|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
9-402 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 793.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 9 SKFDPDENGHFGIFGGRYVPETLMPILQELETEYKKYRFDKEFWNEVNALLKDYVGRENPLYFAKSISEEI-GAKVYLKR 87
Cdd:PRK04346 1 TYTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLgGAKIYLKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 88 EDLNHTGAHKVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMGAKDVARQELNVFRMKLLGAKVI 167
Cdd:PRK04346 81 EDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 168 AVESGSKTLKDAMNDAIRYWVTNARDTFYIIGTVAGPHPYPMMVRDFQAIIGYEARKQILEKENKLPDYVVACIGGGSNA 247
Cdd:PRK04346 161 PVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 248 IGMFSHFLEDEEVTCIGIEAGGLGLDTNMHGCSLEKGTPGVLHGQCSYLLQDEDGQVLEAHSISAGLDYPGIGPEHSFHK 327
Cdd:PRK04346 241 IGIFHPFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1435909103 328 DNKTVKYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAYLKKAKEKLKD-KIVIVNLSGRGDKDMIQAKSLLDFE 402
Cdd:PRK04346 321 DIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKdQIIVVNLSGRGDKDVFTVAKLLGVI 396
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
7-402 |
0e+00 |
|
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: 787.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 7 KISKFDPDENGHFGIFGGRYVPETLMPILQELETEYKKYRFDKEFWNEVNALLKDYVGRENPLYFAKSISEEI-GAKVYL 85
Cdd:COG0133 2 SSLYSLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLgGAKIYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 86 KREDLNHTGAHKVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMGAKDVARQELNVFRMKLLGAK 165
Cdd:COG0133 82 KREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 166 VIAVESGSKTLKDAMNDAIRYWVTNARDTFYIIGTVAGPHPYPMMVRDFQAIIGYEARKQILEKENKLPDYVVACIGGGS 245
Cdd:COG0133 162 VVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 246 NAIGMFSHFLEDEEVTCIGIEAGGLGLDTNMHGCSLEKGTPGVLHGQCSYLLQDEDGQVLEAHSISAGLDYPGIGPEHSF 325
Cdd:COG0133 242 NAIGIFYPFLDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHAY 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1435909103 326 HKDNKTVKYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAYLK-KAKEKLKDKIVIVNLSGRGDKDMIQAKSLLDFE 402
Cdd:COG0133 322 LKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALkLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGLE 399
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
12-401 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 655.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 12 DPDENGHFGIFGGRYVPETLMPILQELETEYKKYRFDKEFWNEVNALLKDYVGRENPLYFAKSISEEI-GAKVYLKREDL 90
Cdd:PRK13028 8 MPDADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEELgGAQIYLKREDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 91 NHTGAHKVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMGAKDVARQELNVFRMKLLGAKVIAVE 170
Cdd:PRK13028 88 NHTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLGAEVVPVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 171 SGSKTLKDAMNDAIRYWVTNARDTFYIIGTVAGPHPYPMMVRDFQAIIGYEARKQILEKENKLPDYVVACIGGGSNAIGM 250
Cdd:PRK13028 168 RGGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNAIGL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 251 FSHFLEDEEVTCIGIEAGGLGLDTNMHGCSLEKGTPGVLHGQCSYLLQDEDGQVLEAHSISAGLDYPGIGPEHSFHKDNK 330
Cdd:PRK13028 248 FSAFLDDESVRLVGVEPAGRGLDLGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPEHAYLKDIG 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435909103 331 TVKYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAY-LKKAKEKLKDKIVIVNLSGRGDKDMIQAKSLLDF 401
Cdd:PRK13028 328 RVEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYaIKLAPELSKDETILVNLSGRGDKDIDYVAEMLGL 399
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
17-399 |
0e+00 |
|
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: 649.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 17 GHFGIFGGRYVPETLMPILQELETEYKKYRFDKEFWNEVNALLKDYVGRENPLYFAKSISEEIG-AKVYLKREDLNHTGA 95
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGgAKIYLKREDLNHTGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 96 HKVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMGAKDVARQELNVFRMKLLGAKVIAVESGSKT 175
Cdd:TIGR00263 81 HKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 176 LKDAMNDAIRYWVTNARDTFYIIGTVAGPHPYPMMVRDFQAIIGYEARKQILEKENKLPDYVVACIGGGSNAIGMFSHFL 255
Cdd:TIGR00263 161 LKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 256 EDEEVTCIGIEAGGLGLDTNMHGCSLEKGTPGVLHGQCSYLLQDEDGQVLEAHSISAGLDYPGIGPEHSFHKDNKTVKYD 335
Cdd:TIGR00263 241 DDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATYE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1435909103 336 SITDEEALEAFVWLSRSEGIIPAFESAHAIAYLKKAK-EKLKDKIVIVNLSGRGDKDMIQAKSLL 399
Cdd:TIGR00263 321 AITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIApTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
10-392 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 609.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 10 KFDPDENGHFGIFGGRYVPETLMPILQELETEYKKYRFDKEFWNEVNALLKDYVGRENPLYFAKSISEEIGAKVYLKRED 89
