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Conserved domains on  [gi|31377775|ref|NP_036216|]
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glutamate dehydrogenase 2, mitochondrial precursor [Homo sapiens]

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];
104-555 9.42e-135

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism];


:

Pssm-ID: 223411  Cd Length: 411  Bit Score: 402.00  E-value: 9.42e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 104 GILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAK 183
Cdd:COG0334  23 GVLERLKEPERVIQVRIPVRMDDGSVKVFRGYRVQHNSALGPYKGGVRFHPYVTLEEVKALSFWMTLKNALAGLPYGGGK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 184 AGVKINPKNYTENELEKITRRFTMELAKkgFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHydiNAHACVTGKPISQG 263
Cdd:COG0334 103 GGIIVDPKGLSDGELERLSRAFGRAIYR--LIGPDTDIPAPDVGTNPQDMAWMMDEYSKIVGN---SAPGVFTGKPLELG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 264 GIHGRISATGRGVFHGIEnfinEASYMsiLGMtpGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGI 343
Cdd:COG0334 178 GSLGRSEATGYGVFYAIR----EALKA--LGD--DLEGARVAVQGFGNVGQYAAEKLHELGAKVVAVSDSKGGIYDEDGL 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 344 DPKELEDFKLQHGSILGFPKAKPYEG-SILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNI 422
Cdd:COG0334 250 DVEALLELKERRGSVAEYAGAEYITNeELLEVDCDILIPCALENVITEDNADQLKAKIVVEGANGPTTPEADEILLERGI 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 423 LVIPDLYLNAGGVTVSYFEWLKNLNhvsygRLTFKYERdsnyhlllsVQESLERKfgkhggtipivptaefqdsisgase 502
Cdd:COG0334 330 LVVPDILANAGGVIVSYLEWVQNAQ-----GLYWTEEE---------VDEKLERI------------------------- 370
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 31377775 503 kdivhsalaytMERSARQIMHTAMKYnlGLDLRTAAYVNAIEKVFKVYSEAGV 555
Cdd:COG0334 371 -----------MVNAFEAVYQAAKEY--GVDLRTAAYILAFERVADAMKARGW 410
 
Name Accession Description Interval E-value
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism];
104-555 9.42e-135

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 223411  Cd Length: 411  Bit Score: 402.00  E-value: 9.42e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 104 GILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAK 183
Cdd:COG0334  23 GVLERLKEPERVIQVRIPVRMDDGSVKVFRGYRVQHNSALGPYKGGVRFHPYVTLEEVKALSFWMTLKNALAGLPYGGGK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 184 AGVKINPKNYTENELEKITRRFTMELAKkgFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHydiNAHACVTGKPISQG 263
Cdd:COG0334 103 GGIIVDPKGLSDGELERLSRAFGRAIYR--LIGPDTDIPAPDVGTNPQDMAWMMDEYSKIVGN---SAPGVFTGKPLELG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 264 GIHGRISATGRGVFHGIEnfinEASYMsiLGMtpGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGI 343
Cdd:COG0334 178 GSLGRSEATGYGVFYAIR----EALKA--LGD--DLEGARVAVQGFGNVGQYAAEKLHELGAKVVAVSDSKGGIYDEDGL 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 344 DPKELEDFKLQHGSILGFPKAKPYEG-SILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNI 422
Cdd:COG0334 250 DVEALLELKERRGSVAEYAGAEYITNeELLEVDCDILIPCALENVITEDNADQLKAKIVVEGANGPTTPEADEILLERGI 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 423 LVIPDLYLNAGGVTVSYFEWLKNLNhvsygRLTFKYERdsnyhlllsVQESLERKfgkhggtipivptaefqdsisgase 502
Cdd:COG0334 330 LVVPDILANAGGVIVSYLEWVQNAQ-----GLYWTEEE---------VDEKLERI------------------------- 370
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 31377775 503 kdivhsalaytMERSARQIMHTAMKYnlGLDLRTAAYVNAIEKVFKVYSEAGV 555
Cdd:COG0334 371 -----------MVNAFEAVYQAAKEY--GVDLRTAAYILAFERVADAMKARGW 410
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
263-548 7.75e-115

