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Conserved domains on  [gi|124442028|gb|ABN11661|]
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glutamate dehydrogenase, partial [Bacillus subtilis]

Protein Classification

Glu/Leu/Phe/Val dehydrogenase( domain architecture ID 11417382)

Glu/Leu/Phe/Val family dehydrogenase (DH) such as glutamate DH, leucine DH, or valine DH, which catalyzes the reversible, NAD-dependent deamination of glutamate, leucine, or valine, respectively

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
1-320 0e+00

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis


:

Pssm-ID: 440103 [Multi-domain]  Cd Length: 411  Bit Score: 522.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   1 TKGGIRFHPNVTEKEVKAvkaLSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAP 80
Cdd:COG0334   66 YKGGIRFHPSVNLDEVKA---LAFWMTFKNALTGLPFGGGKGGIDFDPKGLSDGELERLTRRFMTELYRHIGPDTDIPAP 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  81 DVFTNSQIMAWMMDEYSRIDEFNSPGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSY 160
Cdd:COG0334  143 DVGTGAREMAWMMDEYSRITGETVPGVVTGKPLELGGSLGRTEATGRGVVYFAREALKKLGLSLEGKTVAVQGFGNVGSY 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 161 LAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKLFN-DTITNQELLELDCDILVPAAIENQITEENAH 239
Cdd:COG0334  223 AAELLHELGAKVVAVSDSSGGIYDPDGIDLDALKEHKEERGSVAGYPGaEFITNEELLELDCDILIPAALENVITEENAK 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 240 NIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEM 319
Cdd:COG0334  303 RLKAKIVAEGANGPTTPEADEILAERGILVAPDILANAGGVTVSYFEWVQNLQRYSWTEEEVDERLEEIMVDAFDAVFET 382

                 .
gi 124442028 320 A 320
Cdd:COG0334  383 A 383
 
Name Accession Description Interval E-value
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
1-320 0e+00

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440103 [Multi-domain]  Cd Length: 411  Bit Score: 522.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   1 TKGGIRFHPNVTEKEVKAvkaLSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAP 80
Cdd:COG0334   66 YKGGIRFHPSVNLDEVKA---LAFWMTFKNALTGLPFGGGKGGIDFDPKGLSDGELERLTRRFMTELYRHIGPDTDIPAP 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  81 DVFTNSQIMAWMMDEYSRIDEFNSPGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSY 160
Cdd:COG0334  143 DVGTGAREMAWMMDEYSRITGETVPGVVTGKPLELGGSLGRTEATGRGVVYFAREALKKLGLSLEGKTVAVQGFGNVGSY 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 161 LAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKLFN-DTITNQELLELDCDILVPAAIENQITEENAH 239
Cdd:COG0334  223 AAELLHELGAKVVAVSDSSGGIYDPDGIDLDALKEHKEERGSVAGYPGaEFITNEELLELDCDILIPAALENVITEENAK 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 240 NIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEM 319
Cdd:COG0334  303 RLKAKIVAEGANGPTTPEADEILAERGILVAPDILANAGGVTVSYFEWVQNLQRYSWTEEEVDERLEEIMVDAFDAVFET 382

                 .
gi 124442028 320 A 320
Cdd:COG0334  383 A 383
GdhA_Arch NF040817
glutamate dehydrogenase;
1-320 2.15e-144

glutamate dehydrogenase;


Pssm-ID: 468757 [Multi-domain]  Cd Length: 419  Bit Score: 413.54  E-value: 2.15e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   1 TKGGIRFHPNVTekeVKAVKALSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAP 80
Cdd:NF040817  68 TKGGIRWHPEET---LSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYEDIPAP 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  81 DVFTNSQIMAWMMDEYSRIDEFNSP--GFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAG 158
Cdd:NF040817 145 DVYTNPQIMAWMMDEYETISRRKTPafGIITGKPLSIGGSLGREEATARGASYTIREAAKVLGIDLKGKTIAIQGYGNAG 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 159 SYLAKFM-HDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKLFNDT-ITNQELLELDCDILVPAAIENQITEE 236
Cdd:NF040817 225 YYLAKIMsEELGMKVVAVSDSKGGIYNPDGLNADEVLKWKKEHGSVKDFPGATnITNEELLELEVDVLAPAAIEEVITKK 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 237 NAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNI 316
Cdd:NF040817 305 NADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTLEEVREKLDKKMTKAFYDV 384