Cdd:PRK13803 215 KYLSDPAGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSDIYGARIYLKRED 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 90 LNHTGAHKVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMGAKDVARQELNVFRMKLLGAKVIAV 169
Cdd:PRK13803 295 LNHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIPV 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 170 ESGSKTLKDAMNDAIRYWVTNARDTFYIIGTVAGPHPYPMMVRDFQAIIGYEARKQILEKENKLPDYVVACIGGGSNAIG 249
Cdd:PRK13803 375 LSGSKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 250 MFSHFLEDEEVTCIGIEAGGLGLDTNMHGCSLEKGTPGVLHGQCSYLLQDEDGQVLEAHSISAGLDYPGIGPEHSFHKDN 329
Cdd:PRK13803 455 IFYHFLDDPSVKLIGVEAGGKGVNTGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANLFET 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1435909103 330 KTVKYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAYLKKAKEKLKDK-IVIVNLSGRGDKDM 392
Cdd:PRK13803 535 GRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKdIVIVNLSGRGDKDI 598
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
33-392 |
0e+00 |
|
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: 607.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 33 PILQELETEYKKYRFDKEFWNEVNALLKDYVGRENPLYFAKSISEEI-GAKVYLKREDLNHTGAHKVNNVIAQGLLAKKL 111
Cdd:cd06446 1 PALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKINNALGQALLAKRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 112 GKTKVIAETGAGQHGVATATIAALLGLECTIFMGAKDVARQELNVFRMKLLGAKVIAVESGSKTLKDAMNDAIRYWVTNA 191
Cdd:cd06446 81 GKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 192 RDTFYIIGTVAGPHPYPMMVRDFQAIIGYEARKQILEKENKLPDYVVACIGGGSNAIGMFSHFLEDEEVTCIGIEAGGLG 271
Cdd:cd06446 161 EDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 272 LDTNMHGCSLEKGTPGVLHGQCSYLLQDEDGQVLEAHSISAGLDYPGIGPEHSFHKDNKTVKYDSITDEEALEAFVWLSR 351
Cdd:cd06446 241 LETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLAR 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1435909103 352 SEGIIPAFESAHAIAYLK-KAKEKLKDKIVIVNLSGRGDKDM 392
Cdd:cd06446 321 TEGIIPALESSHAIAYAIkLAKKLGKEKVIVVNLSGRGDKDL 362
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
13-402 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 591.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 13 PDENGHFGIFGGRYVPETLMPILQELETEYKKYRFDKEFWNEVNALLKDYVGRENPLYFAKSISE------EIGAKVYLK 86
Cdd:PLN02618 13 PDSFGRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEhykradGEGPEIYLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 87 REDLNHTGAHKVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMGAKDVARQELNVFRMKLLGAKV 166
Cdd:PLN02618 93 REDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 167 IAVESGSKTLKDAMNDAIRYWVTNARDTFYIIGTVAGPHPYPMMVRDFQAIIGYEARKQILEKENKLPDYVVACIGGGSN 246
Cdd:PLN02618 173 RPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 247 AIGMFSHFLEDEEVTCIGIEAGGLGLDTNMHGCSLEKGTPGVLHGQCSYLLQDEDGQVLEAHSISAGLDYPGIGPEHSFH 326
Cdd:PLN02618 253 AMGLFHEFIDDEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYPGVGPEHSFL 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1435909103 327 KDNKTVKYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAYLKKAKEKLKDKI-VIVNLSGRGDKDMIQAKSLLDFE 402
Cdd:PLN02618 333 KDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTkVVVNCSGRGDKDVNTAIKYLQVS 409
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
15-395 |
6.63e-155 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 453.33 E-value: 6.63e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 15 ENGHFGIFGGRYVPETLMPILQELETEYKKYRFDKEFWNEVNALLKDYVGRENPLY----FAKSISEEIG--AKVYLKRE 88
Cdd:PRK13802 275 QGPYWGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTeaprFAERVKEKTGldARVFLKRE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 89 DLNHTGAHKVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMGAKDVARQELNVFRMKLLGAKVIA 168
Cdd:PRK13802 355 DLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGAEVVE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 169 VESGSKTLKDAMNDAIRYWVTNARDTFYIIGTVAGPHPYPMMVRDFQAIIGYEARKQILEKEN-KLPDYVVACIGGGSNA 247
Cdd:PRK13802 435 VTLGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiDHPDAICACVGGGSNA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 248 IGMFSHFLEDEEVTCIGIEAGGLGLDTNMHGCSLEKGTP--GVLHGQCSYLLQDEDGQVLEAHSISAGLDYPGIGPEHSF 325
Cdd:PRK13802 515 IGVMNAFLDDERVNLYGYEAGGNGPESGKHAIRFAPGTGelGMFQGAKSYLLENDEGQTLDTYSISAGLDYASVGPEHAW 594
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1435909103 326 HKDNKTVKYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAYLKKAKEKLKDK-----IVIVNLSGRGDKDMIQA 395
Cdd:PRK13802 595 LKDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAAADLKAKgyehpVMIVNISGRGDKDMNTA 669
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
68-387 |
1.56e-57 |
|
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: 188.49 E-value: 1.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAKVYLKREDLNHTGAHKVNNVIAQGLLAKKLGKTK--VIAETGAGQHGVATATIAALLGLECTIFMG 145
