NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|955349710|ref|XP_014619379|]
View 

3-dehydroquinate synthase isoform X1 [Glycine max]

Protein Classification

3-dehydroquinate synthase( domain architecture ID 10791474)

3-dehydroquinate synthase catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate to dehydroquinate in the shikimate pathway

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02834 PLN02834
3-dehydroquinate synthase
 3-416 0e+00

3-dehydroquinate synthase


:

Pssm-ID: 215448  Cd Length: 433  Bit Score: 717.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710   3 STATNFSLSLCANQQTPiPKPSFFSNNNHLHFNSnnnwawASVSTSRKSRICATSSQVMDPSAAKSEPALPTIVEVDLGS 82
Cdd:PLN02834   4 SSADNSESNTPTVLSRS-PSDAFFDQNSSIESSK------EGDLTEVIHEKCPVSGANKSEVTKTASATVTTVVKVDLGD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  83 RSYPIYIGSGLLNQPDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNPNVSVESVILPDGEQYKDMDTLMKVFDKA 162
Cdd:PLN02834  77 RSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 163 IESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLIDTD 242
Cdd:PLN02834 157 LESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 243 TLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 322
Cdd:PLN02834 237 TLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 323 FGH---------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPETVTVDMFKSVMAVDKKVADG 381
Cdd:PLN02834 317 FGHaietgpgygewlhgeavaagtVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAVDKKVADG 396

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 955349710 382 LLRLILLKGPLGNCVFTGDYDRKALDNTLRAFCKS 416
Cdd:PLN02834 397 LLRLILLKGELGNCVFTGDFDREALEETLRAFCKS 431
 
Name Accession Description Interval E-value
PLN02834 PLN02834
3-dehydroquinate synthase
 3-416 0e+00

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 717.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710   3 STATNFSLSLCANQQTPiPKPSFFSNNNHLHFNSnnnwawASVSTSRKSRICATSSQVMDPSAAKSEPALPTIVEVDLGS 82
Cdd:PLN02834   4 SSADNSESNTPTVLSRS-PSDAFFDQNSSIESSK------EGDLTEVIHEKCPVSGANKSEVTKTASATVTTVVKVDLGD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  83 RSYPIYIGSGLLNQPDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNPNVSVESVILPDGEQYKDMDTLMKVFDKA 162
Cdd:PLN02834  77 RSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 163 IESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLIDTD 242
Cdd:PLN02834 157 LESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 243 TLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 322
Cdd:PLN02834 237 TLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 323 FGH---------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPETVTVDMFKSVMAVDKKVADG 381
Cdd:PLN02834 317 FGHaietgpgygewlhgeavaagtVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAVDKKVADG 396

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 955349710 382 LLRLILLKGPLGNCVFTGDYDRKALDNTLRAFCKS 416
Cdd:PLN02834 397 LLRLILLKGELGNCVFTGDFDREALEETLRAFCKS 431
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 74-410 0e+00

3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440106  Cd Length: 355  Bit Score: 513.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  74 TIVEVDLGSRSYPIYIGSGLLNQ-PDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNpnVSVESVILPDGEQYKDM 152
Cdd:COG0337    2 QTLTVNLGERSYDIRIGRGLLDElGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAG--FEVHLLVLPDGEASKTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 153 DTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFY 232
Cdd:COG0337   80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 233 QPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESG 312
Cdd:COG0337  160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 313 LRATLNLGHTFGH--------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPEtVTVDMFKSVM 372
Cdd:COG0337  240 LRALLNFGHTFGHaieaatgyrllhgeavaigmVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAAM 318

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 955349710 373 AVDKKVADGLLRLILLKGpLGNCVFTGDYDRKALDNTL 410
Cdd:COG0337  319 KRDKKVRGGKLRFVLLRG-IGKAVIVDDVDEELLRAAL 355
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 84-410 3.55e-160

Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.


Pssm-ID: 341474  Cd Length: 343  Bit Score: 454.59  E-value: 3.55e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  84 SYPIYIGSGLLNQPDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNPNVSVesVILPDGEQYKDMDTLMKVFDKAI 163
Cdd:cd08195    1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEV--IVIPAGEKSKSLETVERIYDFLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 164 ESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLIDTDT 243
Cdd:cd08195   79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 244 LNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTF 323
Cdd:cd08195  159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 324 GH--------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPEtVTVDMFKSVMAVDKKVADGLL 383
Cdd:cd08195  239 GHaiesasgykllhgeavaigmVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGKI 317

                        330       340
                 ....*....|....*....|....*..
gi 955349710 384 RLILLKGPlGNCVFTGDYDRKALDNTL 410
Cdd:cd08195  318 RFVLLKGI-GKAVIVDDVSEEEIREAL 343
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 140-378 8.51e-136

3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.


