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: 2-Oct-2020
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:
Feature 1                                         # ###                  ##    #                
1LEH_B      146 PSPVTAYGVYRGMKAAAKEafGSDSLEGLAVSVQGLGNVAKALCKKLNTEGAKLVVTDVNk-aAVSAAVAEe--GADAVA 222 Bacillus sphaericus
1BW9_A      150 SAFTTAVGVFEAMKATVAHr-GLGSLDGLTVLVQGLGAVGGSLASLAAEAGAQLLVADTDt-eRVAHAVAL---GHTAVA 224 Rhodococcus sp.
1C1X_B      149 SAFTTAVGVFEAMKATVAHr-GLGSLDGLTVLVQGLGAVGGSLASLAAEAGAQLLVADTDt-eRVAHAVAL---GHTAVA 223 Rhodococcus sp.
NP_293882   153 TSSVTGYGVYRGMKAAAKHalGAESLRGVRVAILGVGAVGRTLAQHLSREGAKLTVADFRp-dRAQALAEEl--GHVTVV 229 Deinococcus radi...
YP_300003   160 PSPWTAYGVFVGIQAAAQYrlDRKSLTGLSVAVQGLGSVGWELCRRLHEAGAILTVADIDa-gRTTRAQQQf--GARVVS 236 Ralstonia eutrop...
NP_300976   147 PSIYTAHGGFLCIKETAKYlwGSSSLRGKKIAIQGIGSVGRRLLQSLFFEGAELYVADVLe-rAVQDAARLy--GATIVP 223 Chlamydophila pn...
ZP_01308374 138 PSPTTAKGIVLGLAEAVEQa-FNQSVQGLTVAIQGLGHVGMVLAESLHQQGAKIIVCDVDe-qKVDYAVKHf--DAKAVS 213 Oceanobacter sp....
ZP_01131384 161 PADATAAGVHASILATCEAlfGTREVAGRHLVISGLGQVGGRLARSLTAAGAVLTVTDVNl-dRKLLAAEL---DANWVD 236 marine actinobac...
YP_703129   146 TGKPTAYGTYLALQEAIRFqeGTGTLTGKTVAVMGLGAVGWSMAEYLLDGGARLIVSDIDqtrAADFLAAHpgrPVESVP 225 Rhodococcus sp. ...
YP_760323   144 PSPYTARGVRLAMEAVALHvlGARSLEGVRVAVQGLGGVGANLCRELSERGAKLIVADINq-qRVERICDEf--RAERAE 220 Hyphomonas neptu...
Feature 1                      ##                    # #                                        
1LEH_B      223 p-NAIYGVTCDIFAPCALGAVLNDFTIPQLKAKVIAGSADNQLKd------PRHGKYLHELGIVYAPDYVINAGGVINVA 295 Bacillus sphaericus
1BW9_A      225 l-EDVLSTPCDVFAPCAMGGVITTEVARTLDCSVVAGAANNVIAd------EAASDILHARGILYAPDFVANAGGAIHLV 297 Rhodococcus sp.
1C1X_B      224 l-EDVLSTPCDVFAPCAMGGVITTEVARTLDCSVVAGAANNVIAd------EAASDILHARGILYAPDFVANAGGAIHLV 296 Rhodococcus sp.
NP_293882   230 pvGEIFDVPCDVFAPCGFGHSVQSADVPRLQCRLIAGGEHHPLT-------RRGEEAVKEAGIMYVPDFAINSAGLIAAA 302 Deinococcus radi...
YP_300003   237 p-EAITAVDADIFAPCALGAVITAAVAENCRFQIIAGGANNQLAs------LAEGDTLHQRGVFYAPDFLINAGGIVSCA 309 Ralstonia eutrop...
NP_300976   224 t-EEIHALECDIFSPCARGNVIRKDNLADLNCKAIVGVANNQLEd------SSAGMMLHERGILYGPDYLVNAGGLLNVA 296 Chlamydophila pn...
ZP_01308374 214 v-NEIYSQQCDVFSPCGLGLSINDNTIKQLKCKVIAGCANNQLAh------DGLGQQLHDLGILYTPDYVINSGGLIYAS 286 Oceanobacter sp....
ZP_01131384 237 a-DEAHSVVADIYVPCGMGGALSPRVIRELNVSGVVGAANNQLAq------HDGAEALTERGILWAPDFVVNGGGVIYLD 309 marine actinobac...
YP_703129   226 v-GAIIDVDADVFCPCAIGGILDEDTIRRITFRYVFGPANNQLKattqdeeIRLANLLAERGILFQTEWWHNTAGVLCGA 304 Rhodococcus sp. ...
YP_760323   221 a-ETILFSEVDILAPCALGGVMTEASVPKVRARAVVGGANNQLLn------AAAGQMLFDRQITYAPDYLVNAGGIIMVA 293 Hyphomonas neptu...
Feature 1                                                             
1LEH_B      296 DELYgyn---rtrAMKRVDGIYDSIEKIFAISKr-dGVPSYVAADRMAEERIAK 345 Bacillus sphaericus
1BW9_A      298 GREVlgws--esvVHERAVAIGDTLNQVFEISDn-dGVTPDEAARTLAGRRARE 348 Rhodococcus sp.
1C1X_B      297 GREVlgws--esvVHERAVAIGDTLNQVFEISDn-dGVTPDEAARTLAGRRARE 347 Rhodococcus sp.
NP_293882   303 TGVN---------MDQAGERVYQTVSRIMSVATq-yGKPPHVVARKMAERRIDL 346 Deinococcus radiodurans R1
YP_300003   310 REYLggvd--dsaLRDEVAGIRDRVLGLAQRVEs-tRQAPARAAVTWAHEVLSR 360 Ralstonia eutropha JMP134
NP_300976   297 AAIEgrvy-apkeVLLKVEELPIVLSKLYNQSKt-tGKDLVALSDSFVEDKLLA 348 Chlamydophila pneumoniae J138
ZP_01308374 287 SNFRgls---ldkIDHQVLKLKDTLNKIFILSKq-kNIPTQVIADEMAEHVLYG 336 Oceanobacter sp. RED65
ZP_01131384 310 MAGEpdad--advINARVAAIGDTVATIFRDAAa-qGITTLDAAERLAQSRLVV 360 marine actinobacterium PHSC20C1
YP_703129   305 EEYLrgadanttdLMAKVERIVPAKTWANLTQAkalGITPTENAYRTCVDTIYQ 358 Rhodococcus sp. RHA1
YP_760323   294 AEYFgths--qagVLADVERIFDRTCQVLLSSRk-tGAPPHLIADHMAAKVIET 344 Hyphomonas neptunium ATCC 15444

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