Cdd:cd00640 2 PLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPkgVIIESTGGNTGIALAAAAARLGLKCTIVMP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 146 AKDvarQELNVFRMKLLGAKVIAVESGsktLKDAMNDAIRYWVTNaRDTFYIigtvagpHPY-PMMVRDFQAIIGYEARK 224
Cdd:cd00640 82 EGA---SPEKVAQMRALGAEVVLVPGD---FDDAIALAKELAEED-PGAYYV-------NQFdNPANIAGQGTIGLEILE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 225 QILEKEnklPDYVVACIGGGSNAIGMFSHFLED-EEVTCIGIEAGglgldtnmhgcslekgtpgvlhgqcsyllqdedgq 303
Cdd:cd00640 148 QLGGQK---PDAVVVPVGGGGNIAGIARALKELlPNVKVIGVEPE----------------------------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 304 vleahsisagldypgigpehsfhkdnktvkYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAYLKKAKEKLKD-KIVIV 382
Cdd:cd00640 190 ------------------------------VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKgKTVVV 239
|
....*
gi 1435909103 383 NLSGR 387
Cdd:cd00640 240 ILTGG 244
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
28-392 |
1.00e-46 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 165.35 E-value: 1.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 28 PETLMPIL------QELETEykkyrfdkEFWN---EVNALLKdyVGRENPLYFAKSISEEIG--AKVYLKREDLNHTGAH 96
Cdd:PRK12391 40 PEDLAPIFpmelieQEVSTE--------RYIDipeEVREIYR--LWRPTPLIRARRLEKALGtpAKIYYKYEGVSPTGSH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 97 KVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMgakdvARQELNV--FR---MKLLGAKVIA--- 168
Cdd:PRK12391 110 KPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACALFGLECTVFM-----VRVSYEQkpYRrslMETYGAEVIPsps 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 169 --VESGSKTLKD----------AMNDAIRYWVTNArDTFYIIGTVAgphPYPMMvrdFQAIIGYEARKQiLEKENKLPDY 236
Cdd:PRK12391 185 dlTEAGRKILAEdpdhpgslgiAISEAVEDAAKRP-DTKYALGSVL---NHVLL---HQTVIGLEAKKQ-LELAGEYPDV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 237 VVACIGGGSNAIGMFSHFLEDE-----EVTCIGIEAgglgldtnmhgcsleKGTPGVLHGQCSYLLQDEDG--QVLEAHS 309
Cdd:PRK12391 257 VIGCVGGGSNFAGLAFPFLGDKlegkkDTRFIAVEP---------------AACPTLTKGEYAYDFGDTAGltPLLKMYT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 310 I----------SAGLDYPGIGPEHSFHKDNKTVKYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAYL----KKAKEKL 375
Cdd:PRK12391 322 LghdfvpppihAGGLRYHGMAPLVSLLVHEGLIEARAYPQTEVFEAAVLFARTEGIVPAPESSHAIAAAideaLKAKEEG 401
|
410
....*....|....*..
gi 1435909103 376 KDKIVIVNLSGRGDKDM 392
Cdd:PRK12391 402 EEKVILFNLSGHGLLDL 418
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
68-366 |
6.94e-43 |
|
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: 151.69 E-value: 6.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAKVYLKREDLNHTGAHKVNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMGAK 147
Cdd:pfam00291 9 PLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 148 DVARqelNVFRMKLLGAKVIAVESGSKTLKDAMNDAIR-----YWVTNARDTFYIIGtvagphpypmmvrdfQAIIGYEa 222
Cdd:pfam00291 89 APPG---KLLLMRALGAEVVLVGGDYDEAVAAARELAAegpgaYYINQYDNPLNIEG---------------YGTIGLE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 223 rkqILEKENKLPDYVVACIGGGSNAIGMFSHFLEDE-EVTCIGIEAGGlgldTNMHGCSLEKGTPGVLHgqcsyllqded 301
Cdd:pfam00291 150 ---ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGpDVRVIGVEPEG----APALARSLAAGRPVPVP----------- 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1435909103 302 gqvlEAHSISAGLDYPGIGPEHSFHKDNKTV-KYDSITDEEALEAFVWLSRSEGIIPAFESAHAIA 366
Cdd:pfam00291 212 ----VADTIADGLGVGDEPGALALDLLDEYVgEVVTVSDEEALEAMRLLARREGIVVEPSSAAALA 273
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
28-392 |
1.38e-39 |
|
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport and metabolism]; Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440961 Cd Length: 433 Bit Score: 146.43 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 28 PETLMP------ILQELETEykkyRFdKEFWNEVNALLKdyVGRENPLYFAKSISEEIG--AKVYLKREDLNHTGAHKVN 99
Cdd:COG1350 41 PEDLAPifpmelIEQEMSTE----RW-IEIPEEVREIYR--LWRPSPLYRARRLEKALGtpAKIYYKYEGVSPAGSHKPN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 100 NVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAALLGLECTIFMgakdvarqelnV--------FR---MKLLGAKVIA 168
Cdd:COG1350 114 TAVAQAYYNKKEGIKRLTTETGAGQWGSALSFACALFGLECTVYM-----------VkvsyeqkpYRrsmMETYGAEVIP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 169 -----VESGSKTLKD----------AMNDAIRYWVTNArDTFYIIGTVAGpHpypmmVRDFQAIIGYEARKQiLEKENKL 233
Cdd:COG1350 183 spsdlTEAGRKILAEdpdtpgslgiAISEAVEDAATRD-DTKYALGSVLN-H-----VLLHQTVIGLEAKKQ-LEKAGEY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 234 PDYVVACIGGGSNAIGMFSHFLED-----EEVTCIGIEAGglgldtnmhGC-SLEKG------------TPgvLHGQcsY 295
Cdd:COG1350 255 PDVVIGCAGGGSNFAGLAFPFLRDklrgkKDVRFIAVEPA---------ACpTLTRGvyaydfgdtaglTP--LLKM--Y 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 296 LLqdedGQVLEAHSISA-GLDYPGIGPEHSFHKDNKTVKYDSITDEEALEAFVWLSRSEGIIPAFESAHAIAY-----LK 369
Cdd:COG1350 322 TL----GHDFIPPPIHAgGLRYHGMAPLVSQLYHDGLIEAVAYPQLEVFEAGVLFARTEGIVPAPESAHAIKAaideaLK 397
|
410 420
....*....|....*....|...
