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Conserved domains on  [gi|759450879|ref|WP_043172420|]
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ketopantoate reductase family protein [Bordetella bronchiseptica]

Protein Classification

ketopantoate reductase family protein( domain architecture ID 11449024)

ketopantoate reductase family protein similar to 2-dehydropantoate 2-reductase, which catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid

CATH:  3.40.50.720|1.10.1040.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  20180265|20876192|30945211|31869345|25704928
SCOP:  4000112

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-303 3.26e-91

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 273.27  E-value: 3.26e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAeHVQAMSEQGLRVEGASGDR-VARLRAYRE-APAEPVDLIIIAVKAA 78
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGA-HAEALRENGLRLESPDGDRtTVPVPAVTDpEELGPADLVLVAVKAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  79 QAGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAaFGASLSGPGHVHHNGMSAVRMGAYAGLGAEKL 158
Cdd:COG1893   80 DLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVT-IGATREEPGVVRHTGGGRLVLGELDGGPSERL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 159 DGIAEVWRGAGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAVED 238
Cdd:COG1893  159 EALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDD 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759450879 239 PVAHVRAFGERIRGAKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQREEA 303
Cdd:COG1893  239 LEERVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAG 303
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-303 3.26e-91

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 273.27  E-value: 3.26e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAeHVQAMSEQGLRVEGASGDR-VARLRAYRE-APAEPVDLIIIAVKAA 78
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGA-HAEALRENGLRLESPDGDRtTVPVPAVTDpEELGPADLVLVAVKAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  79 QAGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAaFGASLSGPGHVHHNGMSAVRMGAYAGLGAEKL 158
Cdd:COG1893   80 DLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVT-IGATREEPGVVRHTGGGRLVLGELDGGPSERL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 159 DGIAEVWRGAGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAVED 238
Cdd:COG1893  159 EALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDD 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759450879 239 PVAHVRAFGERIRGAKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQREEA 303
Cdd:COG1893  239 LEERVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAG 303
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-305 1.12e-70

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 220.88  E-value: 1.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQGLRVEGasGDRVARLRAYREAPA-EPVDLIIIAVKAAQ 79
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLED--GEITVPVLAADDPAElGPQDLVILAVKAYQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  80 AGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAAfGASLSGPGHVHHNGMSAVRMGAYAGLGAEkLD 159
Cdd:PRK06522  79 LPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTH-AAELEGPGVVRHTGGGRLKIGEPDGESAA-AE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 160 GIAEVWRGAGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAVEDP 239
Cdd:PRK06522 157 ALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEEV 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759450879 240 VAHVRAFGERIRGAKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQREEAWK 305
Cdd:PRK06522 237 REYVRQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERG 302
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-303 4.79e-60

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: 193.29  E-value: 4.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   10 AMGSVYAGLLAANGHEVIAVDRWaEHVQAMSEQGLRVEGASGDRVARLRAYREAPAE--PVDLIIIAVKAAQAGSAAAQA 87
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARG-EQLEALNQEGLRIVSLGGEFQFRPVSAATSPEElpPADLVIITVKAYQTEEAAALL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   88 RAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAaFGASLSGPGHVHHNGMSAVRMGAYAGlGAEKLDGIAEVWRG 167
Cdd:TIGR00745  80 LPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVT-HGAVREEPGVVHHAGLGATKIGDYVG-ENEAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  168 AGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAvEDPVAHVRAFG 247
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLP-DDEVEELVRAV 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 759450879  248 ERIRGAKPSVML-DHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQREEA 303
Cdd:TIGR00745 237 IRMTAENTSSMLqDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-149 3.22e-38

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 132.36  E-value: 3.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879    3 IAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVqAMSEQGLRVEGASGDRVARLRAYREAPA--EPVDLIIIAVKAAQA 80
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELA-AIKKNGLRLTSPGGERIVPPPAVTSASEslGPIDLVIVTVKAYQT 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759450879   81 GSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIaAAFGASLSGPGHVHHNGMSAVRMGA 149
Cdd:pfam02558  80 EEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGV-TTHGAFREGPGHVHHAGPGRITIGE 147
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-303 3.26e-91

