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Conserved domains on  [gi|1209301886|ref|WP_088347046|]
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MULTISPECIES: 2-dehydropantoate 2-reductase [Rhodomicrobium]

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
 4-335 4.13e-120

2-dehydropantoate 2-reductase; Reviewed


The actual alignment was detected with superfamily member PRK08229:

Pssm-ID: 481242 [Multi-domain]  Cd Length: 341  Bit Score: 349.30  E-value: 4.13e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   4 PDARITVAGAGSIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLSGFDERIPAARLSVTADPAALKAASLVLVT 83
Cdd:PRK08229    1 MMARICVLGAGSIGCYLGGRLAAAGADVTLIGRARIGDELRAHGLTLTDYRGRDVRVPPSAIAFSTDPAALATADLVLVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  84 VKSAATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVIEAGRA--E 161
Cdd:PRK08229   81 VKSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMVPFNVISRGPGAFHQGTSGALAIEASPAlrP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 162 LRALLAVPGLDLAVTADIAGVQWGKLLLNLNNALNALSGLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIVPVPGTPIA 241
Cdd:PRK08229  161 FAAAFARAGLPLVTHEDMRAVQWAKLLLNLNNAVNALSGLPLKEELAQRSYRRCLALAQREALRVLKAAGIRPARLTPLP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 242 ARFLPRILRLPTAIFRAVAAPMLQIDPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK-----R 316
Cdd:PRK08229  241 PAWIPRLLRLPDPLFRRLAGRMLAIDPLARSSMSDDLAAGRATEIDWINGEIVRLAGRLGAPAPVNARLCALVHeaeraG 320

                         330
                  ....*....|....*....
gi 1209301886 317 AEAAAAGPPGLTPDAVSAP 335
Cdd:PRK08229  321 ARPAWSGEALLAELRIAAP 339
 
Name Accession Description Interval E-value
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
 4-335 4.13e-120

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 349.30  E-value: 4.13e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   4 PDARITVAGAGSIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLSGFDERIPAARLSVTADPAALKAASLVLVT 83
Cdd:PRK08229    1 MMARICVLGAGSIGCYLGGRLAAAGADVTLIGRARIGDELRAHGLTLTDYRGRDVRVPPSAIAFSTDPAALATADLVLVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  84 VKSAATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVIEAGRA--E 161
Cdd:PRK08229   81 VKSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMVPFNVISRGPGAFHQGTSGALAIEASPAlrP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 162 LRALLAVPGLDLAVTADIAGVQWGKLLLNLNNALNALSGLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIVPVPGTPIA 241
Cdd:PRK08229  161 FAAAFARAGLPLVTHEDMRAVQWAKLLLNLNNAVNALSGLPLKEELAQRSYRRCLALAQREALRVLKAAGIRPARLTPLP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 242 ARFLPRILRLPTAIFRAVAAPMLQIDPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK-----R 316
Cdd:PRK08229  241 PAWIPRLLRLPDPLFRRLAGRMLAIDPLARSSMSDDLAAGRATEIDWINGEIVRLAGRLGAPAPVNARLCALVHeaeraG 320

                         330
                  ....*....|....*....
gi 1209301886 317 AEAAAAGPPGLTPDAVSAP 335
Cdd:PRK08229  321 ARPAWSGEALLAELRIAAP 339
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 7-315 4.25e-75

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: 233.21  E-value: 4.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   7 RITVAGAGSIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLsgfDERIPAARLSVTADPAALKAASLVLVTVKS 86
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESP---DGDRTTVPVPAVTDPEELGPADLVLVAVKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  87 AATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVIEAGR------- 159
Cdd:COG1893    79 YDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDggpserl 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 160 AELRALLAVPGLDLAVTADIAGVQWGKLLL-NLNNALNALSGLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIvpvpgt 238
Cdd:COG1893   159 EALAELLEAAGIPVEVSDDIRGALWEKLLLnAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGV------ 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209301886 239 piaarflprilRLPTAIFRAVAAPMLQIDPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK 315
Cdd:COG1893   233 -----------PLPEDDLEERVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLK 298
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 15-315 6.03e-57