gi 1435909103 370 KAKEKLKDKIVIvNLSGRGDKDM 392
Cdd:COG1350 398 CKEEGEEKTILF-NLSGHGHFDL 419
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
68-366 |
1.76e-18 |
|
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: 86.41 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAKVYLKREDLNHTGAHKVNNVIAQGLLAKKLGKTKVI-AETGAGqhGVATATIAALLGLECTIFMGA 146
Cdd:COG0498 68 PLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVcASSGNG--SAALAAYAARAGIEVFVFVPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 147 KDVArqELNVFRMKLLGAKVIAVEsGSKTlkDAMNDAIRYwvtNARDTFYIIGTVagpHPYpmmVRDFQAIIGYEarkqI 226
Cdd:COG0498 146 GKVS--PGQLAQMLTYGAHVIAVD-GNFD--DAQRLVKEL---AADEGLYAVNSI---NPA---RLEGQKTYAFE----I 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 227 LEKENKLPDYVVACIGGGSNAIGMFSHFLEDEEvtcigieaggLGLDTNMhgcslekgtPGVLHGQ---CSYLLQD---- 299
Cdd:COG0498 208 AEQLGRVPDWVVVPTGNGGNILAGYKAFKELKE----------LGLIDRL---------PRLIAVQatgCNPILTAfetg 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435909103 300 -EDGQVLEAHSISAGLD--YPGIGPE--HSFHKDNKTVkyDSITDEEALEAFVWLSRSEGIIPAFESAHAIA 366
Cdd:COG0498 269 rDEYEPERPETIAPSMDigNPSNGERalFALRESGGTA--VAVSDEEILEAIRLLARREGIFVEPATAVAVA 338
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
57-244 |
1.01e-17 |
|
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: 82.92 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 57 ALLKDYVgRENPLYFAKSISEEIGAKVYLKREDLNHTGAHKV----NNVIAqglLAKKLGKTKVIAETgAGQHGVATATI 132
Cdd:cd01562 9 ARIKPVV-RRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIrgayNKLLS---LSEEERAKGVVAAS-AGNHAQGVAYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 133 AALLGLECTIFMgAKDVARQELNvfRMKLLGAKViaVESGSkTLKDAMNDAIRYwvtnARDT--FYIigtvagpHPY--P 208
Cdd:cd01562 84 AKLLGIPATIVM-PETAPAAKVD--ATRAYGAEV--VLYGE-DFDEAEAKAREL----AEEEglTFI-------HPFddP 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1435909103 209 MMVRDfQAIIGYEarkqILEKENKLpDYVVACIGGG 244
Cdd:cd01562 147 DVIAG-QGTIGLE----ILEQVPDL-DAVFVPVGGG 176
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
68-366 |
1.10e-16 |
|
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: 80.33 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAK-VYLKREDLNHTGAHKvNNVIAQGL-LAKKLGKTKVIAETgAGQHGVATATIAALLGLECTIFMG 145
Cdd:cd01563 24 PLVRAPRLGERLGGKnLYVKDEGLNPTGSFK-DRGMTVAVsKAKELGVKAVACAS-TGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 146 AkDVARQELNvfRMKLLGAKVIAVESG-SKTLKDAMNDAIRYW--VTNARDTFYIIGtvagphpypmmvrdfQAIIGYEA 222
Cdd:cd01563 102 A-GKALGKLA--QALAYGATVLAVEGNfDDALRLVRELAEENWiyLSNSLNPYRLEG---------------QKTIAFEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 223 RKQIlekENKLPDYVVACIGGGSNAIGMFSHFLE-------DEEVTCIGIEAgglgldtnmHGCSlekgtPGVLHgqcsY 295
Cdd:cd01563 164 AEQL---GWEVPDYVVVPVGNGGNITAIWKGFKElkelgliDRLPRMVGVQA---------EGAA-----PIVRA----F 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1435909103 296 LLQDEDGQVLE-----AHSISAGldYPGIGPE--HSFHKDNKTVkyDSITDEEALEAFVWLSRSEGIIPAFESAHAIA 366
Cdd:cd01563 223 KEGKDDIEPVEnpetiATAIRIG--NPASGPKalRAVRESGGTA--VAVSDEEILEAQKLLARTEGIFVEPASAASLA 296
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
57-267 |
3.45e-16 |
|
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: 78.92 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 57 ALLKDYVgRENPLYFAKSISEEIGAKVYLKREDLNHTGAHKVN---NVIAQglLAKKLGKTKVIAETgAGQHGVATATIA 133
Cdd:COG1171 16 ARIAGVV-RRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRgayNALAS--LSEEERARGVVAAS-AGNHAQGVAYAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 134 ALLGLECTIFMgAKDVARQELNvfRMKLLGAKVIAVESgskTLKDAMNDAIRYwvtnARDT--FYIigtvagpHPY-PMM 210
Cdd:COG1171 92 RLLGIPATIVM-PETAPAVKVA--ATRAYGAEVVLHGD---TYDDAEAAAAEL----AEEEgaTFV-------HPFdDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1435909103 211 VRDFQAIIGYEarkqILEkENKLPDYVVACIGGGSNAIGMFSHFLE-DEEVTCIGIEA 267
Cdd:COG1171 155 VIAGQGTIALE----ILE-QLPDLDAVFVPVGGGGLIAGVAAALKAlSPDIRVIGVEP 207
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
68-355 |
4.69e-14 |
|
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: 72.16 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAKVYLKREDLNHTGAHK-------VNNVIAQGLLakKLGKTkvIAETGAGQHGVATATIAALLGLEC 140
Cdd:cd01561 4 PLVRLNRLSPGTGAEIYAKLEFFNPGGSVKdrialymIEDAEKRGLL--KPGTT--IIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 141 TIFMGAK-DVARQELnvfrMKLLGAKVIAVEsgsKTLKDAMNDAIRYwvtnARDtfyiigtVAGPHPYPMMVRDFQAIIG 219
Cdd:cd01561 80 IIVMPETmSEEKRKL----LRALGAEVILTP---EAEADGMKGAIAK----ARE-------LAAETPNAFWLNQFENPAN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 220 YEAR-----KQILEKENKLPDYVVACIGGGSNAIGMFSHFLE-DEEVTCIGIEAGGLGLdtnmhgcsLEKGTPGvlhgqc 293
