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Conserved domains on  [gi|119622782|gb|EAX02377|]
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transaldolase 1, isoform CRA_a, partial [Homo sapiens]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 1-72 5.58e-38

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member cd00957:

Pssm-ID: 473867 [Multi-domain]  Cd Length: 313  Bit Score: 127.73  E-value: 5.58e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119622782   1 MPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:cd00957   43 LPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGTEILKLIPGRVSTEVDARLSFDTNATIAKARKLI 114
 
Name Accession Description Interval E-value
Transaldolase_TalAB cd00957
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ...
 1-72 5.58e-38

Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The enzyme catalyses the reversible transfer of a dyhydroxyacetone moiety, derived from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. The catalytic mechanism is similar to other class I aldolases. The enzyme is found in the non-oxidative branch of the pentose phosphate pathway and forms a dimer in solution.


Pssm-ID: 188644 [Multi-domain]  Cd Length: 313  Bit Score: 127.73  E-value: 5.58e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119622782   1 MPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:cd00957   43 LPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGTEILKLIPGRVSTEVDARLSFDTNATIAKARKLI 114
PRK05269 PRK05269
transaldolase B; Provisional
 1-72 9.96e-37

transaldolase B; Provisional


Pssm-ID: 235381 [Multi-domain]  Cd Length: 318  Bit Score: 124.50  E-value: 9.96e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119622782   1 MPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:PRK05269  45 IPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVNFGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLI 116
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 39-72 7.99e-11

Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.


Pssm-ID: 395737 [Multi-domain]  Cd Length: 226  Bit Score: 54.85  E-value: 7.99e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 119622782   39 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:pfam00923  45 AEIKEIGDGPVSLEVDPRLADDTEGTIEEARRLI 78
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 26-72 7.80e-10

Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439946 [Multi-domain]  Cd Length: 214  Bit Score: 52.00  E-value: 7.80e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119622782  26 IKNAIDKLFVLFGAEILKKIPGRVSTEVdarLSFDKDAMVARARRLI 72
Cdd:COG0176   32 IAKAGIKDFVEDIREICDIVDGPVSAEV---LATDTEGMIAEARRLA 75
 
Name Accession Description Interval E-value
Transaldolase_TalAB cd00957
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ...
 1-72 5.58e-38

Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The enzyme catalyses the reversible transfer of a dyhydroxyacetone moiety, derived from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. The catalytic mechanism is similar to other class I aldolases. The enzyme is found in the non-oxidative branch of the pentose phosphate pathway and forms a dimer in solution.


Pssm-ID: 188644 [Multi-domain]  Cd Length: 313  Bit Score: 127.73  E-value: 5.58e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119622782   1 MPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:cd00957   43 LPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGTEILKLIPGRVSTEVDARLSFDTNATIAKARKLI 114
PRK05269 PRK05269
transaldolase B; Provisional
 1-72 9.96e-37

transaldolase B; Provisional


Pssm-ID: 235381 [Multi-domain]  Cd Length: 318  Bit Score: 124.50  E-value: 9.96e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119622782   1 MPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:PRK05269  45 IPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVNFGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLI 116
PRK12346 PRK12346
transaldolase A; Provisional
 1-72 5.29e-35

transaldolase A; Provisional


Pssm-ID: 183458  Cd Length: 316  Bit Score: 120.21  E-value: 5.29e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119622782   1 MPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:PRK12346  44 LPQYQHLIDDAIAWGKKQGGTQEQQVVAACDKLAVNFGAEILKSVPGRVSTEVDARLSFDREKSIEKARHLV 115
Transaldolase cd00439
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ...
 1-72 3.68e-27

Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates.


Pssm-ID: 188631 [Multi-domain]  Cd Length: 252  Bit Score: 98.19  E-value: 3.68e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119622782   1 MPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKI--PGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:cd00439   37 TSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYDQTeaDGRVSVEVSARLADDTQGMVEAAKYLS 110
PRK12309 PRK12309
transaldolase;
1-72 2.15e-26

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 98.65  E-value: 2.15e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119622782   1 MPAYQELVEEAIAYGRKLGGSQ---EDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:PRK12309  46 MPQYQSIVDETLRQARKELGSDapvEDVVALAFDRLAVAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLI 120
PTZ00411 PTZ00411
transaldolase-like protein; Provisional
 1-72 2.56e-26

transaldolase-like protein; Provisional


Pssm-ID: 240406  Cd Length: 333  Bit Score: 97.50  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622782   1 MPAYQELVEEAIAYGRKLGG----------SQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARR 70
Cdd:PTZ00411  45 MPEYAHLIDDAIKYAKANVSrlrdpllsdeEKEELVELVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARK 124


                 ..
gi 119622782  71 LI 72
Cdd:PTZ00411 125 II 126
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 39-72 7.99e-11

Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.


Pssm-ID: 395737 [Multi-domain]  Cd Length: 226  Bit Score: 54.85  E-value: 7.99e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 119622782   39 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLI 72
Cdd:pfam00923  45 AEIKEIGDGPVSLEVDPRLADDTEGTIEEARRLI 78
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 26-72 7.80e-10

Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439946 [Multi-domain]  Cd Length: 214  Bit Score: 52.00  E-value: 7.80e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119622782  26 IKNAIDKLFVLFGAEILKKIPGRVSTEVdarLSFDKDAMVARARRLI 72
Cdd:COG0176   32 IAKAGIKDFVEDIREICDIVDGPVSAEV---LATDTEGMIAEARRLA 75
PRK03343 PRK03343
transaldolase; Validated
 47-71 5.06e-04

transaldolase; Validated


Pssm-ID: 235117  Cd Length: 368  Bit Score: 36.34  E-value: 5.06e-04
                         10        20
                 ....*....|....*....|....*
gi 119622782  47 GRVSTEVDARLSFDKDAMVARARRL 71
Cdd:PRK03343 104 GRVSIEVSPRLAHDTEATIAEARRL 128
Transaldolase_like cd00955
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
 2-71 5.18e-03

Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants and bacteria. Transaldolase is found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates.


Pssm-ID: 188642 [Multi-domain]  Cd Length: 338  Bit Score: 33.45  E-value: 5.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119622782   2 PAYQELVEEAIAYGRKLGGSQED----QIKNAIDKLFVLFgaEILKKIPGRVSTEVDARLSFDKDAMVARARRL 71
Cdd:cd00955   44 AAYDDQIRALKGQGLDAEAIYEAlaieDIQDACDLLAPVY--EQTGGNDGYVSLEVSPRLADDTQGTIAEAKRL 115
 
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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