NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568065404|ref|WP_024053062|]
View 

MULTISPECIES: 3-dehydroquinate synthase [Streptococcus]

Protein Classification

3-dehydroquinate synthase family protein( domain architecture ID 10785327)

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

CATH:  1.20.1090.10|3.40.50.1970
EC:  4.2.3.-
Gene Ontology:  GO:0003856|GO:0046872|GO:0003856|GO:0000166
PubMed:  9685163
SCOP:  4002924|3001905

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 2-353 2.00e-166

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: 468.42  E-value: 2.00e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   2 KLNVNIPNHPYDIVIEKGTLAKAGEWLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTV 81
Cdd:COG0337    3 TLTVNLGERSYDIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLETL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  82 NKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPD 161
Cdd:COG0337   83 ERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 162 GVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVELWQELFD-----MDGSPksilEHAESIIYHSCNVKRKLVVEDELDN 236
Cdd:COG0337  163 AVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEEnadalLARDP----EALEEAIARSCEIKAEVVAADERES 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 237 GVRLYLNFGHTIGHAVEATAGYgKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEELYHA 316
Cdd:COG0337  239 GLRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLAA 317

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568065404 317 LLHDKKARGKTIKLVIVPELGRTAI-HQISLEEMKDYL 353
Cdd:COG0337  318 MKRDKKVRGGKLRFVLLRGIGKAVIvDDVDEELLRAAL 355
 
Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 2-353 2.00e-166

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: 468.42  E-value: 2.00e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   2 KLNVNIPNHPYDIVIEKGTLAKAGEWLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTV 81
Cdd:COG0337    3 TLTVNLGERSYDIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLETL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  82 NKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPD 161
Cdd:COG0337   83 ERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 162 GVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVELWQELFD-----MDGSPksilEHAESIIYHSCNVKRKLVVEDELDN 236
Cdd:COG0337  163 AVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEEnadalLARDP----EALEEAIARSCEIKAEVVAADERES 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 237 GVRLYLNFGHTIGHAVEATAGYgKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEELYHA 316
Cdd:COG0337  239 GLRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLAA 317

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568065404 317 LLHDKKARGKTIKLVIVPELGRTAI-HQISLEEMKDYL 353
Cdd:COG0337  318 MKRDKKVRGGKLRFVLLRGIGKAVIvDDVDEELLRAAL 355
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 11-353 8.25e-159

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: 448.43  E-value: 8.25e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEwLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTVNKVYEFLAK 90
Cdd:cd08195    1 SYPILIGSGLLDKLGE-LLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  91 VGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPDGVLIDPDVL 170
Cdd:cd08195   80 AGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 171 KTLGQRELIEGMGEVIKYGLIEDVELWQELFD-MDGSPKSILEHAESIIYHSCNVKRKLVVEDELDNGVRLYLNFGHTIG 249
Cdd:cd08195  160 KTLPEREFRSGLAEVIKYGLIADKELFEFLEKnLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 250 HAVEATAGYgKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEELYHALLHDKKARGKTIK 329
Cdd:cd08195  240 HAIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKIR 318

                        330       340
                 ....*....|....*....|....*
gi 568065404 330 LVIVPELGRTAIHQ-ISLEEMKDYL 353
Cdd:cd08195  319 FVLLKGIGKAVIVDdVSEEEIREAL 343
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 12-353 4.81e-156

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: 441.69  E-value: 4.81e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   12 YDIVIEKGTLAKAGEWLASlwsAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTVNKVYEFLAKV 91
Cdd:TIGR01357   1 YPVHVGEGLLDQLVEELAE---PSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   92 GMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPDGVLIDPDVLK 171
Cdd:TIGR01357  78 GLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  172 TLGQRELIEGMGEVIKYGLIEDVELWQEL--FDMDGSPKSILEHAESIIYHSCNVKRKLVVEDELDNGVRLYLNFGHTIG 249
Cdd:TIGR01357 158 TLPDRELRSGMAEVIKHGLIADAELFDELesNDKLRLNLQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  250 HAVEATAGYGKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQP-WRQEELYHALLHDKKARGKTI 328
Cdd:TIGR01357 238 HAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKdLDVDELLNAMLNDKKNSGGKI 317

                         330       340
                  ....*....|....*....|....*
gi 568065404  329 KLVIVPELGRTAIHQISLEEMKDYL 353
Cdd:TIGR01357 318 RFVLLEEIGKAALAREVPDEMVLEL 342
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 66-324 4.41e-141

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: 400.34  E-value: 4.41e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   66 VFDFLEGEASKNLTTVNKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGV 145
Cdd:pfam01761   1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  146 NTPWAKNMVGTFTQPDGVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVELWQELFDMDGSP-KSILEHAESIIYHSCNV 224
Cdd:pfam01761  81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALlNLDPDALEEAIARSCEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  225 KRKLVVEDELDNGVRLYLNFGHTIGHAVEATAGYGKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVD 304
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240

                         250       260
                  ....*....|....*....|
gi 568065404  305 YQPWRQEELYHALLHDKKAR 324
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKVR 260
PLN02834 PLN02834
3-dehydroquinate synthase
 3-337 3.17e-88

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 272.03  E-value: 3.17e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   3 LNVNIPNHPYDIVIEKGTLAKaGEWLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFL--EGEASKNLTT 80
Cdd:PLN02834  70 VKVDLGDRSYPIYIGSGLLDH-GELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVIlpDGEKYKDMET 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  81 VNKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQP 160
Cdd:PLN02834 149 LMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQP 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 161 DGVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVEL--WQE-----LFDMDgspKSILEHAesiIYHSCNVKRKLVVEDE 233
Cdd:PLN02834 229 QCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFfeWQEanmekLLARD---PGALAYA---IKRSCENKAEVVSLDE 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 234 LDNGVRLYLNFGHTIGHAVEATAGYGKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEEL 313
Cdd:PLN02834 303 KESGLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEM 382