Cdd:cd01561 142 PEAHyettaPEIWEQLDGKVDAFVAGVGTGGTITGVARYLKEkNPNVRIVGVDPVGSVL--------FSGGPPG------ 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1435909103 294 syllqdedgqvleAHSIsagldyPGIGpeHSFHKDN-KTVKYD---SITDEEALEAFVWLSRSEGI 355
Cdd:cd01561 208 -------------PHKI------EGIG--AGFIPENlDRSLIDevvRVSDEEAFAMARRLAREEGL 252
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
59-286 |
1.41e-11 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 65.60 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 59 LKDYVgRENPLYFAKSISEEIGAKVYLKREDLNHTGAHKVN---NVIAQgLLAKKLGKTKVIAEtgAGQH--GVATAtiA 133
Cdd:PRK08639 19 LKDVV-PETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRgayNAISQ-LSDEELAAGVVCAS--AGNHaqGVAYA--C 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 134 ALLGLECTIFMGAKdVARQELNvfRMKLLGAKVIAVESGSKTLKDAMNDAIRYWVTNAR---DTFYIIGTVAGphpypmm 210
Cdd:PRK08639 93 RHLGIPGVIFMPVT-TPQQKID--QVRFFGGEFVEIVLVGDTFDDSAAAAQEYAEETGAtfiPPFDDPDVIAG------- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1435909103 211 vrdfQAIIGYEARKQIleKENKLPDYVVACIGGGSNAIGMfSHFLEDE--EVTCIGIEAGGLgldTNMHGcSLEKGTP 286
Cdd:PRK08639 163 ----QGTVAVEILEQL--EKEGSPDYVFVPVGGGGLISGV-TTYLKERspKTKIIGVEPAGA---ASMKA-ALEAGKP 229
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
68-360 |
1.63e-10 |
|
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: 61.67 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAKV--YLKREDLNHTGA------HKVNNVIAQgllAKKLGKTKVIAeTGAGQ--HGVATATIAALLG 137
Cdd:cd06449 2 PIQYLPRLSEHLGGKVeiYAKRDDCNSGLAfggnkiRKLEYLLPD---ALAKGADTLVT-VGGIQsnHTRQVAAVAAKLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 138 LECTIFMGAKDVARQEL-----NVFRMKLLGAKVIAVESGSKTLKDAMNDAIRYWVTNARDTFYIIGTVAGPHPYpmmvr 212
Cdd:cd06449 78 LKCVLVQENWVPYSDAVydrvgNILLSRIMGADVRLVSAGFDIGIRKSFEEAAEEVEAKGGKPYVIPAGGSEHPL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 213 dfqAIIGY-EARKQILEKENKLP---DYVVACIGGGSNAIGM---FSHFLEDEEVtcIGIEAGGLGldtnmhgcslEKGT 285
Cdd:cd06449 153 ---GGLGYvGFVLEIAQQEEELGfkfDSIVVCSVTGSTHAGLsvgLAALGRQRRV--IGIDASAKP----------EKTK 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1435909103 286 PGVLHGQCSYLLqdedGQVLEAHSISAGLDYPGIGPEHsfhkdnktvkydSITDEEALEAFVWLSRSEGII--PAFE 360
Cdd:cd06449 218 AQVLRIAQAKLA----EEGLEVKEEDVVLDDDYAAPEY------------GIPNDETIEAIKLCARLEGIItdPVYE 278
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
59-244 |
1.20e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 59.40 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 59 LKDYVgRENPLYFAKSISEEIGAKVYLKREDLNHTGAHKVNNVIAQGLLAKKLGK--TKVIAETgAGQHGVATATIAALL 136
Cdd:PRK06608 17 IKQYL-HLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TGNHGQAVAYASKLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 137 GLECTIFMgakdvarqELNVFRMKL-----LGAKVIAV----ESGSKTLKDAMNDAirYWV--TNARDTFYIIGTVAgph 205
Cdd:PRK06608 95 GIKTRIYL--------PLNTSKVKQqaalyYGGEVILTntrqEAEEKAKEDEEQGF--YYIhpSDSDSTIAGAGTLC--- 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1435909103 206 pypmmvrdfqaiigYEARKQILEKenklPDYVVACIGGG 244
Cdd:PRK06608 162 --------------YEALQQLGFS----PDAIFASCGGG 182
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
59-252 |
3.07e-09 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 57.78 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 59 LKDYVgRENPLYFAKSISEEIGAKVYLKREDLNHTGAHKVN---NVIaqGLLAKKLGKTKVIAETgAGQHGVATATIAAL 135
Cdd:PRK06815 14 LRPQV-RVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRgasNKL--RLLNEAQRQQGVITAS-SGNHGQGVALAAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 136 LGLECTIFMgAKDVARQELNvfRMKLLGAKVIAV-ESGSKTLKDAMNDAIRYWVTnardtfYIigtvagpHPYpmmvRDF 214
Cdd:PRK06815 90 AGIPVTVYA-PEQASAIKLD--AIRALGAEVRLYgGDALNAELAARRAAEQQGKV------YI-------SPY----NDP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1435909103 215 QAI-----IGYEARKQILEkenklPDYVVACIGGGsnaiGMFS 252
Cdd:PRK06815 150 QVIagqgtIGMELVEQQPD-----LDAVFVAVGGG----GLIS 183
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
83-244 |
1.01e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 56.12 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 83 VYLKREDLNHTGAHKV----NNviaqgLLAKKLGKTKVIAETGaGQHGVATATIAALLGLECTIFMGAkdVARQElNVFR 158
Cdd:PRK08246 39 VWLKLEHLQHTGSFKArgafNR-----LLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVPATVFVPE--TAPPA-KVAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 159 MKLLGAKVIAVESgskTLKDAMNDAIRY------WVTNARDTfyiIGTVAGphpypmmvrdfQAIIGYEARKQILEkenk 232
Cdd:PRK08246 110 LRALGAEVVVVGA---EYADALEAAQAFaaetgaLLCHAYDQ---PEVLAG-----------AGTLGLEIEEQAPG---- 168
|
170
....*....|..