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  Cd Length: 227  Bit Score: 343.75  E-value: 7.75e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 263 GGIHGRISATGRGVFHGIENFINEASymsilgmtPGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDG 342
Cdd:cd01076   1 GGSLGREEATGRGVAYATREALKKLG--------IGLAGARVAIQGFGNVGSHAARFLHEAGAKVVAVSDSDGTIYNPDG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 343 IDPKELEDFKLQHGSILGFPKAKPYE-GSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERN 421
Cdd:cd01076  73 LDVPALLAYKKEHGSVLGFPGAERITnEELLELDCDILIPAALENQITADNADRIKAKIIVEAANGPTTPEADEILHERG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 422 ILVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRltfkyerdsnyhlllsvqeslerkfgkhggtipivptaefqdsisgas 501
Cdd:cd01076 153 VLVVPDILANAGGVTVSYFEWVQNLQGFYWDE------------------------------------------------ 184
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 31377775 502 ekDIVHSALAYTMERSARQIMHTAMKYnlGLDLRTAAYVNAIEKVFK 548
Cdd:cd01076 185 --EEVNSRLETKMREAFEAVLETAEKY--GVDLRTAAYVLALERVAE 227
PLN02477 PLN02477
glutamate dehydrogenase
122-446 1.66e-114

glutamate dehydrogenase


Pssm-ID: 178095  Cd Length: 410  Bit Score: 349.83  E-value: 1.66e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  122 IRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTENELEKI 201
Cdd:PLN02477  41 IPKDDGTLASFVGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVANIPYGGAKGGIGCDPRDLSESELERL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  202 TRRFTMELakKGFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHydinAHACVTGKPISQGGIHGRISATGRGVFHGIE 281
Cdd:PLN02477 121 TRVFTQKI--HDLIGIHTDVPAPDMGTNAQTMAWILDEYSKFHGF----SPAVVTGKPIDLGGSLGREAATGRGVVFATE 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  282 NFINEasYMSILgmtpgfRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGF 361
Cdd:PLN02477 195 ALLAE--HGKSI------AGQTFVIQGFGNVGSWAAQLIHEKGGKIVAVSDITGAVKNENGLDIPALRKHVAEGGGLKGF 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  362 PKAKPYE-GSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYF 440
Cdd:PLN02477 267 PGGDPIDpDDILVEPCDVLIPAALGGVINKENAADVKAKFIVEAANHPTDPEADEILRKKGVVVLPDIYANSGGVTVSYF 346

                 ....*.
gi 31377775  441 EWLKNL 446
Cdd:PLN02477 347 EWVQNI 352
ELFV_dehydrog_N pfam02812
Glu/Leu/Phe/Val dehydrogenase, dimerisation domain;
113-240 1.59e-72

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


Pssm-ID: 308453  Cd Length: 129  Bit Score: 230.75  E-value: 1.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   113 NHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKN 192
Cdd:pfam02812   2 ERVIQVRVPVKMDDGEVEVFRGYRVQHNTALGPAKGGIRFHPYVNLDEVKALAFLMTYKNALAGLPFGGGKGGIIFDPKK 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 31377775   193 YTENELEKITRRFTMELAKkgFIGPGVDVPAPDMNTGEREMSWIADTY 240
Cdd:pfam02812  82 LSDEELERLTRRFVTELAR--YIGPDTDVPAPDVGTGAREMAWIADEY 127
ELFV_dehydrog smart00839
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glutamate, leucine, phenylalanine and ...
375-448 4.25e-34

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  Cd Length: 102  Bit Score: 125.79  E-value: 4.25e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31377775    375 DCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYFEWLKNLNH 448
Cdd:smart00839   2 NCDIFIPCALQNVINEANANRLGAKIIAEGANMPLTDEADDILEDRGVLYAPDFAANAGGVIVSALEMLQNLAR 75
 
Name Accession Description Interval E-value
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism];
104-555 9.42e-135

