1TDJ


Conserved Protein Domain Family
ACT_ThrD-I_2

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cd04907: ACT_ThrD-I_2 
Click on image for an interactive view with Cn3D
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase)
This CD includes the second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153179
View PSSM: cd04907
Aligned: 39 rows
Threshold Bit Score: 94.1557
Threshold Setting Gi: 940472
Created: 16-Mar-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
putative
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:putative Ile/Val binding site [chemical binding site]
Evidence:
  • Comment:based on comparison with related structures and other data, these residues may be involved in effector binding
  • Citation:PMID 9562556

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                   ######                                                              
1TDJ        433 ERLYSFEFPEsPGALLRFLNTLGt-YWNISLFHYRSHGt-DYGRVLAAFELGdh--ePDFETRLNELGYDCHDETNNPAF 508 Escherichia coli
Q04513      352 KHYFLVNFPQkPGQLRHFLEDILgpDDDITLFEYLKRNnrETGTALVGIHLSeasglDSLLERMEESAIDSRRLEPGTPE 431 Corynebacterium ...
ZP_00380498 344 KHYFIVDFPQePGALRRFLNEILgpEDDIAMFEYVKRSdrETGPAFVGIELGnaedlPNLLERMDASQIEIERVHQNSPM 423 Brevibacterium l...
BAE86108    331 KHYFIVNFPQrPGALKEFVGEVLgpNDDIARFEYTKSNnkEKGPTLIGIELSrkedyQPLIERMDKKGFQYTRINDNPEL 410 Desulfitobacteri...
AAA96639    338 QHYFIVNFPQrAGALREFLDEVLgpNDDITRFEYTKKNnkSNGPALVGIELQnkadyGPLIERMNKKPFHYVEVNKDEDL 417 Bacillus subtilis
CAD78318    331 QHYFIIKFPQrAGALREFLNNVLgpTDDITHFEYTRKHnrETGPALVGLQVAhrddyQGLLDRMAASNIEYQVVNEQRML 410 Rhodopirellula b...
EAR01499    332 KHYFIVRFPQrPGALKQFVAEILgpNDDITHFEYSKKSsrENAPAIVGIELKsatdlQPLIQRMKANNFYGDYLNDKPDL 411 Flavobacteriales...
AAO61956    336 KHYFLVRFPQrAGALKEFVSTILgpNDDITYFQYSKKTskEEGPAVIGIELSdkedfSGMIEKMKHYNIHYQYINDNPDL 415 Aster yellows ph...
YP_417405   338 KHYFILNFPQrPGALREFVNDVLgpQDDITKFEYLKKSsqNTGTVIIGIQLKdhddlIQLKQRVNHFDPSNIYINENKML 417 Staphylococcus a...
ZP_01308742 232 KHYFLVRFPQrAGALKEFVSTILgpNDDITYFQYSKKTskEEGPAVIGIELSdkedfSGMIKKMKHYNIHYQYINDNPDL 311 Candidatus Sulci...
Feature 1           
1TDJ        509 RFFL 512 Escherichia coli
Q04513      432 YEYL 435 Corynebacterium glutamicum
ZP_00380498 424 FRLF 427 Brevibacterium linens BL2
BAE86108    411 FGLL 414 Desulfitobacterium hafniense Y51
AAA96639    418 FHLL 421 Bacillus subtilis
CAD78318    411 FELL 414 Rhodopirellula baltica SH 1
EAR01499    412 FQYL 415 Flavobacteriales bacterium HTCC2170
AAO61956    416 FDIL 419 Aster yellows phytoplasma
YP_417405   418 HSLL 421 Staphylococcus aureus RF122
ZP_01308742 312 FDIL 315 Candidatus Sulcia muelleri str. Hc (Homalodisca coagulata)

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