                        330       340
                 ....*....|....*....|....*.
gi 568065404 314 YHALLH-DKKARGKTIKLVIVP-ELG 337
Cdd:PLN02834 383 FKSLMAvDKKVADGLLRLILLKgELG 408
 
Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 2-353 2.00e-166

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: 468.42  E-value: 2.00e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   2 KLNVNIPNHPYDIVIEKGTLAKAGEWLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTV 81
Cdd:COG0337    3 TLTVNLGERSYDIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLETL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  82 NKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPD 161
Cdd:COG0337   83 ERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 162 GVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVELWQELFD-----MDGSPksilEHAESIIYHSCNVKRKLVVEDELDN 236
Cdd:COG0337  163 AVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEEnadalLARDP----EALEEAIARSCEIKAEVVAADERES 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 237 GVRLYLNFGHTIGHAVEATAGYgKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEELYHA 316
Cdd:COG0337  239 GLRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLAA 317

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568065404 317 LLHDKKARGKTIKLVIVPELGRTAI-HQISLEEMKDYL 353
Cdd:COG0337  318 MKRDKKVRGGKLRFVLLRGIGKAVIvDDVDEELLRAAL 355
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 11-353 8.25e-159

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: 448.43  E-value: 8.25e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEwLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTVNKVYEFLAK 90
Cdd:cd08195    1 SYPILIGSGLLDKLGE-LLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  91 VGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPDGVLIDPDVL 170
Cdd:cd08195   80 AGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 171 KTLGQRELIEGMGEVIKYGLIEDVELWQELFD-MDGSPKSILEHAESIIYHSCNVKRKLVVEDELDNGVRLYLNFGHTIG 249
Cdd:cd08195  160 KTLPEREFRSGLAEVIKYGLIADKELFEFLEKnLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 250 HAVEATAGYgKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEELYHALLHDKKARGKTIK 329
Cdd:cd08195  240 HAIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKIR 318

                        330       340
                 ....*....|....*....|....*
gi 568065404 330 LVIVPELGRTAIHQ-ISLEEMKDYL 353
Cdd:cd08195  319 FVLLKGIGKAVIVDdVSEEEIREAL 343
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 12-353 4.81e-156

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: 441.69  E-value: 4.81e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   12 YDIVIEKGTLAKAGEWLASlwsAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTVNKVYEFLAKV 91
Cdd:TIGR01357   1 YPVHVGEGLLDQLVEELAE---PSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   92 GMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPDGVLIDPDVLK 171
Cdd:TIGR01357  78 GLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  172 TLGQRELIEGMGEVIKYGLIEDVELWQEL--FDMDGSPKSILEHAESIIYHSCNVKRKLVVEDELDNGVRLYLNFGHTIG 249
Cdd:TIGR01357 158 TLPDRELRSGMAEVIKHGLIADAELFDELesNDKLRLNLQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  250 HAVEATAGYGKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQP-WRQEELYHALLHDKKARGKTI 328
Cdd:TIGR01357 238 HAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKdLDVDELLNAMLNDKKNSGGKI 317

                         330       340
                  ....*....|....*....|....*
gi 568065404  329 KLVIVPELGRTAIHQISLEEMKDYL 353
Cdd:TIGR01357 318 RFVLLEEIGKAALAREVPDEMVLEL 342
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 66-324 4.41e-141

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: 400.34  E-value: 4.41e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   66 VFDFLEGEASKNLTTVNKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGV 145
Cdd:pfam01761   1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  146 NTPWAKNMVGTFTQPDGVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVELWQELFDMDGSP-KSILEHAESIIYHSCNV 224
Cdd:pfam01761  81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALlNLDPDALEEAIARSCEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  225 KRKLVVEDELDNGVRLYLNFGHTIGHAVEATAGYGKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVD 304
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240

                         250       260
                  ....*....|....*....|
gi 568065404  305 YQPWRQEELYHALLHDKKAR 324
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKVR 260
PLN02834 PLN02834
3-dehydroquinate synthase
 3-337 3.17e-88

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 272.03  E-value: 3.17e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   3 LNVNIPNHPYDIVIEKGTLAKaGEWLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFL--EGEASKNLTT 80
Cdd:PLN02834  70 VKVDLGDRSYPIYIGSGLLDH-GELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVIlpDGEKYKDMET 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  81 VNKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQP 160
Cdd:PLN02834 149 LMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQP 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 161 DGVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVEL--WQE-----LFDMDgspKSILEHAesiIYHSCNVKRKLVVEDE 233
Cdd:PLN02834 229 QCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFfeWQEanmekLLARD---PGALAYA---IKRSCENKAEVVSLDE 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 234 LDNGVRLYLNFGHTIGHAVEATAGYGKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEEL 313
Cdd:PLN02834 303 KESGLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEKMTVEM 382

                        330       340
                 ....*....|....*....|....*.
gi 568065404 314 YHALLH-DKKARGKTIKLVIVP-ELG 337
Cdd:PLN02834 383 FKSLMAvDKKVADGLLRLILLKgELG 408
DOIS cd08197
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ...
 12-354 1.14e-82

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: 255.20  E-value: 1.14e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  12 YDIVIEKGTLAKAGEWLASLwSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTVNKVYEFLAKV 91
Cdd:cd08197    2 TDIYLGRGILESLLSILEEL-KADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAERLIAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  92 GMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPDGVLIDPDVLK 171
Cdd:cd08197   81 GITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 172 TLGQRELIEGMGEVIKYGLIEDVELWQELFDMDGSPKSILEHA-ESIIYHSCNVKRKLVVEDELDNGVRLYLNFGHTIGH 250
Cdd:cd08197  161 TLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFlEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTVGH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 251 AVEATAGyGKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPV----DYQPwrqEELYHALLHDKK---- 322
Cdd:cd08197  241 AIELLSG-GELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTiipdGISV---EAILEVIRYDNKrgyi 316

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 568065404 323 -ARGKTIKLVIVPELGR------TAIHQISLEEMKDYLE 354
Cdd:cd08197  317 kADADTIRMVLLEKLGKpanpdgDYLTPVPEEIVKEALE 355
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
 34-337 9.27e-79

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: 244.24  E-value: 9.27e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  34 AQKIVVITDNHVASLYAETVKCSLEVTgFEVFVFDFLEGEASKNLTTVNKVYEFLAKVGMTRSDGIVALGGGVVGDLAGF 113
Cdd:cd08169   23 FDQCLIIVDSGVPDLIVNYLAEYFGYY-LEVHVFIIQGGEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGATGDVVGF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 114 AASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPDGVLIDPDVLKTLGQRELIEGMGEVIKYGLIED 193
Cdd:cd08169  102 AAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMALIAD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 194 VELWQELFD-MDGSPKSILEHAESIIYHSCNVKRKLVVEDELDNGVRLYLNFGHTIGHAVEATAGYgKVMHGEAVAIGMV 272
Cdd:cd08169  182 NDFFEFLEDkANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTFGHALELASGY-KIPHGEAVAVGMA 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568065404 273 QVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEE-LYHALLHDKKARGKTIKLVIVPELG 337
Cdd:cd08169  261 YAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPDsLYEYLESDKKSLYGNLGMILLSGVG 326
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
 11-348 1.40e-66

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 218.96  E-value: 1.40e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASlwSAQKIVVITDNHVASlYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTVNKVYEFLAK 90
Cdd:PRK14021 188 PYDVRIGEGAMNHLPQVLGP--KPVKVALIHTQPVQR-HSDRARTLLRQGGYEVSDIVIPDAEAGKTIEVANGIWQRLGN 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  91 VGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPDGVLIDPDVL 170
Cdd:PRK14021 265 EGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTL 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 171 KTLGQRELIEGMGEVIKYGLIEDVELWQ-------ELFDMDGSP---KSILEHAESIIYHSCNVKRKLVVEDELDNGVRL 240
Cdd:PRK14021 345 ATLPNDIFIEGLGEVAKSGFIRDPEILRiledhaaELRAFDGSTflgSPLEDVVAELIERTVKVKAYHVSSDLKEAGLRE 424

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 241 YLNFGHTIGHAVEATAGYgKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEELYhALLH- 319
Cdd:PRK14021 425 FLNYGHTLGHAIEKLEHF-RWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLASLGLPTSWNGGSFDDVL-ALMHr 502

                        330       340
                 ....*....|....*....|....*....
gi 568065404 320 DKKARGKTIKLVIVPELGrtaiHQISLEE 348
Cdd:PRK14021 503 DKKARGNELRFVVLDEIG----HPVHLDN 527
EEVS cd08199
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ...
 12-350 1.05e-64

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: 208.92  E-value: 1.05e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  12 YDIVIEKGTLAKAGEWLASLWSAQ--KIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTTVNKVYEFLA 89
Cdd:cd08199    2 YDVVLVDDLFDPENPTLADAYGRPgrRRLVVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEANKTMETVLRIVDALD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  90 KVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTFTQPDGVLIDPDV 169
Cdd:cd08199   82 DFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 170 LKTLGQRELIEGMGEVIKYGLIEDVELWqELFDMDG-----SPKSILEHAESIIYHScnVKRKL------VVEDELDngv 238
Cdd:cd08199  162 LKTLPRRHIRNGLAEIIKMALVKDAELF-ELLEEHGaalveTRFFQDEVADEIIRRA--IQGMLeelapnLWEHDLE--- 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 239 RLyLNFGHTIGHAVEATAGYgKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVDYQPWRQEELYHALL 318
Cdd:cd08199  236 RL-VDFGHTFSPILEMAAAP-ELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWHPLCTPDLLWRALE 313

                        330       340       350
                 ....*....|....*....|....*....|...
gi 568065404 319 HDKKARGKTIKLVIVPELGRTA-IHQISLEEMK 350
Cdd:cd08199  314 DIVKHRDGLQRLPLPKGIGECVfVNDVTEEELE 346
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
69-350 5.24e-47

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 166.23  E-value: 5.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  69 FLEGEASKNLTTVNKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTP 148
Cdd:PRK13951 211 FPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAIDFA 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 149 WAKNMVGTFTQPDGVLIDPDVLKTLGQRELIEGMGEVIKYGLIE--DVELWQELFDMDgspKSILEHAESIIYHSCNVKR 226
Cdd:PRK13951 291 GVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSgrGVELFDEPEKIE---KRNLRVLSEMVKISVEEKA 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 227 KLVVEDELDNGVRLYLNFGHTIGHAVEATAGygkVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFgLPVDYQ 306
Cdd:PRK13951 368 RIVMEDPYDMGLRHALNLGHTLGHVYEMLEG---VPHGIAVAWGIEKETMYLYRKGIVPKETMRWIVEKVKQI-VPIPVP 443

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568065404 307 PWRQEELYHALLHDKK-ARGKTIKLVIVPELGRtaIHQISLEEMK 350
Cdd:PRK13951 444 SVDVEKARNLILNDKKiLKGSRVRLPYVKEIGK--IEFLEVDPLE 486
aroB PRK06203
3-dehydroquinate synthase; Reviewed
 72-307 9.91e-42

