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Conserved domains on  [gi|6319256|ref|NP_009339|]
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glutamate dehydrogenase (NADP(+)) GDH3 [Saccharomyces cerevisiae S288C]

Protein Classification

dehydrogenase family protein( domain architecture ID 1001438)

dehydrogenase family protein such as glutamate dehydrogenase, which catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate using NAD+ and or NADP+ as cofactor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09414 super family cl32367
NADP-specific glutamate dehydrogenase;
4-454 0e+00

NADP-specific glutamate dehydrogenase;


The actual alignment was detected with superfamily member PRK09414:

Pssm-ID: 181834 [Multi-domain]  Cd Length: 445  Bit Score: 667.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     4 EPEFQQAYDEIVSSVEDskIFEKFPQYKK--VLPIVSVPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFH 81
Cdd:PRK09414  21 QPEFHQAVREVLESLWP--VLEKNPEYAEagILERLVEPERVIIFRVPWVDDKGQVQVNRGFRVQFNSAIGPYKGGLRFH 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    82 PSVNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGY 161
Cdd:PRK09414  99 PSVNLSILKFLGFEQIFKNALTGLPIGGGKGGSDFDPKGKSDAEIMRFCQSFMTELYRHIGPDTDVPAGDIGVGGREIGY 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   162 LFGAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGFGLVYYTQAMIdyATNGkESFEGKRVTISGSGNVAQYAALKVIELG 241
Cdd:PRK09414 179 LFGQYKRLTNRFEGVLTGKGLSFGGSLIRTEATGYGLVYFAEEML--KARG-DSFEGKRVVVSGSGNVAIYAIEKAQQLG 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   242 GIVVSLSDSKGCIISETGITSEQIHDIasAKIRFKSLEEIVDEYSTfseskmKYVAGARPWtHVSnVDIALPCATQNEVS 321
Cdd:PRK09414 256 AKVVTCSDSSGYVYDEEGIDLEKLKEI--KEVRRGRISEYAEEFGA------EYLEGGSPW-SVP-CDIALPCATQNELD 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   322 GDEAKALVASGVKFVAEGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVD 401
Cdd:PRK09414 326 EEDAKTLIANGVKAVAEGANMPSTPEAIEVFLEAG---------VLFAPGKAANAGGVATSGLEMSQNASRLSWTFEEVD 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6319256   402 QELKKIMINCFNDCIQAAQEYSTEKNtntlpsLVKGANIASFVMVADAMLDQG 454
Cdd:PRK09414 397 ARLHDIMKNIHHACVETAEEYGKPGN------YVAGANIAGFVKVADAMLAQG 443
 
Name Accession Description Interval E-value
PRK09414 PRK09414
NADP-specific glutamate dehydrogenase;
4-454 0e+00

NADP-specific glutamate dehydrogenase;


Pssm-ID: 181834 [Multi-domain]  Cd Length: 445  Bit Score: 667.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     4 EPEFQQAYDEIVSSVEDskIFEKFPQYKK--VLPIVSVPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFH 81
Cdd:PRK09414  21 QPEFHQAVREVLESLWP--VLEKNPEYAEagILERLVEPERVIIFRVPWVDDKGQVQVNRGFRVQFNSAIGPYKGGLRFH 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    82 PSVNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGY 161
Cdd:PRK09414  99 PSVNLSILKFLGFEQIFKNALTGLPIGGGKGGSDFDPKGKSDAEIMRFCQSFMTELYRHIGPDTDVPAGDIGVGGREIGY 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   162 LFGAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGFGLVYYTQAMIdyATNGkESFEGKRVTISGSGNVAQYAALKVIELG 241
Cdd:PRK09414 179 LFGQYKRLTNRFEGVLTGKGLSFGGSLIRTEATGYGLVYFAEEML--KARG-DSFEGKRVVVSGSGNVAIYAIEKAQQLG 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   242 GIVVSLSDSKGCIISETGITSEQIHDIasAKIRFKSLEEIVDEYSTfseskmKYVAGARPWtHVSnVDIALPCATQNEVS 321
Cdd:PRK09414 256 AKVVTCSDSSGYVYDEEGIDLEKLKEI--KEVRRGRISEYAEEFGA------EYLEGGSPW-SVP-CDIALPCATQNELD 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   322 GDEAKALVASGVKFVAEGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVD 401
Cdd:PRK09414 326 EEDAKTLIANGVKAVAEGANMPSTPEAIEVFLEAG---------VLFAPGKAANAGGVATSGLEMSQNASRLSWTFEEVD 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6319256   402 QELKKIMINCFNDCIQAAQEYSTEKNtntlpsLVKGANIASFVMVADAMLDQG 454
Cdd:PRK09414 397 ARLHDIMKNIHHACVETAEEYGKPGN------YVAGANIAGFVKVADAMLAQG 443
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
4-454 7.95e-172