                 ....
gi 124442028 317 YEMA 320
Cdd:NF040817 385 YNTA 388
PLN02477 PLN02477
glutamate dehydrogenase
2-319 2.33e-124

glutamate dehydrogenase


Pssm-ID: 178095 [Multi-domain]  Cd Length: 410  Bit Score: 362.16  E-value: 2.33e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   2 KGGIRFHPNVTEKEVKAVKALSIWmslKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAPD 81
Cdd:PLN02477  66 KGGIRYHPEVDPDEVNALAQLMTW---KTAVANIPYGGAKGGIGCDPRDLSESELERLTRVFTQKIHDLIGIHTDVPAPD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  82 VFTNSQIMAWMMDEYSRIDEFnSPGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYL 161
Cdd:PLN02477 143 MGTNAQTMAWILDEYSKFHGF-SPAVVTGKPIDLGGSLGREAATGRGVVFATEALLAEHGKSIAGQTFVIQGFGNVGSWA 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 162 AKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVtKLFN--DTITNQELLELDCDILVPAAIENQITEENAH 239
Cdd:PLN02477 222 AQLIHEKGGKIVAVSDITGAVKNENGLDIPALRKHVAEGGGL-KGFPggDPIDPDDILVEPCDVLIPAALGGVINKENAA 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 240 NIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEM 319
Cdd:PLN02477 301 DVKAKFIVEAANHPTDPEADEILRKKGVVVLPDIYANSGGVTVSYFEWVQNIQGFMWEEEKVNRELDRYMTDAFKALKEM 380
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
116-321 4.32e-106

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.


Pssm-ID: 133445 [Multi-domain]  Cd Length: 227  Bit Score: 309.08  E-value: 4.32e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 116 GGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLD 195
Cdd:cd01076    1 GGSLGREEATGRGVAYATREALKKLGIGLAGARVAIQGFGNVGSHAARFLHEAGAKVVAVSDSDGTIYNPDGLDVPALLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 196 RRDSFGTVTKLFN-DTITNQELLELDCDILVPAAIENQITEENAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVL 274
Cdd:cd01076   81 YKKEHGSVLGFPGaERITNEELLELDCDILIPAALENQITADNADRIKAKIIVEAANGPTTPEADEILHERGVLVVPDIL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 124442028 275 ASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEMAN 321
Cdd:cd01076  161 ANAGGVTVSYFEWVQNLQGFYWDEEEVNSRLETKMREAFEAVLETAE 207
ELFV_dehydrog pfam00208
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;
116-320 4.79e-98

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;


Pssm-ID: 425526 [Multi-domain]  Cd Length: 240  Bit Score: 289.03  E-value: 4.79e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  116 GGSHGRESATAKGVTICIKEAAKKRGID-IKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLL 194
Cdd:pfam00208   1 GGSLGRPEATGYGVVYFVEEMLKKLGGDsLEGKRVAIQGFGNVGSYAALKLHELGAKVVAVSDSSGAIYDPDGLDIEELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  195 DRRDSFGTVTKLFN----DTITNQELLELDCDILVPAAIENQITEENAH-NIR--AKIVVEAANGPTTLEGTKILSDRDI 267
Cdd:pfam00208  81 ELKEERGSVDEYALsggaEYIPNEELWELPCDILVPCATQNEITEENAKtLIKngAKIVVEGANMPTTPEADDILEERGV 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124442028  268 LLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEMA 320
Cdd:pfam00208 161 LVVPDKAANAGGVTVSYLEMVQNLQRLSWTEEEVDEKLKEIMTNAFDAVVETA 213
ELFV_dehydrog smart00839
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glutamate, leucine, phenylalanine and ...
220-321 4.20e-33

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.


