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Conserved domains on  [gi|544677873|ref|WP_021110164|]
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inositol 2-dehydrogenase [Glaesserella parasuis]

Protein Classification

inositol 2-dehydrogenase( domain architecture ID 11500263)

inositol 2-dehydrogenase catalyzes the first step in inositol catabolism; it is involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
1-331 0e+00

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


:

Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 540.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873    1 MLKVGIIGAGRIGRVHSESISKYVKGAEIKAISDIkVTDELTAWAKSMGIPNVYDDYKKILQDPEIDAVLVCSSTNTHAP 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVPGARLKAIVDP-FADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873   81 ISIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGFNRRFDHNFKAIKNRVANGDIGDPHLIRVTSRDPDAPP 160
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDPAPPP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  161 IEYVKVSGGMFFDMTIHDFDMVRYLSGSEVVEVFAAGGVLVNPEIGKAGDIDTAVITLKLANGAIAVIDNSRKAVYGYDQ 240
Cdd:TIGR04380 160 VAYVKVSGGLFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDPAIGEAGDVDTAVITLKFENGAIAVIDNSRRAAYGYDQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  241 RAEVFGSKGAVQTRNDTDSTAVYSCEAGVIAEKPKYFFLERYMQSFADEMACFIDSVVNNKPTLVNGNDGLQPVLIALAA 320
Cdd:TIGR04380 240 RVEVFGSKGMLRAENDTESTVILYDAEGVRGDKPLNFFLERYRDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLALAA 319
                         330
                  ....*....|.
gi 544677873  321 KKSLEENRPVK 331
Cdd:TIGR04380 320 KRSLEEGRPVK 330
 
Name Accession Description Interval E-value
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
1-331 0e+00

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 540.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873    1 MLKVGIIGAGRIGRVHSESISKYVKGAEIKAISDIkVTDELTAWAKSMGIPNVYDDYKKILQDPEIDAVLVCSSTNTHAP 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVPGARLKAIVDP-FADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873   81 ISIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGFNRRFDHNFKAIKNRVANGDIGDPHLIRVTSRDPDAPP 160
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDPAPPP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  161 IEYVKVSGGMFFDMTIHDFDMVRYLSGSEVVEVFAAGGVLVNPEIGKAGDIDTAVITLKLANGAIAVIDNSRKAVYGYDQ 240
Cdd:TIGR04380 160 VAYVKVSGGLFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDPAIGEAGDVDTAVITLKFENGAIAVIDNSRRAAYGYDQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  241 RAEVFGSKGAVQTRNDTDSTAVYSCEAGVIAEKPKYFFLERYMQSFADEMACFIDSVVNNKPTLVNGNDGLQPVLIALAA 320
Cdd:TIGR04380 240 RVEVFGSKGMLRAENDTESTVILYDAEGVRGDKPLNFFLERYRDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLALAA 319
                         330
                  ....*....|.
gi 544677873  321 KKSLEENRPVK 331
Cdd:TIGR04380 320 KRSLEEGRPVK 330
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-334 7.88e-85

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 257.93  E-value: 7.88e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873   1 MLKVGIIGAGRIGRVHSESISKyVKGAEIKAISDIkVTDELTAWAKSMGIPnVYDDYKKILQDPEIDAVLVCSSTNTHAP 80
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAA-LPGVELVAVADR-DPERAEAFAEEYGVR-VYTDYEELLADPDIDAVVIATPNHLHAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  81 ISIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGFNRRFDHNFKAIKNRVANGDIGDPHLIRVT-SRDPDAP 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARfGHPRPAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873 160 PIEYV----KVSGGMFFDMTIHDFDMVRYLSGSEVVEVFAAGGVLVNPEIgkaGDIDTAVITLKLANGAIAVIDNSRKAV 235
Cdd:COG0673  160 PADWRfdpeLAGGGALLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRV---EVDDTAAATLRFANGAVATLEASWVAP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873 236 YG-YDQRAEVFGSKGAVqtrndtdstavysceagviaekpkyfflerymqsfademacFIDSVVNNKPTLVNGNDGLQPV 314
Cdd:COG0673  237 GGeRDERLEVYGTKGTL-----------------------------------------FVDAIRGGEPPPVSLEDGLRAL 275
                        330       340
                 ....*....|....*....|
gi 544677873 315 LIALAAKKSLEENRPVKLSE 334
Cdd:COG0673  276 ELAEAAYESARTGRRVELPD 295
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
2-123 4.18e-29