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: 488.41  E-value: 7.95e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    4 EPEFQQAYDEIVSSVEDskIFEKFPqykKVLPIVSVPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFHPS 83
Cdd:COG0334   1 EPEFLQAVLEQLDSAAP--VLGLDP---GILERLKEPERVIIVRVPVRMDDGSVQVFRGYRVQHNSALGPYKGGIRFHPS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   84 VNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGYLF 163
Cdd:COG0334  76 VNLDEVKALAFWMTFKNALTGLPFGGGKGGIDFDPKGLSDGELERLTRRFMTELYRHIGPDTDIPAPDVGTGAREMAWMM 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  164 GAYRSYKNSWE-GVLTGKGLNWGGSLIRPEATGFGLVYYTQAMIDYAtngKESFEGKRVTISGSGNVAQYAALKVIELGG 242
Cdd:COG0334 156 DEYSRITGETVpGVVTGKPLELGGSLGRTEATGRGVVYFAREALKKL---GLSLEGKTVAVQGFGNVGSYAAELLHELGA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  243 IVVSLSDSKGCIISETGItseqihDIAsakirfkSLEEIVDEYSTFSE-SKMKYVAGARPWTHvsNVDIALPCATQNEVS 321
Cdd:COG0334 233 KVVAVSDSSGGIYDPDGI------DLD-------ALKEHKEERGSVAGyPGAEFITNEELLEL--DCDILIPAALENVIT 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  322 GDEAKALvasGVKFVAEGANMGSTPEAISVFEtarstatnAKDaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVD 401
Cdd:COG0334 298 EENAKRL---KAKIVAEGANGPTTPEADEILA--------ERG-ILVAPDILANAGGVTVSYFEWVQNLQRYSWTEEEVD 365
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 6319256  402 QELKKIMINCFNDCIQAAQEYSTekntntlpSLVKGANIASFVMVADAMLDQG 454
Cdd:COG0334 366 ERLEEIMVDAFDAVFETAEEYGV--------DLRTAAYIAAFERVADAMKARG 410
NAD_bind_2_Glu_DH cd05313
NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; Amino acid dehydrogenase (DH) is ...
178-455 4.52e-142

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: 406.62  E-value: 4.52e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  178 TGKGLNWGGSLIRPEATGFGLVYYTQAMIDYATngkESFEGKRVTISGSGNVAQYAALKVIELGGIVVSLSDSKGCIISE 257
Cdd:cd05313   1 TGKGLSWGGSLIRPEATGYGLVYFVEEMLKDRN---ETLKGKRVAISGSGNVAQYAAEKLLELGAKVVTLSDSKGYVYDP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  258 TGITSEQIHDIASAKIRFKSLeeiVDEYSTFSESkMKYVAGARPWTHVsnVDIALPCATQNEVSGDEAKALVASGVKFVA 337
Cdd:cd05313  78 DGFTGEKLAELKEIKEVRRGR---VSEYAKKYGT-AKYFEGKKPWEVP--CDIAFPCATQNEVDAEDAKLLVKNGCKYVA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  338 EGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVDQELKKIMINCFNDCIQ 417
Cdd:cd05313 152 EGANMPCTAEAIEVFRQAG---------VLFAPGKAANAGGVAVSGLEMSQNSQRLSWTAEEVDAKLKDIMKNIHDACAE 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6319256  418 AAQEYstekntNTLPSLVKGANIASFVMVADAMLDQGD 455
Cdd:cd05313 223 TAKKY------GDPPDLVAGANIAGFLKVADAMLAQGV 254
ELFV_dehydrog pfam00208
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;
185-454 2.04e-113