gi 1435909103 233 lPDYVVACIGGG 244
Cdd:PRK08246 169 -VDTVLVAVGGG 179
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
65-284 |
1.09e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 53.05 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 65 RENPLYFAKSISEEIGAKVYLKREDLNHTGAHKV---NNVIAQgLLAKKLGKTKVIAETgaGQHGVATATIAALLGLECT 141
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLrgaTNALLS-LSAQERARGVVTAST--GNHGRALAYAARALGIRAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 142 IFMGAkdvARQELNVFRMKLLGAKVIAVesgSKTLKDAMNDAIRYwvtnARDTFYiigTVAGPHPYPMMVRDfQAIIGYE 221
Cdd:PRK07476 95 ICMSR---LVPANKVDAIRALGAEVRIV---GRSQDDAQAEVERL----VREEGL---TMVPPFDDPRIIAG-QGTIGLE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1435909103 222 arkqILEkenKLPD--YVVACIGGGsnaiGMFSHfledeevtcIGIEAGGLGLDTNMHGCSLEKG 284
Cdd:PRK07476 161 ----ILE---ALPDvaTVLVPLSGG----GLASG---------VAAAVKAIRPAIRVIGVSMERG 205
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
63-289 |
1.76e-07 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 53.00 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 63 VGRENPLYFAKSISEEIGAKVYLKREDLNHTGAHKVN---NVIAQglLAKKLGKTKVIAETgAGQHGVATATIAALLGLE 139
Cdd:PLN02550 106 VAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRgayNMMAK--LPKEQLDKGVICSS-AGNHAQGVALSAQRLGCD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 140 CTIFMgakDVARQELNVFRMKLLGAKVIAVesgsktlKDAMNDAIRYWVTNARDTFYiigTVAGPHPYPMMVRDfQAIIG 219
Cdd:PLN02550 183 AVIAM---PVTTPEIKWQSVERLGATVVLV-------GDSYDEAQAYAKQRALEEGR---TFIPPFDHPDVIAG-QGTVG 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435909103 220 YEARKQIlekenKLPDYVVACIGGGSNAIGMFSHFLE--DEEVTCIGIEAGglglDTNMHGCSLEKGTPGVL 289
Cdd:PLN02550 249 MEIVRQH-----QGPLHAIFVPVGGGGLIAGIAAYVKrvRPEVKIIGVEPS----DANAMALSLHHGERVML 311
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
68-254 |
1.29e-06 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 49.70 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIG-AKVYLKREDLNHTGAHKVNNVIAQGLLAKKLGKTKVIAETgAGQHGVATATIAALLGLECTIFmga 146
Cdd:PRK06381 17 PLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGT-CGNYGASIAYFARLYGLKAVIF--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 147 kdVARQELN--VFRMKLLGAKVIAVESgsktlkdAMNDAIRYWVTNARDTFYiigtvagphpY---PMMVRDFQAIIGYE 221
Cdd:PRK06381 93 --IPRSYSNsrVKEMEKYGAEIIYVDG-------KYEEAVERSRKFAKENGI----------YdanPGSVNSVVDIEAYS 153
|
170 180 190
....*....|....*....|....*....|....