Pssm-ID: 214847 [Multi-domain]  Cd Length: 102  Bit Score: 117.70  E-value: 4.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   220 DCDILVPAAIENQITEENAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGfywSEE 299
Cdd:smart00839   2 NCDIFIPCALQNVINEANANRLGAKIIAEGANMPLTDEADDILEDRGVLYAPDFAANAGGVIVSALEMLQNLAR---TAE 78
                           90       100
                   ....*....|....*....|..
gi 124442028   300 EVEEKLEKMMVKSFNNIYEMAN 321
Cdd:smart00839  79 EVFTDLSEIMRNALEEIFETAQ 100
 
Name Accession Description Interval E-value
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
1-320 0e+00

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440103 [Multi-domain]  Cd Length: 411  Bit Score: 522.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   1 TKGGIRFHPNVTEKEVKAvkaLSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAP 80
Cdd:COG0334   66 YKGGIRFHPSVNLDEVKA---LAFWMTFKNALTGLPFGGGKGGIDFDPKGLSDGELERLTRRFMTELYRHIGPDTDIPAP 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  81 DVFTNSQIMAWMMDEYSRIDEFNSPGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSY 160
Cdd:COG0334  143 DVGTGAREMAWMMDEYSRITGETVPGVVTGKPLELGGSLGRTEATGRGVVYFAREALKKLGLSLEGKTVAVQGFGNVGSY 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 161 LAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKLFN-DTITNQELLELDCDILVPAAIENQITEENAH 239
Cdd:COG0334  223 AAELLHELGAKVVAVSDSSGGIYDPDGIDLDALKEHKEERGSVAGYPGaEFITNEELLELDCDILIPAALENVITEENAK 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 240 NIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEM 319
Cdd:COG0334  303 RLKAKIVAEGANGPTTPEADEILAERGILVAPDILANAGGVTVSYFEWVQNLQRYSWTEEEVDERLEEIMVDAFDAVFET 382

                 .
gi 124442028 320 A 320
Cdd:COG0334  383 A 383
GdhA_Arch NF040817
glutamate dehydrogenase;
1-320 2.15e-144

glutamate dehydrogenase;


Pssm-ID: 468757 [Multi-domain]  Cd Length: 419  Bit Score: 413.54  E-value: 2.15e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   1 TKGGIRFHPNVTekeVKAVKALSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAP 80
Cdd:NF040817  68 TKGGIRWHPEET---LSTVKALAAWMTWKTAVMDLPYGGGKGGIIVDPKKLSDREKERLARGYIRAIYDVISPYEDIPAP 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  81 DVFTNSQIMAWMMDEYSRIDEFNSP--GFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAG 158
Cdd:NF040817 145 DVYTNPQIMAWMMDEYETISRRKTPafGIITGKPLSIGGSLGREEATARGASYTIREAAKVLGIDLKGKTIAIQGYGNAG 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 159 SYLAKFM-HDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKLFNDT-ITNQELLELDCDILVPAAIENQITEE 236
Cdd:NF040817 225 YYLAKIMsEELGMKVVAVSDSKGGIYNPDGLNADEVLKWKKEHGSVKDFPGATnITNEELLELEVDVLAPAAIEEVITKK 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 237 NAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNI 316
Cdd:NF040817 305 NADNIKAKIVAEVANGPVTPEADEILFEKGILQIPDFLCNAGGVTVSYFEWVQNITGYYWTLEEVREKLDKKMTKAFYDV 384

                 ....
gi 124442028 317 YEMA 320
Cdd:NF040817 385 YNTA 388
PLN02477 PLN02477
glutamate dehydrogenase
2-319 2.33e-124

glutamate dehydrogenase


Pssm-ID: 178095 [Multi-domain]  Cd Length: 410  Bit Score: 362.16  E-value: 2.33e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   2 KGGIRFHPNVTEKEVKAVKALSIWmslKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAPD 81
Cdd:PLN02477  66 KGGIRYHPEVDPDEVNALAQLMTW---KTAVANIPYGGAKGGIGCDPRDLSESELERLTRVFTQKIHDLIGIHTDVPAPD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  82 VFTNSQIMAWMMDEYSRIDEFnSPGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYL 161
Cdd:PLN02477 143 MGTNAQTMAWILDEYSKFHGF-SPAVVTGKPIDLGGSLGREAATGRGVVFATEALLAEHGKSIAGQTFVIQGFGNVGSWA 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 162 AKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVtKLFN--DTITNQELLELDCDILVPAAIENQITEENAH 239
Cdd:PLN02477 222 AQLIHEKGGKIVAVSDITGAVKNENGLDIPALRKHVAEGGGL-KGFPggDPIDPDDILVEPCDVLIPAALGGVINKENAA 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 240 NIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEM 319
Cdd:PLN02477 301 DVKAKFIVEAANHPTDPEADEILRKKGVVVLPDIYANSGGVTVSYFEWVQNIQGFMWEEEKVNRELDRYMTDAFKALKEM 380
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
116-321 4.32e-106

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.