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;


Pssm-ID: 425526 [Multi-domain]  Cd Length: 240  Bit Score: 333.33  E-value: 2.04e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    185 GGSLIRPEATGFGLVYYTQAMIDYAtnGKESFEGKRVTISGSGNVAQYAALKVIELGGIVVSLSDSKGCIISETGItseQ 264
Cdd:pfam00208   1 GGSLGRPEATGYGVVYFVEEMLKKL--GGDSLEGKRVAIQGFGNVGSYAALKLHELGAKVVAVSDSSGAIYDPDGL---D 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    265 IHDIASAKIRFKSLEEIVDEystfseSKMKYVAGARPWTHvsNVDIALPCATQNEVSGDEAKALVASGVKFVAEGANMGS 344
Cdd:pfam00208  76 IEELLELKEERGSVDEYALS------GGAEYIPNEELWEL--PCDILVPCATQNEITEENAKTLIKNGAKIVVEGANMPT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    345 TPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVDQELKKIMINCFNDCIQAAQEYSt 424
Cdd:pfam00208 148 TPEADDILEERG---------VLVVPDKAANAGGVTVSYLEMVQNLQRLSWTEEEVDEKLKEIMTNAFDAVVETAQEYG- 217
                         250       260       270
                  ....*....|....*....|....*....|
gi 6319256    425 ekntntlPSLVKGANIASFVMVADAMLDQG 454
Cdd:pfam00208 218 -------VDLRTGANIAGFERVADAMKARG 240
ELFV_dehydrog smart00839
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glutamate, leucine, phenylalanine and ...
307-422 8.38e-31

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: 114.23  E-value: 8.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     307 NVDIALPCATQNEVSGDEAKALvasGVKFVAEGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEM 386
Cdd:smart00839   2 NCDIFIPCALQNVINEANANRL---GAKIIAEGANMPLTDEADDILEDRG---------VLYAPDFAANAGGVIVSALEM 69
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 6319256     387 AQNSQKvtwTAERVDQELKKIMINCFNDCIQAAQEY 422
Cdd:smart00839  70 LQNLAR---TAEEVFTDLSEIMRNALEEIFETAQKY 102
 
Name Accession Description Interval E-value
PRK09414 PRK09414
NADP-specific glutamate dehydrogenase;
4-454 0e+00

NADP-specific glutamate dehydrogenase;