3-dehydroquinate synthase; Reviewed


Pssm-ID: 235740  Cd Length: 389  Bit Score: 149.66  E-value: 9.91e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  72 GEASKN-LTTVNKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWA 150
Cdd:PRK06203  87 GEAAKNdPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNGINAFGK 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 151 KNMVGTFTQPDGVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVELWQEL---------FDMDgspksILEHAesiIYHS 221
Cdd:PRK06203 167 KNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLeahaaalaaRDPE-----AMEEL---IYRC 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 222 CnvkrKLVVE------DELDNGVRLYLNFGHTIGHAVEATAGYGkVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQM 295
Cdd:PRK06203 239 A----ELHLEhiagggDPFEFGSSRPLDFGHWSAHKLEQLTNYA-LRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILAL 313

                        250
                 ....*....|..
gi 568065404 296 CRKFGLPVdYQP 307
Cdd:PRK06203 314 LRALGFPL-YHP 324
DHQS-like cd08198
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 72-350 1.83e-40

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: 145.79  E-value: 1.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  72 GEASKN-LTTVNKVYEFLAKVGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWA 150
Cdd:cd08198   75 GEAVKNdPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 151 KNMVGTFTQPDGVLIDPDVLKTLGQRELIEGMGEVIKYGLIEDVELWQEL---------FDMDGSPKSILEHAESIIYHS 221
Cdd:cd08198  155 KNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLernaaalrqRDPDAMEKLIRRCAELHLDHI 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 222 CNVKrklvveDELDNGVRLYLNFGHTIGHAVEATAGYgKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGL 301
Cdd:cd08198  235 AASG------DPFETGSARPLDFGHWSAHKLEQLSGY-ALRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGL 307

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568065404 302 PvdyqpwrqeeLYHALLHDKKAR--------------GK-TIKLviVPELGR-TAIHQISLEEMK 350
Cdd:cd08198  308 P----------LWHPLLERDGVLelldgleefrehlgGRlTITL--LRGIGVgVEVHEIDLDLME 360
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 11-304 1.92e-30

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: 116.69  E-value: 1.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLWsaQKIVVITDNHVASLYAETVKCSLEvTGFEVFVFDFLEGEasknlTTVNKVYEFLAK 90
Cdd:cd07766    1 PTRIVFGEGAIAKLGEIKRRGF--DRALVVSDEGVVKGVGEKVADSLK-KGLAVAIFDFVGEN-----PTFEEVKNAVER 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  91 VGMTRSDGIVALGGGVVGDLAGFAASTYMRGIHFVQIPTslTAQVDSSIGGKTGVNTPWAKN-MVGTFTQPDGVLIDPDV 169
Cdd:cd07766   73 ARAAEADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPT--TASTDSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDI 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 170 LKTLGQRELIEGMGEVIKYgliedvelWQELfdmdgspksilehaESIIYHSCNVKrklvvedeLDNGVRLYLNFGHTIG 249
Cdd:cd07766  151 TKGLPPRQVASGGVDALAH--------AVEL--------------EKVVEAATLAG--------MGLFESPGLGLAHAIG 200

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568065404 250 HAVEAtagYGKVMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLPVD 304
Cdd:cd07766  201 HALTA---FEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTH 252
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 11-303 7.06e-20

Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440140 [Multi-domain]  Cd Length: 355  Bit Score: 89.46  E-value: 7.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLwsAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFlEGEASKNltTVNKVyefLAK 90
Cdd:COG0371    6 PRRYVQGEGALDELGEYLADL--GKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVF-GGECSEE--EIERL---AEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  91 VGMTRSDGIVALGGGVVGDLAGFAAstYMRGIHFVQIPTSltAQVD------SSI---GGKTGVNTPWAKNmvgtftqPD 161
Cdd:COG0371   78 AKEQGADVIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI--ASTDapasplSVIyteDGAFDGYSFLAKN-------PD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 162 GVLIDPDVLKTLGQRELIEGMGEVI-KYGLIEDVELWQElfDMDGSP-------------KSILEHAESIIyhsCNVKRK 227
Cdd:COG0371  147 LVLVDTDIIAKAPVRLLAAGIGDALaKWYEARDWSLAHR--DLAGEYyteaavalarlcaETLLEYGEAAI---KAVEAG 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 228 LV---VEDELDNGvrLYL-----NFG---------HTIGHAVEATAGYGKVMHGEAVAIG-MVQvarvaekkgLMPKGIT 289
Cdd:COG0371  222 VVtpaLERVVEAN--LLLsglamGIGssrpgsgaaHAIHNGLTALPETHHALHGEKVAFGtLVQ---------LVLEGRP 290

                        330
                 ....*....|....*..
gi 568065404 290 TDIEQM---CRKFGLPV 303
Cdd:COG0371  291 EEIEELldfLRSVGLPT 307
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 11-303 6.17e-16

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: 77.56  E-value: 6.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLWSA-QKIVVITDNHVASLYAETVKCSLEVTGfEVFVFDFlegeasKNLTTVNKVYEFLA 89
Cdd:cd08174    1 PLILKIEEGALEHLGKYLADRNQGfGKVAIVTGEGIDELLGEDILESLEEAG-EIVTVEE------NTDNSAEELAEKAF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  90 KVGMTrsDGIVALGGGVVGDLAGFAAstYMRGIHFVQIPTSLTAqvD---SSI------GGKTGVNtpwAKNmvgtftqP 160
Cdd:cd08174   74 SLPKV--DAIVGIGGGKVLDVAKYAA--FLSKLPFISVPTSLSN--DgiaSPVavlkvdGKRKSLG---AKM-------P 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 161 DGVLIDPDVLKTLGQRELIEGMGEVI-KYGLIEDvelWQELFD-----MDGSPKSILEHA-ESIIYHscnvKRKLVVEDE 233
Cdd:cd08174  138 YGVIVDLDVIKSAPRRLILAGIGDLIsNITALYD---WKLAEEkggepVDDFAYLLSRTAaDSLLNT----PGKDIKDDE 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 234 ----LDNGvrLYLNfG----------------HTIGHAVEATAGyGKVMHGEAVAIGMVQVARVAEKKglmpkgiTTDIE 293
Cdd:cd08174  211 flkeLAES--LVLS-GiameiagssrpasgseHLISHALDKLFP-GPALHGIQVGLGTYFMSFLQGQR-------YEEIR 279