Pssm-ID: 133445 [Multi-domain]  Cd Length: 227  Bit Score: 309.08  E-value: 4.32e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 116 GGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLD 195
Cdd:cd01076    1 GGSLGREEATGRGVAYATREALKKLGIGLAGARVAIQGFGNVGSHAARFLHEAGAKVVAVSDSDGTIYNPDGLDVPALLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 196 RRDSFGTVTKLFN-DTITNQELLELDCDILVPAAIENQITEENAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVL 274
Cdd:cd01076   81 YKKEHGSVLGFPGaERITNEELLELDCDILIPAALENQITADNADRIKAKIIVEAANGPTTPEADEILHERGVLVVPDIL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 124442028 275 ASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEMAN 321
Cdd:cd01076  161 ANAGGVTVSYFEWVQNLQGFYWDEEEVNSRLETKMREAFEAVLETAE 207
ELFV_dehydrog pfam00208
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;
116-320 4.79e-98

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;


Pssm-ID: 425526 [Multi-domain]  Cd Length: 240  Bit Score: 289.03  E-value: 4.79e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  116 GGSHGRESATAKGVTICIKEAAKKRGID-IKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLL 194
Cdd:pfam00208   1 GGSLGRPEATGYGVVYFVEEMLKKLGGDsLEGKRVAIQGFGNVGSYAALKLHELGAKVVAVSDSSGAIYDPDGLDIEELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  195 DRRDSFGTVTKLFN----DTITNQELLELDCDILVPAAIENQITEENAH-NIR--AKIVVEAANGPTTLEGTKILSDRDI 267
Cdd:pfam00208  81 ELKEERGSVDEYALsggaEYIPNEELWELPCDILVPCATQNEITEENAKtLIKngAKIVVEGANMPTTPEADDILEERGV 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124442028  268 LLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEMA 320
Cdd:pfam00208 161 LVVPDKAANAGGVTVSYLEMVQNLQRLSWTEEEVDEKLKEIMTNAFDAVVETA 213
NAD_bind_Glu_Leu_Phe_Val cd05211
NAD(P) binding domain of glutamate dehydrogenase, leucine dehydrogenase, phenylalanine ...
124-322 5.14e-59

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.


Pssm-ID: 133450 [Multi-domain]  Cd Length: 217  Bit Score: 188.91  E-value: 5.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 124 ATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTV 203
Cdd:cd05211    1 ATGYGVVVAMKAAMKHLGDSLEGLTVAVQGLGNVGWGLAKKLAEEGGKVLAVSDPDGYIYDPGITTEELINYAVALGGSA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 204 TKLFNDTITNQELLELDCDILVPAAIENQITEENAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVS 283
Cdd:cd05211   81 RVKVQDYFPGEAILGLDVDIFAPCALGNVIDLENAKKLKAKVVAEGANNPTTDEALRILHERGIVVAPDIVANAGGVIVS 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 124442028 284 YFEWVQNNQGFYWSEEEVEEKLEKMMVKSFNNIYEMANN 322
Cdd:cd05211  161 YFEWVQNLQRLSWDAEEVRSKLEQVMTDIHNGVFAISER 199
ELFV_dehydrog_N pfam02812
Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
1-98 1.58e-54

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


Pssm-ID: 460706 [Multi-domain]  Cd Length: 129  Bit Score: 174.11  E-value: 1.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028    1 TKGGIRFHPNVTEKEVKAvkaLSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAP 80
Cdd:pfam02812  35 AKGGIRFHPYVNLDEVKA---LAFLMTYKNALAGLPFGGGKGGIIVDPKKLSDEELERLTRRFVRELARYIGPDTDVPAP 111
                          90
                  ....*....|....*...
gi 124442028   81 DVFTNSQIMAWMMDEYSR 98
Cdd:pfam02812 112 DVGTGAREMAWMADEYSK 129
PRK14030 PRK14030
glutamate dehydrogenase; Provisional
2-297 6.14e-52