Pssm-ID: 181834 [Multi-domain]  Cd Length: 445  Bit Score: 667.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     4 EPEFQQAYDEIVSSVEDskIFEKFPQYKK--VLPIVSVPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFH 81
Cdd:PRK09414  21 QPEFHQAVREVLESLWP--VLEKNPEYAEagILERLVEPERVIIFRVPWVDDKGQVQVNRGFRVQFNSAIGPYKGGLRFH 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    82 PSVNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGY 161
Cdd:PRK09414  99 PSVNLSILKFLGFEQIFKNALTGLPIGGGKGGSDFDPKGKSDAEIMRFCQSFMTELYRHIGPDTDVPAGDIGVGGREIGY 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   162 LFGAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGFGLVYYTQAMIdyATNGkESFEGKRVTISGSGNVAQYAALKVIELG 241
Cdd:PRK09414 179 LFGQYKRLTNRFEGVLTGKGLSFGGSLIRTEATGYGLVYFAEEML--KARG-DSFEGKRVVVSGSGNVAIYAIEKAQQLG 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   242 GIVVSLSDSKGCIISETGITSEQIHDIasAKIRFKSLEEIVDEYSTfseskmKYVAGARPWtHVSnVDIALPCATQNEVS 321
Cdd:PRK09414 256 AKVVTCSDSSGYVYDEEGIDLEKLKEI--KEVRRGRISEYAEEFGA------EYLEGGSPW-SVP-CDIALPCATQNELD 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   322 GDEAKALVASGVKFVAEGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVD 401
Cdd:PRK09414 326 EEDAKTLIANGVKAVAEGANMPSTPEAIEVFLEAG---------VLFAPGKAANAGGVATSGLEMSQNASRLSWTFEEVD 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6319256   402 QELKKIMINCFNDCIQAAQEYSTEKNtntlpsLVKGANIASFVMVADAMLDQG 454
Cdd:PRK09414 397 ARLHDIMKNIHHACVETAEEYGKPGN------YVAGANIAGFVKVADAMLAQG 443
PTZ00079 PTZ00079
NADP-specific glutamate dehydrogenase; Provisional
4-454 0e+00

NADP-specific glutamate dehydrogenase; Provisional


Pssm-ID: 185433 [Multi-domain]  Cd Length: 454  Bit Score: 594.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     4 EPEFQQAYDEIVSSVEdsKIFEKFPQYKKVLPIVSVPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFHPS 83
Cdd:PTZ00079  28 QPEFLQAFHEVMTSLK--PLFQKNPKYLGVLERLVEPERVIQFRVPWVDDKGEQRVNRGFRVQYNSALGPYKGGLRFHPS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    84 VNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGYLF 163
Cdd:PTZ00079 106 VNLSILKFLGFEQIFKNSLTTLPMGGGKGGSDFDPKGKSDNEVMRFCQSFMTELYRHIGPDTDVPAGDIGVGGREIGYLF 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   164 GAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGFGLVYYTQAMIdyaTNGKESFEGKRVTISGSGNVAQYAALKVIELGGI 243
Cdd:PTZ00079 186 GQYKKLRNNFEGTLTGKNVKWGGSNIRPEATGYGLVYFVLEVL---KKLNDSLEGKTVVVSGSGNVAQYAVEKLLQLGAK 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   244 VVSLSDSKGCIISETGITSEQIHDIASAK-IRFKSLEEIVDEYSTfseskMKYVAGARPWThvSNVDIALPCATQNEVSG 322
Cdd:PTZ00079 263 VLTMSDSDGYIHEPNGFTKEKLAYLMDLKnVKRGRLKEYAKHSST-----AKYVPGKKPWE--VPCDIAFPCATQNEINL 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   323 DEAKALVASGVKFVAEGANMGSTPEAISVFEtarstatnaKDAVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVDQ 402
Cdd:PTZ00079 336 EDAKLLIKNGCKLVAEGANMPTTIEATHLFK---------KNGVIFCPGKAANAGGVAISGLEMSQNAARLQWTAEEVDE 406
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6319256   403 ELKKIMINCFNDCIQAAQEYSTEKNtntlpsLVKGANIASFVMVADAMLDQG 454
Cdd:PTZ00079 407 KLREIMKSIFEACVKYAEKYGGKSD------LVAGANIAGFLKVADSMIEQG 452
PRK14030 PRK14030
glutamate dehydrogenase; Provisional
4-456 6.05e-176

