1LLQ,1QR6,1VL6,1GQ2


Conserved Protein Domain Family
NAD_bind_malic_enz

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cd00762: NAD_bind_malic_enz 
Click on image for an interactive view with Cn3D
NAD(P) binding domain of malic enzyme
Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Statistics
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PSSM-Id: 133442
Aligned: 4 rows
Threshold Bit Score: 277.176
Created: 4-Feb-2003
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
NAD(P) binding
Conserved site includes 15 residues -Click on image for an interactive view with Cn3D
Feature 1:NAD(P) binding site [chemical binding site]
Evidence:
  • Structure:1QR6_A: human Mt malic enzyme binds NAD, contacts determined at 3.5A
  • Comment:2nd NAD binding site away from active site may be the binding site for ATP, an allosteric inhibitor of the enzyme
  • Structure:1GQ2_A: pigeon liver malic enzyme binds NAD, contacts determined at 3.5A
  • Structure:1LLQ_A: Acsaris suum malic enzyme binds NAD, contacts determined at 3.5A

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                     ####                             ##             
1LLQ_A    296 IQGTASVIVAGLLTCTRVTKKLVSQEKYLFFGAGAASTGIAEMIVHQMQnegiskeeacnRIYLMDIDGLVTKnrkemnp 375 pig roundworm
1QR6_A    280 IQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVXSXVenglseqeaqkKIWXFDKYGLLVKgrkakid 359 human
1VL6_D    168 QQGTAVVVSAAFLNALKLTEKKIEEVKVVVNGIGAAGYNIVKFLLDLGVk----------NVVAVDRKGILNEndpetcl 237 Thermotoga maritim...
1GQ2_A    258 IQGTASVAVAGLLAALRITKNRLSDHTVLFQGAGEAALGIANLIVXAXQkegvskeeaikRIWXVDSKGLIVKgrasltp 337 domestic pigeon
Feature 1                                       ##    #                    ###                
1LLQ_A    376 rhvq-----fakdmpettsILEVIraaRPGALIGAStvrGAFNEEVIRAMAeinERPIIFALSNPTSkaECTAEEAYTFT 450 pig roundworm
1QR6_A    360 syqep--fthsapesipdtFEDAVnilKPSTIIGVAgagRLFTPDVIRAXAsinERPVIFALSNPTAqaECTAEEAYTLT 437 human
1VL6_D    238 neyhleiaritnperlsgdLETALe--GADFFIGVSr-gNILKPEWIKKXS---RKPVIFALANPVP--EIDPELAREAG 309 Thermotoga maritim...
1GQ2_A    338 ekeh-----fahehcexknLEDIVkdiKPTVLIGVAaigGAFTQQILQDXAafnKRPIIFALSNPTSkaECTAEQLYKYT 412 domestic pigeon
Feature 1             #                  # #                                                  
1LLQ_A    451 NgaaLYASGSPFPNfelngh-tykpgqGNNAYIFPGVALGTILFQiRHVDNDLFLLAAKKVASCVTedslkvGRVYPQlk 529 pig roundworm
1QR6_A    438 EgrcLFASGSPFGPvkltdgrvftpgqGNNVYIFPGVALAVILCNtRHISDSVFLEAAKALTSQLTdeelaqGRLYPPla 517 human
1VL6_D    310 Af--IVATGRSDHPn-----------qVNNLLAFPGIXKGAVEKR-SKITKNXLLSAVEAIARSCEpe---pERIIPEaf 372 Thermotoga maritim...
1GQ2_A    413 EgrgIFASGSPFDPvtlpsgqtlypgqGNNSYVFPGVALGVISCGlKHIGDDVFLTTAEVIAQEVSeenlqeGRLYPPlv 492 domestic pigeon
Feature 1                      
1LLQ_A    530 eireISIQIAVEMAKYC 546 pig roundworm
1QR6_A    518 niqeVSINIAIKVTEYL 534 human
1VL6_D    373 d-xkVHLNVYTAVKGSA 388 Thermotoga maritima MSB8
1GQ2_A    493 tiqqVSLKIAVRIAKEA 509 domestic pigeon

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