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Conserved domains on  [gi|501388157|ref|WP_012419723|]
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MULTISPECIES: 3-dehydroquinate synthase [Akkermansia]

Protein Classification

dehydroquinate synthase/iron-containing alcohol dehydrogenase family protein( domain architecture ID 760)

dehydroquinate synthase (DHQS)/iron-containing alcohol dehydrogenase (FeADH) family protein

CATH:  3.40.50.1970
Gene Ontology:  GO:0046872|GO:0030554
PubMed:  9685163|35751426
SCOP:  3001905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHQ_Fe-ADH super family cl02872
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 1-386 0e+00

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.


The actual alignment was detected with superfamily member PRK06203:

Pssm-ID: 445950  Cd Length: 389  Bit Score: 576.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   1 MSLHTLNIRLDFPYRTGFTHGAFRPENDALASLMEQRPG---SRVLVLLEKGLEQFYPQLPSDIDRYFEKNAGVLAYAG- 76
Cdd:PRK06203   1 MRVIRQSFAVTFEYPVYFTRDLFSPENPLLAEVLAADGEgkpKKVLVVIDSGVLRAHPDLLEQITAYFAAHADVLELVAe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  77 CCSVPGGEEAKTGFSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNG 156
Cdd:PRK06203  81 PLVVPGGEAAKNDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 157 INFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSAL 236
Cdd:PRK06203 161 INAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 237 LHASHIACGGDAFELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELP 316
Cdd:PRK06203 241 LHLEHIAGGGDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGFP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 317 VFHPLLSRRTENgACEVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECIREMQEAAGYSVQ 386
Cdd:PRK06203 321 LYHPALATRDSK-GRELLKGLEEFREHLGGRLTITLLTGIGRGIEVHEIDLDLLRQAIARLAERAKASTA 389
 
Name Accession Description Interval E-value
aroB PRK06203
3-dehydroquinate synthase; Reviewed
 1-386 0e+00

3-dehydroquinate synthase; Reviewed


Pssm-ID: 235740  Cd Length: 389  Bit Score: 576.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   1 MSLHTLNIRLDFPYRTGFTHGAFRPENDALASLMEQRPG---SRVLVLLEKGLEQFYPQLPSDIDRYFEKNAGVLAYAG- 76
Cdd:PRK06203   1 MRVIRQSFAVTFEYPVYFTRDLFSPENPLLAEVLAADGEgkpKKVLVVIDSGVLRAHPDLLEQITAYFAAHADVLELVAe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  77 CCSVPGGEEAKTGFSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNG 156
Cdd:PRK06203  81 PLVVPGGEAAKNDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 157 INFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSAL 236
Cdd:PRK06203 161 INAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 237 LHASHIACGGDAFELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELP 316
Cdd:PRK06203 241 LHLEHIAGGGDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGFP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 317 VFHPLLSRRTENgACEVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECIREMQEAAGYSVQ 386
Cdd:PRK06203 321 LYHPALATRDSK-GRELLKGLEEFREHLGGRLTITLLTGIGRGIEVHEIDLDLLRQAIARLAERAKASTA 389
DHQS-like cd08198
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 14-377 1.35e-161

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: 457.80  E-value: 1.35e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  14 YRTGFTHGAFRPENDALASL---MEQRPGSRVLVLLEKGLEQFYPQLPSDIDRYFEKNAGVLAYAG-CCSVPGGEEAKTG 89
Cdd:cd08198    2 YPVCFTHDLFSPDNPLLRALlvrRGPGRRHRVLFVIDSGVAAAHPALVKQIERYFQAHPDRLELVApPLIVPGGEAVKND 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  90 FSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTF 169
Cdd:cd08198   82 PALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGTF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 170 AVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALLHASHIACGGDAF 249
Cdd:cd08198  162 APPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAELHLDHIAASGDPF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 250 ELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPLLSRRTENg 329
Cdd:cd08198  242 ETGSARPLDFGHWSAHKLEQLSGYALRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLPLWHPLLERDGVL- 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 501388157 330 acEVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECIREM 377
Cdd:cd08198  321 --ELLDGLEEFREHLGGRLTITLLRGIGVGVEVHEIDLDLMEEAIDEL 366
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 5-374 9.95e-111