gi 1435909103 222 A-RKQILEKENKLPDYVVACIGGGSNAIGMFSHF 254
Cdd:PRK06381 154 AiAYEIYEALGDVPDAVAVPVGNGTTLAGIYHGF 187
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
63-266 |
1.86e-06 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 49.80 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 63 VGRENPLYFAKSISEEIGAKVYLKREDLNHTGAHKVN---NVIAQgLLAKKLGKTKVIAETGAGQHGVATAtiAALLGLE 139
Cdd:PRK12483 34 VARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRgayNKMAR-LPAEQLARGVITASAGNHAQGVALA--AARLGVK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 140 CTIFMgakDVARQELNVFRMKLLGAKVI-AVESGSKTLKDAMNdairywVTNARDTFYIigtvagpHPY--PMMVRDfQA 216
Cdd:PRK12483 111 AVIVM---PRTTPQLKVDGVRAHGGEVVlHGESFPDALAHALK------LAEEEGLTFV-------PPFddPDVIAG-QG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1435909103 217 IIGYEarkqILEKENKLPDYVVACIGGGSNAIGMFSHFLE-DEEVTCIGIE 266
Cdd:PRK12483 174 TVAME----ILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYvRPEIKVIGVE 220
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
68-249 |
3.18e-06 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 48.67 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAKVYLKREDLnhTG-------AHKVNNVIAQgllAKKLGKTKVIAeTGAGQ--HGVATATIAALLGL 138
Cdd:PRK03910 17 PLEPLPRLSAALGPDIYIKRDDL--TGlalggnkTRKLEFLLAD---ALAQGADTLIT-AGAIQsnHARQTAAAAAKLGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 139 ECTIFMGAKDVARQEL-----NVFRMKLLGAKVIAVESGSktlkdamndairywvtnardtfyiigtvagphpypmmvrD 213
Cdd:PRK03910 91 KCVLLLENPVPTEAENylangNVLLDDLFGAEIHVVPAGT---------------------------------------D 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 1435909103 214 FQAIIgyEARKQILEKENKLPdYVVAciGGGSNAIG 249
Cdd:PRK03910 132 MDAQL--EELAEELRAQGRRP-YVIP--VGGSNALG 162
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
68-367 |
4.70e-06 |
|
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: 48.06 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAKVYLKREDLNHTGAHK---VNNVIAQGLLAKKLGKTKVIAETGaGQHGVATATIAALLGLECTIFM 144
Cdd:cd06448 3 PLIESTALSKTAGCNVFLKLENLQPSGSFKirgIGHLCQKSAKQGLNECVHVVCSSG-GNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 145 gakDVARQELNVFRMKLLGAKVIaveSGSKTLKDAMNdairywvtnardtfYIIGTVAGPHPYPMMVRDF--------QA 216
Cdd:cd06448 82 ---PESTKPRVVEKLRDEGATVV---VHGKVWWEADN--------------YLREELAENDPGPVYVHPFddpliwegHS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 217 IIGYEARKQIleKENKLPDYVVACIGGGsnaiGMFSHFLE------DEEVTCIGIEAgglgldtnmHGC-----SLEKGT 285
Cdd:cd06448 142 SMVDEIAQQL--QSQEKVDAIVCSVGGG----GLLNGIVQglerngWGDIPVVAVET---------EGAhslnaSLKAGK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 286 PGVLHgqcsyllqdedgqvlEAHSISAGLDYPGIGPE--HSFHKDNktVKYDSITDEEALEAFVWLSRSEGII--PAFES 361
Cdd:cd06448 207 LVTLP---------------KITSVATSLGAKTVSSQalEYAQEHN--IKSEVVSDRDAVQACLRFADDERILvePACGA 269
|
....*.
gi 1435909103 362 AHAIAY 367
Cdd:cd06448 270 ALAVVY 275
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
59-362 |
5.59e-06 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 48.06 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 59 LKDYVGrENPLYFAKSISEEIGAKVYLKREDLNHTGAHK---VNNVIAQGLLAKKLGKTKVIAETGAGQHGVATATIAAL 135
Cdd:PLN02356 47 LIDAIG-NTPLIRINSLSEATGCEILGKCEFLNPGGSVKdrvAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 136 LGLECTIFMgAKDVARQELNVfrMKLLGAKVIAVESGSKTLKDA-MNDAIR--------------YWVTNARDTFYIIGT 200
Cdd:PLN02356 126 YGCKCHVVI-PDDVAIEKSQI--LEALGATVERVRPVSITHKDHyVNIARRraleanelaskrrkGSETDGIHLEKTNGC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 201 VAGPHPYPMMVRD----------FQAIIGYEARKQ-----ILEKENKLPDYVVACIGGGSNAIGMfSHFLED--EEVTCI 263
Cdd:PLN02356 203 ISEEEKENSLFSSsctggffadqFENLANFRAHYEgtgpeIWEQTQGNLDAFVAAAGTGGTLAGV-SRFLQEknPNIKCF 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 264 GIEAGGLGLdtnmhgcsLEKGTPGVLhgqcsYLLQDEDGQVLEA--HSISAGLdypGIgpeHSFHKDNKTVKYDSI---T 338
Cdd:PLN02356 282 LIDPPGSGL--------FNKVTRGVM-----YTREEAEGRRLKNpfDTITEGI---GI---NRLTQNFLMAKLDGAfrgT 342
|
330 340
....*....|....*....|....
gi 1435909103 339 DEEALEAFVWLSRSEGIIPAFESA 362
Cdd:PLN02356 343 DKEAVEMSRYLLKNDGLFVGSSSA 366
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
63-244 |
1.13e-05 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 47.44 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 63 VGRENPLYFAKSISEEIGAKVYLKREDLN--HT----GAHkvnNVIAQglLAKKLGKTKVIAETgAGQH--GVATAtiAA 134
Cdd:PRK09224 17 VAQETPLEKAPKLSARLGNQVLLKREDLQpvFSfklrGAY---NKMAQ--LTEEQLARGVITAS-AGNHaqGVALS--AA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 135 LLGLECTIFMgakDVARQELNVFRMKLLGAKViaVESGSkTLKDAMNDAIRYWVTNARdTFYiigtvagpHPY--PmMVR 212
Cdd:PRK09224 89 RLGIKAVIVM---PVTTPDIKVDAVRAFGGEV--VLHGD-SFDEAYAHAIELAEEEGL-TFI--------HPFddP-DVI 152
|
170 180 190
....*....|....*....|....*....|..
