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Conserved domains on  [gi|1834195147|gb|QJD13777|]
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Tryptophan synthase subunit B, partial [Burkholderia cenocepacia]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 1-216 0e+00

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.


The actual alignment was detected with superfamily member PRK04346:

Pssm-ID: 444852  Cd Length: 397  Bit Score: 499.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:PRK04346  149 VFRMKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:PRK04346  229 AVVACVGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLD 308

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:PRK04346  309 YPGVGPEHAYLKDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKL 364
 
Name Accession Description Interval E-value
PRK04346 PRK04346
tryptophan synthase subunit beta; Validated
 1-216 0e+00

tryptophan synthase subunit beta; Validated


Pssm-ID: 235288  Cd Length: 397  Bit Score: 499.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:PRK04346  149 VFRMKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:PRK04346  229 AVVACVGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLD 308

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:PRK04346  309 YPGVGPEHAYLKDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKL 364
TrpB COG0133
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ...
 1-216 2.75e-179

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: 496.48  E-value: 2.75e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:COG0133   152 VFRMKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPD 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:COG0133   232 AVVACVGGGSNAIGIFYPFLDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLD 311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:COG0133   312 YPGVGPEHAYLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKL 367
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 1-216 2.93e-145

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: 408.85  E-value: 2.93e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:cd06446   125 VFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNVEDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPD 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:cd06446   205 VVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGLETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLD 284

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:cd06446   285 YPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLARTEGIIPALESSHAIAYAIKL 340
trpB TIGR00263
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ...
 1-216 9.84e-142

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: 400.97  E-value: 9.84e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:TIGR00263 141 VFRMELLGAKVIPVTSGSGTLKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPD 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:TIGR00263 221 AVIACVGGGSNAIGIFYAFIDDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLD 300

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:TIGR00263 301 YPGVGPEHAYLHETGRATYEAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKI 356
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 3-211 1.10e-10

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: 59.63  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   3 RMKLLGATVVPVESGSRTLKDALNEAMRDWvtniESTFYIigtvagpHPY-PMMVRDFQRVIGDECKVQMpelaGRQPDA 81
Cdd:pfam00291  96 LMRALGAEVVLVGGDYDEAVAAARELAAEG----PGAYYI-------NQYdNPLNIEGYGTIGLEILEQL----GGDPDA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  82 VIACVGGGSNAMGIFYPYID-DTSVQLIGVEAAGdgldTGHHAASLIAGSPGVLHGNRTYllqddngqiiethsvSAGLD 160
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKElGPDVRVIGVEPEG----APALARSLAAGRPVPVPVADTI---------------ADGLG 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1834195147 161 YPGVGPEHAW-LKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIA 211
Cdd:pfam00291 222 VGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALA 273
 
Name Accession Description Interval E-value
PRK04346 PRK04346
tryptophan synthase subunit beta; Validated
 1-216 0e+00

tryptophan synthase subunit beta; Validated


Pssm-ID: 235288  Cd Length: 397  Bit Score: 499.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:PRK04346  149 VFRMKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:PRK04346  229 AVVACVGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLD 308

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:PRK04346  309 YPGVGPEHAYLKDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKL 364
TrpB COG0133
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ...
 1-216 2.75e-179

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: 496.48  E-value: 2.75e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:COG0133   152 VFRMKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPD 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:COG0133   232 AVVACVGGGSNAIGIFYPFLDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLD 311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:COG0133   312 YPGVGPEHAYLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKL 367
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 1-216 2.93e-145

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: 408.85  E-value: 2.93e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:cd06446   125 VFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNVEDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPD 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:cd06446   205 VVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGLETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLD 284

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:cd06446   285 YPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLARTEGIIPALESSHAIAYAIKL 340
trpB TIGR00263
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ...
 1-216 9.84e-142

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: 400.97  E-value: 9.84e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:TIGR00263 141 VFRMELLGAKVIPVTSGSGTLKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPD 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:TIGR00263 221 AVIACVGGGSNAIGIFYAFIDDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLD 300

