|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
8-442 |
0e+00 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 763.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 8 KQALSFTNSTHQLHQSRAIPRDIhVRFPAPVSSPSSRCGLKSKATTRLKVLATSatkvMDHSSSKASSQAPTVVEVDLGT 87
Cdd:PLN02834 2 KSSSADNSESNTPTVLSRSPSDA-FFDQNSSIESSKEGDLTEVIHEKCPVSGAN----KSEVTKTASATVTTVVKVDLGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 88 RSYPIYIGAGLLDQPDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNPNVTVESVILPDGEQFKNMETLMKVFDKA 167
Cdd:PLN02834 77 RSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 168 IESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLIDTD 247
Cdd:PLN02834 157 LESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 248 TLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESGVRATLNLGHT 327
Cdd:PLN02834 237 TLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 328 FGHAVETGVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPETMTVEMFKSIMAVDKKVADG 407
Cdd:PLN02834 317 FGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAVDKKVADG 396
|
410 420 430
....*....|....*....|....*....|....*
gi 350539107 408 KLRLILLKGSLGNCVFTGDYDQKALDETLRAFSKS 442
Cdd:PLN02834 397 LLRLILLKGELGNCVFTGDFDREALEETLRAFCKS 431
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
79-436 |
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: 568.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 79 TVVEVDLGTRSYPIYIGAGLLDQ-PDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNpnVTVESVILPDGEQFKNM 157
Cdd:COG0337 2 QTLTVNLGERSYDIRIGRGLLDElGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAG--FEVHLLVLPDGEASKTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 158 ETLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFY 237
Cdd:COG0337 80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 238 QPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESG 317
Cdd:COG0337 160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 318 VRATLNLGHTFGHAVETGVGYgQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPEtMTVEMFKSI 397
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAA 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 350539107 398 MAVDKKVADGKLRLILLKGsLGNCVFTGDYDQKALDETL 436
Cdd:COG0337 318 MKRDKKVRGGKLRFVLLRG-IGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
89-436 |
2.93e-179 |
|
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: 503.90 E-value: 2.93e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 89 SYPIYIGAGLLDQPDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNPNVTVesVILPDGEQFKNMETLMKVFDKAI 168
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEV--IVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 169 ESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLIDTDT 248
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 249 LNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESGVRATLNLGHTF 328
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 329 GHAVETGVGYgQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPEtMTVEMFKSIMAVDKKVADGK 408
Cdd:cd08195 239 GHAIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGK 316
|
330 340
....*....|....*....|....*...
gi 350539107 409 LRLILLKGsLGNCVFTGDYDQKALDETL 436
Cdd:cd08195 317 IRFVLLKG-IGKAVIVDDVSEEEIREAL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
145-404 |
4.12e-159 |
|
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: 449.64 E-value: 4.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 145 SVILPDGEQFKNMETLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGI 224
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 225 NHPLGKNMIGAFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCEN 304
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 305 KADVVSQDEKESGVRATLNLGHTFGHAVETGVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTS 384
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240
|
250 260
....*....|....*....|
gi 350539107 385 PPEtMTVEMFKSIMAVDKKV 404
Cdd:pfam01761 241 LPD-LDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
90-436 |
2.68e-146 |
|
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: 420.50 E-value: 2.68e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 90 YPIYIGAGLLDQpdLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTdgNPNVTVESVILPDGEQFKNMETLMKVFDKAIE 169
Cdd:TIGR01357 1 YPVHVGEGLLDQ--LVEELAEPSKLVIITDETVADLYGDKLLEALQ--ALGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 170 SRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLIDTDTL 249
Cdd:TIGR01357 77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 250 NTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPT-AFTYAIKRSCENKADVVSQDEKESGVRATLNLGHTF 328
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELeHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 329 GHAVETGVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPETMTVEMFKSIMAVDKKVADGK 408
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGK 316
|
330 340
....*....|....*....|....*...
gi 350539107 409 LRLILLKGsLGNCVFTGDYDQKALDETL 436
Cdd:TIGR01357 317 IRFVLLEE-IGKAALAREVPDEMVLELL 343
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
8-442 |
0e+00 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 763.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 8 KQALSFTNSTHQLHQSRAIPRDIhVRFPAPVSSPSSRCGLKSKATTRLKVLATSatkvMDHSSSKASSQAPTVVEVDLGT 87
Cdd:PLN02834 2 KSSSADNSESNTPTVLSRSPSDA-FFDQNSSIESSKEGDLTEVIHEKCPVSGAN----KSEVTKTASATVTTVVKVDLGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 88 RSYPIYIGAGLLDQPDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNPNVTVESVILPDGEQFKNMETLMKVFDKA 167
Cdd:PLN02834 77 RSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 168 IESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLIDTD 247
Cdd:PLN02834 157 LESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 248 TLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESGVRATLNLGHT 327
Cdd:PLN02834 237 TLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 328 FGHAVETGVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPETMTVEMFKSIMAVDKKVADG 407
Cdd:PLN02834 317 FGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEMFKSLMAVDKKVADG 396
|
410 420 430
....*....|....*....|....*....|....*
gi 350539107 408 KLRLILLKGSLGNCVFTGDYDQKALDETLRAFSKS 442
Cdd:PLN02834 397 LLRLILLKGELGNCVFTGDFDREALEETLRAFCKS 431
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
79-436 |
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: 568.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 79 TVVEVDLGTRSYPIYIGAGLLDQ-PDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNpnVTVESVILPDGEQFKNM 157
Cdd:COG0337 2 QTLTVNLGERSYDIRIGRGLLDElGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAG--FEVHLLVLPDGEASKTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 158 ETLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFY 237
Cdd:COG0337 80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 238 QPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESG 317
Cdd:COG0337 160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 318 VRATLNLGHTFGHAVETGVGYgQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPEtMTVEMFKSI 397
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA-LDPEALLAA 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 350539107 398 MAVDKKVADGKLRLILLKGsLGNCVFTGDYDQKALDETL 436
Cdd:COG0337 318 MKRDKKVRGGKLRFVLLRG-IGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
89-436 |
2.93e-179 |
|
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: 503.90 E-value: 2.93e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 89 SYPIYIGAGLLDQPDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNPNVTVesVILPDGEQFKNMETLMKVFDKAI 168
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEV--IVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 169 ESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLIDTDT 248
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 249 LNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESGVRATLNLGHTF 328
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 329 GHAVETGVGYgQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPEtMTVEMFKSIMAVDKKVADGK 408
Cdd:cd08195 239 GHAIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGK 316
|
330 340
....*....|....*....|....*...
gi 350539107 409 LRLILLKGsLGNCVFTGDYDQKALDETL 436
Cdd:cd08195 317 IRFVLLKG-IGKAVIVDDVSEEEIREAL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
145-404 |
4.12e-159 |
|
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: 449.64 E-value: 4.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 145 SVILPDGEQFKNMETLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGI 224
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 225 NHPLGKNMIGAFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCEN 304
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 305 KADVVSQDEKESGVRATLNLGHTFGHAVETGVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTS 384
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240
|
250 260
....*....|....*....|
gi 350539107 385 PPEtMTVEMFKSIMAVDKKV 404
Cdd:pfam01761 241 LPD-LDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
90-436 |
2.68e-146 |
|
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: 420.50 E-value: 2.68e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 90 YPIYIGAGLLDQpdLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTdgNPNVTVESVILPDGEQFKNMETLMKVFDKAIE 169
Cdd:TIGR01357 1 YPVHVGEGLLDQ--LVEELAEPSKLVIITDETVADLYGDKLLEALQ--ALGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 170 SRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLIDTDTL 249
Cdd:TIGR01357 77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 250 NTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPT-AFTYAIKRSCENKADVVSQDEKESGVRATLNLGHTF 328
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELeHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 329 GHAVETGVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPETMTVEMFKSIMAVDKKVADGK 408
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGK 316
|
330 340
....*....|....*....|....*...
gi 350539107 409 LRLILLKGsLGNCVFTGDYDQKALDETL 436
Cdd:TIGR01357 317 IRFVLLEE-IGKAALAREVPDEMVLELL 343
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
89-436 |
1.40e-95 |
|
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: 291.41 E-value: 1.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 89 SYPIYIGAGLLDQPDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNPNVTVesVILPDGEQFKNMETLMKVFDKAI 168
Cdd:cd08197 1 LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVEL--LVVPAGESNKTLSTLTELAERLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 169 ESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLIDTDT 248
Cdd:cd08197 79 AAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 249 LNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESGVRATLNLGHTF 328
Cdd:cd08197 159 LKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 329 GHAVETgVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPETMTVEMFKSIMAVDKK----- 403
Cdd:cd08197 239 GHAIEL-LSGGELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIPDGISVEAILEVIRYDNKrgyik 317
|
330 340 350
....*....|....*....|....*....|...
gi 350539107 404 VADGKLRLILLKGsLGNCVFTGDYDQKALDETL 436
Cdd:cd08197 318 ADADTIRMVLLEK-LGKPANPDGDYLTPVPEEI 349
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
89-421 |
5.62e-86 |
|
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: 265.81 E-value: 5.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 89 SYPIYIGAGLLDQPDLLQRHIHGKRVLVVTNTTVAPL---YLDKTISALTDGNPnvtvesVILPDGEQFKNMETLMKVFD 165
Cdd:cd08169 1 EYPVFFGEGVFESVNSYIPRDAFDQCLIIVDSGVPDLivnYLAEYFGYYLEVHV------FIIQGGEAYKTFQTVVEELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 166 KAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLID 245
Cdd:cd08169 75 RAAALHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 246 TDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESGVRATLNLG 325
Cdd:cd08169 155 FSFLKTLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 326 HTFGHAVETGVGYGqWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPETMTVEMFKSIMAVDKKVA 405
Cdd:cd08169 235 HTFGHALELASGYK-IPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPDSLYEYLESDKKSL 313
|
330
....*....|....*.
gi 350539107 406 DGKLRLILLKGsLGNC 421
Cdd:cd08169 314 YGNLGMILLSG-VGDG 328
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
89-426 |
1.70e-79 |
|
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: 249.75 E-value: 1.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 89 SYPIYIGAGLLD--QPDLLQRHIH-GKRVLVVTNTTVAPLYLDKtISALTDGNpNVTVESVILPDGEQFKNMETLMKVFD 165
Cdd:cd08199 1 SYDVVLVDDLFDpeNPTLADAYGRpGRRRLVVVDENVDRLYGAR-IRAYFAAH-GIEATILVLPGGEANKTMETVLRIVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 166 KAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLID 245
Cdd:cd08199 79 ALDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 246 TDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLArdpTAFTyaikrscenkADVVSQDEKESGVRATL--- 322
Cdd:cd08199 159 RSFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVE---TRFF----------QDEVADEIIRRAIQGMLeel 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 323 --NL-----------GHTFGHAVETGVGYGqWLHGEAVaagtvmAVDM------SRRLGWIDDSLVQRVQKILQQAKLPT 383
Cdd:cd08199 226 apNLwehdlerlvdfGHTFSPILEMAAAPE-LLHGEAV------AIDMalsavlAYRRGLLSEEELDRILRLMRRLGLPV 298