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: 328.20  E-value: 9.95e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   5 TLNIRL-DFPYRTGFTHGAFRPENDALASLMeqrPGSRVLVLLEKGLEQFYPQlpsDIDRYFEKnAGVLAYAgcCSVPGG 83
Cdd:COG0337    3 TLTVNLgERSYDIRIGRGLLDELGELLAELL---KGRRVLVVTDENVAPLYGE---RLRAALEA-AGFEVHL--LVLPDG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  84 EEAKTgFSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRK 163
Cdd:COG0337   74 EASKT-LETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 164 NYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALLHASHIA 243
Cdd:COG0337  153 NLIGAFHQPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 244 cgGDAFELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPLLS 323
Cdd:COG0337  233 --ADERESGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALD 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501388157 324 rrtengACEVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECI 374
Cdd:COG0337  311 ------PEALLAAMKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 78-323 5.97e-77

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: 238.55  E-value: 5.97e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   78 CSVPGGEEAKTgFSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGI 157
Cdd:pfam01761   2 IVIPDGEKSKT-LETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  158 NFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALL 237
Cdd:pfam01761  81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  238 HASHIAcgGDAFELGSSRPLDFGHWAAHYMETMSGY-TLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELP 316
Cdd:pfam01761 161 KADVVA--QDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLP 238


                  ....*..
gi 501388157  317 VFHPLLS 323
Cdd:pfam01761 239 TSLPDLD 245
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 38-374 2.79e-59

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: 195.54  E-value: 2.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   38 PGSRVLVLLEKGLEQFYPQLPSDIDRYFEKNAGVLayagccSVPGGEEAKTgfsaWETALR---HIVEAGIDRHSYIIAV 114
Cdd:TIGR01357  19 EPSKLVIITDETVADLYGDKLLEALQALGYNVLKL------TVPDGEESKS----LETVQRlydQLLEAGLDRSSTIIAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  115 GGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGL 194
Cdd:TIGR01357  89 GGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLPDRELRSGM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  195 AEVVKVAVVKDASFFNWLETNASA-LAVCERDALEYAVEHSALLHASHIAcgGDAFELGSSRPLDFGHWAAHYMETMSGY 273
Cdd:TIGR01357 169 AEVIKHGLIADAELFDELESNDKLrLNLQELEHLEELIKRSIEVKASIVA--EDEKESGLRAILNFGHTIGHAIEAEAGY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  274 T-LGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPllsrrTENGACEVLKGLEAFREHLGGHLTVLM 352
Cdd:TIGR01357 247 GkIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLP-----KDLDVDELLNAMLNDKKNSGGKIRFVL 321

                         330       340
                  ....*....|....*....|..
gi 501388157  353 LTGIGRGKDVHEIDAALMEECI 374
Cdd:TIGR01357 322 LEEIGKAALAREVPDEMVLELL 343
 
Name Accession Description Interval E-value
aroB PRK06203
3-dehydroquinate synthase; Reviewed
 1-386 0e+00

3-dehydroquinate synthase; Reviewed


Pssm-ID: 235740  Cd Length: 389  Bit Score: 576.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   1 MSLHTLNIRLDFPYRTGFTHGAFRPENDALASLMEQRPG---SRVLVLLEKGLEQFYPQLPSDIDRYFEKNAGVLAYAG- 76
Cdd:PRK06203   1 MRVIRQSFAVTFEYPVYFTRDLFSPENPLLAEVLAADGEgkpKKVLVVIDSGVLRAHPDLLEQITAYFAAHADVLELVAe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  77 CCSVPGGEEAKTGFSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNG 156
Cdd:PRK06203  81 PLVVPGGEAAKNDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 157 INFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSAL 236
Cdd:PRK06203 161 INAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 237 LHASHIACGGDAFELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELP 316
Cdd:PRK06203 241 LHLEHIAGGGDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGFP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 317 VFHPLLSRRTENgACEVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECIREMQEAAGYSVQ 386
Cdd:PRK06203 321 LYHPALATRDSK-GRELLKGLEEFREHLGGRLTITLLTGIGRGIEVHEIDLDLLRQAIARLAERAKASTA 389
DHQS-like cd08198
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 14-377 1.35e-161

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: 457.80  E-value: 1.35e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  14 YRTGFTHGAFRPENDALASL---MEQRPGSRVLVLLEKGLEQFYPQLPSDIDRYFEKNAGVLAYAG-CCSVPGGEEAKTG 89
Cdd:cd08198    2 YPVCFTHDLFSPDNPLLRALlvrRGPGRRHRVLFVIDSGVAAAHPALVKQIERYFQAHPDRLELVApPLIVPGGEAVKND 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  90 FSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTF 169
Cdd:cd08198   82 PALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGTF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 170 AVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALLHASHIACGGDAF 249
Cdd:cd08198  162 APPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAELHLDHIAASGDPF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 250 ELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPLLSRRTENg 329
Cdd:cd08198  242 ETGSARPLDFGHWSAHKLEQLSGYALRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLPLWHPLLERDGVL- 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 501388157 330 acEVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECIREM 377
Cdd:cd08198  321 --ELLDGLEEFREHLGGRLTITLLRGIGVGVEVHEIDLDLMEEAIDEL 366
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 5-374 9.95e-111