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 273.27  E-value: 3.26e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAeHVQAMSEQGLRVEGASGDR-VARLRAYRE-APAEPVDLIIIAVKAA 78
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGA-HAEALRENGLRLESPDGDRtTVPVPAVTDpEELGPADLVLVAVKAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  79 QAGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAaFGASLSGPGHVHHNGMSAVRMGAYAGLGAEKL 158
Cdd:COG1893   80 DLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVT-IGATREEPGVVRHTGGGRLVLGELDGGPSERL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 159 DGIAEVWRGAGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAVED 238
Cdd:COG1893  159 EALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDD 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759450879 239 PVAHVRAFGERIRGAKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQREEA 303
Cdd:COG1893  239 LEERVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAG 303
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-305 1.12e-70

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 220.88  E-value: 1.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQGLRVEGasGDRVARLRAYREAPA-EPVDLIIIAVKAAQ 79
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLED--GEITVPVLAADDPAElGPQDLVILAVKAYQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  80 AGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAAfGASLSGPGHVHHNGMSAVRMGAYAGLGAEkLD 159
Cdd:PRK06522  79 LPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTH-AAELEGPGVVRHTGGGRLKIGEPDGESAA-AE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 160 GIAEVWRGAGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAVEDP 239
Cdd:PRK06522 157 ALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEEV 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759450879 240 VAHVRAFGERIRGAKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQREEAWK 305
Cdd:PRK06522 237 REYVRQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERG 302
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-303 4.79e-60

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: 193.29  E-value: 4.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   10 AMGSVYAGLLAANGHEVIAVDRWaEHVQAMSEQGLRVEGASGDRVARLRAYREAPAE--PVDLIIIAVKAAQAGSAAAQA 87
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARG-EQLEALNQEGLRIVSLGGEFQFRPVSAATSPEElpPADLVIITVKAYQTEEAAALL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   88 RAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAaFGASLSGPGHVHHNGMSAVRMGAYAGlGAEKLDGIAEVWRG 167
Cdd:TIGR00745  80 LPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVT-HGAVREEPGVVHHAGLGATKIGDYVG-ENEAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  168 AGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAvEDPVAHVRAFG 247
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLP-DDEVEELVRAV 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 759450879  248 ERIRGAKPSVML-DHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQREEA 303
Cdd:TIGR00745 237 IRMTAENTSSMLqDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
PRK12921 PRK12921
oxidoreductase;
1-302 2.71e-47

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 160.79  E-value: 2.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAeHVQAMSEQGLRVEGASGDRVARLRAYR--EAPAEPVDLIIIAVKAA 78
Cdd:PRK12921   1 MRIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPK-RAKALRERGLVIRSDHGDAVVPGPVITdpEELTGPFDLVILAVKAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  79 QAGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAaFGASLSGPGHVHHNGMSAVRMGAYAGLGAEKL 158
Cdd:PRK12921  80 QLDAAIPDLKPLVGEDTVIIPLQNGIGQLEQLEPYFGRERVLGGVVF-ISAQLNGDGVVVQRADHRLTFGEIPGQRSERT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 159 DGIAEVWRGAGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAVED 238
Cdd:PRK12921 159 RAVRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGRATVGGILSRPGGRDLARALLRECLAVARAEGAPLRDDV 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759450879 239 PVAHVRAFGERIRGAKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQREE 302
Cdd:PRK12921 239 VEEIVKIFAGAPGDMKTSMLRDMEKGRPLEIDHLQGVLLRRARAHGIPTPILDTVYALLKAYEA 302
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
1-299 5.40e-40

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 142.02  E-value: 5.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRwaEHVQAMSEQGLRVEGASGD-RVARLRAYReAPAE--PVDLIIIAVKA 77
Cdd:PRK06249   6 PRIGIIGTGAIGGFYGAMLARAGFDVHFLLR--SDYEAVRENGLQVDSVHGDfHLPPVQAYR-SAEDmpPCDWVLVGLKT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  78 AQAGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIaAAFGASLSGPGHVHHNGMSAVRMGAYAGLGA-- 155
Cdd:PRK06249  83 TANALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAEHLLGGL-CFICSNRVGPGVIHHLAYGRVNLGYHSGPAAdd 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 156 ---EKLDGIAEVWRGAGFNAQAVDNLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGV 232
Cdd:PRK06249 162 gitARVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNASTDPLMADPDSRALIRALMAEVIQGAAACGH 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759450879 233 PVAvEDPVAHVRAFGERIRGAKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQ 299
Cdd:PRK06249 242 TLP-EGYADHMLAVTERMPDYRPSMYHDFEEGRPLELEAIYANPLAAARAAGCAMPRVEMLYQALEF 307
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-149 3.22e-38

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 132.36  E-value: 3.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879    3 IAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVqAMSEQGLRVEGASGDRVARLRAYREAPA--EPVDLIIIAVKAAQA 80
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELA-AIKKNGLRLTSPGGERIVPPPAVTSASEslGPIDLVIVTVKAYQT 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759450879   81 GSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIaAAFGASLSGPGHVHHNGMSAVRMGA 149
Cdd:pfam02558  80 EEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGV-TTHGAFREGPGHVHHAGPGRITIGE 147
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
 177-301 6.63e-33

Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 462514 [Multi-domain]  Cd Length: 125  Bit Score: 117.71  E-value: 6.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  177 NLPAMQWEKLICNVAYSAPCTLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVPVAVEDPVAHVRAFGERIRGAKPS 256
Cdd:pfam08546   1 DIRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGVALSEDRLIEYVLAVLRKTPDNKSS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 759450879  257 VMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTALVKQRE 301
Cdd:pfam08546  81 MLQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
 1-303 9.12e-22

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 93.53  E-value: 9.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRwAEHVQAMSEQGLRVEGASGDRV----ARLR-AYREAPAEPVDLIIIAV 75
Cdd:PRK08229   3 ARICVLGAGSIGCYLGGRLAAAGADVTLIGR-ARIGDELRAHGLTLTDYRGRDVrvppSAIAfSTDPAALATADLVLVTV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  76 KAAQAGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLAVGIAAaFGASLSGPGHVHHNGMSAVRMGAYAGLga 155
Cdd:PRK08229  82 KSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMVP-FNVISRGPGAFHQGTSGALAIEASPAL-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 156 eklDGIAEVWRGAGFNAQAVDNLPAMQWEKLICNV--AYSApctLTGLTIGEVLDAPHASAVSQAAATEAWNVARALGVP 233
Cdd:PRK08229 159 ---RPFAAAFARAGLPLVTHEDMRAVQWAKLLLNLnnAVNA---LSGLPLKEELAQRSYRRCLALAQREALRVLKAAGIR 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 234 VAVEDPV-------------AHVRAFGERIRG----AKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTAL 296
Cdd:PRK08229 233 PARLTPLppawiprllrlpdPLFRRLAGRMLAidplARSSMSDDLAAGRATEIDWINGEIVRLAGRLGAPAPVNARLCAL 312


                 ....*..
gi 759450879 297 VKQREEA 303
Cdd:PRK08229 313 VHEAERA 319
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
1-295 1.33e-10

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 60.88  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSE-QGLRVEGASGDRVARLRAYREAPAEPVDLIIIAVKAAQ 79
Cdd:PRK05708   3 MTWHILGAGSLGSLWACRLARAGLPVRLILRDRQRLAAYQQaGGLTLVEQGQASLYAIPAETADAAEPIHRLLLACKAYD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  80 AGSAAAQARAMLGPDTLVLTIQNGLGSADSVAEAIGAERLavgIAAAF--GASLSGPGHVHHNGMsavrmgAYAGLGaEK 157
Cdd:PRK05708  83 AEPAVASLAHRLAPGAELLLLQNGLGSQDAVAARVPHARC---IFASSteGAFRDGDWRVVFAGH------GFTWLG-DP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879 158 LDGIAEVW----RGAGFNAQAVDNLPAMQWEKLICNvaysapCTLTGLTI------GEVLDapHASAVsQAAATEAWNVA 227
Cdd:PRK05708 153 RNPTAPAWlddlREAGIPHEWTVDILTRLWRKLALN------CAINPLTVlhdcrnGGLLE--HAQEV-AALCAELSELL 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759450879 228 RALGVPVAVEDPVAHVRAFGERIRGAKPSVMLDHEQRRVSEIDYINGAIPRQAARAGILAPVNQTLTA 295
Cdd:PRK05708 224 RRCGQPAAAANLHEEVQRVIQATAANYSSMYQDVRAGRRTEISYLLGYACRAADRHGLPLPRLQHLQQ 291
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-133 2.88e-06

