|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
1-392 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 798.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 1 MSETLLNPYFGEFGGMYVPEILVPVLKQLEKAFVAAKDDPEFQREFQDLLKNYAGRPTALTLCRNLTKGTK-AKIYLKRE 79
Cdd:PRK04346 2 YTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLGgAKIYLKRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 80 DLLHGGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVP 159
Cdd:PRK04346 82 DLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 160 VQKGSCSLKDACCEAMRDWSANYETTHYLLGTAAGPHPFPTIVREFQKMIGIETKCQILEREGRLPDAVIAAVGGGSNAI 239
Cdd:PRK04346 162 VTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNAI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 240 GMFTDFIDEANVRLIGVEPAGKGIESGEHGAPLGHAKVGIYFGMKSPLMQTEDGQVEESYSVSAGLDFPSVGPQHAYLQS 319
Cdd:PRK04346 242 GIFHPFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKD 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341956663 320 IGRAEYPSITDDEALNAFQELAKHEGIIPALESSHALAQALKMiHQEPNKEQILVVNLSGRGDKDIFTVDKIL 392
Cdd:PRK04346 322 IGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKL-APTLGKDQIIVVNLSGRGDKDVFTVAKLL 393
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
7-392 |
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: 764.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 7 NPYFGEFGGMYVPEILVPVLKQLEKAFVAAKDDPEFQREFQDLLKNYAGRPTALTLCRNLTKGT-KAKIYLKREDLLHGG 85
Cdd:COG0133 11 KGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLgGAKIYLKREDLNHTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 86 AHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVPVQKGSC 165
Cdd:COG0133 91 AHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAEVVPVTSGSR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 166 SLKDACCEAMRDWSANYETTHYLLGTAAGPHPFPTIVREFQKMIGIETKCQILEREGRLPDAVIAAVGGGSNAIGMFTDF 245
Cdd:COG0133 171 TLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGSNAIGIFYPF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 246 IDEANVRLIGVEPAGKGIESGEHGAPLGHAKVGIYFGMKSPLMQTEDGQVEESYSVSAGLDFPSVGPQHAYLQSIGRAEY 325
Cdd:COG0133 251 LDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDTGRAEY 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341956663 326 PSITDDEALNAFQELAKHEGIIPALESSHALAQALKMIhQEPNKEQILVVNLSGRGDKDIFTVDKIL 392
Cdd:COG0133 331 VSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLA-PELSKDQIIVVNLSGRGDKDVDTVAKYL 396
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
9-392 |
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: 676.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 9 YFGEFGGMYVPEILVPVLKQLEKAFVAAKDDPEFQREFQDLLKNYAGRPTALTLCRNLTKGT-KAKIYLKREDLLHGGAH 87
Cdd:TIGR00263 2 YFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALgGAKIYLKREDLNHTGAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 88 KTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVPVQKGSCSL 167
Cdd:TIGR00263 82 KINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 168 KDACCEAMRDWSANYETTHYLLGTAAGPHPFPTIVREFQKMIGIETKCQILEREGRLPDAVIAAVGGGSNAIGMFTDFID 247
Cdd:TIGR00263 162 KDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 248 EANVRLIGVEPAGKGIESGEHGAPLGHAKVGIYFGMKSPLMQTEDGQVEESYSVSAGLDFPSVGPQHAYLQSIGRAEYPS 327
Cdd:TIGR00263 242 DPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATYEA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341956663 328 ITDDEALNAFQELAKHEGIIPALESSHALAQALKMIHQEPnKEQILVVNLSGRGDKDIFTVDKIL 392
Cdd:TIGR00263 322 ITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLP-KDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
1-392 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 661.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 1 MSETLLNPYFGEFGGMYVPEILVPVLKQLEKAFVAAKDDPEFQREFQDLLKNYAGRPTALTLCRNLTKG-TKAKIYLKRE 79
Cdd:PRK13028 6 KSMPDADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEElGGAQIYLKRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 80 DLLHGGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVP 159
Cdd:PRK13028 86 DLNHTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLGAEVVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 160 VQKGSCSLKDACCEAMRDWSANYETTHYLLGTAAGPHPFPTIVREFQKMIGIETKCQILEREGRLPDAVIAAVGGGSNAI 239
Cdd:PRK13028 166 VTRGGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 240 GMFTDFIDEANVRLIGVEPAGKGIESGEHGAPLGHAKVGIYFGMKSPLMQTEDGQVEESYSVSAGLDFPSVGPQHAYLQS 319