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:TIGR00263 301 YPGVGPEHAYLHETGRATYEAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKI 356
PRK13028 PRK13028
tryptophan synthase subunit beta; Provisional
 1-216 1.93e-136

tryptophan synthase subunit beta; Provisional


Pssm-ID: 183851  Cd Length: 402  Bit Score: 388.07  E-value: 1.93e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:PRK13028  153 VFRMKLLGAEVVPVTRGGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:PRK13028  233 AVVACVGGGSNAIGLFSAFLDDESVRLVGVEPAGRGLDLGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLD 312

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:PRK13028  313 YPGVGPEHAYLKDIGRVEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKL 368
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 1-212 2.21e-131

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 382.62  E-value: 2.21e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:PRK13803  361 VERMKLLGANVIPVLSGSKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPD 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:PRK13803  441 AIIACVGGGSNAIGIFYHFLDDPSVKLIGVEAGGKGVNTGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLD 520

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAY 212
Cdd:PRK13803  521 YPGIGPMHANLFETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAY 572
PLN02618 PLN02618
tryptophan synthase, beta chain
 1-216 3.67e-125

tryptophan synthase, beta chain


Pssm-ID: 215333  Cd Length: 410  Bit Score: 359.84  E-value: 3.67e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPD 80
Cdd:PLN02618  162 VFRMRLLGAEVRPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPD 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  81 AVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSPGVLHGNRTYLLQDDNGQIIETHSVSAGLD 160
Cdd:PLN02618  242 VLVACVGGGSNAMGLFHEFIDDEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLD 321

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834195147 161 YPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:PLN02618  322 YPGVGPEHSFLKDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKL 377
PRK13802 PRK13802
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
 1-215 2.20e-93

bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 184335 [Multi-domain]  Cd Length: 695  Bit Score: 287.31  E-value: 2.20e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGSRTLKDALNEAMRDWVTNIESTFYIIGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAG-RQP 79
Cdd:PRK13802  422 VARMRMLGAEVVEVTLGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiDHP 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  80 DAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHHAASLIAGSP--GVLHGNRTYLLQDDNGQIIETHSVSA 157
Cdd:PRK13802  502 DAICACVGGGSNAIGVMNAFLDDERVNLYGYEAGGNGPESGKHAIRFAPGTGelGMFQGAKSYLLENDEGQTLDTYSISA 581

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1834195147 158 GLDYPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVK 215
Cdd:PRK13802  582 GLDYASVGPEHAWLKDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYK 639
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 1-216 8.80e-24

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: 94.89  E-value: 8.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   1 VYRMKLLGATVVPVESGsrtLKDALNEAMRDWVTNiESTFYIigtvagpHPY-PMMVRDFQRVIGDECKVQMPelaGRQP 79
Cdd:cd00640    89 VAQMRALGAEVVLVPGD---FDDAIALAKELAEED-PGAYYV-------NQFdNPANIAGQGTIGLEILEQLG---GQKP 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  80 DAVIACVGGGSNAMGIFYPYIDDT-SVQLIGVEaagdgldtghhaasliagspgvlhgnrtyllqddngqiiethsvsag 158
Cdd:cd00640   155 DAVVVPVGGGGNIAGIARALKELLpNVKVIGVE----------------------------------------------- 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1834195147 159 ldypgvgpehawlkdsgrAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIAYGVKL 216
Cdd:cd00640   188 ------------------PEVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKL 227
PRK12391 PRK12391
TrpB-like pyridoxal phosphate-dependent enzyme;
2-211 9.64e-24

TrpB-like pyridoxal phosphate-dependent enzyme;