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 223411  Cd Length: 411  Bit Score: 402.00  E-value: 9.42e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 104 GILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAK 183
Cdd:COG0334  23 GVLERLKEPERVIQVRIPVRMDDGSVKVFRGYRVQHNSALGPYKGGVRFHPYVTLEEVKALSFWMTLKNALAGLPYGGGK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 184 AGVKINPKNYTENELEKITRRFTMELAKkgFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHydiNAHACVTGKPISQG 263
Cdd:COG0334 103 GGIIVDPKGLSDGELERLSRAFGRAIYR--LIGPDTDIPAPDVGTNPQDMAWMMDEYSKIVGN---SAPGVFTGKPLELG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 264 GIHGRISATGRGVFHGIEnfinEASYMsiLGMtpGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGI 343
Cdd:COG0334 178 GSLGRSEATGYGVFYAIR----EALKA--LGD--DLEGARVAVQGFGNVGQYAAEKLHELGAKVVAVSDSKGGIYDEDGL 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 344 DPKELEDFKLQHGSILGFPKAKPYEG-SILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNI 422
Cdd:COG0334 250 DVEALLELKERRGSVAEYAGAEYITNeELLEVDCDILIPCALENVITEDNADQLKAKIVVEGANGPTTPEADEILLERGI 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 423 LVIPDLYLNAGGVTVSYFEWLKNLNhvsygRLTFKYERdsnyhlllsVQESLERKfgkhggtipivptaefqdsisgase 502
Cdd:COG0334 330 LVVPDILANAGGVIVSYLEWVQNAQ-----GLYWTEEE---------VDEKLERI------------------------- 370
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 31377775 503 kdivhsalaytMERSARQIMHTAMKYnlGLDLRTAAYVNAIEKVFKVYSEAGV 555
Cdd:COG0334 371 -----------MVNAFEAVYQAAKEY--GVDLRTAAYILAFERVADAMKARGW 410
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
263-548 7.75e-115

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  Cd Length: 227  Bit Score: 343.75  E-value: 7.75e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 263 GGIHGRISATGRGVFHGIENFINEASymsilgmtPGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDG 342
Cdd:cd01076   1 GGSLGREEATGRGVAYATREALKKLG--------IGLAGARVAIQGFGNVGSHAARFLHEAGAKVVAVSDSDGTIYNPDG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 343 IDPKELEDFKLQHGSILGFPKAKPYE-GSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERN 421
Cdd:cd01076  73 LDVPALLAYKKEHGSVLGFPGAERITnEELLELDCDILIPAALENQITADNADRIKAKIIVEAANGPTTPEADEILHERG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 422 ILVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRltfkyerdsnyhlllsvqeslerkfgkhggtipivptaefqdsisgas 501
Cdd:cd01076 153 VLVVPDILANAGGVTVSYFEWVQNLQGFYWDE------------------------------------------------ 184
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 31377775 502 ekDIVHSALAYTMERSARQIMHTAMKYnlGLDLRTAAYVNAIEKVFK 548
Cdd:cd01076 185 --EEVNSRLETKMREAFEAVLETAEKY--GVDLRTAAYVLALERVAE 227
PLN02477 PLN02477
glutamate dehydrogenase
122-446 1.66e-114

glutamate dehydrogenase


Pssm-ID: 178095  Cd Length: 410  Bit Score: 349.83  E-value: 1.66e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  122 IRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTENELEKI 201
Cdd:PLN02477  41 IPKDDGTLASFVGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVANIPYGGAKGGIGCDPRDLSESELERL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  202 TRRFTMELakKGFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHydinAHACVTGKPISQGGIHGRISATGRGVFHGIE 281
Cdd:PLN02477 121 TRVFTQKI--HDLIGIHTDVPAPDMGTNAQTMAWILDEYSKFHGF----SPAVVTGKPIDLGGSLGREAATGRGVVFATE 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  282 NFINEasYMSILgmtpgfRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGF 361
Cdd:PLN02477 195 ALLAE--HGKSI------AGQTFVIQGFGNVGSWAAQLIHEKGGKIVAVSDITGAVKNENGLDIPALRKHVAEGGGLKGF 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  362 PKAKPYE-GSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYF 440
Cdd:PLN02477 267 PGGDPIDpDDILVEPCDVLIPAALGGVINKENAADVKAKFIVEAANHPTDPEADEILRKKGVVVLPDIYANSGGVTVSYF 346