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: 328.20  E-value: 9.95e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   5 TLNIRL-DFPYRTGFTHGAFRPENDALASLMeqrPGSRVLVLLEKGLEQFYPQlpsDIDRYFEKnAGVLAYAgcCSVPGG 83
Cdd:COG0337    3 TLTVNLgERSYDIRIGRGLLDELGELLAELL---KGRRVLVVTDENVAPLYGE---RLRAALEA-AGFEVHL--LVLPDG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  84 EEAKTgFSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRK 163
Cdd:COG0337   74 EASKT-LETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 164 NYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALLHASHIA 243
Cdd:COG0337  153 NLIGAFHQPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 244 cgGDAFELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPLLS 323
Cdd:COG0337  233 --ADERESGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALD 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501388157 324 rrtengACEVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECI 374
Cdd:COG0337  311 ------PEALLAAMKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
 14-359 6.80e-78

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: 243.08  E-value: 6.80e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  14 YRTGFTHGAFRPENdalaSLMEQRPGSRVLVLLEKGLEQFYPQlpsDIDRYFEKNAGVLAyagcCSVPGGEEAKTgFSAW 93
Cdd:cd08169    2 YPVFFGEGVFESVN----SYIPRDAFDQCLIIVDSGVPDLIVN---YLAEYFGYYLEVHV----FIIQGGEAYKT-FQTV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  94 ETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTFAVAW 173
Cdd:cd08169   70 VEELERAAALHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 174 ATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALLHASHIACGGDafELGS 253
Cdd:cd08169  150 AVFADFSFLKTLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADED--EQGK 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 254 SRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPLLSRRTengacEV 333
Cdd:cd08169  228 RRGLNYGHTFGHALELASGYKIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALDPD-----SL 302

                        330       340
                 ....*....|....*....|....*.
gi 501388157 334 LKGLEAFREHLGGHLTVLMLTGIGRG 359
Cdd:cd08169  303 YEYLESDKKSLYGNLGMILLSGVGDG 328
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 78-323 5.97e-77

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: 238.55  E-value: 5.97e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   78 CSVPGGEEAKTgFSAWETALRHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGI 157
Cdd:pfam01761   2 IVIPDGEKSKT-LETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  158 NFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALL 237
Cdd:pfam01761  81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  238 HASHIAcgGDAFELGSSRPLDFGHWAAHYMETMSGY-TLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELP 316
Cdd:pfam01761 161 KADVVA--QDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLP 238


                  ....*..
gi 501388157  317 VFHPLLS 323
Cdd:pfam01761 239 TSLPDLD 245
EEVS cd08199
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ...
 14-374 2.43e-72

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: 229.72  E-value: 2.43e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  14 YRTGFTHGAFRPENDALASlMEQRPGSRVLVLLEKGLEQFYPqlpSDIDRYFEKNAGVLAYagcCSVPGGEEAKTgfsaW 93
Cdd:cd08199    2 YDVVLVDDLFDPENPTLAD-AYGRPGRRRLVVVDENVDRLYG---ARIRAYFAAHGIEATI---LVLPGGEANKT----M 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  94 ETALRhIVEA----GIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTF 169
Cdd:cd08199   71 ETVLR-IVDAlddfGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAY 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 170 AVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALaVCERDALEyAVEHSALLHASHI---ACGG 246
Cdd:cd08199  150 YPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAAL-VETRFFQD-EVADEIIRRAIQGmleELAP 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 247 DAFELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPLLSRRT 326
Cdd:cd08199  228 NLWEHDLERLVDFGHTFSPILEMAAAPELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWHPLCTPDL 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 501388157 327 engaceVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECI 374
Cdd:cd08199  308 ------LWRALEDIVKHRDGLQRLPLPKGIGECVFVNDVTEEELERAL 349
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 28-374 4.48e-68

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: 218.47  E-value: 4.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  28 DALASLMEQRPGSRVLVLLEKGLEQFYpqlpsdIDRYFEKNAGVLAYAGCCSVPGGEEAKTgFSAWETALRHIVEAGIDR 107
Cdd:cd08195   12 DKLGELLELKKGSKVVIVTDENVAKLY------GELLLKSLEAAGFKVEVIVIPAGEKSKS-LETVERIYDFLLEAGLDR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 108 HSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTFAVAWATLDDFLFLHSqpL 187
Cdd:cd08195   85 DSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLKT--L 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 188 PLK--RAGLaevvkvavvKDASFFNWLETNASALAVCERDALEYAVEHSALLHASHIAcgGDAFELGSSRPLDFGHWAAH 265
Cdd:cd08195  163 PERefRSGLaevikygliADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVE--EDEREKGLRAILNFGHTFGH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 266 YMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPLLSrrtengacevlkgLEAFREHL- 344
Cdd:cd08195  241 AIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLD-------------PEELLEAMk 307

