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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 140 PAPHAAMGVFAGIRSTAMARLGSDNLEGLRVAIQGLGNVGYALAEQLHAAGAELLVSDIDHGKVQLAMEQLGAHPIANDA 219
Cdd:cd01075     1 PSPPTAYGVFLGMKAAAEHLLGTDSLEGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAELFGATVVAPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 220 LLSTPCDILAPCGLGGVLNSNSVSQLRCSAVAGSANNQLIHLEIADQLERRGILYAPDYVINAGGLIYVSLKHRGEELTT 299
Cdd:cd01075    81 IYSVDADVFAPCALGGVINDDTIPQLKAKAIAGAANNQLADPRHGQMLHERGILYAPDYVVNAGGLINVADELYGGNEAR 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2774295102 300 ITAHLSKISSRLTEVFAHAQAEKRSPARVADELAEKVLY 338
Cdd:cd01075   161 VLAKVEAIYDTLLEIFAQAKQDGITTLEAADRMAEERIA 199

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 140 PAPHAAMGVFAGIRSTAMARLGSDNLEGLRVAIQGLGNVGYALAEQLHAAGAELLVSDIDHGKVQLAMEQLGAHPIANDA 219
Cdd:cd01075     1 PSPPTAYGVFLGMKAAAEHLLGTDSLEGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAELFGATVVAPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 220 LLSTPCDILAPCGLGGVLNSNSVSQLRCSAVAGSANNQLIHLEIADQLERRGILYAPDYVINAGGLIYVSLKHRGEELTT 299
Cdd:cd01075    81 IYSVDADVFAPCALGGVINDDTIPQLKAKAIAGAANNQLADPRHGQMLHERGILYAPDYVVNAGGLINVADELYGGNEAR 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2774295102 300 ITAHLSKISSRLTEVFAHAQAEKRSPARVADELAEKVLY 338
Cdd:cd01075   161 VLAKVEAIYDTLLEIFAQAKQDGITTLEAADRMAEERIA 199

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glutamate, leucine, phenylalanine and valine dehydrogenases are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102  225 CDILAPCGLGGVLNSNSVSQLRCSAVAGSANNQLiHLEIADQLERRGILYAPDYVINAGGLIYVSLKHRG----EELTTI 300
Cdd:smart00839   3 CDIFIPCALQNVINEANANRLGAKIIAEGANMPL-TDEADDILEDRGVLYAPDFAANAGGVIVSALEMLQnlarTAEEVF 81

                           90       100
                   ....*....|....*....|.
gi 2774295102  301 TAHLSKISSRLTEVFAHAQAE 321
Cdd:smart00839  82 TDLSEIMRNALEEIFETAQKY 102

Glu/Leu/Phe/Val dehydrogenase, dimerization domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102  23 LKAVIAIHNSRLGPALGGCRYLAYPSdesaIEDAVRLAQGMSYKAALAGLAQGGGVAVIVRPAHVENRAALFEAFGRCIN 102
Cdd:pfam02812  21 FRGYRVQHNTALGPAKGGIRFHPYVN----LDEVKALAFLMTYKNALAGLPFGGGKGGIIVDPKKLSDEELERLTRRFVR 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2774295102 103 ELdGRYI------TAIDAGTSVADMDCIAQQTQ 129
Cdd:pfam02812  97 EL-ARYIgpdtdvPAPDVGTGAREMAWMADEYS 128

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 140 PAPHAAMGVFAGIRSTAMARLGSDNLEGLRVAIQGLGNVGYALAEQLHAAGAELLVSDIDHGKVQLAMEQLGAHPIANDA 219
Cdd:cd01075     1 PSPPTAYGVFLGMKAAAEHLLGTDSLEGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAELFGATVVAPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 220 LLSTPCDILAPCGLGGVLNSNSVSQLRCSAVAGSANNQLIHLEIADQLERRGILYAPDYVINAGGLIYVSLKHRGEELTT 299
Cdd:cd01075    81 IYSVDADVFAPCALGGVINDDTIPQLKAKAIAGAANNQLADPRHGQMLHERGILYAPDYVVNAGGLINVADELYGGNEAR 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2774295102 300 ITAHLSKISSRLTEVFAHAQAEKRSPARVADELAEKVLY 338
Cdd:cd01075   161 VLAKVEAIYDTLLEIFAQAKQDGITTLEAADRMAEERIA 199