Pssm-ID: 426414  Cd Length: 260  Bit Score: 389.55  E-value: 8.51e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  140 SVILPDGEQYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGI 219
Cdd:pfam01761   1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  220 NHRLGKNMIGTFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCEN 299
Cdd:pfam01761  81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  300 KAEVVSLDEKESGLRATLNLGHTFGH---------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTA 358
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHaiealsgygallhgeavaigmVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240

                         250       260
                  ....*....|....*....|
gi 955349710  359 PPEtVTVDMFKSVMAVDKKV 378
Cdd:pfam01761 241 LPD-LDVEQLLAAMARDKKV 259
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 85-410 7.46e-128

3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273575  Cd Length: 344  Bit Score: 372.35  E-value: 7.46e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710   85 YPIYIGSGLLNQPdyLQRHVHGKRVLVVTNETVAPLYLDKVVDALTrgNPNVSVESVILPDGEQYKDMDTLMKVFDKAIE 164
Cdd:TIGR01357   1 YPVHVGEGLLDQL--VEELAEPSKLVIITDETVADLYGDKLLEALQ--ALGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  165 SRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLIDTDTL 244
Cdd:TIGR01357  77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  245 NTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDP-SVMAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTF 323
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQElEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  324 GH---------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPETVTVDMFKSVMAVDKKVADGL 382
Cdd:TIGR01357 237 GHaieaeagygkiphgeavaigmVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGK 316

                         330       340
                  ....*....|....*....|....*...
gi 955349710  383 LRLILLKGpLGNCVFTGDYDRKALDNTL 410
Cdd:TIGR01357 317 IRFVLLEE-IGKAALAREVPDEMVLELL 343
 
Name Accession Description Interval E-value
PLN02834 PLN02834
3-dehydroquinate synthase
 3-416 0e+00

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 717.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710   3 STATNFSLSLCANQQTPiPKPSFFSNNNHLHFNSnnnwawASVSTSRKSRICATSSQVMDPSAAKSEPALPTIVEVDLGS 82
Cdd:PLN02834   4 SSADNSESNTPTVLSRS-PSDAFFDQNSSIESSK------EGDLTEVIHEKCPVSGANKSEVTKTASATVTTVVKVDLGD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  83 RSYPIYIGSGLLNQPDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNPNVSVESVILPDGEQYKDMDTLMKVFDKA 162
Cdd:PLN02834  77 RSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 163 IESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLIDTD 242
Cdd:PLN02834 157 LESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 243 TLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 322
Cdd:PLN02834 237 TLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 323 FGH---------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPETVTVDMFKSVMAVDKKVADG 381
Cdd:PLN02834 317 FGHaietgpgygewlhgeavaagtVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAVDKKVADG 396

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 955349710 382 LLRLILLKGPLGNCVFTGDYDRKALDNTLRAFCKS 416
Cdd:PLN02834 397 LLRLILLKGELGNCVFTGDFDREALEETLRAFCKS 431
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 74-410 0e+00

3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440106  Cd Length: 355  Bit Score: 513.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  74 TIVEVDLGSRSYPIYIGSGLLNQ-PDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNpnVSVESVILPDGEQYKDM 152
Cdd:COG0337    2 QTLTVNLGERSYDIRIGRGLLDElGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAG--FEVHLLVLPDGEASKTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 153 DTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFY 232
Cdd:COG0337   80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 233 QPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESG 312
Cdd:COG0337  160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 313 LRATLNLGHTFGH--------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPEtVTVDMFKSVM 372
Cdd:COG0337  240 LRALLNFGHTFGHaieaatgyrllhgeavaigmVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAAM 318

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 955349710 373 AVDKKVADGLLRLILLKGpLGNCVFTGDYDRKALDNTL 410
Cdd:COG0337  319 KRDKKVRGGKLRFVLLRG-IGKAVIVDDVDEELLRAAL 355
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 84-410 3.55e-160

Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.


