|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
5-391 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 791.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 5 LNPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGT-NTTLYLKREDLLHG 83
Cdd:PRK04346 7 ENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLgGAKIYLKREDLNHT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 84 GAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGS 163
Cdd:PRK04346 87 GAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVVPVTSGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 164 ATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFAD 243
Cdd:PRK04346 167 RTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNAIGIFHP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 244 FINETDVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRAD 323
Cdd:PRK04346 247 FIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDIGRAE 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446131658 324 YVSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRENPeKEQLLVVNLSGRGDKDIFTVHDIL 391
Cdd:PRK04346 327 YVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLG-KDQIIVVNLSGRGDKDVFTVAKLL 393
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
6-395 |
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: 755.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 6 NPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGT-NTTLYLKREDLLHGG 84
Cdd:COG0133 11 KGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLgGAKIYLKREDLNHTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 85 AHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSA 164
Cdd:COG0133 91 AHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAEVVPVTSGSR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 165 TLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADF 244
Cdd:COG0133 171 TLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGSNAIGIFYPF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 245 INETDVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRADY 324
Cdd:COG0133 251 LDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDTGRAEY 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446131658 325 VSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRENPeKEQLLVVNLSGRGDKDIFTVHDILKARG 395
Cdd:COG0133 331 VSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELS-KDQIIVVNLSGRGDKDVDTVAKYLGLED 400
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
8-391 |
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: 665.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 8 YFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGTNTT-LYLKREDLLHGGAH 86
Cdd:TIGR00263 2 YFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGGAkIYLKREDLNHTGAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 87 KTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATL 166
Cdd:TIGR00263 82 KINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 167 KDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADFIN 246
Cdd:TIGR00263 162 KDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 247 ETDVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRADYVS 326
Cdd:TIGR00263 242 DPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATYEA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446131658 327 ITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMrENPEKEQLLVVNLSGRGDKDIFTVHDIL 391
Cdd:TIGR00263 322 ITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIA-PTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
8-392 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 637.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 8 YFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGTNTT-LYLKREDLLHGGAH 86
Cdd:PRK13028 14 FFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEELGGAqIYLKREDLNHTGAH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 87 KTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATL 166
Cdd:PRK13028 94 KINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLGAEVVPVTRGGRTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 167 KDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADFIN 246
Cdd:PRK13028 174 KEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNAIGLFSAFLD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 247 ETDVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRADYVS 326
Cdd:PRK13028 254 DESVRLVGVEPAGRGLDLGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPEHAYLKDIGRVEYVT 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446131658 327 ITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRENPeKEQLLVVNLSGRGDKDIFTVHDILK 392
Cdd:PRK13028 334 ATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAPELS-KDETILVNLSGRGDKDIDYVAEMLG 398
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
23-387 |
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: 613.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 23 PALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGT-NTTLYLKREDLLHGGAHKTNQVLGQALLAKRM 101
Cdd:cd06446 1 PALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKINNALGQALLAKRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 102 GKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSY 181
Cdd:cd06446 81 GKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 182 ETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADFINETDVGLIGVEPGGHG 261
Cdd:cd06446 161 EDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 262 IETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRADYVSITDDEALEAFKTLCL 341
Cdd:cd06446 241 LETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLAR 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446131658 342 HEGIIPALESSHALAHALKMMRENPeKEQLLVVNLSGRGDKDIFTV 387
Cdd:cd06446 321 TEGIIPALESSHAIAYAIKLAKKLG-KEKVIVVNLSGRGDKDLQTV 365
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