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 47.75  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYA-GLLAA--NGHEVIAVDRWAEHVQAMSEQgLRVEGASGDRVArlrayreapAEPVDLIIIAVKA 77
Cdd:COG0345    3 MKIGFIGAGNMGSAIIkGLLKSgvPPEDIIVSDRSPERLEALAER-YGVRVTTDNAEA---------AAQADVVVLAVKP 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879  78 AQAGSAAAQARAMLGPDTLVLTIQNGLgSADSVAEAIGAERLAV----GIAAAFGASLSG 133
Cdd:COG0345   73 QDLAEVLEELAPLLDPDKLVISIAAGV-TLATLEEALGGGAPVVrampNTPALVGEGVTA 131
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-74 5.10e-05

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 44.29  E-value: 5.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQGLRVegASGDrVARLRAYREAPAEPVDLIIIA 74
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLV--IVGD-ATDEEVLEEAGIEDADAVIAA 166
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 1-75 8.20e-05

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 42.62  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879    1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMS-------EQGLRvEGASGDRVARLRA---YREAPAEpVDL 70
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNsgqipiyEPGLD-ELVKANVSGRLSFttdYSTAIEE-ADV 78


                  ....*
gi 759450879   71 IIIAV 75
Cdd:pfam03721  79 IFIAV 83
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-116 1.07e-04

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 43.47  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMS-------EQGLR---VEGASGDrvaRLRA---YREApAEP 67
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNageipiyEPGLEelvARNVAAG---RLRFttdLAEA-VAE 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759450879  68 VDLIIIAVkaaqagsaaaqaramlGpdtlvlTIQNGLGSAD-----SVAEAIGA 116
Cdd:COG1004   77 ADVVFIAV----------------G------TPSDEDGSADlsyvlAAARSIGE 108
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
1-42 2.66e-04

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 41.98  E-value: 2.66e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQ 42
Cdd:PRK00094   2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINAD 43
trkA PRK09496
Trk system potassium transporter TrkA;
1-75 4.31e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 41.65  E-value: 4.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQgLRVEGASGDrVARLRAYREAPAEPVDLiIIAV 75
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDR-LDVRTVVGN-GSSPDVLREAGAEDADL-LIAV 72
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 1-71 5.24e-04

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 40.86  E-value: 5.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRwaehVQAMSEQGL-RVEGASGDRVARLRAYREAPAEPVDLI 71
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDI----SPEALERARaRIAKLLDKLVKKGKLTEEEADAALARI 70
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 1-75 5.91e-04

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 40.79  E-value: 5.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQGLRVEGASGDRV-ARLRAYREAPA--EPVDLIIIAV 75
Cdd:COG0240    1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLPGVKLpENLRATSDLEEalAGADLVLLAV 78
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-61 8.20e-04

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 40.50  E-value: 8.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQGLRVEGASGDRVARLRAYR 61
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPAPR 61
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 1-30 1.09e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 40.29  E-value: 1.09e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 759450879    1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVD 30
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVD 30
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-46 1.29e-03

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 39.71  E-value: 1.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 759450879   1 MKIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQGLRV 46
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARV 47
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-76 5.53e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 37.82  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759450879   1 MKIAIMGCGAMGS-VYAGLLAAN--GHEVIAVDRWAEHVQAMSEQ-GLRVEGASgdrvarlrayrEAPAEPVDLIIIAVK 76
Cdd:PRK11880   3 KKIGFIGGGNMASaIIGGLLASGvpAKDIIVSDPSPEKRAALAEEyGVRAATDN-----------QEAAQEADVVVLAVK 71
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
 2-42 7.51e-03

NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.


Pssm-ID: 395967 [Multi-domain]  Cd Length: 158  Bit Score: 36.40  E-value: 7.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 759450879    2 KIAIMGCGAMGSVYAGLLAANGHEVIAVDRWAEHVQAMSEQ 42
Cdd:pfam01210   1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTT 41
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-75 8.68e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 37.21  E-value: 8.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759450879   1 MKIAIMGCGAMGSVYA-GLLAANGHEVIAV-DRWAEHVQAMSEQGlrvegasgdRVARLRAYREAPAEP-VDLIIIAV 75
Cdd:COG0673    4 LRVGIIGAGGIGRAHApALAALPGVELVAVaDRDPERAEAFAEEY---------GVRVYTDYEELLADPdIDAVVIAT 72
 
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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