glutamate dehydrogenase; Provisional


Pssm-ID: 184463 [Multi-domain]  Cd Length: 445  Bit Score: 177.33  E-value: 6.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   2 KGGIRFHPNVTekeVKAVKALSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAPD 81
Cdd:PRK14030  88 KGGIRFHPSVN---LSILKFLGFEQTFKNALTTLPMGGGKGGSDFSPRGKSDAEIMRFCQAFMLELWRHIGPDTDVPAGD 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  82 VFTNSQIMAWMMDEYSRID-EFNspGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSY 160
Cdd:PRK14030 165 IGVGGREVGYMFGMYKKLTrEFT--GTLTGKGLEFGGSLIRPEATGFGALYFVHQMLETKGIDIKGKTVAISGFGNVAWG 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 161 LAKFMHDAGAKVVGISDAYGGLYDPEGLD---IDYLLDRRDSFGTVTKLFNDTITNQELL------ELDCDILVPAAIEN 231
Cdd:PRK14030 243 AATKATELGAKVVTISGPDGYIYDPDGISgekIDYMLELRASGNDIVAPYAEKFPGSTFFagkkpwEQKVDIALPCATQN 322
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124442028 232 QITEENAHNIRA---KIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWS 297
Cdd:PRK14030 323 ELNGEDADKLIKngvLCVAEVSNMGCTAEAIDKFIAAKQLFAPGKAVNAGGVATSGLEMSQNAMHLSWS 391
PTZ00079 PTZ00079
NADP-specific glutamate dehydrogenase; Provisional
2-318 1.43e-51

NADP-specific glutamate dehydrogenase; Provisional


Pssm-ID: 185433 [Multi-domain]  Cd Length: 454  Bit Score: 176.46  E-value: 1.43e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   2 KGGIRFHPNVTekeVKAVKALSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAPD 81
Cdd:PTZ00079  97 KGGLRFHPSVN---LSILKFLGFEQIFKNSLTTLPMGGGKGGSDFDPKGKSDNEVMRFCQSFMTELYRHIGPDTDVPAGD 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  82 VFTNSQIMAWMMDEYSRI-DEFNspGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSY 160
Cdd:PTZ00079 174 IGVGGREIGYLFGQYKKLrNNFE--GTLTGKNVKWGGSNIRPEATGYGLVYFVLEVLKKLNDSLEGKTVVVSGSGNVAQY 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 161 LAKFMHDAGAKVVGISDAYGGLYDPEGLD---IDYLLD-RRDSFGTVTKLFNDTIT-----NQELLELDCDILVPAAIEN 231
Cdd:PTZ00079 252 AVEKLLQLGAKVLTMSDSDGYIHEPNGFTkekLAYLMDlKNVKRGRLKEYAKHSSTakyvpGKKPWEVPCDIAFPCATQN 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 232 QITEENA---HNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKM 308
Cdd:PTZ00079 332 EINLEDAkllIKNGCKLVAEGANMPTTIEATHLFKKNGVIFCPGKAANAGGVAISGLEMSQNAARLQWTAEEVDEKLREI 411
                        330
                 ....*....|
gi 124442028 309 MvksfNNIYE 318
Cdd:PTZ00079 412 M----KSIFE 417
PRK09414 PRK09414
NADP-specific glutamate dehydrogenase;
2-297 4.68e-51

NADP-specific glutamate dehydrogenase;


Pssm-ID: 181834 [Multi-domain]  Cd Length: 445  Bit Score: 174.93  E-value: 4.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   2 KGGIRFHPNVTEKevkAVKALSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAPD 81
Cdd:PRK09414  92 KGGLRFHPSVNLS---ILKFLGFEQIFKNALTGLPIGGGKGGSDFDPKGKSDAEIMRFCQSFMTELYRHIGPDTDVPAGD 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  82 VFTNSQIMAWMMDEYSRI-DEFNspGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSY 160
Cdd:PRK09414 169 IGVGGREIGYLFGQYKRLtNRFE--GVLTGKGLSFGGSLIRTEATGYGLVYFAEEMLKARGDSFEGKRVVVSGSGNVAIY 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 161 LAKFMHDAGAKVVGISDAYGGLYDPEGLDIDYLLD----RRDSFGTVTKLFNDT-ITNQELLELDCDILVPAAIENQITE 235
Cdd:PRK09414 247 AIEKAQQLGAKVVTCSDSSGYVYDEEGIDLEKLKEikevRRGRISEYAEEFGAEyLEGGSPWSVPCDIALPCATQNELDE 326
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124442028 236 ENAHNIRA---KIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWS 297
Cdd:PRK09414 327 EDAKTLIAngvKAVAEGANMPSTPEAIEVFLEAGVLFAPGKAANAGGVATSGLEMSQNASRLSWT 391
PRK14031 PRK14031
NADP-specific glutamate dehydrogenase;
2-318 6.19e-49