                        330
                 ....*....|
gi 568065404 294 QMCRKFGLPV 303
Cdd:cd08174  280 DVLKRTGFPL 289
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 11-270 6.23e-14

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: 71.82  E-value: 6.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEASKNLTtvnkvyEFLAK 90
Cdd:cd08173    2 PRNVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVE------KVKKL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  91 VGMTRSDGIVALGGGVVGDLAGFAAstYMRGIHFVQIPTSLT----AQVDSSIGGKTGVNTPWAKnmvgtftQPDGVLID 166
Cdd:cd08173   76 IKESKADFIIGVGGGKVIDVAKYAA--YKLNLPFISIPTSAShdgiASPFASIKGGDKPYSIKAK-------APIAIIAD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 167 PDVLKTLGQRELIEGMGEVI-KYGLIEDvelWQELFDMDGSPKS----ILEH--AESIIYHSCNVKRK------LVVEDE 233
Cdd:cd08173  147 TEIISKAPKRLLAAGCGDLIsNITAVKD---WRLAHRLKGEYYSeyaaSLALmsAKLIIENADLIKPGleegvrTVVKAL 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568065404 234 LDNGVRLYLNfG---------HTIGHAVEATAgYGKVMHGEAVAIG 270
Cdd:cd08173  224 ISSGVAMSIA-GssrpasgseHLFSHALDKLA-PGPALHGEQCGVG 267
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 14-173 3.39e-13

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: 69.78  E-value: 3.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  14 IVIEKGTLAKAGEWLASLWsAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEFLAKVG 92
Cdd:cd08551    4 IVFGAGALARLGEELKALG-GKKVLLVTDPGLVKAgLLDKVLESLKAAGIEVEVFDDVEPNPT--VETVEAAAELAREEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  93 mtrSDGIVALGGGVVGDLAGFAA---------STYM-------RGIHFVQIPTslTAqvdssiGgkTG--VnTPWA---- 150
Cdd:cd08551   81 ---ADLVIAVGGGSVLDTAKAIAvlatnggsiRDYEgigkvpkPGLPLIAIPT--TA------G--TGseV-TPNAvitd 146

                        170       180
                 ....*....|....*....|....*....
gi 568065404 151 ------KNMVGTFTQPDGVLIDPDVLKTL 173
Cdd:cd08551  147 petgrkMGIVSPYLLPDVAILDPELTLSL 175
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 13-324 8.39e-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: 68.31  E-value: 8.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  13 DIVIEKGTLAKAGEWLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFVFDFLEGEasknltTVNKVYEFLAKVG 92
Cdd:cd08175    3 EIVIGEGALKKLPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEG------DLIADEAAVGKVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  93 MT---RSDGIVALGGGVVGDLAGFAAstYMRGIHFVQIPTslTAQVD------SSI---GGKTGVNTPwaknmvgtftQP 160
Cdd:cd08175   77 LElekDTDLIIAVGSGTINDLTKYAA--YKLGIPYISVPT--APSMDgytssgAPIivdGVKKTFPAH----------AP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 161 DGVLIDPDVLKTLGQRELIEGMGEVI-KYGLIEDvelW------------QELFDMDGSP-KSILEHAESIiyhscnVKR 226
Cdd:cd08175  143 KAIFADLDVLANAPQRMIAAGFGDLLgKYTALAD---WklshllggeyycPEVADLVQEAlEKCLDNAEGI------AAR 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 227 KlvvedelDNGVRlYLNFG---------------------HTIGHAVE---ATAGYGKVMHGEAVAIGMVQVARVAEKKG 282
Cdd:cd08175  214 D-------PEAIE-ALMEAlilsglamqlvgnsrpasgaeHHLSHYWEmefLRLGKPPVLHGEKVGVGTLLIAALYILEQ 285

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 568065404 283 LMPkgiTTDIEQMCRKFGLPVDYQ--PWRQEELYHALLHDKKAR 324
Cdd:cd08175  286 LPP---PEELRELLRKAGAPTTPEdlGIDRDLLRDSLRLAKEIR 326
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 11-302 1.28e-12

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: 67.98  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLwSAQKIVVITDNHVASLYAETVKCSLEVTGFEVFV--FDFLEGEASKNlttvnkvyefl 88
Cdd:cd08549    1 PRYTIVGDGAINKIEEILKKL-NLKRVLIITGKNTKAKYCRFFYDQLKTVCDIVYYdnIDNLEDELKKY----------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  89 akvgmTRSDGIVALGGGVVGDLAGFAAstYMRGIHFVQIPTSLTAQVDSSIGGKTGVNTPWAKNMVGTftqPDGVLIDPD 168
Cdd:cd08549   69 -----TFYDCVIGIGGGRSIDTGKYLA--YKLKIPFISVPTSASNDGIASPIVSLRIPGVKKTFMADA---PIAIIADTE 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 169 VLKTLGQRELIEGMGEVIkyGLIEDVELWQELFDMDGSPKSILEHAESI-IYHSC------NVKR----KLVVEDELDNG 237
Cdd:cd08549  139 IIKKSPRRLLSAGIGDLV--SNITAVLDWKLAHKEKGEKYSEFAAILSKtSAKELvsyvlkASDLeeyhRVLVKALVGSG 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568065404 238 VRLYL--------NFGHTIGHAVEATAGYGK---VMHGEAVAIGMVQVARVAEKKGLMPKGITTDIEQMCRKFGLP 302
Cdd:cd08549  217 IAMAIagssrpasGSEHLFSHALDKLKEEYLninVLHGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKKVGAP 292
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 17-303 1.65e-10

Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.


