NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2131129303|ref|WP_228378986|]
View 

MULTISPECIES: tryptophanase [Thermoanaerobacter]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TnaA super family cl42523
Tryptophanase [Amino acid transport and metabolism];
1-55 4.80e-34

Tryptophanase [Amino acid transport and metabolism];


The actual alignment was detected with superfamily member COG3033:

Pssm-ID: 442268  Cd Length: 460  Bit Score: 119.10  E-value: 4.80e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARLEPVE 55
Cdd:COG3033   405 VRLAIPRRVYTQSHMDYVAEALIELYERRESIKGLRIVYEPPVLRHFTARLEPVS 459
 
Name Accession Description Interval E-value
TnaA COG3033
Tryptophanase [Amino acid transport and metabolism];
1-55 4.80e-34

Tryptophanase [Amino acid transport and metabolism];


Pssm-ID: 442268  Cd Length: 460  Bit Score: 119.10  E-value: 4.80e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARLEPVE 55
Cdd:COG3033   405 VRLAIPRRVYTQSHMDYVAEALIELYERRESIKGLRIVYEPPVLRHFTARLEPVS 459
tnaA PRK13238
tryptophanase;
1-55 7.79e-33

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 115.68  E-value: 7.79e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARLEPVE 55
Cdd:PRK13238  406 LRLAIPRRVYTQSHMDYVAEALKAVKENRESIKGLRFTYEPPVLRHFTARLKPVS 460
Tnase_like cd00617
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-51 7.04e-25

Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.


Pssm-ID: 99741  Cd Length: 431  Bit Score: 93.96  E-value: 7.04e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARL 51
Cdd:cd00617   381 VRLAIPRRVYTQDHMDYVAAAVIALYERREDIRGLRIVYEPKLLRHFTARL 431
tnaA_trp_ase TIGR02617
tryptophanase, leader peptide-associated; Members of this family belong to the ...
 1-54 3.72e-22

tryptophanase, leader peptide-associated; Members of this family belong to the beta-eliminating lyase family (pfam01212) and act as tryptophanase (L-tryptophan indole-lyase). The tryptophanases of this family, as a rule, are found with a tryptophanase leader peptide (TnaC) encoded upstream. Both tryptophanases (4.1.99.1) and tyrosine phenol-lyases (EC 4.1.99.2) are found between trusted and noise cutoffs, but this model captures nearly all tryptophanases for which the leader peptide gene tnaC can be found upstream. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131666  Cd Length: 467  Bit Score: 86.53  E-value: 3.72e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARLEPV 54
Cdd:TIGR02617 414 LRLTIPRATYTQTHMDFIIEAFKHVKENAPNIKGLTFTYEPKVLRHFTARLKEV 467
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
1-21 9.92e-05

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 37.20  E-value: 9.92e-05
                          10        20
                  ....*....|....*....|.
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEA 21
Cdd:pfam01212 268 LRLAIPRRVYTNTHMVYVAAA 288
 
Name Accession Description Interval E-value
TnaA COG3033
Tryptophanase [Amino acid transport and metabolism];
1-55 4.80e-34

Tryptophanase [Amino acid transport and metabolism];


Pssm-ID: 442268  Cd Length: 460  Bit Score: 119.10  E-value: 4.80e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARLEPVE 55
Cdd:COG3033   405 VRLAIPRRVYTQSHMDYVAEALIELYERRESIKGLRIVYEPPVLRHFTARLEPVS 459
tnaA PRK13238
tryptophanase;
1-55 7.79e-33

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 115.68  E-value: 7.79e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARLEPVE 55
Cdd:PRK13238  406 LRLAIPRRVYTQSHMDYVAEALKAVKENRESIKGLRFTYEPPVLRHFTARLKPVS 460
Tnase_like cd00617
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-51 7.04e-25

Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.


Pssm-ID: 99741  Cd Length: 431  Bit Score: 93.96  E-value: 7.04e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARL 51
Cdd:cd00617   381 VRLAIPRRVYTQDHMDYVAAAVIALYERREDIRGLRIVYEPKLLRHFTARL 431
tnaA_trp_ase TIGR02617
tryptophanase, leader peptide-associated; Members of this family belong to the ...
 1-54 3.72e-22

tryptophanase, leader peptide-associated; Members of this family belong to the beta-eliminating lyase family (pfam01212) and act as tryptophanase (L-tryptophan indole-lyase). The tryptophanases of this family, as a rule, are found with a tryptophanase leader peptide (TnaC) encoded upstream. Both tryptophanases (4.1.99.1) and tyrosine phenol-lyases (EC 4.1.99.2) are found between trusted and noise cutoffs, but this model captures nearly all tryptophanases for which the leader peptide gene tnaC can be found upstream. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131666  Cd Length: 467  Bit Score: 86.53  E-value: 3.72e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARLEPV 54
Cdd:TIGR02617 414 LRLTIPRATYTQTHMDFIIEAFKHVKENAPNIKGLTFTYEPKVLRHFTARLKEV 467
tyr_phenol_ly TIGR02618
tyrosine phenol-lyase; This model describes a group of tyrosine phenol-lyase (4.1.99.2) ...
 1-52 5.41e-20

tyrosine phenol-lyase; This model describes a group of tyrosine phenol-lyase (4.1.99.2) (beta-tyrosinase), a pyridoxal-phosphate enzyme closely related to tryptophanase (4.1.99.1) (see model TIGR02617). Both belong to the beta-eliminating lyase family (pfam01212) [Energy metabolism, Amino acids and amines]


Pssm-ID: 131667  Cd Length: 450  Bit Score: 80.73  E-value: 5.41e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEAVKRVYARRDKIKGYRFTYEPPILRHFTARLE 52
Cdd:TIGR02618 399 VRLTIPRRVYTYAHMDVVADGIIKLYKHRDDIRGLKMVYEPKQLRFFTARFE 450
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
1-21 9.92e-05

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 37.20  E-value: 9.92e-05
                          10        20
                  ....*....|....*....|.
gi 2131129303   1 MRLTIPRRVYTNSHMDVIAEA 21
Cdd:pfam01212 268 LRLAIPRRVYTNTHMVYVAAA 288
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH