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Conserved domains on  [gi|574607747|emb|CDL72886|]
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NAD-glutamate dehydrogenase, partial [uncultured Zetaproteobacteria bacterium]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Bac_GDH super family cl29306
Bacterial NAD-glutamate dehydrogenase; This family consists of several bacterial proteins ...
69-195 1.60e-11

Bacterial NAD-glutamate dehydrogenase; This family consists of several bacterial proteins which are closely related to NAD-glutamate dehydrogenase found in Streptomyces clavuligerus. Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyze the reversible oxidative deamination of glutamate to ketoglutarate and ammonia.


The actual alignment was detected with superfamily member pfam05088:

Pssm-ID: 452960 [Multi-domain]  Cd Length: 1530  Bit Score: 66.36  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574607747    69 FETTHRHIMVIaCPDQAFYPDAVRAYLQKQGIQPlqqYSVLYPhQFLDKKDGHGLLLIFHFAAATLPSIQY--------- 139
Cdd:pfam05088   13 WQSTHTVVEIV-NDDMPFLVDSVTMELNRQGLTI---HLVVHP-VLVVRRDADGKLVEVLPAADAAAGAAGeslihieid 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574607747   140 ----------VQQSVTHILQGVEASVTDFPDMLGTLENIAAHL--------AEDDAETADLLRWMLDDHYLLFG 195
Cdd:pfam05088   88 rqtdperleaLEAELERVLADVRAAVEDWPAMRARLLAIAAELetapppvsADEVEEAAAFLRWLADDHFTFLG 161
 
Name Accession Description Interval E-value
Bac_GDH pfam05088
Bacterial NAD-glutamate dehydrogenase; This family consists of several bacterial proteins ...
69-195 1.60e-11

Bacterial NAD-glutamate dehydrogenase; This family consists of several bacterial proteins which are closely related to NAD-glutamate dehydrogenase found in Streptomyces clavuligerus. Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyze the reversible oxidative deamination of glutamate to ketoglutarate and ammonia.


Pssm-ID: 428297 [Multi-domain]  Cd Length: 1530  Bit Score: 66.36  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574607747    69 FETTHRHIMVIaCPDQAFYPDAVRAYLQKQGIQPlqqYSVLYPhQFLDKKDGHGLLLIFHFAAATLPSIQY--------- 139
Cdd:pfam05088   13 WQSTHTVVEIV-NDDMPFLVDSVTMELNRQGLTI---HLVVHP-VLVVRRDADGKLVEVLPAADAAAGAAGeslihieid 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574607747   140 ----------VQQSVTHILQGVEASVTDFPDMLGTLENIAAHL--------AEDDAETADLLRWMLDDHYLLFG 195
Cdd:pfam05088   88 rqtdperleaLEAELERVLADVRAAVEDWPAMRARLLAIAAELetapppvsADEVEEAAAFLRWLADDHFTFLG 161
Gdh2 COG2902
NAD-specific glutamate dehydrogenase [Amino acid transport and metabolism];
69-195 1.40e-10

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


Pssm-ID: 442147 [Multi-domain]  Cd Length: 1607  Bit Score: 63.62  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574607747   69 FETTHRHIMVIaCPDQAFYPDAVRAYLQKQGIQPlqqYSVLYPhQFLDKKDGHGLLLIFHFAAATLP-----SIQYV--- 140
Cdd:COG2902    87 WQSTHTVVEIV-TDDMPFLVDSVTMELNRLGLTI---HLVVHP-VLAVERDADGELVEVLPADEAPAdglreSLIHIeid 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574607747  141 -----------QQSVTHILQGVEASVTDFPDMLGTLENIAAHL--------AEDDAETADLLRWMLDDHYLLFG 195
Cdd:COG2902   162 rqtdpealeelEAELERVLADVRAAVEDWPAMRARLLEIAAELeaapppvdADEVAEAAAFLRWLADDHFTFLG 235
 
Name Accession Description Interval E-value
Bac_GDH pfam05088
Bacterial NAD-glutamate dehydrogenase; This family consists of several bacterial proteins ...
69-195 1.60e-11

Bacterial NAD-glutamate dehydrogenase; This family consists of several bacterial proteins which are closely related to NAD-glutamate dehydrogenase found in Streptomyces clavuligerus. Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyze the reversible oxidative deamination of glutamate to ketoglutarate and ammonia.


Pssm-ID: 428297 [Multi-domain]  Cd Length: 1530  Bit Score: 66.36  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574607747    69 FETTHRHIMVIaCPDQAFYPDAVRAYLQKQGIQPlqqYSVLYPhQFLDKKDGHGLLLIFHFAAATLPSIQY--------- 139
Cdd:pfam05088   13 WQSTHTVVEIV-NDDMPFLVDSVTMELNRQGLTI---HLVVHP-VLVVRRDADGKLVEVLPAADAAAGAAGeslihieid 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574607747   140 ----------VQQSVTHILQGVEASVTDFPDMLGTLENIAAHL--------AEDDAETADLLRWMLDDHYLLFG 195
Cdd:pfam05088   88 rqtdperleaLEAELERVLADVRAAVEDWPAMRARLLAIAAELetapppvsADEVEEAAAFLRWLADDHFTFLG 161
Gdh2 COG2902
NAD-specific glutamate dehydrogenase [Amino acid transport and metabolism];
69-195 1.40e-10

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


Pssm-ID: 442147 [Multi-domain]  Cd Length: 1607  Bit Score: 63.62  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574607747   69 FETTHRHIMVIaCPDQAFYPDAVRAYLQKQGIQPlqqYSVLYPhQFLDKKDGHGLLLIFHFAAATLP-----SIQYV--- 140
Cdd:COG2902    87 WQSTHTVVEIV-TDDMPFLVDSVTMELNRLGLTI---HLVVHP-VLAVERDADGELVEVLPADEAPAdglreSLIHIeid 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574607747  141 -----------QQSVTHILQGVEASVTDFPDMLGTLENIAAHL--------AEDDAETADLLRWMLDDHYLLFG 195
Cdd:COG2902   162 rqtdpealeelEAELERVLADVRAAVEDWPAMRARLLEIAAELeaapppvdADEVAEAAAFLRWLADDHFTFLG 235
 
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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