                 ....*.
gi 31377775  441 EWLKNL 446
Cdd:PLN02477 347 EWVQNI 352
ELFV_dehydrog_N pfam02812
Glu/Leu/Phe/Val dehydrogenase, dimerisation domain;
113-240 1.59e-72

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


Pssm-ID: 308453  Cd Length: 129  Bit Score: 230.75  E-value: 1.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   113 NHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKN 192
Cdd:pfam02812   2 ERVIQVRVPVKMDDGEVEVFRGYRVQHNTALGPAKGGIRFHPYVNLDEVKALAFLMTYKNALAGLPFGGGKGGIIFDPKK 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 31377775   193 YTENELEKITRRFTMELAKkgFIGPGVDVPAPDMNTGEREMSWIADTY 240
Cdd:pfam02812  82 LSDEELERLTRRFVTELAR--YIGPDTDVPAPDVGTGAREMAWIADEY 127
ELFV_dehydrog pfam00208
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;
263-546 7.32e-70

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;


Pssm-ID: 306674  Cd Length: 240  Bit Score: 227.78  E-value: 7.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   263 GGIHGRISATGRGVFHgienFINEAsyMSILGMTPgFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDG 342
Cdd:pfam00208   1 GGSLGRPEATGYGVVY----FVEEM--LKKLGGDS-LEGKRVAIQGFGNVGSYAALKLHELGAKVVAVSDSSGAIYDPDG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   343 IDPKELEDFKLQHGSILGFPKAKPYE----GSILEVDCDILIPAATEKQLTKSNAP-RVK--AKIIAEGANGPTTPEADK 415
Cdd:pfam00208  74 LDIEELLELKEERGSVDEYALSPGAEyipnEELWELPCDILVPCATQNEINEENAKtLIKngAKIVVEGANMPTTPEADD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   416 IFLERNILVIPDLYLNAGGVTVSYFEWLKNLNhvsygRLTFKYERdsnyhlllsVQESLERKfgkhggtipivptaefqd 495
Cdd:pfam00208 154 ILEERGVLVVPDKAANAGGVTVSYLEMVQNLQ-----RLSWTEEE---------VDEKLKEI------------------ 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 31377775   496 sisgasekdivhsalaytMERSARQIMHTAMKYnlGLDLRTAAYVNAIEKV 546
Cdd:pfam00208 202 ------------------MTNAFDAVVETAQEY--GVDLRTGANIAGFERV 232
PRK09414 PRK09414
glutamate dehydrogenase; Provisional
125-441 1.25e-50

glutamate dehydrogenase; Provisional


Pssm-ID: 181834  Cd Length: 445  Bit Score: 182.24  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  125 DDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTENELEKITRR 204
Cdd:PRK09414  70 DKGQVQVNRGFRVQFNSAIGPYKGGLRFHPSVNLSILKFLGFEQIFKNALTGLPIGGGKGGSDFDPKGKSDAEIMRFCQS 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  205 FTMELAKkgFIGPGVDVPAPDMNTGEREMSWIAdtyastiGHY-DI-NAHACV-TGKPISQGGIHGRISATGRG-VFhgi 280
Cdd:PRK09414 150 FMTELYR--HIGPDTDVPAGDIGVGGREIGYLF-------GQYkRLtNRFEGVlTGKGLSFGGSLIRTEATGYGlVY--- 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  281 enFINEAsyMSILGMTpgFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFK-LQHGSIL 359
Cdd:PRK09414 218 --FAEEM--LKARGDS--FEGKRVVVSGSGNVAIYAIEKAQQLGAKVVTCSDSSGYVYDEEGIDLEKLKEIKeVRRGRIS 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  360 GFPKAKP--YE--GSILEVDCDILIPAATEKQLTKSNAPRVKA---KIIAEGANGPTTPEADKIFLERNILVIPDLYLNA 432
Cdd:PRK09414 292 EYAEEFGaeYLegGSPWSVPCDIALPCATQNELDEEDAKTLIAngvKAVAEGANMPSTPEAIEVFLEAGVLFAPGKAANA 371