6-386 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 581.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 6 NPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGTNTTLYLKREDLLHGGA 85
Cdd:PRK13803 221 AGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSDIYGARIYLKREDLNHTGS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 86 HKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSAT 165
Cdd:PRK13803 301 HKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIPVLSGSKT 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 166 LKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADFI 245
Cdd:PRK13803 381 LKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIGIFYHFL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 246 NETDVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRADYV 325
Cdd:PRK13803 461 DDPSVKLIGVEAGGKGVNTGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANLFETGRAIYT 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446131658 326 SITDDEALEAFKTLCLHEGIIPALESSHALAhALKMMRENPEKEQLLVVNLSGRGDKDIFT 386
Cdd:PRK13803 541 SVTDEEALDAFKLLAKLEGIIPALESSHALA-YLKEGRKKFKKKDIVIVNLSGRGDKDIPT 600
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
9-395 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 525.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 9 FGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITA------GTNTTLYLKREDLLH 82
Cdd:PLN02618 19 FGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEhykradGEGPEIYLKREDLNH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 83 GGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSG 162
Cdd:PLN02618 99 TGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEVRPVHSG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 163 SATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFA 242
Cdd:PLN02618 179 TATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSNAMGLFH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 243 DFINETDVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRA 322
Cdd:PLN02618 259 EFIDDEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYPGVGPEHSFLKDTGRA 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446131658 323 DYVSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMrENPEKEQLLVVNLSGRGDKDIFTVHDILKARG 395
Cdd:PLN02618 339 EYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLC-PTLPDGTKVVVNCSGRGDKDVNTAIKYLQVSS 410
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
7-386 |
2.29e-158 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 462.19 E-value: 2.29e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 7 PYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITA------GTNTTLYLKREDL 80
Cdd:PRK13802 277 PYWGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTEAPRFAErvkektGLDARVFLKREDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 81 LHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVH 160
Cdd:PRK13802 357 NHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGAEVVEVT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 161 SGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREG-RLPDAVIACVGGGSNAIG 239
Cdd:PRK13802 437 LGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiDHPDAICACVGGGSNAIG 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 240 MFADFINETDVGLIGVEPGGHGIETGEHG---APlKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYL 316
Cdd:PRK13802 517 VMNAFLDDERVNLYGYEAGGNGPESGKHAirfAP-GTGELGMFQGAKSYLLENDEGQTLDTYSISAGLDYASVGPEHAWL 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446131658 317 NSTGRADYVSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRENPEK---EQLLVVNLSGRGDKDIFT 386
Cdd:PRK13802 596 KDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAAADLKAKgyeHPVMIVNISGRGDKDMNT 668
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
57-379 |
2.86e-54 |
|
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: 179.63 E-value: 2.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 57 TALTKCQNITAGTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMG---KTEIIAETGaGQHGVASALASALLGLKCRIY 133
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTG-GNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 134 MGAKDverQSPNVFRMRLMGAEVIPVHSGsatLKDACNEALRDWSgSYETAHYmlgtaagPHPY-PTIVREFQRMIGEET 212
Cdd:cd00640 80 MPEGA---SPEKVAQMRALGAEVVLVPGD---FDDAIALAKELAE-EDPGAYY-------VNQFdNPANIAGQGTIGLEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 213 KAQIlerEGRLPDAVIACVGGGSNAIGMFADFIN-ETDVGLIGVEPgghgietgehgaplkhgrvgiyfgmkapmmqted 291
Cdd:cd00640 146 LEQL---GGQKPDAVVVPVGGGGNIAGIARALKElLPNVKVIGVEP---------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 292 gqieesysisagldfpsvgpqhaylnstgraDYVSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRENPEKEqL 371
Cdd:cd00640 189 -------------------------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGK-T 236
|
....*...
gi 446131658 372 LVVNLSGR 379
Cdd:cd00640 237 VVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
52-378 |
2.77e-47 |
|
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: 163.25 E-value: 2.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 52 YAGRPTALTKCQNITAGTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCR 131
Cdd:pfam00291 3 LGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 132 IYMGAKDVERqspNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMlgtaagpHPYptiVREFQRMIGEE 211
Cdd:pfam00291 83 IVVPEDAPPG---KLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYD-------NPL---NIEGYGTIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 212 tkaqILEREGRLPDAVIACVGGGSNAIGMFADFI-NETDVGLIGVEPgghgietgEHGAPLKHGRVGIYFGMKAPMMQTE 290
Cdd:pfam00291 150 ----ILEQLGGDPDAVVVPVGGGGLIAGIARGLKeLGPDVRVIGVEP--------EGAPALARSLAAGRPVPVPVADTIA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 291 DGqIEESYSISAgLDFPSVGpqhaylnsTGRADYVSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRENPEKEQ 370
Cdd:pfam00291 218 DG-LGVGDEPGA-LALDLLD--------EYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGD 287
|
....*...