Pssm-ID: 341480 [Multi-domain]  Cd Length: 347  Bit Score: 61.40  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  17 EKGTLAKAGEWLASLwsAQKIVVITDNHVASLYAETVKCSLEVTG--FEVFVFdflEGEASKNlttvnKVYEFLAKVGMT 94
Cdd:cd08550    7 EPGILAKAGEYIAPL--GKKALIIGGKTALEAVGEKLEKSLEEAGidYEVEVF---GGECTEE-----NIERLAEKAKEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  95 RSDGIVALGGGVVGDLAGFAAstYMRGIHFVQIPTS------LTAQvdsSI----GGKTGVNTPWAKNmvgtftqPDGVL 164
Cdd:cd08550   77 GADVIIGIGGGKVLDTAKAVA--DRLGLPVVTVPTIaatcaaWSAL---SVlydeEGEFLGYSLLKRS-------PDLVL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 165 IDPDVLKTLGQRELIEGMGEVI-KygliedvelWQEL-FDMDGSPKSILEHA---------ESIIYHSCNVK---RKLVV 230
Cdd:cd08550  145 VDTDIIAAAPVRYLAAGIGDTLaK---------WYEArPSSRGGPDDLALQAavqlaklayDLLLEYGVQAVedvRQGKV 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 231 EDELD----------------NGVRLYLNFGHTIGHA---VEATAGYGkvmHGEAVAIG-MVQVArvAEKKGLmpkgitT 290
Cdd:cd08550  216 TPALEdvvdaiillaglvgslGGGGCRTAAAHAIHNGltkLPETHGTL---HGEKVAFGlLVQLA--LEGRSE------E 284

                        330
                 ....*....|....*.
gi 568065404 291 DIEQM---CRKFGLPV 303
Cdd:cd08550  285 EIEELiefLRRLGLPV 300
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
11-173 1.82e-10

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 61.47  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   11 PYDIVIEKGTLAKAGEWLASLwsAQKIVVITD-NHVASLYAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEFLA 89
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRL--GARALIVTDpGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPT--LEEVDEAAALAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   90 KvgmTRSDGIVALGGGVVGDLAGFAA---------STYMRG-------IHFVQIPT-----SLTAQV----DSSIGGKTG 144
Cdd:pfam00465  77 E---AGADVIIAVGGGSVIDTAKAIAllltnpgdvWDYLGGkpltkpaLPLIAIPTtagtgSEVTPLavitDTETGEKLG 153

                         170       180
                  ....*....|....*....|....*....
gi 568065404  145 VNTPwaknmvgtFTQPDGVLIDPDVLKTL 173
Cdd:pfam00465 154 IFSP--------KLLPDLAILDPELTLTL 174
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
11-173 3.72e-10

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


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 60.52  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLwSAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEFLA 89
Cdd:COG1454    8 PTRIVFGAGALAELGEELKRL-GAKRALIVTDPGLAKLgLLDRVLDALEAAGIEVVVFDDVEPNPT--VETVEAGAAAAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  90 KVGmtrSDGIVALGGGVVGDLA---------GFAASTYM-------RGIHFVQIPTslTA-----------QVDSSIGGK 142
Cdd:COG1454   85 EFG---ADVVIALGGGSAIDAAkaiallatnPGDLEDYLgikkvpgPPLPLIAIPT--TAgtgsevtpfavITDPETGVK 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568065404 143 TGVNTPwakNMVgtftqPDGVLIDPDVLKTL 173
Cdd:COG1454  160 KGIADP---ELL-----PDVAILDPELTLTL 182
Fe-ADH-like cd14865
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 14-111 1.83e-07

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: 341487 [Multi-domain]  Cd Length: 383  Bit Score: 52.54  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  14 IVIEKGTLAKAGEWLASLwSAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEFLAKVG 92
Cdd:cd14865    9 IVSGAGALENLPAELARL-GARRPLIVTDKGLAAAgLLKKVEDALGDAIEIVGVFDDVPPDSS--VAVVNEAAARAREAG 85

                         90
                 ....*....|....*....
gi 568065404  93 mtrSDGIVALGGGVVGDLA 111
Cdd:cd14865   86 ---ADGIIAVGGGSVIDTA 101
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 11-111 1.99e-07

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: 52.15  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLwSAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEFLA 89
Cdd:cd08194    1 PRTIIIGGGALEELGEEAASL-GGKRALIVTDKVMVKLgLVDKVTQLLAEAGIAYAVFDDVVSEPT--DEMVEEGLALYK 77

                         90       100
                 ....*....|....*....|..
gi 568065404  90 KVGmtrSDGIVALGGGVVGDLA 111
Cdd:cd08194   78 EGG---CDFIVALGGGSPIDTA 96
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 11-270 4.08e-07