                 ....*....
gi 31377775  433 GGVTVSYFE 441
Cdd:PRK09414 372 GGVATSGLE 380
PTZ00079 PTZ00079
NADP-specific glutamate dehydrogenase; Provisional
97-445 8.07e-48

NADP-specific glutamate dehydrogenase; Provisional


Pssm-ID: 185433  Cd Length: 454  Bit Score: 174.54  E-value: 8.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   97 QKRNRVRGIL-RIIKPcNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVV 175
Cdd:PTZ00079  47 QKNPKYLGVLeRLVEP-ERVIQFRVPWVDDKGEQRVNRGFRVQYNSALGPYKGGLRFHPSVNLSILKFLGFEQIFKNSLT 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  176 DVPFGGAKAGVKINPKNYTENELEKITRRFTMELAKkgFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHYDinahaCV 255
Cdd:PTZ00079 126 TLPMGGGKGGSDFDPKGKSDNEVMRFCQSFMTELYR--HIGPDTDVPAGDIGVGGREIGYLFGQYKKLRNNFE-----GT 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  256 -TGKPISQGGIHGRISATGRGVFHGIENF---INEasymsilgmtpGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVG 331
Cdd:PTZ00079 199 lTGKNVKWGGSNIRPEATGYGLVYFVLEVlkkLND-----------SLEGKTVVVSGSGNVAQYAVEKLLQLGAKVLTMS 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  332 ESDGSIWNPDGIDPKELE---DFK----------LQHGSILG-FPKAKPYegsilEVDCDILIPAATEKQLTKSNAPRV- 396
Cdd:PTZ00079 268 DSDGYIHEPNGFTKEKLAylmDLKnvkrgrlkeyAKHSSTAKyVPGKKPW-----EVPCDIAFPCATQNEINLEDAKLLi 342
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 31377775  397 --KAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYFEWLKN 445
Cdd:PTZ00079 343 knGCKLVAEGANMPTTIEATHLFKKNGVIFCPGKAANAGGVAISGLEMSQN 393
PRK14030 PRK14030
glutamate dehydrogenase; Provisional
86-451 8.50e-46

glutamate dehydrogenase; Provisional


Pssm-ID: 184463  Cd Length: 445  Bit Score: 168.48  E-value: 8.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   86 VKDLRTQESEEQKrnrVRGILRIIKPcNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALA 165
Cdd:PRK14030  31 VEDVYNQHPEFEK---AKIIERIVEP-DRIFTFRVPWVDDKGEVQVNLGYRVQFNNAIGPYKGGIRFHPSVNLSILKFLG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  166 SLMTYKCAVVDVPFGGAKAGVKINPKNYTENELEKITRRFTMELAKkgFIGPGVDVPAPDMNTGEREMSWIADTYASTIG 245
Cdd:PRK14030 107 FEQTFKNALTTLPMGGGKGGSDFSPRGKSDAEIMRFCQAFMLELWR--HIGPDTDVPAGDIGVGGREVGYMFGMYKKLTR 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  246 HYdinaHACVTGKPISQGGIHGRISATGRGVFHGIENFInEASYMSIlgmtpgfRDKTFVVQGFGNVGLHSMRYLHRFGA 325
Cdd:PRK14030 185 EF----TGTLTGKGLEFGGSLIRPEATGFGALYFVHQML-ETKGIDI-------KGKTVAISGFGNVAWGAATKATELGA 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  326 KCIAVGESDGSIWNPDGIDPKELeDFKLQ---HGSILGFPKAKPYEGSIL-------EVDCDILIPAATEKQLTKSNAPR 395
Cdd:PRK14030 253 KVVTISGPDGYIYDPDGISGEKI-DYMLElraSGNDIVAPYAEKFPGSTFfagkkpwEQKVDIALPCATQNELNGEDADK 331
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 31377775  396 V---KAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYFEWLKNLNHVSY 451
Cdd:PRK14030 332 LiknGVLCVAEVSNMGCTAEAIDKFIAAKQLFAPGKAVNAGGVATSGLEMSQNAMHLSW 390
PRK14031 PRK14031
glutamate dehydrogenase; Provisional
125-453 1.22e-44