glutamate dehydrogenase; Provisional


Pssm-ID: 184463 [Multi-domain]  Cd Length: 445  Bit Score: 500.13  E-value: 6.05e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     4 EPEFQQAYDEIVSSVEDskIFEKFPQYKK--VLPIVSVPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFH 81
Cdd:PRK14030  17 ESEYLQAVKEVLLSVED--VYNQHPEFEKakIIERIVEPDRIFTFRVPWVDDKGEVQVNLGYRVQFNNAIGPYKGGIRFH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    82 PSVNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGY 161
Cdd:PRK14030  95 PSVNLSILKFLGFEQTFKNALTTLPMGGGKGGSDFSPRGKSDAEIMRFCQAFMLELWRHIGPDTDVPAGDIGVGGREVGY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   162 LFGAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGFGLVYYTQAMIDyaTNGkESFEGKRVTISGSGNVAQYAALKVIELG 241
Cdd:PRK14030 175 MFGMYKKLTREFTGTLTGKGLEFGGSLIRPEATGFGALYFVHQMLE--TKG-IDIKGKTVAISGFGNVAWGAATKATELG 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   242 GIVVSLSDSKGCIISETGITSEQIHDIASAKirfKSLEEIVDEYST-FSESkmKYVAGARPWThvSNVDIALPCATQNEV 320
Cdd:PRK14030 252 AKVVTISGPDGYIYDPDGISGEKIDYMLELR---ASGNDIVAPYAEkFPGS--TFFAGKKPWE--QKVDIALPCATQNEL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   321 SGDEAKALVASGVKFVAEGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERV 400
Cdd:PRK14030 325 NGEDADKLIKNGVLCVAEVSNMGCTAEAIDKFIAAK---------QLFAPGKAVNAGGVATSGLEMSQNAMHLSWSAEEV 395
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6319256   401 DQELKKIMINCFNDCIQAAQEysteknTNTLPSLVKGANIASFVMVADAMLDQGDV 456
Cdd:PRK14030 396 DEKLHQIMSGIHEQCVKYGKE------GDGYINYVKGANIAGFMKVAKAMLAQGVV 445
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
4-454 7.95e-172

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: 488.41  E-value: 7.95e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    4 EPEFQQAYDEIVSSVEDskIFEKFPqykKVLPIVSVPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFHPS 83
Cdd:COG0334   1 EPEFLQAVLEQLDSAAP--VLGLDP---GILERLKEPERVIIVRVPVRMDDGSVQVFRGYRVQHNSALGPYKGGIRFHPS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   84 VNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGYLF 163
Cdd:COG0334  76 VNLDEVKALAFWMTFKNALTGLPFGGGKGGIDFDPKGLSDGELERLTRRFMTELYRHIGPDTDIPAPDVGTGAREMAWMM 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  164 GAYRSYKNSWE-GVLTGKGLNWGGSLIRPEATGFGLVYYTQAMIDYAtngKESFEGKRVTISGSGNVAQYAALKVIELGG 242
Cdd:COG0334 156 DEYSRITGETVpGVVTGKPLELGGSLGRTEATGRGVVYFAREALKKL---GLSLEGKTVAVQGFGNVGSYAAELLHELGA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  243 IVVSLSDSKGCIISETGItseqihDIAsakirfkSLEEIVDEYSTFSE-SKMKYVAGARPWTHvsNVDIALPCATQNEVS 321
Cdd:COG0334 233 KVVAVSDSSGGIYDPDGI------DLD-------ALKEHKEERGSVAGyPGAEFITNEELLEL--DCDILIPAALENVIT 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  322 GDEAKALvasGVKFVAEGANMGSTPEAISVFEtarstatnAKDaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVD 401
Cdd:COG0334 298 EENAKRL---KAKIVAEGANGPTTPEADEILA--------ERG-ILVAPDILANAGGVTVSYFEWVQNLQRYSWTEEEVD 365
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 6319256  402 QELKKIMINCFNDCIQAAQEYSTekntntlpSLVKGANIASFVMVADAMLDQG 454
Cdd:COG0334 366 ERLEEIMVDAFDAVFETAEEYGV--------DLRTAAYIAAFERVADAMKARG 410
PRK14031 PRK14031
NADP-specific glutamate dehydrogenase;
3-454 4.08e-164