gi 446131658 371 LLVVNLSG 378
Cdd:pfam00291 288 RVVVVLTG 295
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
54-380 |
1.96e-42 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 153.79 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 54 GRPTALTKCQNITA--GTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCR 131
Cdd:PRK12391 75 WRPTPLIRARRLEKalGTPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACALFGLECT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 132 IYMgAKDVERQSPnvFR---MRLMGAEVIP-----VHSGSATLKD----------ACNEALRDwSGSYETAHYMLGTAAg 193
Cdd:PRK12391 155 VFM-VRVSYEQKP--YRrslMETYGAEVIPspsdlTEAGRKILAEdpdhpgslgiAISEAVED-AAKRPDTKYALGSVL- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 194 PHpyptiVREFQRMIGEETKAQiLEREGRLPDAVIACVGGGSNAIGMFADFINE-----TDVGLIGVEPgghgietgeHG 268
Cdd:PRK12391 230 NH-----VLLHQTVIGLEAKKQ-LELAGEYPDVVIGCVGGGSNFAGLAFPFLGDklegkKDTRFIAVEP---------AA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 269 AP-LKHGRVGIYFGMKA---PMMQtedgqieeSYSI----------SAGLDFPSVGPQHAYLNSTGRADYVSITDDEALE 334
Cdd:PRK12391 295 CPtLTKGEYAYDFGDTAgltPLLK--------MYTLghdfvpppihAGGLRYHGMAPLVSLLVHEGLIEARAYPQTEVFE 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446131658 335 AFKTLCLHEGIIPALESSHALA----HALKMMRENPEKeqLLVVNLSGRG 380
Cdd:PRK12391 367 AAVLFARTEGIVPAPESSHAIAaaidEALKAKEEGEEK--VILFNLSGHG 414
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
54-380 |
1.72e-35 |
|
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: 134.87 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 54 GRPTALTKCQNITA--GTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCR 131
Cdd:COG1350 76 WRPSPLYRARRLEKalGTPAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALSFACALFGLECT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 132 IYMgAKDVERQSPnvFR---MRLMGAEVIP-----VHSGSATLKD----------ACNEALRDwSGSYETAHYMLGTAAG 193
Cdd:COG1350 156 VYM-VKVSYEQKP--YRrsmMETYGAEVIPspsdlTEAGRKILAEdpdtpgslgiAISEAVED-AATRDDTKYALGSVLN 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 194 pHpyptiVREFQRMIGEETKAQiLEREGRLPDAVIACVGGGSNAIGMFADFINE-----TDVGLIGVEPGghgietgehG 268
Cdd:COG1350 232 -H-----VLLHQTVIGLEAKKQ-LEKAGEYPDVVIGCAGGGSNFAGLAFPFLRDklrgkKDVRFIAVEPA---------A 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 269 AP-LKHGRVGIYFGMKA---PMMQTedgqieesY---------SISA-GLDFPSVGPQHAYLNSTGRADYVSITDDEALE 334
Cdd:COG1350 296 CPtLTRGVYAYDFGDTAgltPLLKM--------YtlghdfippPIHAgGLRYHGMAPLVSQLYHDGLIEAVAYPQLEVFE 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446131658 335 AFKTLCLHEGIIPALESSHALAHALKMMRENPE--KEQLLVVNLSGRG 380
Cdd:COG1350 368 AGVLFARTEGIVPAPESAHAIKAAIDEALKCKEegEEKTILFNLSGHG 415
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
49-378 |
4.22e-15 |
|
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: 75.22 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 49 LKNYAgRPTALTKCQNITAGTNTTLYLKREDLLHGGAHK----TNQVLgqaLLAKRMGKTEIIAETgAGQHGVASALASA 124
Cdd:cd01562 11 IKPVV-RRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKirgaYNKLL---SLSEEERAKGVVAAS-AGNHAQGVAYAAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 125 LLGLKCRIYM--GAKDVERQspnvfRMRLMGAEVIPVhsgSATLKDACNEALRDwsgSYETAHYMLgtaagpHPY--PTI 200
Cdd:cd01562 86 LLGIPATIVMpeTAPAAKVD-----ATRAYGAEVVLY---GEDFDEAEAKAREL---AEEEGLTFI------HPFddPDV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 201 VrEFQRMIGEEtkaqILEREGRLpDAVIACVGGGSNA--IGMFADFINeTDVGLIGVEPgghgietgEHGAPLKHgrvgi 278
Cdd:cd01562 149 I-AGQGTIGLE----ILEQVPDL-DAVFVPVGGGGLIagIATAVKALS-PNTKVIGVEP--------EGAPAMAQ----- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 279 yfGMKApmmqtedGQI---EESYSISAGLDFPSVGPQHAYLNSTGRADYVSITDDEALEAFKTLCLHEGIIpaLESSHAL 355
Cdd:cd01562 209 --SLAA-------GKPvtlPEVDTIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLV--AEPAGAL 277
|
330 340
....*....|....*....|....