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: 186.35  E-value: 6.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  15 SIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLsgfDERIPAARLSVTADPAALKAASLVLVTVKSAATKGMAG 94
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSL---GGEFQFRPVSAATSPEELPPADLVIITVKAYQTEEAAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  95 EIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVI------EAGRAELRALLAV 168
Cdd:TIGR00745  78 LLLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIgdyvgeNEAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 169 PGLDLAVTADIAGVQWGKLLLNLNN-ALNALSGLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIVPVPGtpiaarflpr 247
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAInPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDD---------- 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209301886 248 ilrlptAIFRAVAApMLQIDPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK 315
Cdd:TIGR00745 228 ------EVEELVRA-VIRMTAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLK 288
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 8-155 4.65e-34

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: 122.34  E-value: 4.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   8 ITVAGAGSIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLSGfDERIPAArlSVTADPAALKAASLVLVTVKSA 87
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLRLTSPGG-ERIVPPP--AVTSASESLGPIDLVIVTVKAY 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209301886  88 ATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVI 155
Cdd:pfam02558  78 QTEEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITI 145
 
Name Accession Description Interval E-value
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
 4-335 4.13e-120

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 349.30  E-value: 4.13e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   4 PDARITVAGAGSIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLSGFDERIPAARLSVTADPAALKAASLVLVT 83
Cdd:PRK08229    1 MMARICVLGAGSIGCYLGGRLAAAGADVTLIGRARIGDELRAHGLTLTDYRGRDVRVPPSAIAFSTDPAALATADLVLVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  84 VKSAATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVIEAGRA--E 161
Cdd:PRK08229   81 VKSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMVPFNVISRGPGAFHQGTSGALAIEASPAlrP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 162 LRALLAVPGLDLAVTADIAGVQWGKLLLNLNNALNALSGLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIVPVPGTPIA 241
Cdd:PRK08229  161 FAAAFARAGLPLVTHEDMRAVQWAKLLLNLNNAVNALSGLPLKEELAQRSYRRCLALAQREALRVLKAAGIRPARLTPLP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 242 ARFLPRILRLPTAIFRAVAAPMLQIDPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK-----R 316
Cdd:PRK08229  241 PAWIPRLLRLPDPLFRRLAGRMLAIDPLARSSMSDDLAAGRATEIDWINGEIVRLAGRLGAPAPVNARLCALVHeaeraG 320

                         330
                  ....*....|....*....
gi 1209301886 317 AEAAAAGPPGLTPDAVSAP 335
Cdd:PRK08229  321 ARPAWSGEALLAELRIAAP 339
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 7-315 4.25e-75

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: 233.21  E-value: 4.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   7 RITVAGAGSIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLsgfDERIPAARLSVTADPAALKAASLVLVTVKS 86
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESP---DGDRTTVPVPAVTDPEELGPADLVLVAVKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  87 AATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVIEAGR------- 159
Cdd:COG1893    79 YDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDggpserl 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 160 AELRALLAVPGLDLAVTADIAGVQWGKLLL-NLNNALNALSGLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIvpvpgt 238
Cdd:COG1893   159 EALAELLEAAGIPVEVSDDIRGALWEKLLLnAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGV------ 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209301886 239 piaarflprilRLPTAIFRAVAAPMLQIDPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK 315
Cdd:COG1893   233 -----------PLPEDDLEERVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLK 298
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 15-315 6.03e-57

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: 186.35  E-value: 6.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  15 SIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLsgfDERIPAARLSVTADPAALKAASLVLVTVKSAATKGMAG 94
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSL---GGEFQFRPVSAATSPEELPPADLVIITVKAYQTEEAAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  95 EIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVI------EAGRAELRALLAV 168
Cdd:TIGR00745  78 LLLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIgdyvgeNEAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 169 PGLDLAVTADIAGVQWGKLLLNLNN-ALNALSGLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIVPVPGtpiaarflpr 247
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAInPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDD---------- 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209301886 248 ilrlptAIFRAVAApMLQIDPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK 315
Cdd:TIGR00745 228 ------EVEELVRA-VIRMTAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLK 288
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 7-316 1.95e-48

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 164.64  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   7 RITVAGAGSIGCFIGGALARAGRKVTLLAR-PRMVEELQSCGLHLTDlsgfDERIPAARlsVTADPAALKAASLVLVTVK 85
Cdd:PRK06522    2 KIAILGAGAIGGLFGAALAQAGHDVTLVARrGAHLDALNENGLRLED----GEITVPVL--AADDPAELGPQDLVILAVK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  86 SAATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFN--------VVHMGEGRFHRGTSGQVVIEA 157
Cdd:PRK06522   76 AYQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAaelegpgvVRHTGGGRLKIGEPDGESAAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 158 grAELRALLAVPGLDLAVTADIAGVQWGKLLL-NLNNALNALSGLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIvpvp 236
Cdd:PRK06522  156 --EALADLLNAAGLDVEWSPDIRTEIWRKLWVnCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGV---- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 237 gtpiaarflprilRLPTAIFRAVAAPMLQIDPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVKR 316
Cdd:PRK06522  230 -------------HLSVEEVREYVRQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKA 296
PRK12921 PRK12921
oxidoreductase;
7-315 2.50e-37