NADP-specific glutamate dehydrogenase;


Pssm-ID: 184464 [Multi-domain]  Cd Length: 444  Bit Score: 470.18  E-value: 4.08e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     3 SEPEFQQAYDEIVSSVEDSkiFEKFPQYKKVLPI--VSVPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRF 80
Cdd:PRK14031  16 NEPEYHQAVEEVLSTIEEE--YNKHPEFDKANLIerLCIPDRVYQFRVTWVDDKGNVQTNMGYRVQHNNAIGPYKGGIRF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    81 HPSVNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIG 160
Cdd:PRK14031  94 HASVNLGILKFLAFEQTFKNSLTTLPMGGGKGGSDFSPRGKSNAEVMRFCQAFMLELWRHIGPETDVPAGDIGVGGREVG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   161 YLFGAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGFGLVYYTQAMIdyATNGKEsFEGKRVTISGSGNVAQYAALKVIEL 240
Cdd:PRK14031 174 FMFGMYKKLSHEFTGTFTGKGREFGGSLIRPEATGYGNIYFLMEML--KTKGTD-LKGKVCLVSGSGNVAQYTAEKVLEL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   241 GGIVVSLSDSKGCIISETGITSEQIHDIASAKIRFKS-LEEIVDEYSTfseskmKYVAGARPWTHvsNVDIALPCATQNE 319
Cdd:PRK14031 251 GGKVVTMSDSDGYIYDPDGIDREKLDYIMELKNLYRGrIREYAEKYGC------KYVEGARPWGE--KGDIALPSATQNE 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   320 VSGDEAKALVASGVKFVAEGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAER 399
Cdd:PRK14031 323 LNGDDARQLVANGVIAVSEGANMPSTPEAIKVFQDAK---------ILYAPGKAANAGGVSVSGLEMTQNSIKLSWSSEE 393
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6319256   400 VDQELKKIMINCFNDCIQaaqeYSTEknTNTLPSLVKGANIASFVMVADAMLDQG 454
Cdd:PRK14031 394 VDEKLKSIMKNIHEACVQ----YGTE--ADGYVNYVKGANVAGFMKVAKAMMAQG 442
NAD_bind_2_Glu_DH cd05313
NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; Amino acid dehydrogenase (DH) is ...
178-455 4.52e-142

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: 406.62  E-value: 4.52e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  178 TGKGLNWGGSLIRPEATGFGLVYYTQAMIDYATngkESFEGKRVTISGSGNVAQYAALKVIELGGIVVSLSDSKGCIISE 257
Cdd:cd05313   1 TGKGLSWGGSLIRPEATGYGLVYFVEEMLKDRN---ETLKGKRVAISGSGNVAQYAAEKLLELGAKVVTLSDSKGYVYDP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  258 TGITSEQIHDIASAKIRFKSLeeiVDEYSTFSESkMKYVAGARPWTHVsnVDIALPCATQNEVSGDEAKALVASGVKFVA 337
Cdd:cd05313  78 DGFTGEKLAELKEIKEVRRGR---VSEYAKKYGT-AKYFEGKKPWEVP--CDIAFPCATQNEVDAEDAKLLVKNGCKYVA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  338 EGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVDQELKKIMINCFNDCIQ 417
Cdd:cd05313 152 EGANMPCTAEAIEVFRQAG---------VLFAPGKAANAGGVAVSGLEMSQNSQRLSWTAEEVDAKLKDIMKNIHDACAE 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6319256  418 AAQEYstekntNTLPSLVKGANIASFVMVADAMLDQGD 455
Cdd:cd05313 223 TAKKY------GDPPDLVAGANIAGFLKVADAMLAQGV 254
ELFV_dehydrog pfam00208
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;
185-454 2.04e-113

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;