gi 446131658 356 A-HALKMMRENPEKEQLLVVnLSG 378
Cdd:cd01562 278 AlAALLSGKLDLKGKKVVVV-LSG 300
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
52-242 |
8.15e-14 |
|
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: 71.75 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 52 YAGRPTALTKCQNITAGTNTTLYLKREDLLH---GG--AHKTNQVLGQALlakRMGKTEIIAeTGAGQ--HGVASALASA 124
Cdd:COG2515 7 LAFLPTPLQPLPRLSAALGVELWIKRDDLTGpaiGGnkTRKLEYLLADAL---AQGADTLVT-FGGAQsnHARATAAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 125 LLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDwsgSYEtahymlgtAAGPHPY------- 197
Cdd:COG2515 83 KLGLKCVLVLRGEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRDEAMEAVAA---ELR--------ARGGKPYvipeggs 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446131658 198 -PTIVREFQRmIGEETKAQiLEREGRLPDAVIACVGGGSNAIGMFA 242
Cdd:COG2515 152 nPLGALGYVE-AAAELAAQ-LAELGVDFDYIVVASGSGGTLAGLVA 195
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
57-383 |
1.95e-12 |
|
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: 67.62 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 57 TALTKCQNITA-GTNTTLYLKREDLLHGGAHKTnqvLGQALL---AKRMGKTEIIAETgAGQHGVASALASALLGLKCRI 132
Cdd:cd01563 23 TPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKD---RGMTVAvskAKELGVKAVACAS-TGNTSASLAAYAARAGIKCVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 133 YMGAkDVERQspNVFRMRLMGAEVIPVHsgsaTLKDACNEALRDWS--GSYETAHYMlgtaagpHPYptivrefqRMIGE 210
Cdd:cd01563 99 FLPA-GKALG--KLAQALAYGATVLAVE----GNFDDALRLVRELAeeNWIYLSNSL-------NPY--------RLEGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 211 ETKA-QILEREG-RLPDAVIACVGGGSNAIGMFADFINETDVGLIGVEPGGHGIETgEHGAPlkhgrvgIYFGMKAPMMQ 288
Cdd:cd01563 157 KTIAfEIAEQLGwEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQA-EGAAP-------IVRAFKEGKDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 289 TEdgQIEESYSISAGLD--FPSVGPQ--HAYLNSTGRAdyVSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRE 364
Cdd:cd01563 229 IE--PVENPETIATAIRigNPASGPKalRAVRESGGTA--VAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREE 304
|
330 340
....*....|....*....|
gi 446131658 365 NP-EKEQLLVVNLSGRGDKD 383
Cdd:cd01563 305 GIiDKGERVVVVLTGHGLKD 324
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
57-374 |
6.03e-12 |
|
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: 65.61 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 57 TALTKCQNITAGTNTTLYLKREDLLHGGAHK---TNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIY 133
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKdriALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 134 MGAK-DVERQSpnvfRMRLMGAEVIPV----HSGSATLKDACNEALRD-----WSGSYET-----AHYmLGTAagphpyP 198
Cdd:cd01561 83 MPETmSEEKRK----LLRALGAEVILTpeaeADGMKGAIAKARELAAEtpnafWLNQFENpanpeAHY-ETTA------P 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 199 TIVREFQRMIgeetkaqileregrlpDAVIACVG-GGSnaIGMFADFINETD--VGLIGVEPGGHGIETGehGAPLKHGR 275
Cdd:cd01561 152 EIWEQLDGKV----------------DAFVAGVGtGGT--ITGVARYLKEKNpnVRIVGVDPVGSVLFSG--GPPGPHKI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 276 VGIYFGMKAPMMQTE--DGQIEesysisagldfpsvgpqhaylnstgradyvsITDDEALEAFKTLCLHEGIIPALESSH 353
Cdd:cd01561 212 EGIGAGFIPENLDRSliDEVVR-------------------------------VSDEEAFAMARRLAREEGLLVGGSSGA 260
|
330 340
....*....|....*....|.