Cdd:PRK13028 246 GLFSAFLDDESVRLVGVEPAGRGLDLGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPEHAYLKD 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341956663 320 IGRAEYPSITDDEALNAFQELAKHEGIIPALESSHALAQALKMIhQEPNKEQILVVNLSGRGDKDIFTVDKIL 392
Cdd:PRK13028 326 IGRVEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLA-PELSKDETILVNLSGRGDKDIDYVAEML 397
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
24-388 |
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: 613.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 24 PVLKQLEKAFVAAKDDPEFQREFQDLLKNYAGRPTALTLCRNLTKGTK-AKIYLKREDLLHGGAHKTNQVLGQILLAKRM 102
Cdd:cd06446 1 PALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLGgAKIYLKREDLNHTGAHKINNALGQALLAKRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 103 GKTRIIAETGAGQHGVATALACAMLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVPVQKGSCSLKDACCEAMRDWSANY 182
Cdd:cd06446 81 GKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 183 ETTHYLLGTAAGPHPFPTIVREFQKMIGIETKCQILEREGRLPDAVIAAVGGGSNAIGMFTDFIDEANVRLIGVEPAGKG 262
Cdd:cd06446 161 EDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 263 IESGEHGAPLGHAKVGIYFGMKSPLMQTEDGQVEESYSVSAGLDFPSVGPQHAYLQSIGRAEYPSITDDEALNAFQELAK 342
Cdd:cd06446 241 LETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLAR 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 341956663 343 HEGIIPALESSHALAQALKmIHQEPNKEQILVVNLSGRGDKDIFTV 388
Cdd:cd06446 321 TEGIIPALESSHAIAYAIK-LAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
7-390 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 566.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 7 NPYFGEFGGMYVPEILVPVLKQLEKAFVAAKDDPEFQREFQDLLKNYAGRPTALTLCRNLTKGTKAKIYLKREDLLHGGA 86
Cdd:PRK13803 221 AGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSDIYGARIYLKREDLNHTGS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 87 HKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVPVQKGSCS 166
Cdd:PRK13803 301 HKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIPVLSGSKT 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 167 LKDACCEAMRDWSANYETTHYLLGTAAGPHPFPTIVREFQKMIGIETKCQILEREGRLPDAVIAAVGGGSNAIGMFTDFI 246
Cdd:PRK13803 381 LKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIGIFYHFL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 247 DEANVRLIGVEPAGKGIESGEHGAPLGHAKVGIYFGMKSPLMQTEDGQVEESYSVSAGLDFPSVGPQHAYLQSIGRAEYP 326
Cdd:PRK13803 461 DDPSVKLIGVEAGGKGVNTGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANLFETGRAIYT 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341956663 327 SITDDEALNAFQELAKHEGIIPALESSHALAqALKMIHQEPNKEQILVVNLSGRGDKDIFTVDK 390
Cdd:PRK13803 541 SVTDEEALDAFKLLAKLEGIIPALESSHALA-YLKEGRKKFKKKDIVIVNLSGRGDKDIPTLKE 603
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
10-396 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 531.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 10 FGEFGGMYVPEILVPVLKQLEKAFVAAKDDPEFQREFQDLLKNYAGRPTALTLCRNLT------KGTKAKIYLKREDLLH 83
Cdd:PLN02618 19 FGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTehykraDGEGPEIYLKREDLNH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 84 GGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVPVQKG 163
Cdd:PLN02618 99 TGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEVRPVHSG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 164 SCSLKDACCEAMRDWSANYETTHYLLGTAAGPHPFPTIVREFQKMIGIETKCQILEREGRLPDAVIAAVGGGSNAIGMFT 243
Cdd:PLN02618 179 TATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSNAMGLFH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 244 DFIDEANVRLIGVEPAGKGIESGEHGAPLGHAKVGIYFGMKSPLMQTEDGQVEESYSVSAGLDFPSVGPQHAYLQSIGRA 323
Cdd:PLN02618 259 EFIDDEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYPGVGPEHSFLKDTGRA 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341956663 324 EYPSITDDEALNAFQELAKHEGIIPALESSHALAQALKMIHQEPNKEQIlVVNLSGRGDKDIFTVDKILTEKG 396
Cdd:PLN02618 339 EYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKV-VVNCSGRGDKDVNTAIKYLQVSS 410
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
8-390 |
5.74e-162 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 471.44 E-value: 5.74e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 8 PYFGEFGGMYVPEILVPVLKQLEKAFVAAKDDPEFQREFQDLLKNYAGRPTALTLCRNLTK------GTKAKIYLKREDL 81
Cdd:PRK13802 277 PYWGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTEAPRFAErvkektGLDARVFLKREDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 82 LHGGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVPVQ 161