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 135.37  E-value: 2.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   7 RITVAGAGSIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLSGfDERIPaarLSVTADPAALKA-ASLVLVTVK 85
Cdd:PRK12921    2 RIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPKRAKALRERGLVIRSDHG-DAVVP---GPVITDPEELTGpFDLVILAVK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  86 SAATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFN--------VVHMGEGRFHRGTSGQVVIEA 157
Cdd:PRK12921   78 AYQLDAAIPDLKPLVGEDTVIIPLQNGIGQLEQLEPYFGRERVLGGVVFISaqlngdgvVVQRADHRLTFGEIPGQRSER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 158 GRAeLRALLAVPGLDLAVTADIAGVQWGKLLLNLNNALNALSG-LPLREQLQDRAWRRLMAAQIEEALAVYAAAGIVPVP 236
Cdd:PRK12921  158 TRA-VRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGrATVGGILSRPGGRDLARALLRECLAVARAEGAPLRD 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209301886 237 GTPIaarflpRILRlptaIFRAVAAPMlqidpeaRSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK 315
Cdd:PRK12921  237 DVVE------EIVK----IFAGAPGDM-------KTSMLRDMEKGRPLEIDHLQGVLLRRARAHGIPTPILDTVYALLK 298
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 8-155 4.65e-34

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: 122.34  E-value: 4.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   8 ITVAGAGSIGCFIGGALARAGRKVTLLARPRMVEELQSCGLHLTDLSGfDERIPAArlSVTADPAALKAASLVLVTVKSA 87
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLRLTSPGG-ERIVPPP--AVTSASESLGPIDLVIVTVKAY 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209301886  88 ATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGVVGFNVVHMGEGRFHRGTSGQVVI 155
Cdd:pfam02558  78 QTEEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITI 145
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
 200-315 6.96e-18

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: 78.42  E-value: 6.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 200 GLPLREQLQDRAWRRLMAAQIEEALAVYAAAGIvpvpgtpiaarflprilRLPTAIFRAVAAPMLQIDPEARSSMWEDLV 279
Cdd:pfam08546  24 GCTNGELLDSPEARALIRALMREAVAVAQAEGV-----------------ALSEDRLIEYVLAVLRKTPDNKSSMLQDVE 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1209301886 280 RRRPTEIDFLQGAILRLARRHGVAAPLCERVAALVK 315
Cdd:pfam08546  87 AGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLK 122
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
1-313 2.35e-17

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 81.16  E-value: 2.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   1 MPGPDARITVAGAGSIGCFIGGALARAGRKVTLLARpRMVEELQSCGLHLTDLSGfDERIPAARlsVTADPAALKAASLV 80
Cdd:PRK06249    1 MDSETPRIGIIGTGAIGGFYGAMLARAGFDVHFLLR-SDYEAVRENGLQVDSVHG-DFHLPPVQ--AYRSAEDMPPCDWV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  81 LVTVKSAATKGMAGEIAAQRTPGAVVLSLQNGVDNLPALRSLLGETNVLGGV-------VGFNVV-HMGEGR----FHRG 148
Cdd:PRK06249   77 LVGLKTTANALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAEHLLGGLcficsnrVGPGVIhHLAYGRvnlgYHSG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 149 TSGQVVIEAGRAELRALLAVPGLDLAVTADIAGVQWGKlllnlNNALNALSGL------PLREQLQDRAWRRLMAAQIEE 222
Cdd:PRK06249  157 PAADDGITARVEEGAALFRAAGIDSQAMPDLAQARWQK-----LVWNIPYNGLsvllnaSTDPLMADPDSRALIRALMAE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 223 ALAVYAAAGIvpvpgtPIAARFLPRILrlptaifrAVAAPMlqidPEARSSMWEDLVRRRPTEIDFLQGAILRLARRHGV 302
Cdd:PRK06249  232 VIQGAAACGH------TLPEGYADHML--------AVTERM----PDYRPSMYHDFEEGRPLELEAIYANPLAAARAAGC 293

