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2-dehydropantoate 2-reductase [Thermococcus kodakarensis]

Protein Classification

2-dehydropantoate 2-reductase( domain architecture ID 11482284)

2-dehydropantoate 2-reductase catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid

CATH:  3.40.50.720|1.10.1040.10
EC:  1.1.1.169
Gene Ontology:  GO:0008677|GO:0015940|GO:0050661
SCOP:  4000112

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-296 1.89e-107

2-dehydropantoate 2-reductase; Reviewed


:

Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 314.87  E-value: 1.89e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRR-EQVDAINKNGLHVFGAEEFTVKPKATIYAPEEPPDLLILAVKSYSTK 79
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRgAHLDALNENGLRLEDGEITVPVLAADDPAELGPQDLVILAVKAYQLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  80 TALECARQCIGRNTWVLSIQNGLGNEELALKYTP--NVMGGVTTNGAMLVEWGKVLWAGKGITVIGRyPTGRDDFVDEVA 157
Cdd:PRK06522  81 AALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGpeRVLGGVVTHAAELEGPGVVRHTGGGRLKIGE-PDGESAAAEALA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 158 SVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPLELL 237
Cdd:PRK06522 160 DLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEEVREY 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 238 WDT-IERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKER 296
Cdd:PRK06522 240 VRQvIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKES 299
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-296 1.89e-107

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 314.87  E-value: 1.89e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRR-EQVDAINKNGLHVFGAEEFTVKPKATIYAPEEPPDLLILAVKSYSTK 79
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRgAHLDALNENGLRLEDGEITVPVLAADDPAELGPQDLVILAVKAYQLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  80 TALECARQCIGRNTWVLSIQNGLGNEELALKYTP--NVMGGVTTNGAMLVEWGKVLWAGKGITVIGRyPTGRDDFVDEVA 157
Cdd:PRK06522  81 AALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGpeRVLGGVVTHAAELEGPGVVRHTGGGRLKIGE-PDGESAAAEALA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 158 SVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPLELL 237
Cdd:PRK06522 160 DLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEEVREY 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 238 WDT-IERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKER 296
Cdd:PRK06522 240 VRQvIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKES 299
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-299 1.12e-105

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: 310.25  E-value: 1.12e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHVFGA--EEFTVKPKATIYAPE-EPPDLLILAVKSYS 77
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPdgDRTTVPVPAVTDPEElGPADLVLVAVKAYD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  78 TKTALECARQCIGRNTWVLSIQNGLGNEELALKYTP--NVMGGVTTNGAMLVEWGKVLWAGKGITVIGRYPTGRDDFVDE 155
Cdd:COG1893   81 LEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGaeRVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSERLEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 156 VASVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPLE 235
Cdd:COG1893  161 LAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDDLE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499570135 236 -LLWDTIERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKERINR 299
Cdd:COG1893  241 eRVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAGRA 305
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-296 8.97e-96

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: 284.58  E-value: 8.97e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   10 SIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHVFGA-EEFTVKP--KATIYAPEEPPDLLILAVKSYSTKTALECAR 86
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLgGEFQFRPvsAATSPEELPPADLVIITVKAYQTEEAAALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   87 QCIGRNTWVLSIQNGLGNEELALKY--TPNVMGGVTTNGAMLVEWGKVLWAGKGITVIGRYPtGRDDFVDEVASVFNEAG 164
Cdd:TIGR00745  81 PLIGKNTKVLFLQNGLGHEERLRELlpARRILGGVVTHGAVREEPGVVHHAGLGATKIGDYV-GENEAVEALAELLNEAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  165 IDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEF-EIHPLELLWDTIER 243
Cdd:TIGR00745 160 IPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLpDDEVEELVRAVIRM 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499570135  244 TRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKER 296
Cdd:TIGR00745 240 TAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEA 292
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-143 5.32e-46