gi 446131658 354 ALAHALKMMRENPEKEQLLVV 374
Cdd:cd01561 261 AVAAALKLAKRLGPGKTIVTI 281
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
55-378 |
9.12e-12 |
|
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: 65.44 E-value: 9.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 55 RPTALTKCQNITAGTNTTLYLKREDLLHGGAHKtnqVLG----QALLAKRMGKTEIIAETgAGQHGVASALASALLGLKC 130
Cdd:COG1171 23 RRTPLLRSPTLSERLGAEVYLKLENLQPTGSFK---LRGaynaLASLSEEERARGVVAAS-AGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 131 RIYM--GAKDVERQspnvfRMRLMGAEVIPVhsgSATLKDACNEALRDwsgSYETAHYMLgtaagpHPY--PTIVrEFQR 206
Cdd:COG1171 99 TIVMpeTAPAVKVA-----ATRAYGAEVVLH---GDTYDDAEAAAAEL---AEEEGATFV------HPFddPDVI-AGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 207 MIGEEtkaqILEREGRLpDAVIACVGGGS--NAIGMFADFINEtDVGLIGVEPgghgietgeHGAP-----LKHGRVgiy 279
Cdd:COG1171 161 TIALE----ILEQLPDL-DAVFVPVGGGGliAGVAAALKALSP-DIRVIGVEP---------EGAAamyrsLAAGEP--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 280 fgmkapmmqtedGQIEESYSISAGLDFPSVGPqHAY-LNSTGRADYVSITDDEALEAFKTLCLHEGIIpaLESSHALA-H 357
Cdd:COG1171 223 ------------VTLPGVDTIADGLAVGRPGE-LTFeILRDLVDDIVTVSEDEIAAAMRLLLERTKIV--VEPAGAAAlA 287
|
330 340
....*....|....*....|.
gi 446131658 358 ALKMMRENPEKEQLLVVnLSG 378
Cdd:COG1171 288 ALLAGKERLKGKRVVVV-LSG 307
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
57-383 |
1.20e-11 |
|
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: 65.61 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 57 TALTKCQNITAGTNTTLYLKREDLLHGGAHKTN--QVLGQalLAKRMGKTEII-AETGAGqhgvASALA--SALLGLKCR 131
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRamQVAVS--LALERGAKTIVcASSGNG----SAALAayAARAGIEVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 132 IYMGAKDV----ERQspnvfrMRLMGAEVIPVHsGSatlKDACNEALRDWSGSYEtahymLGTAAGPHPYptiVREFQRM 207
Cdd:COG0498 141 VFVPEGKVspgqLAQ------MLTYGAHVIAVD-GN---FDDAQRLVKELAADEG-----LYAVNSINPA---RLEGQKT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 208 IGEEtkaqILEREGRLPDAVIACVGGGSNAIGMFADFINETDVG-------LIGVEPGG-----HGIETGEHGAPLKHGR 275
Cdd:COG0498 203 YAFE----IAEQLGRVPDWVVVPTGNGGNILAGYKAFKELKELGlidrlprLIAVQATGcnpilTAFETGRDEYEPERPE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 276 vgiyfgMKAPMMqtedgQIEESYSISAGLDfpsvgpqhaYLNSTGrADYVSITDDEALEAFKTLCLHEGIIPALESSHAL 355
Cdd:COG0498 279 ------TIAPSM-----DIGNPSNGERALF---------ALRESG-GTAVAVSDEEILEAIRLLARREGIFVEPATAVAV 337
|
330 340
....*....|....*....|....*....