Pssm-ID: 341474  Cd Length: 343  Bit Score: 454.59  E-value: 3.55e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  84 SYPIYIGSGLLNQPDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNPNVSVesVILPDGEQYKDMDTLMKVFDKAI 163
Cdd:cd08195    1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEV--IVIPAGEKSKSLETVERIYDFLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 164 ESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLIDTDT 243
Cdd:cd08195   79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 244 LNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTF 323
Cdd:cd08195  159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 324 GH--------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPEtVTVDMFKSVMAVDKKVADGLL 383
Cdd:cd08195  239 GHaiesasgykllhgeavaigmVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGKI 317

                        330       340
                 ....*....|....*....|....*..
gi 955349710 384 RLILLKGPlGNCVFTGDYDRKALDNTL 410
Cdd:cd08195  318 RFVLLKGI-GKAVIVDDVSEEEIREAL 343
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 140-378 8.51e-136

3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.


Pssm-ID: 426414  Cd Length: 260  Bit Score: 389.55  E-value: 8.51e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  140 SVILPDGEQYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGI 219
Cdd:pfam01761   1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  220 NHRLGKNMIGTFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCEN 299
Cdd:pfam01761  81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  300 KAEVVSLDEKESGLRATLNLGHTFGH---------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTA 358
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHaiealsgygallhgeavaigmVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240

                         250       260
                  ....*....|....*....|
gi 955349710  359 PPEtVTVDMFKSVMAVDKKV 378
Cdd:pfam01761 241 LPD-LDVEQLLAAMARDKKV 259
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 85-410 7.46e-128

3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273575  Cd Length: 344  Bit Score: 372.35  E-value: 7.46e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710   85 YPIYIGSGLLNQPdyLQRHVHGKRVLVVTNETVAPLYLDKVVDALTrgNPNVSVESVILPDGEQYKDMDTLMKVFDKAIE 164
Cdd:TIGR01357   1 YPVHVGEGLLDQL--VEELAEPSKLVIITDETVADLYGDKLLEALQ--ALGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  165 SRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLIDTDTL 244
Cdd:TIGR01357  77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  245 NTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDP-SVMAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTF 323
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQElEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  324 GH---------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTAPPETVTVDMFKSVMAVDKKVADGL 382
Cdd:TIGR01357 237 GHaieaeagygkiphgeavaigmVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGK 316

                         330       340
                  ....*....|....*....|....*...
gi 955349710  383 LRLILLKGpLGNCVFTGDYDRKALDNTL 410
Cdd:TIGR01357 317 IRFVLLEE-IGKAALAREVPDEMVLELL 343
DOIS cd08197
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ...
 84-401 6.76e-85

2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose; 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. They are important antibacterial agents. DOIS is a homolog of the dehydroquinate synthase which catalyzes the cyclization of 3-deoxy-D-arabino-heputulosonate-7-phosphate to dehydroquinate (DHQ) in the shikimate pathway.


Pssm-ID: 341476  Cd Length: 355  Bit Score: 263.29  E-value: 6.76e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  84 SYPIYIGSGLLNQPDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNpnVSVESVILPDGEQYKDMDTLMKVFDKAI 163
Cdd:cd08197    1 LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAG--IPVELLVVPAGESNKTLSTLTELAERLI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 164 ESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLIDTDT 243
Cdd:cd08197   79 AAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 244 LNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTF 323
Cdd:cd08197  159 LKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 324 GHVM--------------AVDM------SYRLGWIDDSLVKRVGDILKQAKLPTAPPETVTVDMFKSVMAVDKK-----V 378
Cdd:cd08197  239 GHAIellsggelshgeavAIGMcvaaeiSHLLGLLSEEDVDKHYELLEKIGLPTIIPDGISVEAILEVIRYDNKrgyikA 318

                        330       340
                 ....*....|....*....|....
gi 955349710 379 ADGLLRLILLKGpLGNCVFT-GDY 401
Cdd:cd08197  319 DADTIRMVLLEK-LGKPANPdGDY 341
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
 84-395 1.75e-76

Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.


Pssm-ID: 341448 [Multi-domain]  Cd Length: 328  Bit Score: 240.77  E-value: 1.75e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  84 SYPIYIGSGLL---NQPDYLQRHVhgkRVLVVTNETVAPLYLDKVVDALTRGNPnvsVESVILPDGEQYKDMDTLMKVFD 160
Cdd:cd08169    1 EYPVFFGEGVFesvNSYIPRDAFD---QCLIIVDSGVPDLIVNYLAEYFGYYLE---VHVFIIQGGEAYKTFQTVVEELE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 161 KAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLID 240
Cdd:cd08169   75 RAAALHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFAD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 241 TDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSLDEKESGLRATLNLG 320
Cdd:cd08169  155 FSFLKTLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 321 HTF--------------GHVMAVDMSY------RLGWIDDSLVKRVGDILKQAKLPTAPPETVTVDMFKSVMAVDKKVAD 380
Cdd:cd08169  235 HTFghalelasgykiphGEAVAVGMAYaakianRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPDSLYEYLESDKKSLY 314

                        330
                 ....*....|....*
gi 955349710 381 GLLRLILLKGpLGNC 395
Cdd:cd08169  315 GNLGMILLSG-VGDG 328
EEVS cd08199
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ...
 84-400 3.25e-76

2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.