Cdd:PRK13802 357 NHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGAEVVEVT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 162 KGSCSLKDACCEAMRDWSANYETTHYLLGTAAGPHPFPTIVREFQKMIGIETKCQILEREG-RLPDAVIAAVGGGSNAIG 240
Cdd:PRK13802 437 LGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiDHPDAICACVGGGSNAIG 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 241 MFTDFIDEANVRLIGVEPAGKGIESGEHG---APlGHAKVGIYFGMKSPLMQTEDGQVEESYSVSAGLDFPSVGPQHAYL 317
Cdd:PRK13802 517 VMNAFLDDERVNLYGYEAGGNGPESGKHAirfAP-GTGELGMFQGAKSYLLENDEGQTLDTYSISAGLDYASVGPEHAWL 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341956663 318 QSIGRAEYPSITDDEALNAFQELAKHEGIIPALESSHALAQALKM---IHQEPNKEQILVVNLSGRGDKDIFTVDK 390
Cdd:PRK13802 596 KDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAaadLKAKGYEHPVMIVNISGRGDKDMNTAGK 671
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
58-380 |
7.02e-55 |
|
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: 181.17 E-value: 7.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 58 TALTLCRNLTKGTKAKIYLKREDLLHGGAHKTNQVLGQILLAKRMG---KTRIIAETGaGQHGVATALACAMLDMPCRIY 134
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTG-GNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 135 MGAKDverQSPNVFRMRLMGAEVVPVQKGscsLKDACCEAMRDWsANYETTHYLlgtaagpHPF-PTIVREFQKMIGIET 213
Cdd:cd00640 80 MPEGA---SPEKVAQMRALGAEVVLVPGD---FDDAIALAKELA-EEDPGAYYV-------NQFdNPANIAGQGTIGLEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 214 KCQIlerEGRLPDAVIAAVGGGSNAIGMFTDFI-DEANVRLIGVEPagkgiesgehgaplghakvgiyfgmksplmqted 292
Cdd:cd00640 146 LEQL---GGQKPDAVVVPVGGGGNIAGIARALKeLLPNVKVIGVEP---------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 293 gqveESYSVSagldfpsvgpqhaylqsigraeypsitDDEALNAFQELAKHEGIIPALESSHALAQALKMIhQEPNKEQI 372
Cdd:cd00640 189 ----EVVTVS---------------------------DEEALEAIRLLAREEGILVEPSSAAALAAALKLA-KKLGKGKT 236
|
....*...
gi 341956663 373 LVVNLSGR 380
Cdd:cd00640 237 VVVILTGG 244
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
55-381 |
2.29e-49 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 172.28 E-value: 2.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 55 GRPTALTLCRNLTK--GTKAKIYLKREDLLHGGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCR 132
Cdd:PRK12391 75 WRPTPLIRARRLEKalGTPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACALFGLECT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 133 IYMgAKDVERQSPnvFR---MRLMGAEVVP-----VQKG----------SCSLKDACCEAMRDwSANYETTHYLLGTAAg 194
Cdd:PRK12391 155 VFM-VRVSYEQKP--YRrslMETYGAEVIPspsdlTEAGrkilaedpdhPGSLGIAISEAVED-AAKRPDTKYALGSVL- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 195 PHpfptiVREFQKMIGIETKCQiLEREGRLPDAVIAAVGGGSNAIGMFTDFI-----DEANVRLIGVEPAG-----KGIE 264
Cdd:PRK12391 230 NH-----VLLHQTVIGLEAKKQ-LELAGEYPDVVIGCVGGGSNFAGLAFPFLgdkleGKKDTRFIAVEPAAcptltKGEY 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 265 SGEHG-----AP------LGHAKV--GIYfgmksplmqtedgqveesysvSAGLDFPSVGPQHAYLQSIGRAEYPSITDD 331
Cdd:PRK12391 304 AYDFGdtaglTPllkmytLGHDFVppPIH---------------------AGGLRYHGMAPLVSLLVHEGLIEARAYPQT 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 341956663 332 EALNAFQELAKHEGIIPALESSHALAQALK--MIHQEPNKEQILVVNLSGRG 381
Cdd:PRK12391 363 EVFEAAVLFARTEGIVPAPESSHAIAAAIDeaLKAKEEGEEKVILFNLSGHG 414
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
53-379 |
8.23e-48 |
|
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: 164.41 E-value: 8.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 53 YAGRPTALTLCRNLTKGTKAKIYLKREDLLHGGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCR 132
Cdd:pfam00291 3 LGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 133 IYMGAKDVERqspNVFRMRLMGAEVVPVQKGSCSLKDACCEAMRDWSANYETTHYLlgtaagpHPFptiVREFQKMIGIE 212
Cdd:pfam00291 83 IVVPEDAPPG---KLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYD-------NPL---NIEGYGTIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 213 tkcqILEREGRLPDAVIAAVGGGSNAIGMFTDFIDEA-NVRLIGVEPAGkgiesgehGAPLGHAKVGIYFGMKSPLMQTE 291
Cdd:pfam00291 150 ----ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGpDVRVIGVEPEG--------APALARSLAAGRPVPVPVADTIA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 292 DGqveesysvSAGLDFPSVGPQHAYLQSIGRAEypSITDDEALNAFQELAKHEGIIPALESSHALAQALKMIHQEPNKEQ 371
Cdd:pfam00291 218 DG--------LGVGDEPGALALDLLDEYVGEVV--TVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGD 287
|
....*...