NADP-specific glutamate dehydrogenase;


Pssm-ID: 184464 [Multi-domain]  Cd Length: 444  Bit Score: 169.34  E-value: 6.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   2 KGGIRFHPNVTEKevkAVKALSIWMSLKCGIIDLPYGGGKGGIVCDPRDMSFRELERLSRGYVRAISQIVGPTKDVPAPD 81
Cdd:PRK14031  88 KGGIRFHASVNLG---ILKFLAFEQTFKNSLTTLPMGGGKGGSDFSPRGKSNAEVMRFCQAFMLELWRHIGPETDVPAGD 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  82 VFTNSQIMAWMMDEYSRIDEFNSpGFITGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYL 161
Cdd:PRK14031 165 IGVGGREVGFMFGMYKKLSHEFT-GTFTGKGREFGGSLIRPEATGYGNIYFLMEMLKTKGTDLKGKVCLVSGSGNVAQYT 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 162 AKFMHDAGAKVVGISDAYGGLYDPEGLD---IDYLLDRRDSFGTVTKLFNDT-----ITNQELLELDCDILVPAAIENQI 233
Cdd:PRK14031 244 AEKVLELGGKVVTMSDSDGYIYDPDGIDrekLDYIMELKNLYRGRIREYAEKygckyVEGARPWGEKGDIALPSATQNEL 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 234 TEENAHNIRAK---IVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWSEEEVEEKLEKMMv 310
Cdd:PRK14031 324 NGDDARQLVANgviAVSEGANMPSTPEAIKVFQDAKILYAPGKAANAGGVSVSGLEMTQNSIKLSWSSEEVDEKLKSIM- 402

                 ....*...
gi 124442028 311 ksfNNIYE 318
Cdd:PRK14031 403 ---KNIHE 407
NAD_bind_2_Glu_DH cd05313
NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; Amino acid dehydrogenase (DH) is ...
109-297 4.43e-35

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.


Pssm-ID: 133455 [Multi-domain]  Cd Length: 254  Bit Score: 127.73  E-value: 4.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 109 TGKPLVLGGSHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISDAYGGLYDPEGL 188
Cdd:cd05313    1 TGKGLSWGGSLIRPEATGYGLVYFVEEMLKDRNETLKGKRVAISGSGNVAQYAAEKLLELGAKVVTLSDSKGYVYDPDGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 189 ---DIDYLLDRRDSFGTVTKLFNDT------ITNQELLELDCDILVPAAIENQITEENAHNIRA---KIVVEAANGPTTL 256
Cdd:cd05313   81 tgeKLAELKEIKEVRRGRVSEYAKKygtakyFEGKKPWEVPCDIAFPCATQNEVDAEDAKLLVKngcKYVAEGANMPCTA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 124442028 257 EGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGFYWS 297
Cdd:cd05313  161 EAIEVFRQAGVLFAPGKAANAGGVAVSGLEMSQNSQRLSWT 201
ELFV_dehydrog smart00839
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glutamate, leucine, phenylalanine and ...
220-321 4.20e-33

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.


Pssm-ID: 214847 [Multi-domain]  Cd Length: 102  Bit Score: 117.70  E-value: 4.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   220 DCDILVPAAIENQITEENAHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFEWVQNNQGfywSEE 299
Cdd:smart00839   2 NCDIFIPCALQNVINEANANRLGAKIIAEGANMPLTDEADDILEDRGVLYAPDFAANAGGVIVSALEMLQNLAR---TAE 78
                           90       100
                   ....*....|....*....|..
gi 124442028   300 EVEEKLEKMMVKSFNNIYEMAN 321
Cdd:smart00839  79 EVFTDLSEIMRNALEEIFETAQ 100
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
125-280 3.88e-22