gi 446131658 356 AHALKMMRENP-EKEQLLVVNLSGRGDKD 383
Cdd:COG0498 338 AGLRKLREEGEiDPDEPVVVLSTGHGLKF 366
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
55-259 |
7.72e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 62.66 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 55 RPTALTKCQNITAGTnTTLYLKREDLLHGGAHKTNQVLgQALLAKRMGKTEIIAETGaGQHGVASALASALLGLKCRIYm 134
Cdd:PRK08246 22 RRTPVLEADGAGFGP-APVWLKLEHLQHTGSFKARGAF-NRLLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVPATVF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 135 gakdVERQSP--NVFRMRLMGAEVIPVHSGSATLKDACnEALRDWSGsyetahymlgtAAGPHPY--PTIVrefqrmIGE 210
Cdd:PRK08246 98 ----VPETAPpaKVARLRALGAEVVVVGAEYADALEAA-QAFAAETG-----------ALLCHAYdqPEVL------AGA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446131658 211 ETKAQILEREGRLPDAVIACVGGGSNAIGMFADFINETDVglIGVEPGG 259
Cdd:PRK08246 156 GTLGLEIEEQAPGVDTVLVAVGGGGLIAGIAAWFEGRARV--VAVEPEG 202
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
73-257 |
1.09e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 56.32 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 73 LYLKREDLLHGGAHKTNQVLGQALLAKRMGK--TEIIAETgAGQHGVASALASALLGLKCRIYMgakdverqSPNVFRMR 150
Cdd:PRK06608 40 IFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TGNHGQAVAYASKLFGIKTRIYL--------PLNTSKVK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 151 LM-----GAEVIPvhsgSATLKDACNEALRDwsgSYETAHYMlgtaagpHPY--PTIVrefqrmIGEETKAQ-ILEREGR 222
Cdd:PRK06608 111 QQaalyyGGEVIL----TNTRQEAEEKAKED---EEQGFYYI-------HPSdsDSTI------AGAGTLCYeALQQLGF 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 446131658 223 LPDAVIACVGGGSNAIG-MFADFINETDVGLIGVEP 257
Cdd:PRK06608 171 SPDAIFASCGGGGLISGtYLAKELISPTSLLIGSEP 206
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
56-259 |
7.12e-08 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 54.04 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 56 PTALTKCQNITAGTNTTLYLKREDL-------LHGGAHKTNQvlgqalLAKRMGKTEIIAETgAGQH--GVAsaLASALL 126
Cdd:PRK08639 25 ETPLQRNDYLSEKYGANVYLKREDLqpvrsykLRGAYNAISQ------LSDEELAAGVVCAS-AGNHaqGVA--YACRHL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 127 GLKCRIYMGAKdverqSPN--VFRMRLMGAEVIPVHSGSATLKDACNEALRDwsgSYETAHYMLgtaagpHPY--PTIvr 202
Cdd:PRK08639 96 GIPGVIFMPVT-----TPQqkIDQVRFFGGEFVEIVLVGDTFDDSAAAAQEY---AEETGATFI------PPFddPDV-- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446131658 203 efqrMIGEETKA-QILEREGRL--PDAVIACVGGGSNAIGM---FADFINETDVglIGVEPGG 259
Cdd:PRK08639 160 ----IAGQGTVAvEILEQLEKEgsPDYVFVPVGGGGLISGVttyLKERSPKTKI--IGVEPAG 216
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
57-367 |
1.78e-06 |
|
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: 49.28 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 57 TALTKCQNITAGTNTTLYLKREDLLHGGAHKTnqVLGQALL--AKRMGK----TEIIaETGAGQHGVASALASALLGLKC 130
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKD--RIALSMIedAEKRGLlkpgGTIV-EATSGNTGIGLAMVAAAKGYRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 131 RIYMGAK-DVERQSpnvfRMRLMGAEVIPVhSGSATLKDACNEALR---DWSGS-----YE-----TAHYmLGTAagphp 196
Cdd:COG0031 91 ILVMPETmSKERRA----LLRAYGAEVVLT-PGAEGMKGAIDKAEElaaETPGAfwpnqFEnpanpEAHY-ETTG----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 197 yPTIVREFqrmigeetkaqilerEGRlPDAVIACVG-GGSnaIGMFADFINET--DVGLIGVEP-GGHGIETGEHGaplK 272
Cdd:COG0031 160 -PEIWEQT---------------DGK-VDAFVAGVGtGGT--ITGVGRYLKERnpDIKIVAVEPeGSPLLSGGEPG---P 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 273 HGRVGIyfgmkapmmqtEDGQIEESYSISAgLDfpsvgpqhaylnstgraDYVSITDDEALEAFKTLCLHEGIIPALESS 352
Cdd:COG0031 218 HKIEGI-----------GAGFVPKILDPSL-ID-----------------EVITVSDEEAFAMARRLAREEGILVGISSG 268
|
330
....*....|....*
gi 446131658 353 HALAHALKMMRENPE 367
Cdd:COG0031 269 AAVAAALRLAKRLGP 283
