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Conserved domains on  [gi|167736376|ref|NP_001019827|]
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aspartate dehydrogenase domain-containing protein isoform 2 [Homo sapiens]

Protein Classification

L-aspartate dehydrogenase family protein( domain architecture ID 10395547)

L-aspartate dehydrogenase family protein catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate

CATH:  3.40.50.720
EC:  1.4.1.21
Gene Ontology:  GO:0033735|GO:0009435|GO:0070403
PubMed:  25704928|30945211|12496312

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Asp_DH_C pfam01958
Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate ...
 68-156 3.04e-21

Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta domain. Enzymatic characterization of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH. It has been proposed that in Thermotoga maritima, TM1643 catalyzes the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway.


:

Pssm-ID: 426531 [Multi-domain]  Cd Length: 87  Bit Score: 82.54  E-value: 3.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736376   68 TVLYEGPVRGLCPFAPRNSNTMAAAALAapSLGFDGVIGVLVADTSLtDMHVVDVELSGPRGPTGRSFAVHTRRENPAeP 147
Cdd:pfam01958   3 TVLFEGPAREAVKLFPKNVNVAAALALA--GIGFDRTRVRLVADPAA-DRNIHEIEVEGDFGEFRFRVENVPSPDNPK-T 78


                  ....*....
gi 167736376  148 GAVTGSATV 156
Cdd:pfam01958  79 SALAALSAI 87
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 12-35 2.25e-03

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member pfam03447:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 116  Bit Score: 36.13  E-value: 2.25e-03
                          10        20
                  ....*....|....*....|....
gi 167736376   12 RPDLVVEVAHPKIIHESGAQILRH 35
Cdd:pfam03447  58 DPDVVVECASSEAVAELVLDALKA 81
 
Name Accession Description Interval E-value
Asp_DH_C pfam01958
Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate ...
 68-156 3.04e-21

Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta domain. Enzymatic characterization of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH. It has been proposed that in Thermotoga maritima, TM1643 catalyzes the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway.


Pssm-ID: 426531 [Multi-domain]  Cd Length: 87  Bit Score: 82.54  E-value: 3.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736376   68 TVLYEGPVRGLCPFAPRNSNTMAAAALAapSLGFDGVIGVLVADTSLtDMHVVDVELSGPRGPTGRSFAVHTRRENPAeP 147
Cdd:pfam01958   3 TVLFEGPAREAVKLFPKNVNVAAALALA--GIGFDRTRVRLVADPAA-DRNIHEIEVEGDFGEFRFRVENVPSPDNPK-T 78


                  ....*....
gi 167736376  148 GAVTGSATV 156
Cdd:pfam01958  79 SALAALSAI 87
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 12-35 2.25e-03

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 36.13  E-value: 2.25e-03
                          10        20
                  ....*....|....*....|....
gi 167736376   12 RPDLVVEVAHPKIIHESGAQILRH 35
Cdd:pfam03447  58 DPDVVVECASSEAVAELVLDALKA 81
AspD COG1712
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
10-35 9.56e-03

L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];


Pssm-ID: 441318 [Multi-domain]  Cd Length: 263  Bit Score: 35.55  E-value: 9.56e-03
                         10        20
                 ....*....|....*....|....*.
gi 167736376  10 SRRPDLVVEVAHPKIIHESGAQILRH 35
Cdd:COG1712   57 AADPDLVVEAASQAAVREHGPAVLEA 82
 
Name Accession Description Interval E-value
Asp_DH_C pfam01958
Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate ...
 68-156 3.04e-21

Aspartate dehydrogenase, C-terminal; This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta domain. Enzymatic characterization of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH. It has been proposed that in Thermotoga maritima, TM1643 catalyzes the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway.


Pssm-ID: 426531 [Multi-domain]  Cd Length: 87  Bit Score: 82.54  E-value: 3.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167736376   68 TVLYEGPVRGLCPFAPRNSNTMAAAALAapSLGFDGVIGVLVADTSLtDMHVVDVELSGPRGPTGRSFAVHTRRENPAeP 147
Cdd:pfam01958   3 TVLFEGPAREAVKLFPKNVNVAAALALA--GIGFDRTRVRLVADPAA-DRNIHEIEVEGDFGEFRFRVENVPSPDNPK-T 78


                  ....*....
gi 167736376  148 GAVTGSATV 156
Cdd:pfam01958  79 SALAALSAI 87
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 12-35 2.25e-03

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 36.13  E-value: 2.25e-03
                          10        20
                  ....*....|....*....|....
gi 167736376   12 RPDLVVEVAHPKIIHESGAQILRH 35
Cdd:pfam03447  58 DPDVVVECASSEAVAELVLDALKA 81
AspD COG1712
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
10-35 9.56e-03

L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];


Pssm-ID: 441318 [Multi-domain]  Cd Length: 263  Bit Score: 35.55  E-value: 9.56e-03
                         10        20
                 ....*....|....*....|....*.
gi 167736376  10 SRRPDLVVEVAHPKIIHESGAQILRH 35
Cdd:COG1712   57 AADPDLVVEAASQAAVREHGPAVLEA 82
 
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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