gi 1435909103 213 DFQAIIGYEarkqILEKENKLPDYVVACIGGG 244
Cdd:PRK09224 153 AGQGTIAME----ILQQHPHPLDAVFVPVGGG 180
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
68-267 |
4.60e-04 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 41.94 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKSISEEIGAKV--YLKREDLNHT---GAHK-------VNNVIAQGllakklgktkviAET----GAGQ--HGVAT 129
Cdd:PRK12390 17 PIHPLKRLSAHLGGKVelYAKREDCNSGlafGGNKtrkleylVPDALAQG------------ADTlvsiGGVQsnHTRQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 130 ATIAALLGLECtifmgakdVARQEL-------------NVFRMKLLGAKVIAVESG-SKTLKDAMNDAIRYwVTNARDTF 195
Cdd:PRK12390 85 AAVAAHLGMKC--------VLVQENwvnyedavydrvgNILLSRIMGADVRLVPDGfDIGIRKSWEDALED-VRAAGGKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1435909103 196 YIIGTVAGPHPYpmmvrdfqAIIGY-----EARKQilEKENKLP-DYVVACIGGGSNAIGMFSHFLEDEEVT-CIGIEA 267
Cdd:PRK12390 156 YAIPAGASDHPL--------GGLGFvgfaeEVRAQ--EAELGFKfDYIVVCSVTGSTQAGMVVGFAADGRARrVIGIDA 224
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
54-244 |
8.03e-04 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 41.26 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 54 EVNALLKDYVgRENPLYFAKSISEEIGAKVYLKREDLNHTGAHKV---NNVIAQglLAKKLGKTKVIAETgAGQHGVATA 130
Cdd:PRK08638 16 EAKQRLAGRI-RKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIrgaFNKLSS--LTDAEKRKGVVACS-AGNHAQGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 131 TIAALLGLECTIFM--GAKdVARQELNvfrmKLLGAKVIavesgsktLK-DAMNDAIRYWVTNARDTFYIIgtvagPHPY 207
Cdd:PRK08638 92 LSCALLGIDGKVVMpkGAP-KSKVAAT----CGYGAEVV--------LHgDNFNDTIAKVEEIVEEEGRTF-----IPPY 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1435909103 208 -PMMVRDFQAIIGYEARKQILEKENklpdyVVACIGGG 244
Cdd:PRK08638 154 dDPKVIAGQGTIGLEILEDLWDVDT-----VIVPIGGG 186
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
68-263 |
2.25e-03 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 39.80 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 68 PLYFAKsISEEIGAKVYLKREDLNHTGAHK---VNNVIAQGLLAKKLGktKVIAETgaGQHGVATATIAALLGLECTIFM 144
Cdd:PRK05638 68 PLIRAR-ISEKLGENVYIKDETRNPTGSFRdrlATVAVSYGLPYAANG--FIVASD--GNAAASVAAYSARAGKEAFVVV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 145 GAKdVARQELnvFRMKLLGAKVIavesgskTLKDAMNDAIRY--------WVTNARDTFYIIGTvagphpypmmvrDFQA 216
Cdd:PRK05638 143 PRK-VDKGKL--IQMIAFGAKII-------RYGESVDEAIEYaeelarlnGLYNVTPEYNIIGL------------EGQK 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1435909103 217 IIGYEarkqILEKENklPDYVVACIGGGSNAIGMFSHFLEDEEVTCI 263
Cdd:PRK05638 201 TIAFE----LWEEIN--PTHVIVPTGSGSYLYSIYKGFKELLEIGVI 241
|
|
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
66-151 |
3.11e-03 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 39.49 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 66 ENPLYFAKSISEEIGAKVYLKREDLN--HTGAHKVNNViaQGLLAKKLGK-TKVIAETGA--GQHGVATATIAALLGLEC 140
Cdd:PRK14045 21 ETPIQYLPNISRELGADVYVKRDDLTglGIGGNKIRKL--EYLLGDALSRgADVVITVGAvhSNHAFVTGLAAKKLGLDA 98
|
90
....*....|.
gi 1435909103 141 TIFMGAKDVAR 151
Cdd:PRK14045 99 VLVLRGKEELK 109
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
66-144 |
3.80e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 39.11 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 66 ENPLYFAKSISEEIGAKVYLKREDLNHTGAHKVN---NVIAQglLAKKLGKTKVIAETgAGQHGVATATIAALLGLECTI 142
Cdd:PRK07334 23 RTPCVHSRTLSQITGAEVWLKFENLQFTASFKERgalNKLLL--LTEEERARGVIAMS-AGNHAQGVAYHAQRLGIPATI 99
|
..
gi 1435909103 143 FM 144
Cdd:PRK07334 100 VM 101
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
78-256 |
3.88e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 39.04 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 78 EIGAKVYLKREDLNHTGAHKVNNVIAQGLLAKKLGKTKVIAETgAGQHGVATATIAALLGLECTIFMgaKDVARQElNVF 157
Cdd:PRK08329 69 KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDS-SGNAALSLALYSLSEGIKVHVFV--SYNASKE-KIS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 158 RMKLLGAKVIAVEsGSKTlkDAMNDAIRY-------WVTNARDTFYIIGTvagphpypmmvrdfqAIIGYEARKQIleke 230
Cdd:PRK08329 145 LLSRLGAELHFVE-GDRM--EVHEEAVKFskrnnipYVSHWLNPYFLEGT---------------KTIAYEIYEQI---- 202
|
170 180
....*....|....*....|....*.
gi 1435909103 231 nKLPDYVVACIGGGSNAIGMFSHFLE 256
Cdd:PRK08329 203 -GVPDYAFVPVGSGTLFLGIWKGFKE 227
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
59-144 |
6.90e-03 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 38.08 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435909103 59 LKDYVGReNPLYFAKSISEEIGAKVYLKREDLNHTGAHKVN---NVIAQGLLAKKlgKTKVIAETgAGQHGVATATIAAL 135
Cdd:PRK07048 18 LAGVAHR-TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRgayNALSQFSPEQR--RAGVVTFS-SGNHAQAIALSARL 93
|
....*....
gi 1435909103 136 LGLECTIFM 144
Cdd:PRK07048 94 LGIPATIVM 102
|
|
| |