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


Pssm-ID: 179139  Cd Length: 350  Bit Score: 51.05  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLWSAQKIVVITDNHVASLYAETVKCSLEVTGfEVFVFdfLEGEASKNltTVNKVYEFLAK 90
Cdd:PRK00843  11 PRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAG-DVEVV--IVDEATME--EVEKVEEKAKD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  91 VGmtrSDGIVALGGGVVGDLAGFAAstYMRGIHFVQIPTslTAQVD------SSI---GGKTGVNTpwaknmvgtfTQPD 161
Cdd:PRK00843  86 VN---AGFLIGVGGGKVIDVAKLAA--YRLGIPFISVPT--AASHDgiasprASIkggGKPVSVKA----------KPPL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 162 GVLIDPDVLKTLGQRELIEGMGEVI-KYGLIEDVELWQELFD------------MdgSPKSILEHAESIIYHSCNVKRkL 228
Cdd:PRK00843 149 AVIADTEIIAKAPYRLLAAGCGDIIsNYTAVKDWRLAHRLRGeyyseyaaalslM--TAKMLIENADIIKPGLEESAR-L 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568065404 229 VVEDELDNGV--------RLYLNFGHTIGHAVEATAGyGKVMHGEAVAIG 270
Cdd:PRK00843 226 VVKALISSGVamsiagssRPASGSEHLFSHALDRLAP-GPALHGEQCGVG 274
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
 19-122 8.97e-07

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: 50.24  E-value: 8.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  19 GTLAKAGEWLASLwSAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEFLAKvgmTRSD 97
Cdd:cd08190    9 GATRELGMDLKRL-GAKKVLVVTDPGLAKLgLVERVLESLEKAGIEVVVYDGVRVEPT--DESFEEAIEFAKE---GDFD 82

                         90       100
                 ....*....|....*....|....*..
gi 568065404  98 GIVALGGGVVGDLAGFAA--STYMRGI 122
Cdd:cd08190   83 AFVAVGGGSVIDTAKAANlyATHPGDF 109
Fe-ADH-like cd14863
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 19-355 1.08e-06

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: 341485 [Multi-domain]  Cd Length: 380  Bit Score: 49.84  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  19 GTLAKAGEwLASLWSAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEFLAKVGmtrSD 97
Cdd:cd14863   13 GAVEQIGE-LLKELGCKKVLLVTDKGLKKAgIVDKIIDLLEEAGIEVVVFDDVEPDPP--DEIVDEAAEIAREEG---AD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  98 GIVALGGGVVGDLA-----------------GFAASTYMRGIHFVQIPT--------SLTAQV-DSSIGGKTGVntpwak 151
Cdd:cd14863   87 GVIGIGGGSVLDTAkaiavlltnpgpiidyaLAGPPVPKPGIPLIAIPTtagtgsevTPIAVItDEENGVKKSL------ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 152 nmVGTFTQPDGVLIDPDVLKTLgqreliegmgevikygliedvelwqelfdmdgsPKSI--------LEHA--------- 214
Cdd:cd14863  161 --LGPFLVPDLAILDPELTVGL---------------------------------PPSLtaatgmdaLSHAieaytskla 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 215 ----ESIIYHSCnvkrKLVVE------DELDN--------------GVRLY---LNFGHTIGHAVEATAGygkVMHGEAV 267
Cdd:cd14863  206 npmtDALALQAI----RLIVKnlpravKDGDNlearenmllasnlaGIAFNnagTHIGHAIAHALGALYH---IPHGLAC 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404 268 AIGMVQV------------ARVAEKKGLMPKGITTD---------IEQMCRKFGLPVDYQPWRqeelyhallHDKKARGK 326
Cdd:cd14863  279 ALALPVVlefnaeaypekvKKIAKALGVSFPGESDEelgeavadaIREFMKELGIPSLFEDYG---------IDKEDLDK 349

                        410       420
                 ....*....|....*....|....*....
gi 568065404 327 TIKLVIVPELGRTAIHQISLEEMKDYLEK 355
Cdd:cd14863  350 IAEAVLKDPFAMFNPRPITEEEVAEILEA 378
Fe-ADH-like cd14864
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 9-133 1.50e-06

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: 341486 [Multi-domain]  Cd Length: 376  Bit Score: 49.61  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404   9 NHPYDIVIEKGTLAKAGEWLASLwsAQKIVVITD-NHVASLYAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEf 87
Cdd:cd14864    2 KIPPNIVFGADSLERIGEEVKEY--GSRFLLITDpVLKESGLADKIVSSLEKAGISVIVFDEIPASAT--SDTIDEAAE- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568065404  88 LAKVGmtRSDGIVALGGGVVGDLAGFAASTY----------------MRGIHFVQIPTSLTA 133
Cdd:cd14864   77 LARKA--GADGIIAVGGGKVLDTAKAVAILAnndggaydflegakpkKKPLPLIAVPTTPRS 136
Fe-ADH-like cd08196
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 10-167 9.44e-06

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: 341475 [Multi-domain]  Cd Length: 367  Bit Score: 46.80  E-value: 9.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  10 HPYDIVIEKGTLAKAGEWLASLwSAQKIVVITDNHVA-SLYAETVKCSLEvtGFEVFVFDflegEASKN--LTTVNKVYE 86
Cdd:cd08196    5 QPVKIIFGEGILKELPDIIKEL-GGKRGLLVTDPSFIkSGLAKRIVESLK--GRIVAVFS----DVEPNptVENVDKCAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  87 FLAKVGMtrsDGIVALGGGVVGDLAGFAASTYM-----------------RGIHFVQIPTslTAQVDSSIggktgvnTPW 149
Cdd:cd08196   78 LARENGA---DFVIAIGGGSVLDTAKAAACLAKtdgsiedylegkkkipkKGLPLIAIPT--TAGTGSEV-------TPV 145

                        170       180
                 ....*....|....*....|....*...
gi 568065404 150 A----------KNMVGTFTQPDGVLIDP 167
Cdd:cd08196  146 AvltdkekgkkAPLVSPGFYPDIAIVDP 173
Fe-ADH-like cd17814
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 14-111 4.00e-05