                         330
                  ....*....|.
gi 1209301886 303 AAPlceRVAAL 313
Cdd:PRK06249  294 AMP---RVEML 301
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
6-109 3.06e-10

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


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 60.47  E-value: 3.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   6 ARITVAGAGSIGCFIGGALARAGRKVTLLAR-PRMVEELQSCGLHLTDLSGFdeRIPAArLSVTADPA-ALKAASLVLVT 83
Cdd:PRK00094    2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARdPEQAAEINADRENPRYLPGI--KLPDN-LRATTDLAeALADADLILVA 78

                          90       100
                  ....*....|....*....|....*.
gi 1209301886  84 VKSAATKGMAGEIAAQRTPGAVVLSL 109
Cdd:PRK00094   79 VPSQALREVLKQLKPLLPPDAPIVWA 104
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 6-109 3.85e-09

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: 56.97  E-value: 3.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   6 ARITVAGAGSIGCFIGGALARAGRKVTLLAR-PRMVEELQSCGLHLTDLSGFdeRIPaARLSVTADPA-ALKAASLVLVT 83
Cdd:COG0240     1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRdPEVAEEINETRENPRYLPGV--KLP-ENLRATSDLEeALAGADLVLLA 77

                          90       100
                  ....*....|....*....|....*.
gi 1209301886  84 VKSAATKGMAGEIAAQRTPGAVVLSL 109
Cdd:COG0240    78 VPSQALREVLEQLAPLLPPGAPVVSA 103
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
6-305 1.16e-05

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 46.24  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   6 ARITVAGAGSIGCFIGGALARAGRKVTLLAR--PRMVEELQSCGLHLtdlsgfDERIPAARLSVTAD-PAALKAASLVLV 82
Cdd:PRK05708    3 MTWHILGAGSLGSLWACRLARAGLPVRLILRdrQRLAAYQQAGGLTL------VEQGQASLYAIPAEtADAAEPIHRLLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886  83 TVKSAATKGMAGEIAAQRTPGAVVLSLQNGV-------DNLPALRSLLGETNVLGGVVG-FNVVHMGEGRFHRGTSGQVV 154
Cdd:PRK05708   77 ACKAYDAEPAVASLAHRLAPGAELLLLQNGLgsqdavaARVPHARCIFASSTEGAFRDGdWRVVFAGHGFTWLGDPRNPT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886 155 IEAGRAELRAllavPGLDLAVTADIAGVQWGKLLLNLNNAlnalsglPLREQLQDRAWRRLMAAQIEEALAVYAAAgIVP 234
Cdd:PRK05708  157 APAWLDDLRE----AGIPHEWTVDILTRLWRKLALNCAIN-------PLTVLHDCRNGGLLEHAQEVAALCAELSE-LLR 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209301886 235 VPGTPIAARFL-PRILRlptaIFRAVAAPMlqidpearSSMWEDLVRRRPTEIDFLQGAILRLARRHGVAAP 305
Cdd:PRK05708  225 RCGQPAAAANLhEEVQR----VIQATAANY--------SSMYQDVRAGRRTEISYLLGYACRAADRHGLPLP 284
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
 8-113 8.49e-05

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: 42.18  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   8 ITVAGAGSIGCFIGGALARAGRKVTLLAR-PRMVEELQSCGLHLTDLSGFDerIPAArLSVTADPA-ALKAASLVLVTVK 85
Cdd:pfam01210   2 IAVLGAGSWGTALAKVLADNGHEVRLWGRdEELIEEINTTHENVRYLPGIK--LPEN-LKATTDLAeALKGADIIVIVVP 78

                          90       100
                  ....*....|....*....|....*...
gi 1209301886  86 SAATKGMAGEIAAQRTPGAVVLSLQNGV 113
Cdd:pfam01210  79 SQALREVLKQLKGLLKPDAILVSLSKGI 106
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 7-80 2.45e-03

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: 38.94  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301886   7 RITVAGAGSIGCFIGGALARAGRKVTLL---------ARPRMVEELQscglHLTDLSGFDERIPAA---RLSVTADPAAL 74
Cdd:COG1250     4 KVAVIGAGTMGAGIAAVFANAGYEVVLLdispealerARARIAKLLD----KLVKKGKLTEEEADAalaRITPTTDLAAL 79


                  ....*.
gi 1209301886  75 KAASLV 80
Cdd:COG1250    80 ADADLV 85
 
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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