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: 152.39  E-value: 5.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135    3 IYVLGAGSIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHVFGA-EEFTVKPKATIYAPE--EPPDLLILAVKSYSTK 79
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLRLTSPgGERIVPPPAVTSASEslGPIDLVIVTVKAYQTE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499570135   80 TALECARQCIGRNTWVLSIQNGLGNEELALKY--TPNVMGGVTTNGAMLVEWGKVLWAGKGITVIG 143
Cdd:pfam02558  81 EALEDIAPLLGPNTVVLLLQNGLGHEEVLREAvpRERVLGGVTTHGAFREGPGHVHHAGPGRITIG 146
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 5-59 3.84e-03

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 38.49  E-value: 3.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499570135   5 VLGAGSIGSLFGALLARAG-NDVTLIGRREQVDAINKNglhvFGAEEFTVKPKATI 59
Cdd:cd08269  135 VIGAGFIGLLFLQLAAAAGaRRVIAIDRRPARLALARE----LGATEVVTDDSEAI 186
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-296 1.89e-107

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 314.87  E-value: 1.89e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRR-EQVDAINKNGLHVFGAEEFTVKPKATIYAPEEPPDLLILAVKSYSTK 79
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRgAHLDALNENGLRLEDGEITVPVLAADDPAELGPQDLVILAVKAYQLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  80 TALECARQCIGRNTWVLSIQNGLGNEELALKYTP--NVMGGVTTNGAMLVEWGKVLWAGKGITVIGRyPTGRDDFVDEVA 157
Cdd:PRK06522  81 AALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGpeRVLGGVVTHAAELEGPGVVRHTGGGRLKIGE-PDGESAAAEALA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 158 SVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPLELL 237
Cdd:PRK06522 160 DLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEEVREY 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 238 WDT-IERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKER 296
Cdd:PRK06522 240 VRQvIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKES 299
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-299 1.12e-105

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: 310.25  E-value: 1.12e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHVFGA--EEFTVKPKATIYAPE-EPPDLLILAVKSYS 77
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPdgDRTTVPVPAVTDPEElGPADLVLVAVKAYD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  78 TKTALECARQCIGRNTWVLSIQNGLGNEELALKYTP--NVMGGVTTNGAMLVEWGKVLWAGKGITVIGRYPTGRDDFVDE 155
Cdd:COG1893   81 LEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGaeRVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSERLEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 156 VASVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPLE 235
Cdd:COG1893  161 LAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDDLE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499570135 236 -LLWDTIERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKERINR 299
Cdd:COG1893  241 eRVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAGRA 305
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-296 8.97e-96

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: 284.58  E-value: 8.97e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   10 SIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHVFGA-EEFTVKP--KATIYAPEEPPDLLILAVKSYSTKTALECAR 86
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLgGEFQFRPvsAATSPEELPPADLVIITVKAYQTEEAAALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   87 QCIGRNTWVLSIQNGLGNEELALKY--TPNVMGGVTTNGAMLVEWGKVLWAGKGITVIGRYPtGRDDFVDEVASVFNEAG 164
Cdd:TIGR00745  81 PLIGKNTKVLFLQNGLGHEERLRELlpARRILGGVVTHGAVREEPGVVHHAGLGATKIGDYV-GENEAVEALAELLNEAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  165 IDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEF-EIHPLELLWDTIER 243
Cdd:TIGR00745 160 IPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLpDDEVEELVRAVIRM 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499570135  244 TRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKER 296
Cdd:TIGR00745 240 TAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEA 292
PRK12921 PRK12921
oxidoreductase;
1-296 2.27e-49