Pssm-ID: 341478  Cd Length: 349  Bit Score: 240.51  E-value: 3.25e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  84 SYPIYIGSGLLN--QPDYLQRHVH-GKRVLVVTNETVAPLYLDKVVDALTRGNpnVSVESVILPDGEQYKDMDTLMKVFD 160
Cdd:cd08199    1 SYDVVLVDDLFDpeNPTLADAYGRpGRRRLVVVDENVDRLYGARIRAYFAAHG--IEATILVLPGGEANKTMETVLRIVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 161 KAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFYQPQCVLID 240
Cdd:cd08199   79 ALDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 241 TDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLAR--DPSVMAYAIKRscenKAEVVSLDE-----KESGL 313
Cdd:cd08199  159 RSFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVETrfFQDEVADEIIR----RAIQGMLEElapnlWEHDL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 314 RATLNLGHTF--------------GHVMAVDM------SYRLGWIDDSLVKRVGDILKQAKLPTAPPeTVTVDMFKSVMA 373
Cdd:cd08199  235 ERLVDFGHTFspilemaaapellhGEAVAIDMalsavlAYRRGLLSEEELDRILRLMRRLGLPVWHP-LCTPDLLWRALE 313

                        330       340
                 ....*....|....*....|....*..
gi 955349710 374 VDKKVADGLLRLILLKGpLGNCVFTGD 400
Cdd:cd08199  314 DIVKHRDGLQRLPLPKG-IGECVFVND 339
aroB PRK06203
3-dehydroquinate synthase; Reviewed
 84-366 8.75e-56

3-dehydroquinate synthase; Reviewed


Pssm-ID: 235740  Cd Length: 389  Bit Score: 188.57  E-value: 8.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  84 SYPIYIGSGL--LNQP---DYLQRHVHG--KRVLVVTNETVAPLY--LDKVVDALTRGNPNV---SVESVILPDGEQYK- 150
Cdd:PRK06203  13 EYPVYFTRDLfsPENPllaEVLAADGEGkpKKVLVVIDSGVLRAHpdLLEQITAYFAAHADVlelVAEPLVVPGGEAAKn 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 151 DMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGT 230
Cdd:PRK06203  93 DPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNGINAFGKKNFLGT 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 231 FYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAEVVSL--DE 308
Cdd:PRK06203 173 FAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAELHLEHIAGggDP 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955349710 309 KESGLRATLNLGHTFGH---------------V---MAVDM--SYRLGWIDDSLVKRVGDILKQAKLPTAPPETVTVD 366
Cdd:PRK06203 253 FEFGSSRPLDFGHWSAHkleqltnyalrhgeaVaigIALDSlySYLLGLLSEAEAQRILALLRALGFPLYHPALATRD 330
DHQS-like cd08198
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 84-361 1.01e-55

Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; This family contains dehydroquinate synthase-like proteins. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. The activity of DHQS requires NAD as cofactor. Proteins of this family share sequence similarity and functional motifs with that of dehydroquinate synthase, but the specific function has not been characterized.


Pssm-ID: 341477  Cd Length: 366  Bit Score: 187.78  E-value: 1.01e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  84 SYPIYIGSGLLNQPDYLQRHVHGK-------RVLVVTNETVA---PLYLDKVVDALTRGNPNVSV--ESVILPDGEQYK- 150
Cdd:cd08198    1 SYPVCFTHDLFSPDNPLLRALLVRrgpgrrhRVLFVIDSGVAaahPALVKQIERYFQAHPDRLELvaPPLIVPGGEAVKn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 151 DMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGT 230
Cdd:cd08198   81 DPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 231 FYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAIKRSCENKAE--VVSLDE 308
Cdd:cd08198  161 FAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAELHLDhiAASGDP 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 955349710 309 KESGLRATLNLGHTFGH---VM---------------AVDMSY--RLGWIDDSLVKRVGDILKQAKLPTAPPE 361
Cdd:cd08198  241 FETGSARPLDFGHWSAHkleQLsgyalrhgeavaigiALDSLYarLLGLLSREDFDRILALLQNLGLPLWHPL 313
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
 75-411 3.03e-49