NAD(P) binding domain of glutamate dehydrogenase, 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 NAD(P)+. This subfamily includes glutamate, leucine, phenylalanine, and valine DHs. Glutamate DH is a multi-domain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. As in other NAD+-dependent DHs, monomers in this family have 2 domains separated by a deep cleft. Here the c-terminal domain contains a modified NAD-binding Rossmann fold with 7 rather than the usual 6 beta strands and one strand anti-parrallel to the others. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 145 AMGVFAGIRStAMARLGsDNLEGLRVAIQGLGNVGYALAEQLHAAGAE-LLVSDIDHG----------KVQLAMEQLGA- 212
Cdd:cd05211     3 GYGVVVAMKA-AMKHLG-DSLEGLTVAVQGLGNVGWGLAKKLAEEGGKvLAVSDPDGYiydpgitteeLINYAVALGGSa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 213 -----HPIANDALLSTPCDILAPCGLGGVLNSNSVSQLRCSAVAGSANNQLIHlEIADQLERRGILYAPDYVINAGGLIY 287
Cdd:cd05211    81 rvkvqDYFPGEAILGLDVDIFAPCALGNVIDLENAKKLKAKVVAEGANNPTTD-EALRILHERGIVVAPDIVANAGGVIV 159

                  .
gi 2774295102 288 V 288
Cdd:cd05211   160 S 160

NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; 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+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 147 GVFAGIRStAMARLGsDNLEGLRVAIQGLGNVGYALAEQLHAAGAELL-VSD----------IDHGKVQLAMEQLG---- 211
Cdd:cd01076    13 GVAYATRE-ALKKLG-IGLAGARVAIQGFGNVGSHAARFLHEAGAKVVaVSDsdgtiynpdgLDVPALLAYKKEHGsvlg 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 212 ---AHPIANDALLSTPCDILAPCGLGGVLNSNSVSQLRCSAVAGSANNQLihLEIADQ-LERRGILYAPDYVINAGGLIy 287
Cdd:cd01076    91 fpgAERITNEELLELDCDILIPAALENQITADNADRIKAKIIVEAANGPT--TPEADEiLHERGVLVVPDILANAGGVT- 167

                  ..
gi 2774295102 288 VS 289
Cdd:cd01076   168 VS 169

Glu/Leu/Phe/Val dehydrogenase, dimerization domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102  23 LKAVIAIHNSRLGPALGGCRYLAYPSdesaIEDAVRLAQGMSYKAALAGLAQGGGVAVIVRPAHVENRAALFEAFGRCIN 102
Cdd:pfam02812  21 FRGYRVQHNTALGPAKGGIRFHPYVN----LDEVKALAFLMTYKNALAGLPFGGGKGGIIVDPKKLSDEELERLTRRFVR 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2774295102 103 ELdGRYI------TAIDAGTSVADMDCIAQQTQ 129
Cdd:pfam02812  97 EL-ARYIgpdtdvPAPDVGTGAREMAWMADEYS 128

NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; 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+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia asimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 163 DNLEGLRVAIQGLGNVGYALAEQLHAAGAELL-VSD----------IDHGKVQL---------------AMEQLGAHPIA 216
Cdd:cd05313    34 ETLKGKRVAISGSGNVAQYAAEKLLELGAKVVtLSDskgyvydpdgFTGEKLAElkeikevrrgrvseyAKKYGTAKYFE 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2774295102 217 NDALLSTPCDILAPCGLGGVLNSNSVSQLR---CSAVAGSAN----NQLIHLeiadqLERRGILYAPDYVINAGG 284
Cdd:cd05313   114 GKKPWEVPCDIAFPCATQNEVDAEDAKLLVkngCKYVAEGANmpctAEAIEV-----FRQAGVLFAPGKAANAGG 183

NADP-specific glutamate dehydrogenase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2774295102 155 TAMARLGSDNLEGLRVAIQGLGNVGYALAEQLHAAGAELL-VSDID------------------------HGKVQLAMEQ 209
Cdd:PRK14031  216 MEMLKTKGTDLKGKVCLVSGSGNVAQYTAEKVLELGGKVVtMSDSDgyiydpdgidrekldyimelknlyRGRIREYAEK 295

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2774295102 210 LGAHPIANDALLSTPCDILAPCGLGGVLNSNSVSQL---RCSAVAGSANNQLIHlEIADQLERRGILYAPDYVINAGGL 285
Cdd:PRK14031  296 YGCKYVEGARPWGEKGDIALPSATQNELNGDDARQLvanGVIAVSEGANMPSTP-EAIKVFQDAKILYAPGKAANAGGV 373

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2774295102 155 TAMARLGSDN---LEGLRVAIQGLGNVGYALAEQLHAAGAELLVSD 197
Cdd:cd12158   100 SALLVLAQRQgfsLKGKTVGIVGVGNVGSRLARRLEALGMNVLLCD 145

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2774295102 169 RVAIQGLGNVGYALAEQLHAAGAELLVSDIDHGKVQLAMEqLGAH 213
Cdd:COG1064   165 RVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARE-LGAD 208