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.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 91.89  E-value: 3.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 125 TAKGVTICIKEAAKKR--GIDIKGARVVVQGFGNAGSYLAKFMHDAGAKVVGIsdaygglydpeglDIDylLDRRDSfgt 202
Cdd:cd01075    5 TAYGVFLGMKAAAEHLlgTDSLEGKTVAVQGLGKVGYKLAEHLLEEGAKLIVA-------------DIN--EEAVAR--- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 203 VTKLFNDTI-TNQELLELDCDILVPAAIENQITEENAHNIRAKIVVEAANGPTTLEG-TKILSDRDILLVPDVLASAGGV 280
Cdd:cd01075   67 AAELFGATVvAPEEIYSVDADVFAPCALGGVINDDTIPQLKAKAIAGAANNQLADPRhGQMLHERGILYAPDYVVNAGGL 146
PTZ00324 PTZ00324
glutamate dehydrogenase 2; Provisional
34-286 5.39e-10

glutamate dehydrogenase 2; Provisional


Pssm-ID: 240359 [Multi-domain]  Cd Length: 1002  Bit Score: 60.58  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028   34 DLPYGGGKGGIVCDPRDMS-FREL--ERLSRGYVRAISQIVGPTKDVP-----------APDVFTNSQIMAWMMdeySRI 99
Cdd:PTZ00324  536 DIPEGGSKGTILLSSRYLNkFAQVrcQHAFLQYIDALLDVMLPGEKVVdhlkqeeiiflGPDEHTTGTLMDWAA---LHA 612
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  100 DEFNSP---GFITGKPLVLGG-SHGRESATAKGVTICIKEAAKKRGIDIKGARVVVQGF--GNAGSYLAKFMHDagaKVV 173
Cdd:PTZ00324  613 KKRGYPfwkSFTTGKSPSMGGiPHDTYGMTTRSVRAYVTGILEKLGLNEEEVTKFQTGGpdGDLGSNELLLSKE---KTV 689
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028  174 GISDAYGGLYDPEGLDIDYlLDRRDSFGTVTKLFNDTITNQE---LLELDCDILVP--AAIEN----------------- 231
Cdd:PTZ00324  690 GIVDGSGVLHDPEGLNREE-LRRLAHHRLPAREFDESKLSPQgflVLTDDRDVKLPdgTIVESglrfrnefhllpysdad 768
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124442028  232 ----------QITEEN--------AHNIRAKIVVEAANGPTTLEGTKILSDRDILLVPDVLASAGGVTVSYFE 286
Cdd:PTZ00324  769 vfvpcggrprSVTLFNvgrffdekNGKLRFKIIVEGANLFITQDARLALEECGVILFKDASANKGGVTSSSLE 841
NAD_bind_amino_acid_DH cd05191
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ...
124-177 3.25e-07

NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (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.


Pssm-ID: 133449 [Multi-domain]  Cd Length: 86  Bit Score: 47.37  E-value: 3.25e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124442028 124 ATAKGVTICIKEAAKKRGIDIKGARVVVQGFGNAGSYLAKFMHDAGAKVVGISD 177
Cdd:cd05191    1 ATAAGAVALLKAAGKVTNKSLKGKTVVVLGAGEVGKGIAKLLADEGGKKVVLCD 54
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
148-256 1.10e-05

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 46.40  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 148 RVVVQGFGNAGSYLAKFMH----------DAGAKVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKL--FNDTITNQE 215
Cdd:PRK06270   4 KIALIGFGGVGQGVAELLAekreylkkryGLDLKVVAIADSSGSAIDPDGLDLELALKVKEETGKLADYpeGGGEISGLE 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 124442028 216 LL-ELDCDILVPAAIENQITEENA-HNIRA-----KIVVEAANGPTTL 256
Cdd:PRK06270  84 VIrSVDADVVVEATPTNIETGEPAlSHCRKalergKHVVTSNKGPLAL 131
PRK08374 PRK08374
homoserine dehydrogenase; Provisional
148-225 2.77e-04

homoserine dehydrogenase; Provisional


Pssm-ID: 169409 [Multi-domain]  Cd Length: 336  Bit Score: 42.10  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124442028 148 RVVVQGFGNAGSYLAK--------FMHDAGA--KVVGISDAYGGLYDPEGLDIDYLLDRRDSFGTVTKLFND----TITN 213
Cdd:PRK08374   4 KVSIFGFGNVGRAVAEvlaeksrvFKERYGVelKVVSITDTSGTIWLPEDIDLREAKEVKENFGKLSNWGNDyevyNFSP 83
                         90
                 ....*....|...
gi 124442028 214 QELL-ELDCDILV 225
Cdd:PRK08374  84 EEIVeEIDADIVV 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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