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
52-239 |
2.63e-06 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 48.67 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 52 YAGRPTALTKCQNITAGTNTTLYLKREDL--LHGGAHKTNQ---VLGQALlakRMGKTEIIAeTGAGQ--HGVASALASA 124
Cdd:PRK03910 11 LAGLPTPLEPLPRLSAALGPDIYIKRDDLtgLALGGNKTRKlefLLADAL---AQGADTLIT-AGAIQsnHARQTAAAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 125 LLGLKCRIYM-----GAKDVERQSPNVFRMRLMGAEVIPVHSGSatlkDAcNEALRDWSGSYEtahymlgtAAGPHPYpt 199
Cdd:PRK03910 87 KLGLKCVLLLenpvpTEAENYLANGNVLLDDLFGAEIHVVPAGT----DM-DAQLEELAEELR--------AQGRRPY-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446131658 200 ivrefqrmigeetkaqileregrlpdaVIAcvGGGSNAIG 239
Cdd:PRK03910 152 ---------------------------VIP--VGGSNALG 162
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
55-234 |
5.30e-06 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 47.77 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 55 RPTALTKCQNITAGTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYM 134
Cdd:PRK06815 19 RVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 135 GakdvERQSP-NVFRMRLMGAEVIpvhsgsaTLKDACNEALRdWSGSYETAHYMlgtaagphPYPTIVREFQRMIGEETK 213
Cdd:PRK06815 99 P----EQASAiKLDAIRALGAEVR-------LYGGDALNAEL-AARRAAEQQGK--------VYISPYNDPQVIAGQGTI 158
|
170 180
....*....|....*....|.
gi 446131658 214 AQILEREGRLPDAVIACVGGG 234
Cdd:PRK06815 159 GMELVEQQPDLDAVFVAVGGG 179
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
57-374 |
9.94e-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: 46.91 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 57 TALTKCQNITAGTNTTLYLKREDLLHGGAHKTNQV---LGQALLAKRMGKTEIIAETGaGQHGVASALASALLGLKCRIY 133
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIghlCQKSAKQGLNECVHVVCSSG-GNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 134 MgakdverqsPN------VFRMRLMGAEVIPVHSgsaTLKDACNEAlrdwsgsyetAHYMLGTAAGP---HPY--PTIVR 202
Cdd:cd06448 81 V---------PEstkprvVEKLRDEGATVVVHGK---VWWEADNYL----------REELAENDPGPvyvHPFddPLIWE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 203 EFQRMIgEETKAQILEREgrLPDAVIACVGGGsnaiGMFADFIN------ETDVGLIGVEpgghgietgEHGAPLKHGrv 276
Cdd:cd06448 139 GHSSMV-DEIAQQLQSQE--KVDAIVCSVGGG----GLLNGIVQglerngWGDIPVVAVE---------TEGAHSLNA-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 277 giyfGMKAPMMQTedgqIEESYSISAGLDFPSVGPQHayLNSTGRADYVS--ITDDEALEAFKTLCLHEGII--PALESS 352
Cdd:cd06448 201 ----SLKAGKLVT----LPKITSVATSLGAKTVSSQA--LEYAQEHNIKSevVSDRDAVQACLRFADDERILvePACGAA 270
|
330 340
....*....|....*....|....*
gi 446131658 353 HALA---HALKMMRENPEKEQLLVV 374
Cdd:cd06448 271 LAVVysgKILDLQLEVLLTPLDNVV 295
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
57-378 |
4.31e-05 |
|
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: 45.10 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 57 TALTKCQNITA--GTNTTLYLKREDLLHGGAHKTNQVLGQALL---AKRMGKTEIIAeTGAGQ--HGVASALASALLGLK 129
Cdd:cd06449 1 TPIQYLPRLSEhlGGKVEIYAKRDDCNSGLAFGGNKIRKLEYLlpdALAKGADTLVT-VGGIQsnHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 130 C----RIYMGAKD-VERQSPNVFRMRLMGAEVIPVHSGSATLKDAcnealrdwsgSYETAHYMLgTAAGPHPYPTIVREF 204
Cdd:cd06449 80 CvlvqENWVPYSDaVYDRVGNILLSRIMGADVRLVSAGFDIGIRK----------SFEEAAEEV-EAKGGKPYVIPAGGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 205 QRMIG--------EETKAQiLEREGRLPDAVIACVGGGSNAIGMFADF-INETDVGLIGVEPGGHGIETgehgaplkhgR 275
Cdd:cd06449 149 EHPLGglgyvgfvLEIAQQ-EEELGFKFDSIVVCSVTGSTHAGLSVGLaALGRQRRVIGIDASAKPEKT----------K 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 276 VGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGpqhaylnstgradyvsITDDEALEAFKTLCLHEGII--PALESSh 353
Cdd:cd06449 218 AQVLRIAQAKLAEEGLEVKEEDVVLDDDYAAPEYG----------------IPNDETIEAIKLCARLEGIItdPVYEGK- 280
|
330 340
....*....|....*....|....*..