glutamate dehydrogenase; Provisional


Pssm-ID: 184464  Cd Length: 444  Bit Score: 165.49  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  125 DDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTENELEKITRR 204
Cdd:PRK14031  66 DKGNVQTNMGYRVQHNNAIGPYKGGIRFHASVNLGILKFLAFEQTFKNSLTTLPMGGGKGGSDFSPRGKSNAEVMRFCQA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  205 FTMELAKkgFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHYDinahACVTGKPISQGGIHGRISATGRGVFHGIENFI 284
Cdd:PRK14031 146 FMLELWR--HIGPETDVPAGDIGVGGREVGFMFGMYKKLSHEFT----GTFTGKGREFGGSLIRPEATGYGNIYFLMEML 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  285 NEASYmsilgmtpGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFK----LQHGSILG 360
Cdd:PRK14031 220 KTKGT--------DLKGKVCLVSGSGNVAQYTAEKVLELGGKVVTMSDSDGYIYDPDGIDREKLDYIMelknLYRGRIRE 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  361 F---------PKAKPYEGSilevdCDILIPAATEKQLTKSNAPRVKAK---IIAEGANGPTTPEADKIFLERNILVIPDL 428
Cdd:PRK14031 292 YaekygckyvEGARPWGEK-----GDIALPSATQNELNGDDARQLVANgviAVSEGANMPSTPEAIKVFQDAKILYAPGK 366
                        330       340
                 ....*....|....*....|....*
gi 31377775  429 YLNAGGVTVSYFEWLKNLNHVSYGR 453
Cdd:PRK14031 367 AANAGGVSVSGLEMTQNSIKLSWSS 391
NAD_bind_Glu_Leu_Phe_Val cd05211
NAD(P) binding domain of glutamate dehydrogenase, leucine dehydrogenase, phenylalanine ...
271-451 5.13e-40

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  Cd Length: 217  Bit Score: 146.16  E-value: 5.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 271 ATGRGVFHGIEnfineaSYMSILGMTPgfRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPdGIDPKELED 350
Cdd:cd05211   1 ATGYGVVVAMK------AAMKHLGDSL--EGLTVAVQGLGNVGWGLAKKLAEEGGKVLAVSDPDGYIYDP-GITTEELIN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 351 FKLQHGSILGFPKAKPYEG-SILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNILVIPDLY 429
Cdd:cd05211  72 YAVALGGSARVKVQDYFPGeAILGLDVDIFAPCALGNVIDLENAKKLKAKVVAEGANNPTTDEALRILHERGIVVAPDIV 151
                       170       180
                ....*....|....*....|..
gi 31377775 430 LNAGGVTVSYFEWLKNLNHVSY 451
Cdd:cd05211 152 ANAGGVIVSYFEWVQNLQRLSW 173
ELFV_dehydrog smart00839
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glutamate, leucine, phenylalanine and ...
375-448 4.25e-34

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  Cd Length: 102  Bit Score: 125.79  E-value: 4.25e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31377775    375 DCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYFEWLKNLNH 448
Cdd:smart00839   2 NCDIFIPCALQNVINEANANRLGAKIIAEGANMPLTDEADDILEDRGVLYAPDFAANAGGVIVSALEMLQNLAR 75
NAD_bind_2_Glu_DH cd05313
NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; Amino acid dehydrogenase (DH) is ...
256-453 1.82e-30

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  Cd Length: 254  Bit Score: 120.03  E-value: 1.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 256 TGKPISQGGIHGRISATGRGVFHGIENFINEasymsilgMTPGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDG 335
Cdd:cd05313   1 TGKGLSWGGSLIRPEATGYGLVYFVEEMLKD--------RNETLKGKRVAISGSGNVAQYAAEKLLELGAKVVTLSDSKG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 336 SIWNPDGIDPKELE---DFKLQHGSILG-----FPKAKPYEG-SILEVDCDILIPAATEKQLTKSNAPR-VKA--KIIAE 403
Cdd:cd05313  73 YVYDPDGFTGEKLAelkEIKEVRRGRVSeyakkYGTAKYFEGkKPWEVPCDIAFPCATQNEVDAEDAKLlVKNgcKYVAE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 31377775 404 GANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYFEWLKNLNHVSYGR 453
Cdd:cd05313 153 GANMPCTAEAIEVFRQAGVLFAPGKAANAGGVAVSGLEMSQNSQRLSWTA 202
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
272-435 2.96e-17