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 166.19  E-value: 2.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHV-FGAEEFTVKPKATIyAPEE---PPDLLILAVKSY 76
Cdd:PRK12921   1 MRIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPKRAKALRERGLVIrSDHGDAVVPGPVIT-DPEEltgPFDLVILAVKAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  77 STKTALECARQCIGRNTWVLSIQNGLGNEELALKYTP--NVMGGVTTNGAMLVEWGKVLWAGKGITVIGRYPTGRDDFVD 154
Cdd:PRK12921  80 QLDAAIPDLKPLVGEDTVIIPLQNGIGQLEQLEPYFGreRVLGGVVFISAQLNGDGVVVQRADHRLTFGEIPGQRSERTR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 155 EVASVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPL 234
Cdd:PRK12921 160 AVRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGRATVGGILSRPGGRDLARALLRECLAVARAEGAPLRDDVV 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499570135 235 ELLWDTIERTREN-YNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKER 296
Cdd:PRK12921 240 EEIVKIFAGAPGDmKTSMLRDMEKGRPLEIDHLQGVLLRRARAHGIPTPILDTVYALLKAYEA 302
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-143 5.32e-46

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: 152.39  E-value: 5.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135    3 IYVLGAGSIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHVFGA-EEFTVKPKATIYAPE--EPPDLLILAVKSYSTK 79
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLRLTSPgGERIVPPPAVTSASEslGPIDLVIVTVKAYQTE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499570135   80 TALECARQCIGRNTWVLSIQNGLGNEELALKY--TPNVMGGVTTNGAMLVEWGKVLWAGKGITVIG 143
Cdd:pfam02558  81 EALEDIAPLLGPNTVVLLLQNGLGHEEVLREAvpRERVLGGVTTHGAFREGPGHVHHAGPGRITIG 146
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
1-299 5.57e-33

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 123.53  E-value: 5.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRREqVDAINKNGLHVFGAE-EFTVKPKATIYAPEEPP--DLLILAVKSYS 77
Cdd:PRK06249   6 PRIGIIGTGAIGGFYGAMLARAGFDVHFLLRSD-YEAVRENGLQVDSVHgDFHLPPVQAYRSAEDMPpcDWVLVGLKTTA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  78 TKTALECARQCIGRNTWVLSIQNGLGNEELALKYTPN--VMGGVTTNGAMLVEWGKVLWAGKGITVIGRY-----PTGRD 150
Cdd:PRK06249  85 NALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAehLLGGLCFICSNRVGPGVIHHLAYGRVNLGYHsgpaaDDGIT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 151 DFVDEVASVFNEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFE 230
Cdd:PRK06249 165 ARVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNASTDPLMADPDSRALIRALMAEVIQGAAACGHTLP 244

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499570135 231 IHPLELLWDTIERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKERINR 299
Cdd:PRK06249 245 EGYADHMLAVTERMPDYRPSMYHDFEEGRPLELEAIYANPLAAARAAGCAMPRVEMLYQALEFLDRRNR 313
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
 172-295 6.75e-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: 6.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  172 NAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDDPHLEGISVDIAREGCMVAQQLGIEFEIHPL-ELLWDTIERTRENYNS 250
Cdd:pfam08546   1 DIRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGVALSEDRLiEYVLAVLRKTPDNKSS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499570135  251 TLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELLWVLVKAKE 295
Cdd:pfam08546  81 MLQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
1-287 7.09e-30

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 115.20  E-value: 7.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGR-REQVDAINKNG---LHVFGAEEFTVKPKATIYAPEePPDLLILAVKSY 76
Cdd:PRK05708   3 MTWHILGAGSLGSLWACRLARAGLPVRLILRdRQRLAAYQQAGgltLVEQGQASLYAIPAETADAAE-PIHRLLLACKAY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  77 STKTALECARQCIGRNTWVLSIQNGLGNEELALKYTPN--VMGGVTTNGAMLVEWGKVLWAGKGITVIG--RYPTGRDdF 152
Cdd:PRK05708  82 DAEPAVASLAHRLAPGAELLLLQNGLGSQDAVAARVPHarCIFASSTEGAFRDGDWRVVFAGHGFTWLGdpRNPTAPA-W 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 153 VDEVAsvfnEAGIDTSVTENAIGWKWAKAIVNSVINGLGTVLEVKNGHLKDdpHLEGISVDIAREGCMV--------AQQ 224
Cdd:PRK05708 161 LDDLR----EAGIPHEWTVDILTRLWRKLALNCAINPLTVLHDCRNGGLLE--HAQEVAALCAELSELLrrcgqpaaAAN 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499570135 225 LGIEfeihplelLWDTIERTRENYNSTLQDIWRGRETEVDYIHGKIVEYARSVGMEAPRNELL 287
Cdd:PRK05708 235 LHEE--------VQRVIQATAANYSSMYQDVRAGRRTEISYLLGYACRAADRHGLPLPRLQHL 289
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
 1-296 2.04e-25