gi 446131658 354 ALAHALKMMREN--PEKEQLLVVNLSG 378
Cdd:cd06449 281 SMQGMIDLVRNGefKEGSKVLFIHLGG 307
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
102-386 |
7.79e-05 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 44.22 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 102 GKTEIIAETGaGQHGVASALASALLGLKCRIYMGAK-DVERQspnvFRMRLMGAEV--IPVHSGSATLKDACNEALRDWS 178
Cdd:PLN00011 68 GKSTLIEATA-GNTGIGLACIGAARGYKVILVMPSTmSLERR----IILRALGAEVhlTDQSIGLKGMLEKAEEILSKTP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 179 GSYETAHYMLGTAAGPHpYPTIVREFQRmigeetkaqilEREGRLpDAVIACVGGGSNAIGMfADFINET--DVGLIGVE 256
Cdd:PLN00011 143 GGYIPQQFENPANPEIH-YRTTGPEIWR-----------DSAGKV-DILVAGVGTGGTATGV-GKFLKEKnkDIKVCVVE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 257 PGGHGIETGehGAPLKHGRVGIYFGMkapmmqtedgqieesysISAGLDFPSVGpqhaylnstgraDYVSITDDEALEAF 336
Cdd:PLN00011 209 PVESAVLSG--GQPGPHLIQGIGSGI-----------------IPFNLDLTIVD------------EIIQVTGEEAIETA 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446131658 337 KTLCLHEGIIPALESSHALAHALKMMRENPEKEQLLVVNLSGRGDKDIFT 386
Cdd:PLN00011 258 KLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLST 307
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
55-257 |
8.29e-04 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 41.32 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 55 RPTALTKCQNITAGTNTTLYLKREDL-------LHGGAHKTNQVLGQALlakrmGKTEIIAEtgAGQHGVASALASALLG 127
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLqpvfsfkIRGAYNKMARLPAEQL-----ARGVITAS--AGNHAQGVALAAARLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 128 LKCRIYMgakdvERQSPN--VFRMRLMGAEVIpVHSGSATLKDACNEALRDWSGsyetahymlgtAAGPHPY--PTIVRE 203
Cdd:PRK12483 109 VKAVIVM-----PRTTPQlkVDGVRAHGGEVV-LHGESFPDALAHALKLAEEEG-----------LTFVPPFddPDVIAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446131658 204 fQRMIGEETKAQileREGRLpDAVIACVGGGSNAIGMfADFIN--ETDVGLIGVEP 257
Cdd:PRK12483 172 -QGTVAMEILRQ---HPGPL-DAIFVPVGGGGLIAGI-AAYVKyvRPEIKVIGVEP 221
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
56-244 |
5.46e-03 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 38.47 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 56 PTALTKCQNITA--GTNTTLYLKREDLLHG---GAHKTNQVlgQALLAKRMGKTeiiAETGAGQHGVAS------ALASA 124
Cdd:PRK12390 15 PTPIHPLKRLSAhlGGKVELYAKREDCNSGlafGGNKTRKL--EYLVPDALAQG---ADTLVSIGGVQSnhtrqvAAVAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131658 125 LLGLKCRI----YMGAKD-VERQSPNVFRMRLMGAEVIPVHSG-SATLKDACNEALRDWSgsyetahymlgtAAGPHPYP 198
Cdd:PRK12390 90 HLGMKCVLvqenWVNYEDaVYDRVGNILLSRIMGADVRLVPDGfDIGIRKSWEDALEDVR------------AAGGKPYA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446131658 199 TIVREFQRMIG--------EETKAQilERE-GRLPDAVIACVGGGSNAIGMFADF 244
Cdd:PRK12390 158 IPAGASDHPLGglgfvgfaEEVRAQ--EAElGFKFDYIVVCSVTGSTQAGMVVGF 210
|
|
| |