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 350539107 384 SPPETMTVEMFKSIMAVDKKvADGKLRLILLKGsLGNCVFTGD 426
Cdd:cd08199 299 WHPLCTPDLLWRALEDIVKH-RDGLQRLPLPKG-IGECVFVND 339
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
89-387 |
3.40e-62 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 206.29 E-value: 3.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 89 SYPIYIGAGL--LDQPDLLQ-----RHIHGKRVLVVTNTTVAPLY--LDKTISALTDGNPNV---TVESVILPDGEQFKN 156
Cdd:PRK06203 13 EYPVYFTRDLfsPENPLLAEvlaadGEGKPKKVLVVIDSGVLRAHpdLLEQITAYFAAHADVlelVAEPLVVPGGEAAKN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 157 METLMKVFDKAIESR-LDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGA 235
Cdd:PRK06203 93 DPALVEALHAAINRHgIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNGINAFGKKNFLGT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 236 FYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQ--DE 313
Cdd:PRK06203 173 FAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAELHLEHIAGggDP 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 350539107 314 KESGVRATLNLGHTFGHAVETGVGYGqWLHGEAVAAGtvMAVDM--SRRLGWIDDSLVQRVQKILQQAKLPTSPPE 387
Cdd:PRK06203 253 FEFGSSRPLDFGHWSAHKLEQLTNYA-LRHGEAVAIG--IALDSlySYLLGLLSEAEAQRILALLRALGFPLYHPA 325
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
61-437 |
3.51e-61 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 207.79 E-value: 3.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 61 SATKVMDHSSSKAssqaptvVEVD-LGTRSYPIYIGAGLLDQ-PDLLqrhihGKRVLVVTNTTVAPL--YLDKTISALTD 136
Cdd:PRK14021 166 AAKKLIDMVAERT-------VHVTgAGIEPYDVRIGEGAMNHlPQVL-----GPKPVKVALIHTQPVqrHSDRARTLLRQ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 137 GNPNVTveSVILPDGEQFKNMETLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDS 216
Cdd:PRK14021 234 GGYEVS--DIVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 217 SVGGKTGINHPLGKNMIGAFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAF-- 294
Cdd:PRK14021 312 STGGKTGINTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRAFDGSTFlg 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 295 -------TYAIKRSCENKADVVSQDEKESGVRATLNLGHTFGHAVETgVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDS 367
Cdd:PRK14021 392 spledvvAELIERTVKVKAYHVSSDLKEAGLREFLNYGHTLGHAIEK-LEHFRWRHGNAVAVGMVYAAELAHLLGYIDQD 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 368 LVQRVQKILQQAKLPTSpPETMTVEMFKSIMAVDKKVADGKLRLILLkGSLGNCVFTGDYDQKALDETLR 437
Cdd:PRK14021 471 LVDYHRSLLASLGLPTS-WNGGSFDDVLALMHRDKKARGNELRFVVL-DEIGHPVHLDNPPAEAVEEAFR 538
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
144-387 |
1.30e-59 |
|
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: 198.95 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 144 ESVILPDGEQFKNMETLMKVFDKAIES-RLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKT 222
Cdd:cd08198 68 PPLIVPGGEAVKNDPALVEEILSAIHDhGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 223 GINHPLGKNMIGAFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSC 302
Cdd:cd08198 148 GINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 303 ENKAD--VVSQDEKESGVRATLNLGHTFGHAVETGVGYgQWLHGEAVAAGtvMAVDM--SRRLGWIDDSLVQRVQKILQQ 378
Cdd:cd08198 228 ELHLDhiAASGDPFETGSARPLDFGHWSAHKLEQLSGY-ALRHGEAVAIG--IALDSlyARLLGLLSREDFDRILALLQN 304
|
....*....