Pssm-ID: 425526 [Multi-domain]  Cd Length: 240  Bit Score: 333.33  E-value: 2.04e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    185 GGSLIRPEATGFGLVYYTQAMIDYAtnGKESFEGKRVTISGSGNVAQYAALKVIELGGIVVSLSDSKGCIISETGItseQ 264
Cdd:pfam00208   1 GGSLGRPEATGYGVVYFVEEMLKKL--GGDSLEGKRVAIQGFGNVGSYAALKLHELGAKVVAVSDSSGAIYDPDGL---D 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    265 IHDIASAKIRFKSLEEIVDEystfseSKMKYVAGARPWTHvsNVDIALPCATQNEVSGDEAKALVASGVKFVAEGANMGS 344
Cdd:pfam00208  76 IEELLELKEERGSVDEYALS------GGAEYIPNEELWEL--PCDILVPCATQNEITEENAKTLIKNGAKIVVEGANMPT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    345 TPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVDQELKKIMINCFNDCIQAAQEYSt 424
Cdd:pfam00208 148 TPEADDILEERG---------VLVVPDKAANAGGVTVSYLEMVQNLQRLSWTEEEVDEKLKEIMTNAFDAVVETAQEYG- 217
                         250       260       270
                  ....*....|....*....|....*....|
gi 6319256    425 ekntntlPSLVKGANIASFVMVADAMLDQG 454
Cdd:pfam00208 218 -------VDLRTGANIAGFERVADAMKARG 240
ELFV_dehydrog_N pfam02812
Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
40-167 3.13e-64

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


Pssm-ID: 460706 [Multi-domain]  Cd Length: 129  Bit Score: 203.00  E-value: 3.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     40 PERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFHPSVNLSILKFLGFEQIFKNALTGLDMGGGKGGLCVDLK 119
Cdd:pfam02812   1 PERVIQVRVPVKMDDGEVEVFRGYRVQHNTALGPAKGGIRFHPYVNLDEVKALAFLMTYKNALAGLPFGGGKGGIIVDPK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 6319256    120 GKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGYLFGAYR 167
Cdd:pfam02812  81 KLSDEELERLTRRFVRELARYIGPDTDVPAPDVGTGAREMAWMADEYS 128
PLN02477 PLN02477
glutamate dehydrogenase
19-424 1.31e-56

glutamate dehydrogenase


Pssm-ID: 178095 [Multi-domain]  Cd Length: 410  Bit Score: 192.67  E-value: 1.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    19 EDSKIFEKFPQYKKVLPIvsvPERIIQFRVTWENDNGEQEVAQGYRVQFNSAKGPYKGGLRFHPSVNLSILKFLGFEQIF 98
Cdd:PLN02477  13 EAARLLGLDSKLEKSLLI---PFREIKVECTIPKDDGTLASFVGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256    99 KNALTGLDMGGGKGGLCVDLKGKSDNEIRRICYAFMRELSRHIGKDTDVPAGDIGVGGREIGYLFGAYRSYKNSWEGVLT 178
Cdd:PLN02477  90 KTAVANIPYGGAKGGIGCDPRDLSESELERLTRVFTQKIHDLIGIHTDVPAPDMGTNAQTMAWILDEYSKFHGFSPAVVT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   179 GKGLNWGGSLIRPEATGFGLVYYTQAMIdyATNGKeSFEGKRVTISGSGNVAQYAALKVIELGGIVVSLSDSKGCIISET 258
Cdd:PLN02477 170 GKPIDLGGSLGREAATGRGVVFATEALL--AEHGK-SIAGQTFVIQGFGNVGSWAAQLIHEKGGKIVAVSDITGAVKNEN 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   259 GItseqihDIAsakirfkSLEEIVDEYSTfseskMKYVAGARPWTHVSNV----DIALPCATQNEVSGDEAKALVAsgvK 334
Cdd:PLN02477 247 GL------DIP-------ALRKHVAEGGG-----LKGFPGGDPIDPDDILvepcDVLIPAALGGVINKENAADVKA---K 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256   335 FVAEGANMGSTPEAISVFetarstatnAKDAVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVDQELKKIMINCFND 414
Cdd:PLN02477 306 FIVEAANHPTDPEADEIL---------RKKGVVVLPDIYANSGGVTVSYFEWVQNIQGFMWEEEKVNRELDRYMTDAFKA 376
                        410
                 ....*....|
gi 6319256   415 CIQAAQEYST 424
Cdd:PLN02477 377 LKEMCKTHNC 386
NAD_bind_Glu_Leu_Phe_Val cd05211
NAD(P) binding domain of glutamate dehydrogenase, leucine dehydrogenase, phenylalanine ...
193-422 7.88e-34