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: 341489 [Multi-domain]  Cd Length: 374  Bit Score: 45.23  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  14 IVIEKGTLAKAGEWLASLwSAQKIVVITDNHV--ASLYAETVKCsLEVTGFEVFVFDflegeaskNLTTVNKVYEFLAKV 91
Cdd:cd17814    7 FIFGVGARKLAGRYAKNL-GARKVLVVTDPGVikAGWVDEVLDS-LEAEGLEYVVFS--------DVTPNPRDFEVMEGA 76

                         90       100
                 ....*....|....*....|...
gi 568065404  92 GMTRS---DGIVALGGGVVGDLA 111
Cdd:cd17814   77 ELYREegcDGIVAVGGGSPIDCA 99
Fe-ADH-like cd14862
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 33-111 4.34e-05

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: 44.91  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  33 SAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDFLEGEASknLTTVNKVYEFLAkvgMTRSDGIVALGGGVVGDLA 111
Cdd:cd14862   23 SGKRALIVTDKVLVKLgLLKKVLKRLLQAGFEVEVFDEVEPEPP--LETVLKGAEAMR---EFEPDLIIALGGGSVMDAA 97
HEPD cd08182
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ...
 11-173 1.54e-04

Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.


Pssm-ID: 341461 [Multi-domain]  Cd Length: 370  Bit Score: 43.37  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAGEWLASLwSAQKIVVITDNH-VASLYAETVKCSLEVtGFEVFVFDFlegeASKNlTTVNKVYEFLA 89
Cdd:cd08182    1 PVKIIFGPGALAELKDLLGGL-GARRVLLVTGPSaVRESGAADILDALGG-RIPVVVFSD----FSPN-PDLEDLERGIE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  90 KVGMTRSDGIVALGGGVVGDLA-GFAASTYM-----------------RGIHFVQIPTslTAqvdssiGgkTG--VnTPW 149
Cdd:cd08182   74 LFRESGPDVIIAVGGGSVIDTAkAIAALLGSpgenllllrtgekapeeNALPLIAIPT--TA------G--TGseV-TPF 142

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568065404 150 A-----KNMV-----GTFTQPDGVLIDPDVLKTL 173
Cdd:cd08182  143 AtiwdeAEGKkyslaHPSLYPDAAILDPELTLSL 176
HVD cd08193
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ...
 14-115 6.33e-04

5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.


Pssm-ID: 341472 [Multi-domain]  Cd Length: 379  Bit Score: 41.34  E-value: 6.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  14 IVIEKGTLAKAGEwLASLWSAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDflEGEASKNLTTVnkvyefLAKVG 92
Cdd:cd08193    7 IICGAGAAARLGE-LLRELGARRVLLVTDPGLVKAgLADPALAALEAAGIAVTVFD--DVVADPPEAVV------EAAVE 77

                         90       100
                 ....*....|....*....|....*.
gi 568065404  93 MTRS---DGIVALGGGVVGDLAGFAA 115
Cdd:cd08193   78 QAREagaDGVIGFGGGSSMDVAKLVA 103
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 17-129 6.79e-04

Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.


Pssm-ID: 341451 [Multi-domain]  Cd Length: 346  Bit Score: 40.96  E-value: 6.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  17 EKGTLAKAGEWLASLwSAQKIVVITDN---HVASLYAEtvkcSLEVTGFEVFVFDfleGEASKNlttvnKVYEFLAKVGM 93
Cdd:cd08172    7 EEGALKELPELLSEF-GIKRPLIIHGEkswQAAKPYLP----KLFEIEYPVLRYD---GECSYE-----EIDRLAEEAKE 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568065404  94 TRSDGIVALGGGVVGDLAGFAAstYMRGIHFVQIPT 129
Cdd:cd08172   74 HQADVIIGIGGGKVLDTAKAVA--DKLNIPLILIPT 107
AAD_C cd08178
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ...
 11-111 2.29e-03

C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.


Pssm-ID: 341457 [Multi-domain]  Cd Length: 400  Bit Score: 39.48  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  11 PYDIVIEKGTLAKAgewLASLWSAQKIVVITDNHVASL-YAETVKCSLEVTGFEVFVFDFLEGEAsknltTVNKVYEFLA 89
Cdd:cd08178    3 PPKIYFEPGCLPYL---LLELPGVKRAFIVTDRVLYKLgYVDKVLDVLEARGVETEVFSDVEPDP-----TLSTVRKGLE 74

                         90       100
                 ....*....|....*....|..
gi 568065404  90 KVGMTRSDGIVALGGGVVGDLA 111
Cdd:cd08178   75 AMNAFKPDVIIALGGGSAMDAA 96
NADPH_BDH cd08179
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ...
 10-173 9.96e-03

NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.


Pssm-ID: 341458 [Multi-domain]  Cd Length: 379  Bit Score: 37.55  E-value: 9.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  10 HPYDIVIEKGTLakagEWLASLwSAQKIVVITDNHV--ASLYAETVKCSLEVTGFEVFVFDFLEGEASknlttVNKVYEF 87
Cdd:cd08179    4 VPRDIYFGEGAL----EYLKTL-KGKRAFIVTGGGSmkRNGFLDKVEDYLKEAGMEVKVFEGVEPDPS-----VETVEKG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568065404  88 LAKVGMTRSDGIVALGGGVVGD-------------------LAGFAASTYMRGIHFVQIP-TSLTAQ--------VDSSI 139
Cdd:cd08179   74 AEAMREFEPDWIIAIGGGSVIDaakamwvfyeypeltfedaLVPFPLPELRKKARFIAIPsTSGTGSevtrasviTDTEK 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568065404 140 GGKTGVNTPwakNMVgtftqPDGVLIDPDVLKTL 173
Cdd:cd08179  154 GIKYPLASF---EIT-----PDVAILDPELTMTM 179
 
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