gi 350539107 379 AKLPTSPPE 387
Cdd:cd08198 305 LGLPLWHPL 313
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
146-423 |
2.41e-42 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 155.83 E-value: 2.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 146 VILPDGEQFKNMETLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGIN 225
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAID 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 226 HPLGKNMIGAFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLI--RDAEFFEWQEQnmplLLARDPTAFTYAIKRSCE 303
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILsgRGVELFDEPEK----IEKRNLRVLSEMVKISVE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 304 NKADVVSQDEKESGVRATLNLGHTFGHAVETGVGYGqwlHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQakLPT 383
Cdd:PRK13951 365 EKARIVMEDPYDMGLRHALNLGHTLGHVYEMLEGVP---HGIAVAWGIEKETMYLYRKGIVPKETMRWIVEKVKQ--IVP 439
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 350539107 384 SPPETMTVEMFKSIMAVDKKVADG-KLRLILLKgSLGNCVF 423
Cdd:PRK13951 440 IPVPSVDVEKARNLILNDKKILKGsRVRLPYVK-EIGKIEF 479
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
90-384 |
3.55e-29 |
|
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: 115.15 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 90 YPIYIGAGLLDQPDLLQRHiHGKRVLVVTNTTVAPLYLDKTISALTDGnpnVTVESVILPDGEqfKNMETLMKVFDKAIE 169
Cdd:cd07766 2 TRIVFGEGAIAKLGEIKRR-GFDRALVVSDEGVVKGVGEKVADSLKKG---LAVAIFDFVGEN--PTFEEVKNAVERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 170 SRLDrrcTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAqvDSSVGGKTGINHPLGKN-MIGAFYQPQCVLIDTDT 248
Cdd:cd07766 76 AEAD---AVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 249 LNTLPDRELASGLAEVIKYGLIRDAeffewqeqnmplllardptaftyAIKRSCENKADVVSqdekesgvRATLNLGHTF 328
Cdd:cd07766 151 TKGLPPRQVASGGVDALAHAVELEK-----------------------VVEAATLAGMGLFE--------SPGLGLAHAI 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 350539107 329 GHAVETGVGYgqwLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTS 384
Cdd:cd07766 200 GHALTAFEGI---PHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTH 252
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
92-353 |
1.78e-15 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 77.24 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 92 IYIGAGLLDQ-PDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDgnpNVTVESVILPDGeqfkNMETLMKVFDKAIES 170
Cdd:PRK00843 14 VVVGHGVLDDiGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLED---AGDVEVVIVDEA----TMEEVEKVEEKAKDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 171 RLDrrcTFVALGGGVIGDMCGYAaaSYLRGVNFIQIPTTV----MAQVDSSVGGkTGINHPLGKNMigafyqPQCVLIDT 246
Cdd:PRK00843 87 NAG---FLIGVGGGKVIDVAKLA--AYRLGIPFISVPTAAshdgIASPRASIKG-GGKPVSVKAKP------PLAVIADT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 247 DTLNTLPDRELASGLAEVI-KYGLIRD---------AEFFEWQEQnMPLLLARdpTAFTYA--IKRSCENKADVVSQDEK 314
Cdd:PRK00843 155 EIIAKAPYRLLAAGCGDIIsNYTAVKDwrlahrlrgEYYSEYAAA-LSLMTAK--MLIENAdiIKPGLEESARLVVKALI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 350539107 315 ESGV--------RATLNLGHTFGHAVETgVGYGQWLHGEAVAAGTVM 353
Cdd:PRK00843 232 SSGVamsiagssRPASGSEHLFSHALDR-LAPGPALHGEQCGVGTII 277
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
92-387 |
3.28e-15 |
|