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 103.54  E-value: 2.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRREQVDAINKNGLHV--FGAEEFTVKPKATIYAPE----EPPDLLILAVK 74
Cdd:PRK08229   3 ARICVLGAGSIGCYLGGRLAAAGADVTLIGRARIGDELRAHGLTLtdYRGRDVRVPPSAIAFSTDpaalATADLVLVTVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  75 SYSTKTALECARQCIGRNTWVLSIQNGLGNEELALKYTPNVM---GGVTTNgamLVEWGKVLW--AGKGITVIGRYPTGR 149
Cdd:PRK08229  83 SAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATvlaGMVPFN---VISRGPGAFhqGTSGALAIEASPALR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 150 DdfvdeVASVFNEAGIDTSVTENAIGWKWAKAI--VNSVINGLGtvlevkNGHLKD---DPHLEGISVDIAREGCMVAQQ 224
Cdd:PRK08229 160 P-----FAAAFARAGLPLVTHEDMRAVQWAKLLlnLNNAVNALS------GLPLKEelaQRSYRRCLALAQREALRVLKA 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135 225 LGIE-FEIHPLELLW----------------------DTIERTrenynSTLQDIWRGRETEVDYIHGKIVEYARSVGMEA 281
Cdd:PRK08229 229 AGIRpARLTPLPPAWiprllrlpdplfrrlagrmlaiDPLARS-----SMSDDLAAGRATEIDWINGEIVRLAGRLGAPA 303

                        330
                 ....*....|....*
gi 499570135 282 PRNELLWVLVKAKER 296
Cdd:PRK08229 304 PVNARLCALVHEAER 318
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 1-44 5.27e-08

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: 53.50  E-value: 5.27e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRR-EQVDAINKNGLH 44
Cdd:COG0240    1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDpEVAEEINETREN 45
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
1-41 1.20e-07

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


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 52.38  E-value: 1.20e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRR-EQVDAINKN 41
Cdd:PRK00094   2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDpEQAAEINAD 43
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-98 8.89e-05

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: 43.13  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGS-LFGALLAR--AGNDVTLIGRR-EQVDAI-NKNGLHVFGAEEFTVKPkatiyapeepPDLLILAVKS 75
Cdd:COG0345    3 MKIGFIGAGNMGSaIIKGLLKSgvPPEDIIVSDRSpERLEALaERYGVRVTTDNAEAAAQ----------ADVVVLAVKP 72

                         90       100
                 ....*....|....*....|...
gi 499570135  76 YSTKTALECARQCIGRNTWVLSI 98
Cdd:COG0345   73 QDLAEVLEELAPLLDPDKLVISI 95
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-169 2.30e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 42.06  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGS-LFGALLAR--AGNDVTLIGRREQVDAinknglhvFGAEEFTVKPKATIYAPEEPPDLLILAVKSYS 77
Cdd:PRK11880   3 KKIGFIGGGNMASaIIGGLLASgvPAKDIIVSDPSPEKRA--------ALAEEYGVRAATDNQEAAQEADVVVLAVKPQV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135  78 TKTALECARQCIgrNTWVLSIQNGLGN---EELALKYTPNV--MggvtTNGAMLVewgkvlwaGKGITVIgrYPTGR--- 149
Cdd:PRK11880  75 MEEVLSELKGQL--DKLVVSIAAGVTLarlERLLGADLPVVraM----PNTPALV--------GAGMTAL--TANALvsa 138

