1LEH,1BW9,1C1X


Conserved Protein Domain Family
NAD_bind_Leu_Phe_Val_DH

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cd01075: NAD_bind_Leu_Phe_Val_DH 
Click on image for an interactive view with Cn3D
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase
Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. 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: 133444
View PSSM: cd01075
Aligned: 27 rows
Threshold Bit Score: 175.473
Threshold Setting Gi: 46578791
Created: 30-Apr-2009
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
NAD bindingPhe binding
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:NAD binding site [chemical binding site]
Evidence:
  • Structure:1BW9_A: Rhodococcus Phe DH binds NAD, contacts determined at 3.5A
    View structure with Cn3D
  • Structure:1CIX_B: Rhodococcus Phe DH binds NAD, contacts determined at 3.5A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                          # ###                  ##    #                
1LEH_B       146 PSPVTAYGVYRGMKAAAKEafGSDSLEGLAVSVQGLGNVAKALCKKLNTEGAKLVVTDVNk-aAVSAAVAEe--GADAVA 222
1BW9_A       150 SAFTTAVGVFEAMKATVAHr-GLGSLDGLTVLVQGLGAVGGSLASLAAEAGAQLLVADTDt-eRVAHAVAL---GHTAVA 224
1C1X_B       149 SAFTTAVGVFEAMKATVAHr-GLGSLDGLTVLVQGLGAVGGSLASLAAEAGAQLLVADTDt-eRVAHAVAL---GHTAVA 223
gi 15805195  153 TSSVTGYGVYRGMKAAAKHalGAESLRGVRVAILGVGAVGRTLAQHLSREGAKLTVADFRp-dRAQALAEEl--GHVTVV 229
gi 73539636  160 PSPWTAYGVFVGIQAAAQYrlDRKSLTGLSVAVQGLGSVGWELCRRLHEAGAILTVADIDa-gRTTRAQQQf--GARVVS 236
gi 15836452  147 PSIYTAHGGFLCIKETAKYlwGSSSLRGKKIAIQGIGSVGRRLLQSLFFEGAELYVADVLe-rAVQDAARLy--GATIVP 223
gi 94501863  138 PSPTTAKGIVLGLAEAVEQa-FNQSVQGLTVAIQGLGHVGMVLAESLHQQGAKIIVCDVDe-qKVDYAVKHf--DAKAVS 213
gi 88856729  161 PADATAAGVHASILATCEAlfGTREVAGRHLVISGLGQVGGRLARSLTAAGAVLTVTDVNl-dRKLLAAEL---DANWVD 236
gi 111020157 146 TGKPTAYGTYLALQEAIRFqeGTGTLTGKTVAVMGLGAVGWSMAEYLLDGGARLIVSDIDqtrAADFLAAHpgrPVESVP 225
gi 114799095 144 PSPYTARGVRLAMEAVALHvlGARSLEGVRVAVQGLGGVGANLCRELSERGAKLIVADINq-qRVERICDEf--RAERAE 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                       ##                    # #                                        
1LEH_B       223 p-NAIYGVTCDIFAPCALGAVLNDFTIPQLKAKVIAGSADNQLKd------PRHGKYLHELGIVYAPDYVINAGGVINVA 295
1BW9_A       225 l-EDVLSTPCDVFAPCAMGGVITTEVARTLDCSVVAGAANNVIAd------EAASDILHARGILYAPDFVANAGGAIHLV 297
1C1X_B       224 l-EDVLSTPCDVFAPCAMGGVITTEVARTLDCSVVAGAANNVIAd------EAASDILHARGILYAPDFVANAGGAIHLV 296
gi 15805195  230 pvGEIFDVPCDVFAPCGFGHSVQSADVPRLQCRLIAGGEHHPLT-------RRGEEAVKEAGIMYVPDFAINSAGLIAAA 302
gi 73539636  237 p-EAITAVDADIFAPCALGAVITAAVAENCRFQIIAGGANNQLAs------LAEGDTLHQRGVFYAPDFLINAGGIVSCA 309
gi 15836452  224 t-EEIHALECDIFSPCARGNVIRKDNLADLNCKAIVGVANNQLEd------SSAGMMLHERGILYGPDYLVNAGGLLNVA 296
gi 94501863  214 v-NEIYSQQCDVFSPCGLGLSINDNTIKQLKCKVIAGCANNQLAh------DGLGQQLHDLGILYTPDYVINSGGLIYAS 286
gi 88856729  237 a-DEAHSVVADIYVPCGMGGALSPRVIRELNVSGVVGAANNQLAq------HDGAEALTERGILWAPDFVVNGGGVIYLD 309
gi 111020157 226 v-GAIIDVDADVFCPCAIGGILDEDTIRRITFRYVFGPANNQLKattqdeeIRLANLLAERGILFQTEWWHNTAGVLCGA 304
gi 114799095 221 a-ETILFSEVDILAPCALGGVMTEASVPKVRARAVVGGANNQLLn------AAAGQMLFDRQITYAPDYLVNAGGIIMVA 293
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
Feature 1                                                              
1LEH_B       296 DELYgyn---rtrAMKRVDGIYDSIEKIFAISKr-dGVPSYVAADRMAEERIAK 345
1BW9_A       298 GREVlgws--esvVHERAVAIGDTLNQVFEISDn-dGVTPDEAARTLAGRRARE 348
1C1X_B       297 GREVlgws--esvVHERAVAIGDTLNQVFEISDn-dGVTPDEAARTLAGRRARE 347
gi 15805195  303 TGVN---------MDQAGERVYQTVSRIMSVATq-yGKPPHVVARKMAERRIDL 346
gi 73539636  310 REYLggvd--dsaLRDEVAGIRDRVLGLAQRVEs-tRQAPARAAVTWAHEVLSR 360
gi 15836452  297 AAIEgrvy-apkeVLLKVEELPIVLSKLYNQSKt-tGKDLVALSDSFVEDKLLA 348
gi 94501863  287 SNFRgls---ldkIDHQVLKLKDTLNKIFILSKq-kNIPTQVIADEMAEHVLYG 336
gi 88856729  310 MAGEpdad--advINARVAAIGDTVATIFRDAAa-qGITTLDAAERLAQSRLVV 360
gi 111020157 305 EEYLrgadanttdLMAKVERIVPAKTWANLTQAkalGITPTENAYRTCVDTIYQ 358
gi 114799095 294 AEYFgths--qagVLADVERIFDRTCQVLLSSRk-tGAPPHLIADHMAAKVIET 344

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