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: 76.44 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 92 IYIGAGLLDQ-PDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNPNVTVESVILPDGEqfknmETLMKVFDKAIES 170
Cdd:cd08173 5 VVVGHGAINKiGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEA-----AEVEKVKKLIKES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 171 RLDrrcTFVALGGGVIGDMCGYAAasYLRGVNFIQIPTTvmAQVDssvggktGINHPL------GKNM-IGAfYQPQCVL 243
Cdd:cd08173 80 KAD---FIIGVGGGKVIDVAKYAA--YKLNLPFISIPTS--ASHD-------GIASPFasikggDKPYsIKA-KAPIAII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 244 IDTDTLNTLPDRELASGLAEVI-KYGLIRDaeffeWQeqnmpllLARDPT---------AFTYAIKRSCENKADVVSQDE 313
Cdd:cd08173 145 ADTEIISKAPKRLLAAGCGDLIsNITAVKD-----WR-------LAHRLKgeyyseyaaSLALMSAKLIIENADLIKPGL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 314 KESG---VRATLNLG----------------HTFGHAVETgVGYGQWLHGEAVAAGTVMavdMSR--RLGWiddslvQRV 372
Cdd:cd08173 213 EEGVrtvVKALISSGvamsiagssrpasgseHLFSHALDK-LAPGPALHGEQCGVGTIM---MAYlhGGDW------KEI 282
|
330
....*....|....*
gi 350539107 373 QKILQQAKLPTSPPE 387
Cdd:cd08173 283 REALKKIGAPTTAKE 297
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
93-348 |
5.86e-14 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 71.56 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 93 YIGAGLLDQ-PDLLQRHiHGKRVLVVTNTTVAPLYLDKTISALTDGNPNVTVESVILPDGeqfkNMETLMKVFDKAIESR 171
Cdd:pfam13685 1 VIGPGALGRlGEYLAEL-GFRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGNA----DMETAEKLVGALRERD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 172 LDrrcTFVALGGGVIGDMCGYAAasYLRGVNFIQIPTTvmAQVDssvggktGINHPL-------GKNMIGAfYQPQCVLI 244
Cdd:pfam13685 76 AD---AVVGVGGGTVIDLAKYAA--FKLGKPFISVPTA--ASND-------GFASPGasltvdgKKRSIPA-AAPFGVIA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 245 DTDTLNTLPDRELASGLAEVI-KYGLIRDAEFFEWQEQNMPLLLARDptaftyaikRSCENKADVVSQDEKESGVRATLN 323
Cdd:pfam13685 141 DTDVIAAAPRRLLASGVGDLLaKITAVADWELAHAEEVAAPLALLSA---------AMVMNFADRPLRDPGDIEALAELL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 350539107 324 LG----------------HTFGHAVETgVGYGQWLHGEAVA 348
Cdd:pfam13685 212 SAlamggagssrpasgseHLISHALDM-IAPKQALHGEQVG 251
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
92-385 |
5.63e-13 |
|
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: 69.46 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 92 IYIGAGLLDQ-PDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNpnVTVESVILPDGEQ-FKNMETLMKVFDkaie 169
Cdd:cd08175 4 IVIGEGALKKlPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAG--VTVCLLIFPGEGDlIADEAAVGKVLL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 170 sRLDRRCTF-VALGGGVIGDMCGYAaaSYLRGVNFIQIPTTvmaqvdSSVGGKTGINHPLgknMIGAFYQ------PQCV 242
Cdd:cd08175 78 -ELEKDTDLiIAVGSGTINDLTKYA--AYKLGIPYISVPTA------PSMDGYTSSGAPI---IVDGVKKtfpahaPKAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 243 LIDTDTLNTLPDRELASGLAEVI-KYGLIRDaeffeWqeqnmplLLAR-------DPTAFT---YAIKRSCENKADVVSQ 311
Cdd:cd08175 146 FADLDVLANAPQRMIAAGFGDLLgKYTALAD-----W-------KLSHllggeyyCPEVADlvqEALEKCLDNAEGIAAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 312 DEK----------ESGVrATLNLG---------HTFGHAVET---GVGYGQWLHGEAVAAGTVMAVDMsrrlgWIDDSL- 368
Cdd:cd08175 214 DPEaiealmealiLSGL-AMQLVGnsrpasgaeHHLSHYWEMeflRLGKPPVLHGEKVGVGTLLIAAL-----YILEQLp 287
|
330
....*....|....*...