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 501388157 345 ------GGHLTVLMLTGIGRGKDVHEIDAALMEECI 374
Cdd:cd08195  308 rdkknrGGKIRFVLLKGIGKAVIVDDVSEEEIREAL 343
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 38-374 2.79e-59

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: 195.54  E-value: 2.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157   38 PGSRVLVLLEKGLEQFYPQLPSDIDRYFEKNAGVLayagccSVPGGEEAKTgfsaWETALR---HIVEAGIDRHSYIIAV 114
Cdd:TIGR01357  19 EPSKLVIITDETVADLYGDKLLEALQALGYNVLKL------TVPDGEESKS----LETVQRlydQLLEAGLDRSSTIIAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  115 GGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGL 194
Cdd:TIGR01357  89 GGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLPDRELRSGM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  195 AEVVKVAVVKDASFFNWLETNASA-LAVCERDALEYAVEHSALLHASHIAcgGDAFELGSSRPLDFGHWAAHYMETMSGY 273
Cdd:TIGR01357 169 AEVIKHGLIADAELFDELESNDKLrLNLQELEHLEELIKRSIEVKASIVA--EDEKESGLRAILNFGHTIGHAIEAEAGY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  274 T-LGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPllsrrTENGACEVLKGLEAFREHLGGHLTVLM 352
Cdd:TIGR01357 247 GkIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLP-----KDLDVDELLNAMLNDKKNSGGKIRFVL 321

                         330       340
                  ....*....|....*....|..
gi 501388157  353 LTGIGRGKDVHEIDAALMEECI 374
Cdd:TIGR01357 322 LEEIGKAALAREVPDEMVLELL 343
PLN02834 PLN02834
3-dehydroquinate synthase
 38-377 2.33e-49

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 172.26  E-value: 2.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  38 PGSRVLVLLEKGLEQFYPQlpsDIDRYFEKNAGVLAYAGCCsVPGGEEAKTgFSAWETALRHIVEAGIDRHSYIIAVGGG 117
Cdd:PLN02834  99 HGKRVLVVTNETVAPLYLE---KVVEALTAKGPELTVESVI-LPDGEKYKD-METLMKVFDKALESRLDRRCTFVALGGG 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 118 AFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEV 197
Cdd:PLN02834 174 VIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEV 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 198 VKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALLHASHIAcgGDAFELGSSRPLDFGHWAAHYMETMSGY-TLG 276
Cdd:PLN02834 254 VKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVS--LDEKESGLRATLNLGHTFGHAIETGPGYgEWL 331

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 277 HAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPVFHPllsrrtENGACEVLKGLEAF-REHLGGHLTVLMLTG 355
Cdd:PLN02834 332 HGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPP------EKMTVEMFKSLMAVdKKVADGLLRLILLKG 405

                        330       340
                 ....*....|....*....|...
gi 501388157 356 -IGRGKDVHEIDAALMEECIREM 377
Cdd:PLN02834 406 eLGNCVFTGDFDREALEETLRAF 428
DOIS cd08197
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ...
 28-317 6.77e-43

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: 153.12  E-value: 6.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  28 DALASLMEQRPGSRVLVLLEKGLEQFYpqlpsdIDRYFEKNAGVLAYAGCCSVPGGEEAKTgFSAWETALRHIVEAGIDR 107
Cdd:cd08197   12 ESLLSILEELKADRHFLVTDSNVNDLY------GDRLLEGLKKAGIPVELLVVPAGESNKT-LSTLTELAERLIAAGITR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 108 HSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTFAVAWATLDDFLFLHSQPL 187
Cdd:cd08197   85 RSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLKTLPP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 188 PLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYAVEHSALLHASHIAcgGDAFELGSSRPLDFGHWAAHYM 267
Cdd:cd08197  165 RQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLS--NDPYEKKEGLILEYGHTVGHAI 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 501388157 268 ETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPV 317
Cdd:cd08197  243 ELLSGGELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPT 292
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
 80-379 3.11e-20