                        170       180
                 ....*....|....*....|....*....
gi 499570135 150 --DDFVDEVASVF-------NEAGIDTSV 169
Cdd:PRK11880 139 edRELVENLLSAFgkvvwvdDEKQMDAVT 167
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
 3-41 2.42e-04

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: 40.64  E-value: 2.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 499570135    3 IYVLGAGSIGSLFGALLARAGNDVTLIGRR-EQVDAINKN 41
Cdd:pfam01210   2 IAVLGAGSWGTALAKVLADNGHEVRLWGRDeELIEEINTT 41
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 2-125 8.24e-04

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 40.84  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   2 RIYVLGAGSIGSLFGALLARAGNDVTLIGRREQV-----DAINKNGLHVFGAEEFTVKPKATIYAPEEPPDLLILAVKSY 76
Cdd:COG1249  170 SLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpgedPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDG 249

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499570135  77 STKTALECAR--QCIGR--NTwvlsiqNGLGNEELALKYTPNvmGGVTTNGAM 125
Cdd:COG1249  250 GGEEAVEADKvlVATGRrpNT------DGLGLEAAGVELDER--GGIKVDEYL 294
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
5-34 2.58e-03

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 39.05  E-value: 2.58e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 499570135   5 VLGA-GSIGSLFGALLARAGNDVTLIGRREQ 34
Cdd:COG5322  156 VVGAtGSIGSVCARLLAREVKRLTLVARNLE 186
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 5-59 3.84e-03

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 38.49  E-value: 3.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499570135   5 VLGAGSIGSLFGALLARAG-NDVTLIGRREQVDAINKNglhvFGAEEFTVKPKATI 59
Cdd:cd08269  135 VIGAGFIGLLFLQLAAAAGaRRVIAIDRRPARLALARE----LGATEVVTDDSEAI 186
PRK14618 PRK14618
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 1-120 4.26e-03

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


Pssm-ID: 237770 [Multi-domain]  Cd Length: 328  Bit Score: 38.31  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRR----EQVDAINKNGLHVFGA---EEftVKPKATIYAPEEPPDLLILAV 73
Cdd:PRK14618   5 MRVAVLGAGAWGTALAVLAASKGVPVRLWARRpefaAALAAERENREYLPGValpAE--LYPTADPEEALAGADFAVVAV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499570135  74 KSYSTKTALEcarqCIGRNTWVLSIQNGLGNEELALKYTPNVMGGVT 120
Cdd:PRK14618  83 PSKALRETLA----GLPRALGYVSCAKGLAPDGGRLSELARVLEFLT 125
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 1-28 6.26e-03

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 37.71  E-value: 6.26e-03
                         10        20
                 ....*....|....*....|....*...
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTL 28
Cdd:PRK06129   3 GSVAIIGAGLIGRAWAIVFARAGHEVRL 30
PRK00711 PRK00711
D-amino acid dehydrogenase;
1-33 7.74e-03

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 37.47  E-value: 7.74e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 499570135   1 MRIYVLGAGSIGSLFGALLARAGNDVTLIGRRE 33
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQP 33
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 3-87 8.94e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 35.64  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499570135    3 IYVLGAGSIGSLFGALLARAGN--DVTLIGR-REQVDAINKN-GLHVFGAEEFTVK-PKATIYAPEEPPDLLILAVKSYS 77
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFDvdRITVADRtLEKAQALAAKlGGVRFIAVAVDADnYEAVLAALLKEGDLVVNLSPPTL 80

                          90
                  ....*....|
gi 499570135   78 TKTALECARQ 87
Cdd:pfam03435  81 SLDVLKACIE 90
 
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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