gi 350539107 369 -VQRVQKILQQAKLPTSP 385
Cdd:cd08175 288 pPEELRELLRKAGAPTTP 305
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
179-387 |
2.95e-11 |
|
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: 64.51 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 179 VALGGGVIGDMCGYAaaSYLRGVNFIQIPTTvmAQVD--SSVGGKTGINHPLGKNMIGAfyqPQCVLIDTDTLNTLPDRE 256
Cdd:cd08549 75 IGIGGGRSIDTGKYL--AYKLKIPFISVPTS--ASNDgiASPIVSLRIPGVKKTFMADA---PIAIIADTEIIKKSPRRL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 257 LASGLAEVI-KYGLIRDAEFFEWQEQNMplllaRDPTA--FTYAIKRSCENKADVVSQDEK----------ESGVrATLN 323
Cdd:cd08549 148 LSAGIGDLVsNITAVLDWKLAHKEKGEK-----YSEFAaiLSKTSAKELVSYVLKASDLEEyhrvlvkalvGSGI-AMAI 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 350539107 324 LG---------HTFGHAVETGV---GYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPE 387
Cdd:cd08549 222 AGssrpasgseHLFSHALDKLKeeyLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKKVGAPTTAKQ 297
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
94-402 |
7.37e-09 |
|
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: 57.15 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 94 IGAGLLDQ-PDLLQRHIHG-KRVLVVTNTTVAPLYLDKTISALTDGNPNVTVESVILPDgeqfknMETLMKVFDK----- 166
Cdd:cd08174 6 IEEGALEHlGKYLADRNQGfGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEENTDNS------AEELAEKAFSlpkvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 167 AIesrldrrctfVALGGGVIGDMCGYAAasYLRGVNFIQIPTTVmaqvdSSVG-----------GKTginHPLGKNMiga 235
Cdd:cd08174 80 AI----------VGIGGGKVLDVAKYAA--FLSKLPFISVPTSL-----SNDGiaspvavlkvdGKR---KSLGAKM--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 236 fyqPQCVLIDTDTLNTLPDRELASGLAEVI-KYGLIRDaeffeWQeqnmpllLARDPTA-----FTYAIKR-SCENkadV 308
Cdd:cd08174 137 ---PYGVIVDLDVIKSAPRRLILAGIGDLIsNITALYD-----WK-------LAEEKGGepvddFAYLLSRtAADS---L 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 309 VSQDEKESGVRATLNL--------G----------------HTFGHAVETgVGYGQWLHGEAVAAGTVMavdMSrrlgWI 364
Cdd:cd08174 199 LNTPGKDIKDDEFLKElaeslvlsGiameiagssrpasgseHLISHALDK-LFPGPALHGIQVGLGTYF---MS----FL 270
|
330 340 350
....*....|....*....|....*....|....*....
gi 350539107 365 DDSLVQRVQKILQQAKLPTSPPET-MTVEMFksIMAVDK 402
Cdd:cd08174 271 QGQRYEEIRDVLKRTGFPLNPSDLgLTKEEF--IEAVKL 307
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
92-260 |
3.25e-08 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 55.30 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 92 IYIGAGLLDQ-PDLLQRHihGKRVLVVTNTTVAPL-YLDKTISALTDGNPNVTVESVILPDGEQfknmETLMKVFDKAIE 169
Cdd:pfam00465 4 IVFGAGALAElGEELKRL--GARALIVTDPGSLKSgLLDKVLASLEEAGIEVVVFDGVEPEPTL----EEVDEAAALARE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 170 SRLDrrcTFVALGGG-------VIGDMCGY--AAASYLRG-------VNFIQIPTTV-----MAQV----DSSVGGKTGI 224
Cdd:pfam00465 78 AGAD---VIIAVGGGsvidtakAIALLLTNpgDVWDYLGGkpltkpaLPLIAIPTTAgtgseVTPLavitDTETGEKLGI 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 350539107 225 NHPlgkNMIgafyqPQCVLIDTDTLNTLPDRELASG 260
Cdd:pfam00465 155 FSP---KLL-----PDLAILDPELTLTLPPRLTAAT 182
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
92-259 |
1.21e-05 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 47.04 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 92 IYIGAGLLDQ-PDLLQRHiHGKRVLVVTNTTVAPL-YLDKTISALTDGNPNVTVESVILPDgeqfKNMETLMKVFDKAIE 169