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: 126.51  E-value: 7.88e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  193 ATGFGLVYYTQAMIDYATNgkeSFEGKRVTISGSGNVAQYAALKVIELGGIVVSLSDSKGCIISETGITSEqihdiasaK 272
Cdd:cd05211   1 ATGYGVVVAMKAAMKHLGD---SLEGLTVAVQGLGNVGWGLAKKLAEEGGKVLAVSDPDGYIYDPGITTEE--------L 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  273 IRFKSLEEIVDEYSTFSeskmkYVAGARPWThvSNVDIALPCATQNEVSGDEAKALVAsgvKFVAEGANMGSTPEAISVF 352
Cdd:cd05211  70 INYAVALGGSARVKVQD-----YFPGEAILG--LDVDIFAPCALGNVIDLENAKKLKA---KVVAEGANNPTTDEALRIL 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  353 EtarstatnaKDAVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVDQELKKIMINCFNDCIQAAQEY 422
Cdd:cd05211 140 H---------ERGIVVAPDIVANAGGVIVSYFEWVQNLQRLSWDAEEVRSKLEQVMTDIHNGVFAISERD 200
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
185-424 2.72e-31

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: 119.95  E-value: 2.72e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  185 GGSLIRPEATGFGLVYYTQAMIDYAtngKESFEGKRVTISGSGNVAQYAALKVIELGGIVVSLSDSKGCIISETGItseQ 264
Cdd:cd01076   1 GGSLGREEATGRGVAYATREALKKL---GIGLAGARVAIQGFGNVGSHAARFLHEAGAKVVAVSDSDGTIYNPDGL---D 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  265 IHDIASAKIRFKSL-----------EEIVDEystfseskmkyvagarpwthvsNVDIALPCATQNEVSGDEAKALVAsgv 333
Cdd:cd01076  75 VPALLAYKKEHGSVlgfpgaeritnEELLEL----------------------DCDILIPAALENQITADNADRIKA--- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256  334 KFVAEGANMGSTPEAISVFetarstatnAKDAVWFGPPKAANLGGVAVSGLEMAQNSQKVTWTAERVDQELKKIMINCFN 413
Cdd:cd01076 130 KIIVEAANGPTTPEADEIL---------HERGVLVVPDILANAGGVTVSYFEWVQNLQGFYWDEEEVNSRLETKMREAFE 200
                       250
                ....*....|.
gi 6319256  414 DCIQAAQEYST 424
Cdd:cd01076 201 AVLETAEKYGV 211
ELFV_dehydrog smart00839
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glutamate, leucine, phenylalanine and ...
307-422 8.38e-31

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: 114.23  E-value: 8.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319256     307 NVDIALPCATQNEVSGDEAKALvasGVKFVAEGANMGSTPEAISVFETARstatnakdaVWFGPPKAANLGGVAVSGLEM 386
Cdd:smart00839   2 NCDIFIPCALQNVINEANANRL---GAKIIAEGANMPLTDEADDILEDRG---------VLYAPDFAANAGGVIVSALEM 69
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 6319256     387 AQNSQKvtwTAERVDQELKKIMINCFNDCIQAAQEY 422
Cdd:smart00839  70 LQNLAR---TAEEVFTDLSEIMRNALEEIFETAQKY 102
 
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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