Pssm-ID: 237087  Cd Length: 427  Bit Score: 97.56  E-value: 9.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   2 YR---MKLLGATVVP-----VESGSRTLKD----------ALNEAMRDWVTNiESTFYIIGTVAgphPYPMMvrdFQRVI 63
Cdd:PRK12391  167 YRrslMETYGAEVIPspsdlTEAGRKILAEdpdhpgslgiAISEAVEDAAKR-PDTKYALGSVL---NHVLL---HQTVI 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  64 GDECKVQMpELAGRQPDAVIACVGGGSNAMGIFYPYIDD-----TSVQLIGVEAAG-----------DGLDTGhhaasli 127
Cdd:PRK12391  240 GLEAKKQL-ELAGEYPDVVIGCVGGGSNFAGLAFPFLGDklegkKDTRFIAVEPAAcptltkgeyayDFGDTA------- 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147 128 agspGVLHGNRTYLLQDDngqIIETHSVSAGLDYPGVGPEHAWLKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESS 207
Cdd:PRK12391  312 ----GLTPLLKMYTLGHD---FVPPPIHAGGLRYHGMAPLVSLLVHEGLIEARAYPQTEVFEAAVLFARTEGIVPAPESS 384


                  ....
gi 1834195147 208 HAIA 211
Cdd:PRK12391  385 HAIA 388
COG1350 COG1350
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ...
 2-211 1.48e-21

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: 91.35  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   2 YR---MKLLGATVVP-----VESGSRTLKD----------ALNEAMRDWVTNiESTFYIIGTVAGpHpypmmVRDFQRVI 63
Cdd:COG1350   168 YRrsmMETYGAEVIPspsdlTEAGRKILAEdpdtpgslgiAISEAVEDAATR-DDTKYALGSVLN-H-----VLLHQTVI 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  64 GDECKVQMpELAGRQPDAVIACVGGGSNAMGIFYPYIDD-----TSVQLIGVEAA--------------GD--GLdT--- 119
Cdd:COG1350   241 GLEAKKQL-EKAGEYPDVVIGCAGGGSNFAGLAFPFLRDklrgkKDVRFIAVEPAacptltrgvyaydfGDtaGL-Tpll 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147 120 -----GHH--AASLIAGspgvlhgnrtyllqddngqiiethsvsaGLDYPGVGPEHAWLKDSG--RAQYVPITDA-EALK 189
Cdd:COG1350   319 kmytlGHDfiPPPIHAG----------------------------GLRYHGMAPLVSQLYHDGliEAVAYPQLEVfEAGV 370

                         250       260
                  ....*....|....*....|..
gi 1834195147 190 AFhdcCRIEGIIPALESSHAIA 211
Cdd:COG1350   371 LF---ARTEGIVPAPESAHAIK 389
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 3-211 1.10e-10

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: 59.63  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   3 RMKLLGATVVPVESGSRTLKDALNEAMRDWvtniESTFYIigtvagpHPY-PMMVRDFQRVIGDECKVQMpelaGRQPDA 81
Cdd:pfam00291  96 LMRALGAEVVLVGGDYDEAVAAARELAAEG----PGAYYI-------NQYdNPLNIEGYGTIGLEILEQL----GGDPDA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147  82 VIACVGGGSNAMGIFYPYID-DTSVQLIGVEAAGdgldTGHHAASLIAGSPGVLHGNRTYllqddngqiiethsvSAGLD 160
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKElGPDVRVIGVEPEG----APALARSLAAGRPVPVPVADTI---------------ADGLG 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1834195147 161 YPGVGPEHAW-LKDSGRAQYVPITDAEALKAFHDCCRIEGIIPALESSHAIA 211
Cdd:pfam00291 222 VGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALA 273
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 3-131 6.90e-04

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: 39.78  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834195147   3 RMKLLGATVVPVEsgsRTLKDALNEAMRDwvtNIESTFYIIgtvagpHPY--PMMVRDfQRVIGDECKVQMPELagrqpD 80
Cdd:cd01562   106 ATRAYGAEVVLYG---EDFDEAEAKAREL---AEEEGLTFI------HPFddPDVIAG-QGTIGLEILEQVPDL-----D 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1834195147  81 AVIACVGGGSNAMGI------FYPyiddtSVQLIGVEAAG-DGLdtghhAASLIAGSP 131
Cdd:cd01562   168 AVFVPVGGGGLIAGIatavkaLSP-----NTKVIGVEPEGaPAM-----AQSLAAGKP 215
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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