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Conserved domains on  [gi|197927274|ref|NP_001128142|]
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4-hydroxy-2-oxoglutarate aldolase, mitochondrial isoform 2 [Homo sapiens]

Protein Classification

dihydrodipicolinate synthase family protein( domain architecture ID 10087124)

dihydrodipicolinate synthase family protein belongs to the pyruvate-dependent class I aldolases

CATH:  3.20.20.70
EC:  4.-.-.-
Gene Ontology:  GO:0009436|GO:0071704|GO:0016829
PubMed:  28271480|1463470
SCOP:  4003216

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 70-158 5.76e-21

Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.


:

Pssm-ID: 188630 [Multi-domain]  Cd Length: 281  Bit Score: 86.45  E-value: 5.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274  70 RGAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELSPA 149
Cdd:cd00408  193 LGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLSEE 272


                 ....*....
gi 197927274 150 EEEALRMDF 158
Cdd:cd00408  273 ERAKLEALL 281
 
Name Accession Description Interval E-value
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 70-158 5.76e-21

Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.


Pssm-ID: 188630 [Multi-domain]  Cd Length: 281  Bit Score: 86.45  E-value: 5.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274  70 RGAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELSPA 149
Cdd:cd00408  193 LGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLSEE 272


                 ....*....
gi 197927274 150 EEEALRMDF 158
Cdd:cd00408  273 ERAKLEALL 281
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 71-155 7.63e-18

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 77.89  E-value: 7.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274  71 GAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELSPAE 150
Cdd:COG0329  198 GADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLIRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEE 277


                 ....*
gi 197927274 151 EEALR 155
Cdd:COG0329  278 RAELR 282
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 71-155 1.90e-04

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 40.36  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274  71 GAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQH---RLIEPNAAVtrrfGI-PGLKKIMDWFGYYGGPCRAPLQEL 146
Cdd:PRK04147 200 GADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHecnDVIDLLIKN----GVyPGLKEILHYMGVDAGLCRKPFKPV 275


                 ....*....
gi 197927274 147 SPAEEEALR 155
Cdd:PRK04147 276 DEKYLPALK 284
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 71-155 4.81e-03

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 36.19  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274   71 GAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGP-CRAPLQELSPA 149
Cdd:pfam00701 198 GADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEE 277


                  ....*.
gi 197927274  150 EEEALR 155
Cdd:pfam00701 278 ERPELE 283
 
Name Accession Description Interval E-value
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 70-158 5.76e-21

Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.


Pssm-ID: 188630 [Multi-domain]  Cd Length: 281  Bit Score: 86.45  E-value: 5.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274  70 RGAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELSPA 149
Cdd:cd00408  193 LGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALFKEGNPAPVKAALALLGLDAGPVRLPLVPLSEE 272


                 ....*....
gi 197927274 150 EEEALRMDF 158
Cdd:cd00408  273 ERAKLEALL 281
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 71-155 7.63e-18

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 77.89  E-value: 7.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274  71 GAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELSPAE 150
Cdd:COG0329  198 GADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLIRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEE 277


                 ....*
gi 197927274 151 EEALR 155
Cdd:COG0329  278 RAELR 282
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 71-156 3.16e-08

N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases.


Pssm-ID: 188641 [Multi-domain]  Cd Length: 288  Bit Score: 51.16  E-value: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274  71 GAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGPCRAPLQELSPAE 150
Cdd:cd00954  199 GADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDVITVLIKNGLYPTLKAILRLMGLDAGPCRLPLRKVTEKA 278


                 ....*.
gi 197927274 151 EEALRM 156
Cdd:cd00954  279 LAKAKE 284
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 71-155 1.90e-04

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 40.36  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274  71 GAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQH---RLIEPNAAVtrrfGI-PGLKKIMDWFGYYGGPCRAPLQEL 146
Cdd:PRK04147 200 GADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHecnDVIDLLIKN----GVyPGLKEILHYMGVDAGLCRKPFKPV 275


                 ....*....
gi 197927274 147 SPAEEEALR 155
Cdd:PRK04147 276 DEKYLPALK 284
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 71-155 4.81e-03

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 36.19  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927274   71 GAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAAVTRRFGIPGLKKIMDWFGYYGGP-CRAPLQELSPA 149
Cdd:pfam00701 198 GADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLIKILFAEPNPIPIKTALELLGLVVGPtCRLPLTPLSEE 277


                  ....*.
gi 197927274  150 EEEALR 155
Cdd:pfam00701 278 ERPELE 283
 
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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