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Conserved domains on  [gi|2078422651|ref|XP_023744068|]
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uncharacterized protein LOC111892229 [Lactuca sativa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06522 super family cl46902
2-dehydropantoate 2-reductase; Reviewed
96-307 8.06e-05

2-dehydropantoate 2-reductase; Reviewed


The actual alignment was detected with superfamily member TIGR00745:

Pssm-ID: 481242 [Multi-domain]  Cd Length: 293  Bit Score: 43.83  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651  96 IIVGGGRVGKALQQMGagedLLV--KRGEPV---------PIDFPGP--ILVCTRNDDLDAVLQSTPQ--SRWNDLVFFQ 160
Cdd:TIGR00745  18 TLLARGEQLEALNQEG----LRIvsLGGEFQfrpvsaatsPEELPPAdlVIITVKAYQTEEAAALLLPliGKNTKVLFLQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651 161 NGM--LEPWFEskgLGDADQVLA---YFAVAKLGeppiDGITDTNPEGLTaAFGKWGS------AVADRLRAGGLSckvL 229
Cdd:TIGR00745  94 NGLghEERLRE---LLPARRILGgvvTHGAVREE----PGVVHHAGLGAT-KIGDYVGeneaveALAELLNEAGIP---A 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651 230 EKEP-FQKQMLEKLIWISAFMLVGARHpGATVGAV--EKDFRSEVGSLISELASAAATEKGIVFEEGVEERLCAYARAVS 306
Cdd:TIGR00745 163 ELHGdILAAIWKKLLVNAAINPLTALL-DCKNGELleNPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVIRMTA 241

                  .
gi 2078422651 307 H 307
Cdd:TIGR00745 242 E 242
 
Name Accession Description Interval E-value
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
96-307 8.06e-05

2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate 2-reductase, one of four enzymes required for the de novo biosynthesis of pantothenate (vitamin B5) from Asp and 2-oxoisovalerate. Although few members of the seed alignment are characterized experimentally, nearly all from complete genomes are found in a genome-wide (but not local) context of all three other pantothenate-biosynthetic enzymes (TIGR00222, TIGR00018, TIGR00223). The gene encoding this enzyme is designated apbA in Salmonella typhimurium and panE in Escherichia coli; this protein functions as a monomer and functions in the alternative pyrimidine biosynthetic, or APB, pathway, used to synthesize the pyrimidine moiety of thiamine. Note, synthesis of the pyrimidine moiety of thiamine occurs either via the first five steps in de novo purine biosynthesis, which uses the pur gene products, or through the APB pathway. Note that this family includes both NADH and NADPH-dependent enzymes, and enzymes with broad specificity, such as a D-mandelate dehydrogease that is also a 2-dehydropantoate 2-reductase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273247 [Multi-domain]  Cd Length: 293  Bit Score: 43.83  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651  96 IIVGGGRVGKALQQMGagedLLV--KRGEPV---------PIDFPGP--ILVCTRNDDLDAVLQSTPQ--SRWNDLVFFQ 160
Cdd:TIGR00745  18 TLLARGEQLEALNQEG----LRIvsLGGEFQfrpvsaatsPEELPPAdlVIITVKAYQTEEAAALLLPliGKNTKVLFLQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651 161 NGM--LEPWFEskgLGDADQVLA---YFAVAKLGeppiDGITDTNPEGLTaAFGKWGS------AVADRLRAGGLSckvL 229
Cdd:TIGR00745  94 NGLghEERLRE---LLPARRILGgvvTHGAVREE----PGVVHHAGLGAT-KIGDYVGeneaveALAELLNEAGIP---A 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651 230 EKEP-FQKQMLEKLIWISAFMLVGARHpGATVGAV--EKDFRSEVGSLISELASAAATEKGIVFEEGVEERLCAYARAVS 306
Cdd:TIGR00745 163 ELHGdILAAIWKKLLVNAAINPLTALL-DCKNGELleNPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVIRMTA 241

                  .
gi 2078422651 307 H 307
Cdd:TIGR00745 242 E 242
 
Name Accession Description Interval E-value
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
96-307 8.06e-05

2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate 2-reductase, one of four enzymes required for the de novo biosynthesis of pantothenate (vitamin B5) from Asp and 2-oxoisovalerate. Although few members of the seed alignment are characterized experimentally, nearly all from complete genomes are found in a genome-wide (but not local) context of all three other pantothenate-biosynthetic enzymes (TIGR00222, TIGR00018, TIGR00223). The gene encoding this enzyme is designated apbA in Salmonella typhimurium and panE in Escherichia coli; this protein functions as a monomer and functions in the alternative pyrimidine biosynthetic, or APB, pathway, used to synthesize the pyrimidine moiety of thiamine. Note, synthesis of the pyrimidine moiety of thiamine occurs either via the first five steps in de novo purine biosynthesis, which uses the pur gene products, or through the APB pathway. Note that this family includes both NADH and NADPH-dependent enzymes, and enzymes with broad specificity, such as a D-mandelate dehydrogease that is also a 2-dehydropantoate 2-reductase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273247 [Multi-domain]  Cd Length: 293  Bit Score: 43.83  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651  96 IIVGGGRVGKALQQMGagedLLV--KRGEPV---------PIDFPGP--ILVCTRNDDLDAVLQSTPQ--SRWNDLVFFQ 160
Cdd:TIGR00745  18 TLLARGEQLEALNQEG----LRIvsLGGEFQfrpvsaatsPEELPPAdlVIITVKAYQTEEAAALLLPliGKNTKVLFLQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651 161 NGM--LEPWFEskgLGDADQVLA---YFAVAKLGeppiDGITDTNPEGLTaAFGKWGS------AVADRLRAGGLSckvL 229
Cdd:TIGR00745  94 NGLghEERLRE---LLPARRILGgvvTHGAVREE----PGVVHHAGLGAT-KIGDYVGeneaveALAELLNEAGIP---A 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078422651 230 EKEP-FQKQMLEKLIWISAFMLVGARHpGATVGAV--EKDFRSEVGSLISELASAAATEKGIVFEEGVEERLCAYARAVS 306
Cdd:TIGR00745 163 ELHGdILAAIWKKLLVNAAINPLTALL-DCKNGELleNPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVIRMTA 241

                  .
gi 2078422651 307 H 307
Cdd:TIGR00745 242 E 242
 
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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