPVPSGSgTLKDAISEAIRDWVTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 147 KMNFI---------DPFNNV----YTIAGQGTlAKEILnqaEKEDKTFDYVFAAIGGGGLISGVSTYFKAHsPHTKIIGV 213
Cdd:cd06446 160 VEDTHyllgsvvgpHPYPNMvrdfQSVIGEEA-KKQIL---EKEGELPDVVIACVGGGSNAAGLFYPFIND-KDVKLIGV 234
|
....*...
gi 487747924 214 EPTGASSM 221
Cdd:cd06446 235 EAGGCGLE 242
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
22-219 |
1.68e-07 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 53.04 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 22 IVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRgayNAISVLSNEEKNKGITCA-------SAGNHAQGVAYTAKK 94
Cdd:PLN02556 56 LIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDR---PALAMIEDAEKKNLITPGkttliepTSGNMGISLAFMAAM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 95 LNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVL------IGDTFDHClAQALNYTKQHKM--NFIDPFNnvyTIAGQGTL 166
Cdd:PLN02556 133 KGYKMILTMPSYTSLERRVTMRAFG---AELVLtdptkgMGGTVKKA-YELLESTPDAFMlqQFSNPAN---TQVHFETT 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487747924 167 AKEILnqaEKEDKTFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPTGAS 219
Cdd:PLN02556 206 GPEIW---EDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESN 255
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
19-216 |
6.15e-07 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 51.32 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 19 LKNIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYnaiSVLSNEEKNKGITCA-------SAGNHAQGVAYT 91
Cdd:PLN03013 117 VSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGY---SMVTDAEQKGFISPGksvlvepTSGNTGIGLAFI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 92 AKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVL-----------------IGDTFDHCLAQALNYTKQHKMNFidpf 154
Cdd:PLN03013 194 AASRGYRLILTMPASMSMERRVLLKAFG---AELVLtdpakgmtgavqkaeeiLKNTPDAYMLQQFDNPANPKIHY---- 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747924 155 nnvytiagqGTLAKEILNQAEKEdktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPT 216
Cdd:PLN03013 267 ---------ETTGPEIWDDTKGK---VDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPT 316
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
41-202 |
6.52e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 50.89 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 41 NVYLKREDLQWVRSFKLRGAYNAISVLsNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGd 120
Cdd:PRK06450 66 NIWFKLDFLNPTGSYKDRGSVTLISYL-AEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYG- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 121 snVEIVLIGDTFDHCLAQALNYTKQHKMNFIDP-FNNvytiaGQGTLAKEILNQAEKedKTFDYVFAAIGGGGLISGVST 199
Cdd:PRK06450 144 --AEVVRVRGSREDVAKAAENSGYYYASHVLQPqFRD-----GIRTLAYEIAKDLDW--KIPNYVFIPVSAGTLLLGVYS 214
|
...
gi 487747924 200 YFK 202
Cdd:PRK06450 215 GFK 217
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
19-217 |
6.48e-06 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 48.21 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 19 LKNIV-KETPLQFDHYLSQKY-NCN-----VYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVAYT 91
Cdd:PLN02618 59 LKDYVgRETPLYFAERLTEHYkRADgegpeIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 92 AKKLNLKAVIFMPVT-TPRQKIN--QVKFFGdSNVEIVLIGD-TFDHCLAQALNytkqhkmnfiDPFNNVYT-------I 160
Cdd:PLN02618 139 CARFGLECIVYMGAQdMERQALNvfRMRLLG-AEVRPVHSGTaTLKDATSEAIR----------DWVTNVETthyilgsV 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487747924 161 AG-----------QGTLAKEILNQA-EKEDKTFDYVFAAIGGGGLISGVSTYFKAHSpHTKIIGVEPTG 217
Cdd:PLN02618 208 AGphpypmmvrdfHSVIGKETRRQAmEKWGGKPDVLVACVGGGSNAMGLFHEFIDDE-DVRLIGVEAAG 275
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
10-217 |
2.41e-05 |
|
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439903 Cd Length: 400 Bit Score: 46.18 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 10 KDIDEAYLRLKN----------IVKE-----TPLQFDHYLSQKY-NCNVYLKREDLQWVRSFKLrgaYNAI-SVLSNEE- 71
Cdd:COG0133 31 DELEEAYEKAKNdpefqaeldyLLKDyvgrpTPLYFAERLSEKLgGAKIYLKREDLNHTGAHKI---NNALgQALLAKRm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 72 -KNKGITCASAGNHaqGVAyTA---KKLNLKAVIFMPVT-TPRQKINqV---KFFGdSNVEIVLIGD-TfdhcLAQALNY 142