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 175.05  E-value: 3.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  75 IVEVD-LGSRSYPIYIGSGLLNQ-PDYLQRHvhGKRVLVVTNETVAPlYLDKVVDALTRGNPNVSveSVILPDGEQYKDM 152
Cdd:PRK14021 178 TVHVTgAGIEPYDVRIGEGAMNHlPQVLGPK--PVKVALIHTQPVQR-HSDRARTLLRQGGYEVS--DIVIPDAEAGKTI 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 153 DTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGINHRLGKNMIGTFY 232
Cdd:PRK14021 253 EVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFY 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 233 QPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEKNMHLLLARDPS---------VMAYAIKRSCENKAEV 303
Cdd:PRK14021 333 TPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRAFDGStflgspledVVAELIERTVKVKAYH 412

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 304 VSLDEKESGLRATLNLGHTFGH--------------------VMAVDMSYRLGWIDDSLVKRVGDILKQAKLPTApPETV 363
Cdd:PRK14021 413 VSSDLKEAGLREFLNYGHTLGHaieklehfrwrhgnavavgmVYAAELAHLLGYIDQDLVDYHRSLLASLGLPTS-WNGG 491

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 955349710 364 TVDMFKSVMAVDKKVADGLLRLILLKGpLGNCVFTGDYDRKALDNTLR 411
Cdd:PRK14021 492 SFDDVLALMHRDKKARGNELRFVVLDE-IGHPVHLDNPPAEAVEEAFR 538
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
141-391 1.45e-41

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 153.14  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 141 VILPDGEQYKDMDTLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAQVDSSVGGKTGIN 220
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAID 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 221 HRLGKNMIGTFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLI--RDAEFFEWQEKnmhlLLARDPSVMAYAIKRSCE 298
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILsgRGVELFDEPEK----IEKRNLRVLSEMVKISVE 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 299 NKAEVVSLDEKESGLRATLNLGHTFGHV----------MAV--------DMSYRLGWIDDSLVKRVGDILKQakLPTAPP 360
Cdd:PRK13951 365 EKARIVMEDPYDMGLRHALNLGHTLGHVyemlegvphgIAVawgieketMYLYRKGIVPKETMRWIVEKVKQ--IVPIPV 442

                        250       260       270
                 ....*....|....*....|....*....|..
gi 955349710 361 ETVTVDMFKSVMAVDKKVADG-LLRLILLKGP 391
Cdd:PRK13951 443 PSVDVEKARNLILNDKKILKGsRVRLPYVKEI 474
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 85-268 2.15e-26

Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


Pssm-ID: 341447 [Multi-domain]  Cd Length: 271  Bit Score: 107.06  E-value: 2.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  85 YPIYIGSGLLNQPDYLQRHvHGKRVLVVTNETVAPLYLDKVVDALTRGnpnVSVESVILPDGEqyKDMDTLMKVFDKAIE 164
Cdd:cd07766    2 TRIVFGEGAIAKLGEIKRR-GFDRALVVSDEGVVKGVGEKVADSLKKG---LAVAIFDFVGEN--PTFEEVKNAVERARA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 165 SRLDrrcTFVALGGGVIGDMCGFAASAFLRGVNFIQIPTTVMAqvDSSVGGKTGINHRLGKN-MIGTFYQPQCVLIDTDT 243
Cdd:cd07766   76 AEAD---AVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDI 150

                        170       180
                 ....*....|....*....|....*
gi 955349710 244 LNTLPDRELASGLAEVIKYGLIRDA 268
Cdd:cd07766  151 TKGLPPRQVASGGVDALAHAVELEK 175
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
88-313 1.75e-16

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 78.50  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710   88 YIGSGLLNQ-PDYLQRHvHGKRVLVVTNETVAPLYLDKVVDALTRGNPNVSVESVILPDGeqykDMDTLMKVFDKAIESR 166
Cdd:pfam13685   1 VIGPGALGRlGEYLAEL-GFRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGNA----DMETAEKLVGALRERD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  167 LDrrcTFVALGGGVIGDMCGFAAsaFLRGVNFIQIPTTvmAQVDSSVGGKTGINHRLGKNMIGTfYQPQCVLIDTDTLNT 246
Cdd:pfam13685  76 AD---AVVGVGGGTVIDLAKYAA--FKLGKPFISVPTA--ASNDGFASPGASLTVDGKKRSIPA-AAPFGVIADTDVIAA 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955349710  247 LPDRELASGLAEVI-KYGLIRDAEFFEWQEKNMHLLLARDPSVMAYAiKRSCENKAEVVSLDEKESGL 313
Cdd:pfam13685 148 APRRLLASGVGDLLaKITAVADWELAHAEEVAAPLALLSAAMVMNFA-DRPLRDPGDIEALAELLSAL 214
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 87-274 2.64e-13

NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed


Pssm-ID: 179139  Cd Length: 350  Bit Score: 70.69  E-value: 2.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  87 IYIGSGLLNQ-PDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALtrgNPNVSVESVILPDGeqykDMDTLMKVFDKAIES 165
Cdd:PRK00843  14 VVVGHGVLDDiGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENL---EDAGDVEVVIVDEA----TMEEVEKVEEKAKDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 166 RLDrrcTFVALGGGVIGDMCGFAAsaFLRGVNFIQIPTTV----MAQVDSSVGGkTGINHRLGKNMigtfyqPQCVLIDT 241
Cdd:PRK00843  87 NAG---FLIGVGGGKVIDVAKLAA--YRLGIPFISVPTAAshdgIASPRASIKG-GGKPVSVKAKP------PLAVIADT 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 955349710 242 DTLNTLPDRELASGLAEVI-KYGLIRDaeffeWQ 274
Cdd:PRK00843 155 EIIAKAPYRLLAAGCGDIIsNYTAVKD-----WR 183
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 87-262 3.05e-12

Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.


Pssm-ID: 341454  Cd Length: 340  Bit Score: 67.15  E-value: 3.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  87 IYIGSGLLNQ-PDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGnpNVSVESVILPDGEQ-YKDMDTLMKVFDkaie 164
Cdd:cd08175    4 IVIGEGALKKlPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEA--GVTVCLLIFPGEGDlIADEAAVGKVLL---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 165 sRLDRRCTF-VALGGGVIGDMCGFAasAFLRGVNFIQIPTTvmAQVD---SSV------GGKTginhrlgknmigTFY-- 232
Cdd:cd08175   78 -ELEKDTDLiIAVGSGTINDLTKYA--AYKLGIPYISVPTA--PSMDgytSSGapiivdGVKK------------TFPah 140

                        170       180       190
                 ....*....|....*....|....*....|.
gi 955349710 233 QPQCVLIDTDTLNTLPDRELASGLAEVI-KY 262
Cdd:cd08175  141 APKAIFADLDVLANAPQRMIAAGFGDLLgKY 171
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 87-285 7.20e-11

Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.


Pssm-ID: 341452  Cd Length: 343  Bit Score: 62.96  E-value: 7.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  87 IYIGSGLLNQ-PDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNPNVSVESVILpdgeqYKDMDTLMKVFDKAIES 165
Cdd:cd08173    5 VVVGHGAINKiGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIAT-----IEEAAEVEKVKKLIKES 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 166 RLDrrcTFVALGGGVIGDMCGFAasAFLRGVNFIQIPTTvmAQVD------SSVGGKTGINHRLGKnmigtfyQPQCVLI 239
Cdd:cd08173   80 KAD---FIIGVGGGKVIDVAKYA--AYKLNLPFISIPTS--ASHDgiaspfASIKGGDKPYSIKAK-------APIAIIA 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 955349710 240 DTDTLNTLPDRELASGLAEVI-KYGLIRDaeffeWQeknmhllLARD 285
Cdd:cd08173  146 DTEIISKAPKRLLAAGCGDLIsNITAVKD-----WR-------LAHR 180
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 89-270 7.43e-10

Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.


Pssm-ID: 341453 [Multi-domain]  Cd Length: 332  Bit Score: 59.84  E-value: 7.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  89 IGSGLLNQ-PDYLQRHVHG-KRVLVVTNETVAPLYLDKVVDALTRGNPNVSVESVilpdgeqykDMDTLMKVFDKAIesR 166
Cdd:cd08174    6 IEEGALEHlGKYLADRNQGfGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEEN---------TDNSAEELAEKAF--S 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 167 LDRRCTFVALGGGVIGDMCGFAAsaFLRGVNFIQIPTTVmaqvdSSVG-----------GKTginHRLGKNMigtfyqPQ 235
Cdd:cd08174   75 LPKVDAIVGIGGGKVLDVAKYAA--FLSKLPFISVPTSL-----SNDGiaspvavlkvdGKR---KSLGAKM------PY 138