gi 341956663 372 ILVVNLSG 379
Cdd:pfam00291 288 RVVVVLTG 295
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
40-381 |
2.60e-45 |
|
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: 161.45 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 40 PEfqrEFQDLLKNYagRPTALTLCRNLTK--GTKAKIYLKREDLLHGGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHG 117
Cdd:COG1350 66 PE---EVREIYRLW--RPSPLYRARRLEKalGTPAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 118 VATALACAMLDMPCRIYMgAKDVERQSPnvFR---MRLMGAEVVP-----VQKG----------SCSLKDACCEAMRDwS 179
Cdd:COG1350 141 SALSFACALFGLECTVYM-VKVSYEQKP--YRrsmMETYGAEVIPspsdlTEAGrkilaedpdtPGSLGIAISEAVED-A 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 180 ANYETTHYLLGTAAGpHpfptiVREFQKMIGIETKCQiLEREGRLPDAVIAAVGGGSNAIGMFTDFIDE-----ANVRLI 254
Cdd:COG1350 217 ATRDDTKYALGSVLN-H-----VLLHQTVIGLEAKKQ-LEKAGEYPDVVIGCAGGGSNFAGLAFPFLRDklrgkKDVRFI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 255 GVEPAG-----KGIESGEHG-----AP------LGHAKV--GI------YFGMkSPLMqtedgqveeSYSVSAGLdfpsV 310
Cdd:COG1350 290 AVEPAAcptltRGVYAYDFGdtaglTPllkmytLGHDFIppPIhagglrYHGM-APLV---------SQLYHDGL----I 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341956663 311 GPQhAYLQSigraeypsitddEALNAFQELAKHEGIIPALESSHALAQALK--MIHQEPNKEQILVVNLSGRG 381
Cdd:COG1350 356 EAV-AYPQL------------EVFEAGVLFARTEGIVPAPESAHAIKAAIDeaLKCKEEGEEKTILFNLSGHG 415
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
64-375 |
5.51e-17 |
|
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: 80.64 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 64 RNLTKGTKAKIYLKREDLLHGGAHKTNQVLGQILLAKRMGKTR---IIAETGAGQHGVATALACAMLDMPCRIYMGAK-D 139
Cdd:cd01561 9 NRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKpgtTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETmS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 140 VERQSpnvfRMRLMGAEVVPV-------QKGSCSLKDACCEAMRDW--------SANYEtTHYlLGTAagphpfPTIVRE 204
Cdd:cd01561 89 EEKRK----LLRALGAEVILTpeaeadgMKGAIAKARELAAETPNAfwlnqfenPANPE-AHY-ETTA------PEIWEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 205 FQKMIgietkcqileregrlpDAVIAAVGGGsnaiGMFT---DFIDEAN--VRLIGVEPAGKGIESGehGAPLGHAKVGI 279
Cdd:cd01561 157 LDGKV----------------DAFVAGVGTG----GTITgvaRYLKEKNpnVRIVGVDPVGSVLFSG--GPPGPHKIEGI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 280 YFGMKSPLMQTE--DGQVEesysvsagldfpsvgpqhaylqsigraeypsITDDEALNAFQELAKHEGIIPALESSHALA 357
Cdd:cd01561 215 GAGFIPENLDRSliDEVVR-------------------------------VSDEEAFAMARRLAREEGLLVGGSSGAAVA 263
|
330
....*....|....*...