Cdd:COG0133 108 gKKRIIAETGAGQH--GVA-TAtaaALLGLECVVYMGEEdIERQALN-VfrmKLLG-AEVVPVTSGSrT----LKDAVNE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 143 TKQHKM-NFIDPFnnvY---TIAG-----------QGTLAKEILNQA-EKEDKTFDYVFAAIGGG----GLISGvstyFk 202
Cdd:COG0133 179 ALRDWVtNVDDTH---YligSVVGphpypmmvrdfQSVIGREAREQIlEKEGRLPDAVVACVGGGsnaiGIFYP----F- 250
|
250
....*....|....*
gi 487747924 203 AHSPHTKIIGVEPTG 217
Cdd:COG0133 251 LDDESVRLIGVEAGG 265
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
12-217 |
3.36e-05 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 46.18 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 12 IDEAYLRLKNIVKETPlQFDHYLSQK--YNCNVYLKREDLQWVRSFKLRGAYNAISVLSNEEKNKGITCASAGNHAQGVA 89
Cdd:PRK13802 318 LNQRYVGRPSPLTEAP-RFAERVKEKtgLDARVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 90 YTAKKLNLKAVIFM-PVTTPRQKIN--QVKFFGDSNVEIVLigdtFDHCLAQALNYT-KQHKMNFIDPFNNVYTIAGQ-- 163
Cdd:PRK13802 397 TVCAMLGLKCRIYMgQIDARRQALNvaRMRMLGAEVVEVTL----GDRILKDAINEAlRDWVTNVKDTHYLLGTVAGPhp 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487747924 164 ------------GTLAKEILNQAEKEDKTfDYVFAAIGGGGLISGVSTYFkAHSPHTKIIGVEPTG 217
Cdd:PRK13802 473 fpamvrdfqkiiGEEAKQQLQDWYGIDHP-DAICACVGGGSNAIGVMNAF-LDDERVNLYGYEAGG 536
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
10-216 |
3.88e-05 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 45.30 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 10 KDIDEaylrlknIVKETPLQFDHYLSQKYNCNVYLKREDLQWVRSFKLRGAYnaiSVLSNEEKNKGITCA-------SAG 82
Cdd:PLN02565 7 KDVTE-------LIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGY---SMITDAEEKGLIKPGesvliepTSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 83 NHAQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIG---------DTFDHCLAQALN-YTKQHKMNFID 152
Cdd:PLN02565 77 NTGIGLAFMAAAKGYKLIITMPASMSLERRIILLAFG---AELVLTDpakgmkgavQKAEEILAKTPNsYILQQFENPAN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747924 153 PFNNvYTIAG----QGTLAKeilnqaekedktFDYVFAAIGGGGLISGVSTYFKAHSPHTKIIGVEPT 216
Cdd:PLN02565 154 PKIH-YETTGpeiwKGTGGK------------VDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPV 208
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
41-130 |
2.30e-04 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 43.07 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 41 NVYLKREDLQWVRSFKLRGAYNAISvLSNEEKNKGITCASAGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGd 120
Cdd:PRK08197 96 RLWVKDEGLNPTGSFKARGLAVGVS-RAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAG- 173
|
90
....*....|..
gi 487747924 121 SNVEIV--LIGD 130
Cdd:PRK08197 174 AELYLVdgLISD 185
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
187-314 |
4.71e-04 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 41.78 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 187 AIGGGGLISGVSTYFKAHSPHTKIIGVEPTGASSmyqsvvinhsivtLENIDKFvdgaSVARVGDItFDiaKDKVDDYVQ 266
Cdd:PRK11761 174 SMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSS-------------IPGIRRW----PEEYLPKI-FD--ASRVDRVLD 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 487747924 267 VDEGAVCSTILDMYSKQAIVAEPAGALSVSALEQYKKQIENKTIVCIV 314
Cdd:PRK11761 234 VSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENPNAVIVAII 281
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
75-319 |
1.84e-03 |
|
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.
Pssm-ID: 107208 Cd Length: 404 Bit Score: 40.41 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 75 GITCASAGNHAQGVAYTAKKLNLKAVIFMPVTTPRQKINQVKFFGdsnVEIVLIGDTFDHCLAQALNYTKQHKMN-FIDP 153
Cdd:cd06447 136 SIAVGSTGNLGLSIGIMAAALGFKVTVHMSADAKQWKKDKLRSKG---VTVVEYETDYSKAVEEGRKQAAADPMCyFVDD 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 154 FNNV-----YTIAGQgTLAKEILNQAEKEDKT---FDYVFAAIGG--GGLISGVSTYFKAhspHTKIIGVEPTGASSMYQ 223
Cdd:cd06447 213 ENSRdlflgYAVAAS-RLKAQLAELGIKVDAEhplFVYLPCGVGGapGGVAFGLKLIFGD---NVHCFFAEPTHSPCMLL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747924 224 SVV--INHSI----VTLENIDKfVDGASVARVGDITFDIAKDKVDDYVQVDEGavcstilDMYSKQAIVA-------EPA 290
Cdd:cd06447 289 GMAtgLHDKIsvqdIGIDNRTA-ADGLAVGRPSGLVGKLMEPLLSGIYTVEDD-------ELYRLLAMLKdsenievEPS 360
|
250 260
....*....|....*....|....*....
gi 487747924 291 GALSVSALEQYKKQIENKTIVCIVSGGNN 319
Cdd:cd06447 361 AAAGFTGPAQVLSEAEGKRYVRLGYRMEN 389
|
|
| |