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 955349710 236 CVLIDTDTLNTLPDRELASGLAEVI-KYGLIRDAEF 270
Cdd:cd08174  139 GVIVDLDVIKSAPRRLILAGIGDLIsNITALYDWKL 174
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
87-255 6.45e-08

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 54.15  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710   87 IYIGSGLLNQ-PDYLQRHvhGKRVLVVTNETVAPL-YLDKVVDALTRGNPNVSVESVILPDgeqyKDMDTLMKVFDKAIE 164
Cdd:pfam00465   4 IVFGAGALAElGEELKRL--GARALIVTDPGSLKSgLLDKVLASLEEAGIEVVVFDGVEPE----PTLEEVDEAAALARE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  165 SRLDrrcTFVALGGG-------VIGDMCGFAASAFL---------RGVNFIQIPTTV-----MAQV----DSSVGGKTGI 219
Cdd:pfam00465  78 AGAD---VIIAVGGGsvidtakAIALLLTNPGDVWDylggkpltkPALPLIAIPTTAgtgseVTPLavitDTETGEKLGI 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 955349710  220 NHRlgkNMIgtfyqPQCVLIDTDTLNTLPDRELASG 255
Cdd:pfam00465 155 FSP---KLL-----PDLAILDPELTLTLPPRLTAAT 182
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 87-276 9.41e-08

Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.


Pssm-ID: 341479 [Multi-domain]  Cd Length: 331  Bit Score: 53.34  E-value: 9.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  87 IYIGSGLLNQPDYLQRHVHGKRVLVVTNETVAPLYLDKVVDALTRGNPNVSVESVILPDGEQYKdmdtlMKVFDKAIesr 166
Cdd:cd08549    4 TIVGDGAINKIEEILKKLNLKRVLIITGKNTKAKYCRFFYDQLKTVCDIVYYDNIDNLEDELKK-----YTFYDCVI--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 167 ldrrctfvALGGGVIGDMCGFaaSAFLRGVNFIQIPTTvmAQVD--SSVGGKTGINHRLGKNMIGTfyqPQCVLIDTDTL 244
Cdd:cd08549   76 --------GIGGGRSIDTGKY--LAYKLKIPFISVPTS--ASNDgiASPIVSLRIPGVKKTFMADA---PIAIIADTEII 140

                        170       180       190
                 ....*....|....*....|....*....|...
gi 955349710 245 NTLPDRELASGLAEVI-KYGLIRDAEFFEWQEK 276
Cdd:cd08549  141 KKSPRRLLSAGIGDLVsNITAVLDWKLAHKEKG 173
PDD cd08180
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ...
 87-204 2.32e-06

1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.


Pssm-ID: 341459 [Multi-domain]  Cd Length: 333  Bit Score: 49.03  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  87 IYIGSGLLnqpDYLqRHVHGKRVLVVTNETVAPL-YLDKVVDALTRGNPnVSVESVILPDgeqyKDMDTLMKVFDKAIES 165
Cdd:cd08180    7 IYSGEDSL---ERL-KELKGKRVFIVTDPFMVKSgMVDKVTDELDKSNE-VEIFSDVVPD----PSIEVVAKGLAKILEF 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 955349710 166 RLDrrcTFVALGGGVIGDMCGfAASAFLRGVN-------FIQIPTT 204
Cdd:cd08180   78 KPD---TIIALGGGSAIDAAK-AIIYFALKQKgnikkplFIAIPTT 119
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
87-254 2.35e-06

Alcohol dehydrogenase, class IV [Energy production and conversion];


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 49.35  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  87 IYIGSGLLNQ-PDYLQRHvHGKRVLVVTNETVAPL-YLDKVVDALTRGNPNVSVESVILPDgeqyKDMDTLMKVFDKAIE 164
Cdd:COG1454   11 IVFGAGALAElGEELKRL-GAKRALIVTDPGLAKLgLLDRVLDALEAAGIEVVVFDDVEPN----PTVETVEAGAAAARE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 165 SRLDrrcTFVALGGG-VIGdmCGFAASAF---------LRGVN--------FIQIPTT-----------VMaqVDSSVGG 215
Cdd:COG1454   86 FGAD---VVIALGGGsAID--AAKAIALLatnpgdledYLGIKkvpgpplpLIAIPTTagtgsevtpfaVI--TDPETGV 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 955349710 216 KTGINHRlgkNMIgtfyqPQCVLIDTDTLNTLPDRELAS 254
Cdd:COG1454  159 KKGIADP---ELL-----PDVAILDPELTLTLPPSLTAA 189
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 87-248 1.38e-05