gi 341956663 358 QALKMIHQEPNKEQILVV 375
Cdd:cd01561 264 AALKLAKRLGPGKTIVTI 281
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
53-256 |
2.02e-16 |
|
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: 79.45 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 53 YAGRPTALTLCRNLTKGTKAKIYLKREDLLH---GG--AHKTNQVLGQillAKRMGKTRIIAeTGAGQ--HGVATALACA 125
Cdd:COG2515 7 LAFLPTPLQPLPRLSAALGVELWIKRDDLTGpaiGGnkTRKLEYLLAD---ALAQGADTLVT-FGGAQsnHARATAAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 126 MLDMPCRIYMGAKDVERQSPNVFRMRLMGAEVVPVQKGSCSLKDaccEAMRDWSANYEtthyllgtAAGPHPFP------ 199
Cdd:COG2515 83 KLGLKCVLVLRGEEPTPLNGNLLLDRLLGAELHFVSRGEYRDRD---EAMEAVAAELR--------ARGGKPYVipeggs 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341956663 200 ---------TIVREFQkmigietkcQILEREGRLPDAVIAAVGGGSNAIGMFTDF-IDEANVRLIGV 256
Cdd:COG2515 152 nplgalgyvEAAAELA---------AQLAELGVDFDYIVVASGSGGTLAGLVAGLaLLGSDTRVIGI 209
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
47-379 |
5.44e-16 |
|
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: 77.91 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 47 QDLLKNYAgRPTALTLCRNLTKGTKAKIYLKREDLLHGGAHKTNQVLGQILLAKRMGKTR-IIAETgAGQHGVATALACA 125
Cdd:cd01562 8 AARIKPVV-RRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAAS-AGNHAQGVAYAAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 126 MLDMPCRIYM--GAKDVERQspnvfRMRLMGAEVVpvQKGScSLKDACCEAMRDWSanyETTHYLLgtaagpHPF--PTI 201
Cdd:cd01562 86 LLGIPATIVMpeTAPAAKVD-----ATRAYGAEVV--LYGE-DFDEAEAKARELAE---EEGLTFI------HPFddPDV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 202 VrEFQKMIGIEtkcqILEREGRLpDAVIAAVGGGSNAIGMFTdFIDEAN--VRLIGVEPAG--KGIESGEHGAPLghakv 277
Cdd:cd01562 149 I-AGQGTIGLE----ILEQVPDL-DAVFVPVGGGGLIAGIAT-AVKALSpnTKVIGVEPEGapAMAQSLAAGKPV----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 278 giyfgmksplmqtedgQVEESYSVSAGLDFPSVGPQHAYLQSIGRAEYPSITDDEALNAFQELAKHEGIIpaLESSHALA 357
Cdd:cd01562 217 ----------------TLPEVDTIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLV--AEPAGALA 278
|
330 340
....*....|....*....|..
gi 341956663 358 QALKMIHQEPNKEQILVVNLSG 379
Cdd:cd01562 279 LAALLSGKLDLKGKKVVVVLSG 300
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
58-398 |
1.10e-13 |
|
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: 71.77 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 58 TALTLCRNLTKGTKAKIYLKREDLLHGGAHKTN--QVLGQilLAKRMGKTRII-AETGAGqhGVATALACAMLDMPCRIY 134
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRamQVAVS--LALERGAKTIVcASSGNG--SAALAAYAARAGIEVFVF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 135 MGAKDV----ERQspnvfrMRLMGAEVVPVqKGScslKDACCEAMRDWSANYEtthylLGTAAGPHPFptiVREFQKMIG 210
Cdd:COG0498 143 VPEGKVspgqLAQ------MLTYGAHVIAV-DGN---FDDAQRLVKELAADEG-----LYAVNSINPA---RLEGQKTYA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 211 IEtkcqILEREGRLPDAVIAAVGGGSNAIGM---FTDFIDEANV----RLIGVEPAGKgiesgehgAPLGHAkvgiyFGM 283
Cdd:COG0498 205 FE----IAEQLGRVPDWVVVPTGNGGNILAGykaFKELKELGLIdrlpRLIAVQATGC--------NPILTA-----FET 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 284 KSPLMQTEDGQveesySVSAGLD--FPSVGPQ--HAYLQSIGRAEypSITDDEALNAFQELAKHEGIIPALESSHALAQA 359
Cdd:COG0498 268 GRDEYEPERPE-----TIAPSMDigNPSNGERalFALRESGGTAV--AVSDEEILEAIRLLARREGIFVEPATAVAVAGL 340
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 341956663 360 LKMIHQEPNKEQILVV-NLSGRGDKDIFTVDKILTEKGMK 398
Cdd:COG0498 341 RKLREEGEIDPDEPVVvLSTGHGLKFPDAVREALGGEPLA 380
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
56-260 |
2.15e-13 |
|
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: 70.45 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 56 RPTALTLCRNLTKGTKAKIYLKREDLLHGGAHK----TNQVLGqilLAKRMGKTRIIAETgAGQHGVATALACAMLDMPC 131
Cdd:COG1171 23 RRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKlrgaYNALAS---LSEEERARGVVAAS-AGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 132 RIYM--GAKDVERQspnvfRMRLMGAEVVPVQKGScslkDACCEAMRDWSAnyETTHYLLgtaagpHPF--PTIVrEFQK 207
Cdd:COG1171 99 TIVMpeTAPAVKVA-----ATRAYGAEVVLHGDTY----DDAEAAAAELAE--EEGATFV------HPFddPDVI-AGQG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 341956663 208 MIGIEtkcqILEREGRLpDAVIAAVGGGSNAIGMFTdFIDEAN--VRLIGVEPAG 260