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 92.23  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  80 VPGGEEAKTGFSA---WEtalrHIVEAGIDRHSYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNG 156
Cdd:PRK14021 243 IPDAEAGKTIEVAngiWQ----RLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTG 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 157 INFMGRKNYLGTFAVAWATLDDFLFLHSQPLPLKRAGLAEVVKVAVVKDASFFNWLETNASALAVCERDALEYA------ 230
Cdd:PRK14021 319 INTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRAFDGSTFLGSpledvv 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 231 ---VEHSALLHASHIAcgGDAFELGSSRPLDFGHWAAHYMETMSGYTLGHAEAVSVGMCLDILYSVRKGWLPAAEAERII 307
Cdd:PRK14021 399 aelIERTVKVKAYHVS--SDLKEAGLREFLNYGHTLGHAIEKLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHR 476

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501388157 308 SVLKTLELPVfhpllsrrTENGAC--EVLKGLEAFREHLGGHLTVLMLTGIGRGKDVHEIDAALMEECIREMQE 379
Cdd:PRK14021 477 SLLASLGLPT--------SWNGGSfdDVLALMHRDKKARGNELRFVVLDEIGHPVHLDNPPAEAVEEAFRRIQQ 542
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
36-313 6.21e-19

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 88.04  E-value: 6.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  36 QRPGSRVLVLLEKGLEQFYpqlpsdiDRYFEKNAGVLayagccsvPGGEEAKTgFSAWETALRHIVEAGIDRHSYIIAVG 115
Cdd:PRK13951 182 KRVRNEELVFTTERVEKIY-------GRYLPENRLLF--------PDGEEVKT-LEHVSRAYYELVRMDFPRGKTIAGVG 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 116 GGAFLDVAGFAAATAHRGIRLLRIPTTTLSQADSGVGVKNGINFMGRKNYLGTF---------AVAWATLDDFLFLHSQP 186
Cdd:PRK13951 246 GGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAIDFAGVKNVVGTFrmpdyviidPTVTLSMDEGRFEEGVV 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 187 LPLKRAGLaevvkvaVVKDASFFNWLET----NASALAvcerDALEYAVEHSALLHAShiacggDAFELGSSRPLDFGHW 262
Cdd:PRK13951 326 EAFKMTIL-------SGRGVELFDEPEKiekrNLRVLS----EMVKISVEEKARIVME------DPYDMGLRHALNLGHT 388

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501388157 263 AAHYMETMSGytLGHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTL 313
Cdd:PRK13951 389 LGHVYEMLEG--VPHGIAVAWGIEKETMYLYRKGIVPKETMRWIVEKVKQI 437
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 13-317 1.30e-11

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: 64.31  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  13 PYRTGFTHGAfrpendaLASLME--QRPGSRVLVLLEKGLEQFypqLPSDIDRYFEKNAGVLAYagccSVPGGEEAktgF 90
Cdd:cd07766    1 PTRIVFGEGA-------IAKLGEikRRGFDRALVVSDEGVVKG---VGEKVADSLKKGLAVAIF----DFVGENPT---F 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  91 SAWETALRHIVEAGIDrhsYIIAVGGGAFLDVAGFAAATAHRGIRLLRIPTTTLsqADSGVGVKNGINFMGRKN------ 164
Cdd:cd07766   64 EEVKNAVERARAAEAD---AVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAS--TDSEVSPKSVITDKGGKNkqvgph 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157 165 YLGTFAVAwatldDFLFLHSQPLPLKRAGLAevvkvavvkdasffnwletnasalavcerDALEYAVEHSALLHAShIAC 244
Cdd:cd07766  139 YNPDVVFV-----DTDITKGLPPRQVASGGV-----------------------------DALAHAVELEKVVEAA-TLA 183

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501388157 245 GGDAFELGSsrpLDFGHWAAHYMETMSGYTlgHAEAVSVGMCLDILYSVRKGWLPAAEAERIISVLKTLELPV 317
Cdd:cd07766  184 GMGLFESPG---LGLAHAIGHALTAFEGIP--HGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPT 251
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 30-145 3.00e-06

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: 48.67  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501388157  30 LASLMEQRPGSRVLVLL-EKGLEQFYPQLPSDidryFEKNAGVLAYAGCCSVpggEEAKtgfsawetalRHIVEAGIDRH 108
Cdd:cd08172   14 LPELLSEFGIKRPLIIHgEKSWQAAKPYLPKL----FEIEYPVLRYDGECSY---EEID----------RLAEEAKEHQA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 501388157 109 SYIIAVGGGAFLDVAGfaaATAHR-GIRLLRIPT--------TTLS 145
Cdd:cd08172   77 DVIIGIGGGKVLDTAK---AVADKlNIPLILIPTlasncaawTPLS 119
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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