1YGY


Conserved Protein Domain Family
ACT_3PGDH-xct

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cd04902: ACT_3PGDH-xct 
Click on image for an interactive view with Cn3D
C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH)
The C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with an extended C-terminal (xct) region from bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. Some 3PGDH enzymes have an additional domain formed by an extended C-terminal region. This additional domain introduces significant asymmetry to the homotetramer. Adjacent ACT (regulatory) domains interact, creating two serine-binding sites, however, this asymmetric arrangement results in the formation of two different and distinct domain interfaces between identical domains in the asymmetric unit. How this asymmetry influences the mechanism of effector inhibition is still unknown. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153174
View PSSM: cd04902
Aligned: 86 rows
Threshold Bit Score: 73.6581
Threshold Setting Gi: 2313497
Created: 18-Aug-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
putative
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:putative L-serine binding site [chemical binding site]
Evidence:
  • Comment:The sequence alignment of M. tuberculosis 3PGDH (1YGY) with E. coli 3PGDH (1PSD) suggests that this Tyr, Asp, and Asn perform the function of serine binding.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                 # #                 #                                               
1YGY_B           456 NLIIHYVDRPGALGKIGTLLGtaGVNIQAAQLSEdaeGPGATILLRLDQdVPDDVRTAIAAAvDAYKLEVVDL 528 Mycobacterium tube...
4467266          456 MVVLRYEDRPGVVGTVGRIIGeaGLNIAGMQVARatvGGEALAVLTVDDtVPSGVLAEVAAEiGATSARSVNL 528 Streptomyces coeli...
YP_062256        455 LIVMVYDDRPGIVAVYGREFGeaKINIAGMQIARtsaGGKALSVLTVDSsVPEGLLEKVRVAiDADLLQEIDI 527 Leifsonia xyli sub...
ZP_00380344      455 LLIFRYEDRPGIIGQLGQALGanEINIAGMQVSPsatDNDALSVLAVDSaVSEEVVKAVAGAvNASAFSGVSL 527 Brevibacterium lin...
NP_952251        457 MLLLHYADRPGMIGKIGTIMGqhEINIASMNLGRsekKGEAMVILSLDSaVPPQVLEEVRAAtDATFIKAIHM 529 Geobacter sulfurre...
REF_jgi:Tfu_0614 455 MAFFSYHDRPGVVGVVGQLLGqaQVNIAGMQVSRdkeGGAALIALTVDSaIPDETLETISKEiGAEISRVDLV 527 Thermobifida fusca YX
CAI37460         457 NLFLVYPDQPGALGKVGTLLGnkGINIDAAALSPtddEQTATLVLRVSEeLDQQLVEEVKAElNASNAFVLNL 529 Corynebacterium je...
ZP_00997062      455 MAFFSYTDRPGVVGVIGALLGaaDVNIGGMQVARddaAGTALVALTVDNkIPADVVAAIASE-LSADVRVVDL 526 Janibacter sp. HTC...
ZP_01428695      456 LVFLRYADRPGVVGAVGTLLGeaGVNIAAMQVARreaGGETLMTLTVDQaLGADLLTSVADSvGATSVSAADL 528 Salinispora tropic...
ZP_00569647      454 LAFFRYEDRPGIVGAVGALLGeaHINIANAQVSRlsaGGEALMSLSLDDaVAPDILAEIAKIiGASYARAVSI 526 Frankia sp. EAN1pec

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