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: 81.10  E-value: 2.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 272 TGRGVFHGIEnfineASYMSILGmTPGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAvgeSDgsiwnpdgIDPKELEDF 351
Cdd:cd01075   5 TAYGVFLGMK-----AAAEHLLG-TDSLEGKTVAVQGLGKVGYKLAEHLLEEGAKLIV---AD--------INEEAVARA 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775 352 KLQHGsilgfpkAKPYE-GSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEA-DKIFLERNILVIPDLY 429
Cdd:cd01075  68 AELFG-------ATVVApEEIYSVDADVFAPCALGGVINDDTIPQLKAKAIAGAANNQLADPRhGQMLHERGILYAPDYV 140

                ....*.
gi 31377775 430 LNAGGV 435
Cdd:cd01075 141 VNAGGL 146
PTZ00324 PTZ00324
glutamate dehydrogenase 2; Provisional
135-446 2.26e-07

glutamate dehydrogenase 2; Provisional


Pssm-ID: 240359  Cd Length: 1002  Bit Score: 53.65  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   135 YRAQHSQHRTPCKGGIR---------YSTDVS--VDEVKALASLMTYKCAvvDVPFGGAKaGVKINPKNYTENELEKITR 203
Cdd:PTZ00324  486 FRGFHIRFTDIARGGVRmiqsfkeqaYRRNKRsvFDENYNLASTQLLKNK--DIPEGGSK-GTILLSSRYLNKFAQVRCQ 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   204 RFTM-------------ELAKKGFIGPGVDVPAPDMNTGEREMSWiADTYAStighyDINAH---ACVTGKPISQGGI-- 265
Cdd:PTZ00324  563 HAFLqyidalldvmlpgEKVVDHLKQEEIIFLGPDEHTTGTLMDW-AALHAK-----KRGYPfwkSFTTGKSPSMGGIph 636
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   266 --HGRISATGRGVFHGIENF--INEASYMSILGMTPGfrdktfvvqgfGNVGLHSmryLHRFGAKCIAVGESDGSIWNPD 341
Cdd:PTZ00324  637 dtYGMTTRSVRAYVTGILEKlgLNEEEVTKFQTGGPD-----------GDLGSNE---LLLSKEKTVGIVDGSGVLHDPE 702
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775   342 GIDPKELEDFKLQHGSILGFPKAK--PYEGSILEVDCDILIPAAT----------EKQLTK-SNA---------PR---- 395
Cdd:PTZ00324  703 GLNREELRRLAHHRLPAREFDESKlsPQGFLVLTDDRDVKLPDGTivesglrfrnEFHLLPySDAdvfvpcggrPRsvtl 782
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31377775   396 -------------VKAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYFEWLKNL 446
Cdd:PTZ00324  783 fnvgrffdekngkLRFKIIVEGANLFITQDARLALEECGVILFKDASANKGGVTSSSLEVLAAL 846
Gdh2 COG2902
NAD-specific glutamate dehydrogenase [Amino acid transport and metabolism];
342-441 7.11e-03

NAD-specific glutamate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 225455  Cd Length: 1592  Bit Score: 39.28  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377775  342 GIDPKELEDFKLqHGSILGFPKAKPYEGSIlevdcDILIPAATE---------KQLTKSNAPRVKAKIIAEGANGPTTPE 412
Cdd:COG2902 1056 GIDKTELAPNEL-ITAILKAPVDLLWNGGI-----GTYVKASGEtnadvgdraNDAIRVNGEEVRAKVIGEGANLGVTQR 1129
                         90       100
                 ....*....|....*....|....*....
gi 31377775  413 ADKIFLERNILVIPDLYLNAGGVTVSYFE 441
Cdd:COG2902 1130 GRIEFALAGGRINTDAIDNSAGVDCSDHE 1158
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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