Cdd:COG1454 11 IVFGAGALAElGEELKRL-GAKRALIVTDPGLAKLgLLDRVLDALEAAGIEVVVFDDVEPN----PTVETVEAGAAAARE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 170 SRLDrrcTFVALGGG-VIgDMC---------GYAAASYL-------RGVNFIQIPTT-----------VMaqVDSSVGGK 221
Cdd:COG1454 86 FGAD---VVIALGGGsAI-DAAkaiallatnPGDLEDYLgikkvpgPPLPLIAIPTTagtgsevtpfaVI--TDPETGVK 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 350539107 222 TGINHPlgkNMIgafyqPQCVLIDTDTLNTLPDRELAS 259
Cdd:COG1454 160 KGIADP---ELL-----PDVAILDPELTLTLPPSLTAA 189
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
92-253 |
2.35e-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: 46.29 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 92 IYIGAGLLDQ-PDLLQRhIHGKRVLVVTNTTVAPL-YLDKTISALTDGNPNVTVESVILPDGEqfknMETLMKVFDKAIE 169
Cdd:cd08551 4 IVFGAGALARlGEELKA-LGGKKVLLVTDPGLVKAgLLDKVLESLKAAGIEVEVFDDVEPNPT----VETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 170 SRLDrrcTFVALGGG-VIgDMC---------GYAAASYL-------RGVNFIQIPTT---------VMAQVDSSVGGKTG 223
Cdd:cd08551 79 EGAD---LVIAVGGGsVL-DTAkaiavlatnGGSIRDYEgigkvpkPGLPLIAIPTTagtgsevtpNAVITDPETGRKMG 154
|
170 180 190
....*....|....*....|....*....|
gi 350539107 224 INHPlgkNMIgafyqPQCVLIDTDTLNTLP 253
Cdd:cd08551 155 IVSP---YLL-----PDVAILDPELTLSLP 176
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
92-253 |
4.26e-05 |
|
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: 45.18 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 92 IYIGAGLLDQpdlLqRHIHGKRVLVVTNTTVAPL-YLDKTISALTDGNPnVTVESVILPDgeqfKNMETLMKVFDKAIES 170
Cdd:cd08180 7 IYSGEDSLER---L-KELKGKRVFIVTDPFMVKSgMVDKVTDELDKSNE-VEIFSDVVPD----PSIEVVAKGLAKILEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 171 RLDrrcTFVALGGGVIGDMCGYAAASYLRGVN------FIQIPTTvmaqvdSSVG-----------GKTGINHPLGKNMI 233
Cdd:cd08180 78 KPD---TIIALGGGSAIDAAKAIIYFALKQKGnikkplFIAIPTT------SGTGsevtsfavitdPEKGIKYPLVDDSM 148
|
170 180
....*....|....*....|
gi 350539107 234 gafyQPQCVLIDTDTLNTLP 253
Cdd:cd08180 149 ----LPDIAILDPELVKSVP 164
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
88-209 |
7.06e-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: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 88 RSYPIYIGAGLLDQ-PDLLQRHiHGKRVLVVTNTTVAPL-YLDKTISALTDGNPNVTVESVILPDgEQFKNMEtlmkvfd 165
Cdd:cd08189 4 PEPELFEGAGSLLQlPEALKKL-GIKRVLIVTDKGLVKLgLLDPLLDALKKAGIEYVVFDGVVPD-PTIDNVE------- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 350539107 166 KAIESRLDRRCT-FVALGGG-VIgDmCGYAAA----------SYLRGVN--------FIQIPTT 209
Cdd:cd08189 75 EGLALYKENGCDaIIAIGGGsVI-D-CAKVIAaraanpkksvRKLKGLLkvrkklppLIAVPTT 136
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
92-261 |
6.29e-03 |
|
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 is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 38.64 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 92 IYIGAGLLDQ-PDLLQRHihGKRVLVVT-NTTVAPLYLDKTISALTDGNPNVTVESVIlpdGEqfknmETLMKVfDKAIE 169
Cdd:cd08183 4 IVFGRGSLQElGELAAEL--GKRALLVTgRSSLRSGRLARLLEALEAAGIEVALFSVS---GE-----PTVETV-DAAVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350539107 170 SRLDRRCTFV-ALGGG-VIgDmCGYAAAS----------YLRGVN-----------FIQIPTT-----------VMAQVD 215
Cdd:cd08183 73 LAREAGCDVViAIGGGsVI-D-AAKAIAAlltnegsvldYLEVVGkgrpltepplpFIAIPTTagtgsevtknaVLSSPE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 350539107 216 SSVggKTGINHPlgkNMIgafyqPQCVLIDTDTLNTLPdREL--ASGL 261
Cdd:cd08183 151 HGV--KVSLRSP---SML-----PDVALVDPELTLSLP-PEVtaASGL 187
|
|
| |