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


Pssm-ID: 341481 [Multi-domain]  Cd Length: 372  Bit Score: 46.67  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  87 IYIGSGLLNQ-PDYLQRHvHGKRVLVVTNETVAPL-YLDKVVDALTRGNPNVSVESVILPDgeqyKDMDTLMKVFDKAIE 164
Cdd:cd08551    4 IVFGAGALARlGEELKAL-GGKKVLLVTDPGLVKAgLLDKVLESLKAAGIEVEVFDDVEPN----PTVETVEAAAELARE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 165 SRLDrrcTFVALGGG-VIgDmCGFAASAFL-----------------RGVNFIQIPTT---------VMAQVDSSVGGKT 217
Cdd:cd08551   79 EGAD---LVIAVGGGsVL-D-TAKAIAVLAtnggsirdyegigkvpkPGLPLIAIPTTagtgsevtpNAVITDPETGRKM 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 955349710 218 GINHRlgkNMIgtfyqPQCVLIDTDTLNTLP 248
Cdd:cd08551  154 GIVSP---YLL-----PDVAILDPELTLSLP 176
Fe-ADH-like cd08189
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 80-204 6.53e-05

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.


Pssm-ID: 341468 [Multi-domain]  Cd Length: 378  Bit Score: 44.77  E-value: 6.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  80 LGSRSYPIYIGSGLLNQ-PDYLQRHvHGKRVLVVTNETVAPL-YLDKVVDALTRGNPNVSVESVILPDgeqykdmDTLMK 157
Cdd:cd08189    1 LPWPEPELFEGAGSLLQlPEALKKL-GIKRVLIVTDKGLVKLgLLDPLLDALKKAGIEYVVFDGVVPD-------PTIDN 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 955349710 158 VfDKAIESRLDRRCT-FVALGGG-------VIGDM--CGFAASAFLRGVN--------FIQIPTT 204
Cdd:cd08189   73 V-EEGLALYKENGCDaIIAIGGGsvidcakVIAARaaNPKKSVRKLKGLLkvrkklppLIAVPTT 136
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
 86-222 1.49e-04

Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.


Pssm-ID: 341469 [Multi-domain]  Cd Length: 412  Bit Score: 43.69  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  86 PIYIGSGLLNQPDYLQRHVHGKRVLVVTNETVAPL-YLDKVVDALTRGNPNVSV--ESVILPDGEqykdmdTLMKVFDKA 162
Cdd:cd08190    3 NIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLgLVERVLESLEKAGIEVVVydGVRVEPTDE------SFEEAIEFA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710 163 IESRLDrrcTFVALGGG-VIgDMCGFAA------SAFLRGVN---------------FIQIPTTV--------MAQVD-S 211
Cdd:cd08190   77 KEGDFD---AFVAVGGGsVI-DTAKAANlyathpGDFLDYVNapigkgkpvpgplkpLIAIPTTAgtgsettgVAIFDlE 152

                        170
                 ....*....|.
gi 955349710 212 SVGGKTGINHR 222
Cdd:cd08190  153 ELKVKTGISSR 163
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 87-179 5.91e-03

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.


Pssm-ID: 341473 [Multi-domain]  Cd Length: 378  Bit Score: 38.67  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  87 IYIGSGLLNQ-PDYLQRhVHGKRVLVVTNETVAPL-YLDKVVDALTRGNPNVSVESVILPDGEqykdmdtlmkvfDKAIE 164
Cdd:cd08194    4 IIIGGGALEElGEEAAS-LGGKRALIVTDKVMVKLgLVDKVTQLLAEAGIAYAVFDDVVSEPT------------DEMVE 70

                         90       100
                 ....*....|....*....|
gi 955349710 165 SRLDR----RCTF-VALGGG 179
Cdd:cd08194   71 EGLALykegGCDFiVALGGG 90
Fe-ADH-like cd14862
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 98-179 9.85e-03

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341484 [Multi-domain]  Cd Length: 375  Bit Score: 37.97  E-value: 9.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955349710  98 DYLQRHVhGKRVLVVTNETVAPL-YLDKVVDALTRGNPNVSVESVILPDGEqykdMDTLMKVFDKAIESRLDrrcTFVAL 176
Cdd:cd14862   17 SHLEQLS-GKRALIVTDKVLVKLgLLKKVLKRLLQAGFEVEVFDEVEPEPP----LETVLKGAEAMREFEPD---LIIAL 88


                 ...
gi 955349710 177 GGG 179
Cdd:cd14862   89 GGG 91
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH