Summary: Tryptophan synthase alpha chain
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Tryptophan synthase alpha chain Provide feedback
No Pfam abstract.
Hyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR; , J Biol Chem 1988;263:17857-17871.: Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. PUBMED:3053720 EPMC:3053720
Rhee S, Miles EW, Davies DR; , J Biol Chem 1998;273:8553-8555.: Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49. PUBMED:9535826 EPMC:9535826
Internal database links
|Similarity to PfamA using HHSearch:||His_biosynth NanE PcrB|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002028
Tryptophan synthase (EC) catalyzes the last step in the biosynthesis
of tryptophan [PUBMED:2679363, PUBMED:1366510]:
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||tryptophan synthase activity (GO:0004834)|
|Biological process||tryptophan metabolic process (GO:0006568)|
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This large superfamily of TIM barrel enzymes all contain a common phosphate binding site. The phosphate is found in a variety of cofactors and ligands such as FMN [1,2].
The clan contains the following 57 members:Ala_racemase_N ALAD Aldolase AP_endonuc_2 BtpA CdhD CutC DAHP_synth_1 DAHP_synth_2 DeoC DHDPS DHO_dh DHquinase_I DUF1341 DUF2090 DUF556 DUF561 DUF692 DUF993 Dus F_bP_aldolase FMN_dh G3P_antiterm Glu_syn_central Glu_synthase His_biosynth HMGL-like IGPS IMPDH iPGM_N MtrH NanE NAPRTase NeuB NMO OMPdecase Orn_Arg_deC_N Oxidored_FMN PcrB PdxJ PhosphMutase PRAI Pterin_bind QRPTase_C Racemase_4 RhaA Ribul_P_3_epim SOR_SNZ Tagatose_6_P_K ThiG TIM TIM-br_sig_trns TMP-TENI Transaldolase Trp_syntA UvdE UxuA
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Key: available, not generated, — not available.
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Curation and family details
|Author:||Finn RD, Griffiths-Jones SR|
|Number in seed:||18|
|Number in full:||4254|
|Average length of the domain:||247.30 aa|
|Average identity of full alignment:||35 %|
|Average coverage of the sequence by the domain:||89.87 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Trp_syntA domain has been found. There are 94 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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