Cdd:COG1171 161 TIALE----ILEQLPDL-DAVFVPVGGGGLIAGVAA-ALKALSpdIRVIGVEPEG 209
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
57-260 |
6.46e-12 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 66.75 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 57 PTALTLCRNLTKGTKAKIYLKREDL-------LHGGAHKTNQvlgqilLAKRmGKTRIIAETGAGQHGVATALACAMLDM 129
Cdd:PRK08639 25 ETPLQRNDYLSEKYGANVYLKREDLqpvrsykLRGAYNAISQ------LSDE-ELAAGVVCASAGNHAQGVAYACRHLGI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 130 PCRIYMGAKdverqSPN--VFRMRLMGAEVVPVQkgscsLK----DACCEAMRDWSAnyETTHYLLgtaagpHPF--PTI 201
Cdd:PRK08639 98 PGVIFMPVT-----TPQqkIDQVRFFGGEFVEIV-----LVgdtfDDSAAAAQEYAE--ETGATFI------PPFddPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341956663 202 VrEFQKMIGIEtkcqILEREGRL--PDAVIAAVGGGSNAIGMFTDFIDEA-NVRLIGVEPAG 260
Cdd:PRK08639 160 I-AGQGTVAVE----ILEQLEKEgsPDYVFVPVGGGGLISGVTTYLKERSpKTKIIGVEPAG 216
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
58-384 |
1.45e-11 |
|
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: 64.92 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 58 TALTLCRNLTKGTKAK-IYLKREDLLHGGAHKTNQVLGQILLAKRMGKTRIIAETgAGQHGVATALACAMLDMPCRIYMG 136
Cdd:cd01563 23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACAS-TGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 137 AkDVERQspNVFRMRLMGAEVVPVQKGSCSLKDACCEAMRD---WSANYETTHYLLGtaagphpfptivrefQKMIGIEt 213
Cdd:cd01563 102 A-GKALG--KLAQALAYGATVLAVEGNFDDALRLVRELAEEnwiYLSNSLNPYRLEG---------------QKTIAFE- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 214 kcqILEREG-RLPDAVIAAVGGGSNAIGMFTDF--------IDEaNVRLIGVEPAGkgiesgehGAPLGHA-KVGiyfgm 283
Cdd:cd01563 163 ---IAEQLGwEVPDYVVVPVGNGGNITAIWKGFkelkelglIDR-LPRMVGVQAEG--------AAPIVRAfKEG----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 284 ksplmQTEDGQVEESYSVSAGLD--FPSVGPQ--HAYLQSIGRAEypSITDDEALNAFQELAKHEGIIPALESSHALAQA 359
Cdd:cd01563 226 -----KDDIEPVENPETIATAIRigNPASGPKalRAVRESGGTAV--AVSDEEILEAQKLLARTEGIFVEPASAASLAGL 298
|
330 340
....*....|....*....|....*.
gi 341956663 360 LKMIHQ-EPNKEQILVVNLSGRGDKD 384
Cdd:cd01563 299 KKLREEgIIDKGERVVVVLTGHGLKD 324
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
74-260 |
1.49e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 64.59 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 74 IYLKREDLLHGGAHKTNQVLGQiLLAKRMGKTRIIAETGaGQHGVATALACAMLDMPCRIYmgakdVERQSP--NVFRMR 151
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNR-LLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVPATVF-----VPETAPpaKVARLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 152 LMGAEVVPVqkgscslKDACCEAMRDWSANYETTHYLLgtaagPHPF--PTIVREfQKMIGIEtkcqiLEREGRLPDAVI 229
Cdd:PRK08246 112 ALGAEVVVV-------GAEYADALEAAQAFAAETGALL-----CHAYdqPEVLAG-AGTLGLE-----IEEQAPGVDTVL 173
|
170 180 190
....*....|....*....|....*....|.
gi 341956663 230 AAVGGGSNAIGMFTDFidEANVRLIGVEPAG 260
Cdd:PRK08246 174 VAVGGGGLIAGIAAWF--EGRARVVAVEPEG 202
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
64-375 |
3.35e-11 |
|
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: 63.53 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 64 RNLTKGTKAKIYLKREDLLHGGAHKTNQVLGQILLAKRMGK----TRIIaETGAGQHGVATALACAMLDMPCRIYMGAK- 138
Cdd:COG0031 20 NRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLlkpgGTIV-EATSGNTGIGLAMVAAAKGYRLILVMPETm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 139 DVERQSpnvfRMRLMGAEVVPVQkGSCSLKDACCEAMR------DW--------SANYEtTHYlLGTAagphpfPTIVRE 204
Cdd:COG0031 99 SKERRA----LLRAYGAEVVLTP-GAEGMKGAIDKAEElaaetpGAfwpnqfenPANPE-AHY-ETTG------PEIWEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 205 FqkmigietkcqilerEGRlPDAVIAAVGGGsnaiGMFT---DFIDEAN--VRLIGVEPAGKGIESGehGAPLGHAKVGI 279
Cdd:COG0031 166 T---------------DGK-VDAFVAGVGTG----GTITgvgRYLKERNpdIKIVAVEPEGSPLLSG--GEPGPHKIEGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 280 yfgmksplmqtEDGQVEESYSVSAgLDfpsvgpqhaylqsigraEYPSITDDEALNAFQELAKHEGIIPALESSHALAQA 359
Cdd:COG0031 224 -----------GAGFVPKILDPSL-ID-----------------EVITVSDEEAFAMARRLAREEGILVGISSGAAVAAA 274
|
330
....*....|....*.
gi 341956663 360 LKMIHQEPNKEQILVV 375
Cdd:COG0031 275 LRLAKRLGPGKTIVTI 290
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
73-259 |
2.75e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 58.24 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 73 KIYLKREDLLHGGAHKTNQVLGQILLAKRMGK--TRIIAETgAGQHGVATALACAMLDMPCRIYMgakdverqSPNVFRM 150
Cdd:PRK06608 39 EIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TGNHGQAVAYASKLFGIKTRIYL--------PLNTSKV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 151 RLM-----GAEVVpvqkgSCSLKDACCEAMRDwsANYETTHYLlgtaagpHPF--PTIVrefqkmIGIETKCQ-ILEREG 222
Cdd:PRK06608 110 KQQaalyyGGEVI-----LTNTRQEAEEKAKE--DEEQGFYYI-------HPSdsDSTI------AGAGTLCYeALQQLG 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 341956663 223 RLPDAVIAAVGGGSNAIG-MFTDFIDEANVRLIGVEPA 259
Cdd:PRK06608 170 FSPDAIFASCGGGGLISGtYLAKELISPTSLLIGSEPL 207
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
56-259 |
5.48e-09 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 57.01 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 56 RPTALTLCRNLTKGTKAKIYLKREDLLHGGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRIYM 135
Cdd:PRK06815 19 RVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 136 GakdvERQSP-NVFRMRLMGAEVvpvqkgsCSLKDACCEAMRdWSANYETTHYLlgTAAGPHPFPTIVREfQKMIGIEtk 214
Cdd:PRK06815 99 P----EQASAiKLDAIRALGAEV-------RLYGGDALNAEL-AARRAAEQQGK--VYISPYNDPQVIAG-QGTIGME-- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 341956663 215 cqILEREGRLpDAVIAAVGGGS--NAIGMFTDFIDEAnVRLIGVEPA 259
Cdd:PRK06815 162 --LVEQQPDL-DAVFVAVGGGGliSGIATYLKTLSPK-TEIIGCWPA 204
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
58-375 |
1.94e-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: 49.22 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 58 TALTLCRNLTKGTKAKIYLKREDLLHGGAHKTNQV---LGQILLAKRMGKTRIIAETGaGQHGVATALACAMLDMPCRIY 134
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIghlCQKSAKQGLNECVHVVCSSG-GNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 135 MgakdverqsPN------VFRMRLMGAEVVpvQKGScSLKDAcceamrdwsANYETtHYLLGTAAGP---HPF--PTIVR 203
Cdd:cd06448 81 V---------PEstkprvVEKLRDEGATVV--VHGK-VWWEA---------DNYLR-EELAENDPGPvyvHPFddPLIWE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 204 EFQKMIGiETKCQILEREgrLPDAVIAAVGGGsnaiGMFTDFID------EANVRLIGVEpagkgiesgEHGAPLGHAKV 277
Cdd:cd06448 139 GHSSMVD-EIAQQLQSQE--KVDAIVCSVGGG----GLLNGIVQglerngWGDIPVVAVE---------TEGAHSLNASL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 278 giyfgmksplmqtEDGQV---EESYSVSAGLDFPSVGPQH-AYLQsigraEYPS----ITDDEALNAFQELAKHEGII-- 347
Cdd:cd06448 203 -------------KAGKLvtlPKITSVATSLGAKTVSSQAlEYAQ-----EHNIksevVSDRDAVQACLRFADDERILve 264
|
330 340 350
....*....|....*....|....*....|...
gi 341956663 348 PALESS-----HALAQALKMIHQEPNKEQILVV 375
Cdd:cd06448 265 PACGAAlavvySGKILDLQLEVLLTPLDNVVVV 297
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
72-390 |
2.07e-06 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 49.23 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 72 AKIYLKREDLLHGGAHKTNQVLGQILLAKRMGKTRIIAETgAGQHGVATALACAMLDMPCRIYMgAKDVERqsPNVFRMR 151
Cdd:PRK08197 95 GRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPT-NGNAGAAWAAYAARAGIRATIFM-PADAPE--ITRLECA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 152 LMGAEVVPVQkgscSLKDACCEAMRDwsANYETTHYLLGTAAGPHpfptivR-EFQKMIGIEtkcqILEREG-RLPDAVI 229
Cdd:PRK08197 171 LAGAELYLVD----GLISDAGKIVAE--AVAEYGWFDVSTLKEPY------RiEGKKTMGLE----LAEQLGwRLPDVIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 230 AAVGGGSNAIGMFTDF--------IDEANVRLIGVEPAG-----KGIESGEHGAPLGhakvgiyfgmksplmqtedgqvE 296
Cdd:PRK08197 235 YPTGGGVGLIGIWKAFdelealgwIGGKRPRLVAVQAEGcapivKAWEEGKEESEFW----------------------E 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 297 ESYSVSAGLDFPsvgpqhaylQSIG-----RAEYPS------ITDDEALNAFQELAKHEGIIPALESSHALAQALKMIHQ 365
Cdd:PRK08197 293 DAHTVAFGIRVP---------KALGdflvlDAVRETggcaiaVSDDAILAAQRELAREEGLFACPEGAATFAAARQLRES 363
|
330 340
....*....|....*....|....*...
gi 341956663 366 ---EPNkEQILVVNlSGRGDKDIFTVDK 390
Cdd:PRK08197 364 gwlKGD-ERVVLFN-TGSGLKYPDTVPV 389
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
53-240 |
3.60e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 45.21 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 53 YAGRPTALTLCRNLTKGTKAKIYLKREDL--LHGGAHKTNQ---VLGQillAKRMGKTRIIAeTGAGQ--HGVATALACA 125
Cdd:PRK03910 11 LAGLPTPLEPLPRLSAALGPDIYIKRDDLtgLALGGNKTRKlefLLAD---ALAQGADTLIT-AGAIQsnHARQTAAAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 126 MLDMPCRIYM-----GAKDVERQSPNVFRMRLMGAEVVPVQKGScslkDAcCEAMRDWSANYEtthyllgtAAGPHPFpt 200
Cdd:PRK03910 87 KLGLKCVLLLenpvpTEAENYLANGNVLLDDLFGAEIHVVPAGT----DM-DAQLEELAEELR--------AQGRRPY-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 341956663 201 ivrefqkmigietkcqileregrlpdaVIAavGGGSNAIG 240
Cdd:PRK03910 152 ---------------------------VIP--VGGSNALG 162
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
56-258 |
3.71e-05 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 45.56 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 56 RPTALTLCRNLTKGTKAKIYLKREDL-------LHGGAHKTNQvlgqiLLAKRMGKTRIIAEtgAGQHGVATALACAMLD 128
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLqpvfsfkIRGAYNKMAR-----LPAEQLARGVITAS--AGNHAQGVALAAARLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 129 MPCRIYMgakdvERQSPN--VFRMRLMGAEVvpVQKGScSLKDACCEAMRdwSANYETTHYLlgtaagpHPF--PTIVRE 204
Cdd:PRK12483 109 VKAVIVM-----PRTTPQlkVDGVRAHGGEV--VLHGE-SFPDALAHALK--LAEEEGLTFV-------PPFddPDVIAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 341956663 205 fQKMIGIEtkcqIL-EREGRLpDAVIAAVGGGSNAIGM--FTDFIdEANVRLIGVEP 258
Cdd:PRK12483 172 -QGTVAME----ILrQHPGPL-DAIFVPVGGGGLIAGIaaYVKYV-RPEIKVIGVEP 221
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
226-387 |
5.19e-04 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 41.53 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 226 DAVIAAVGGGSNAIGMfTDFIDEAN--VRLIGVEPAGKGIESGehGAPLGHAKVGIYFGMksplmqtedgqveesysVSA 303
Cdd:PLN00011 176 DILVAGVGTGGTATGV-GKFLKEKNkdIKVCVVEPVESAVLSG--GQPGPHLIQGIGSGI-----------------IPF 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 304 GLDFPSVGpqhaylqsigraEYPSITDDEALNAFQELAKHEGIIPALESSHALAQALKMIHQEPNKEQILVVNLSGRGDK 383
Cdd:PLN00011 236 NLDLTIVD------------EIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGER 303
|
....
gi 341956663 384 DIFT 387
Cdd:PLN00011 304 YLST 307
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
58-262 |
7.44e-04 |
|
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: 41.25 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 58 TALTLCRNLTK--GTKAKIYLKREDL---LHGGAHKTNQVLGQILLAKRMGKTRIIAeTGAGQ--HGVATALACAMLDMP 130
Cdd:cd06449 1 TPIQYLPRLSEhlGGKVEIYAKRDDCnsgLAFGGNKIRKLEYLLPDALAKGADTLVT-VGGIQsnHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341956663 131 C----RIYMGAKD-VERQSPNVFRMRLMGAEVVPVQKG-SCSLKDACCEAMRDWSANYETThYLLGTAAGPHPFPTI--V 202
Cdd:cd06449 80 CvlvqENWVPYSDaVYDRVGNILLSRIMGADVRLVSAGfDIGIRKSFEEAAEEVEAKGGKP-YVIPAGGSEHPLGGLgyV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341956663 203 REFQKMIgietkcQILEREGRLPDAVIAAVGGGSNAIGMFTDF-IDEANVRLIGVEPAGKG 262
Cdd:cd06449 159 GFVLEIA------QQEEELGFKFDSIVVCSVTGSTHAGLSVGLaALGRQRRVIGIDASAKP 213
|
|
| |