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 108.45  E-value: 4.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873    2 LKVGIIGAGRIGRVHSESISKYVKGAEIKAISDIKVTDELTAwAKSMGIPnVYDDYKKILQDPEIDAVLVCSSTNTHAPI 81
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEAV-AESFGVE-VYSDLEELLNDPEIDAVIVATPNGLHYDL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 544677873   82 SIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGF 123
Cdd:pfam01408  79 AIAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
2-145 3.52e-12

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 66.28  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873   2 LKVGIIGAGRIGRV-HSESISKyVKGAEIKAISDikvTDELTAWAKSMGIPnVYDDYKKILQDPEIDAVLVCSSTNTHAP 80
Cdd:PRK11579   5 IRVGLIGYGYASKTfHAPLIAG-TPGLELAAVSS---SDATKVKADWPTVT-VVSEPQHLFNDPNIDLIVIPTPNDTHFP 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544677873  81 ISIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGFNRRFDHNFKAIKNRVANGDIGD 145
Cdd:PRK11579  80 LAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGE 144
 
Name Accession Description Interval E-value
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
1-331 0e+00

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 540.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873    1 MLKVGIIGAGRIGRVHSESISKYVKGAEIKAISDIkVTDELTAWAKSMGIPNVYDDYKKILQDPEIDAVLVCSSTNTHAP 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVPGARLKAIVDP-FADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873   81 ISIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGFNRRFDHNFKAIKNRVANGDIGDPHLIRVTSRDPDAPP 160
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDPAPPP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  161 IEYVKVSGGMFFDMTIHDFDMVRYLSGSEVVEVFAAGGVLVNPEIGKAGDIDTAVITLKLANGAIAVIDNSRKAVYGYDQ 240
Cdd:TIGR04380 160 VAYVKVSGGLFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDPAIGEAGDVDTAVITLKFENGAIAVIDNSRRAAYGYDQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  241 RAEVFGSKGAVQTRNDTDSTAVYSCEAGVIAEKPKYFFLERYMQSFADEMACFIDSVVNNKPTLVNGNDGLQPVLIALAA 320
Cdd:TIGR04380 240 RVEVFGSKGMLRAENDTESTVILYDAEGVRGDKPLNFFLERYRDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLALAA 319
                         330
                  ....*....|.
gi 544677873  321 KKSLEENRPVK 331
Cdd:TIGR04380 320 KRSLEEGRPVK 330
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-334 7.88e-85

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 257.93  E-value: 7.88e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873   1 MLKVGIIGAGRIGRVHSESISKyVKGAEIKAISDIkVTDELTAWAKSMGIPnVYDDYKKILQDPEIDAVLVCSSTNTHAP 80
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAA-LPGVELVAVADR-DPERAEAFAEEYGVR-VYTDYEELLADPDIDAVVIATPNHLHAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  81 ISIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGFNRRFDHNFKAIKNRVANGDIGDPHLIRVT-SRDPDAP 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARfGHPRPAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873 160 PIEYV----KVSGGMFFDMTIHDFDMVRYLSGSEVVEVFAAGGVLVNPEIgkaGDIDTAVITLKLANGAIAVIDNSRKAV 235
Cdd:COG0673  160 PADWRfdpeLAGGGALLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRV---EVDDTAAATLRFANGAVATLEASWVAP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873 236 YG-YDQRAEVFGSKGAVqtrndtdstavysceagviaekpkyfflerymqsfademacFIDSVVNNKPTLVNGNDGLQPV 314
Cdd:COG0673  237 GGeRDERLEVYGTKGTL-----------------------------------------FVDAIRGGEPPPVSLEDGLRAL 275
                        330       340
                 ....*....|....*....|
gi 544677873 315 LIALAAKKSLEENRPVKLSE 334
Cdd:COG0673  276 ELAEAAYESARTGRRVELPD 295
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
2-123 4.18e-29

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 108.45  E-value: 4.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873    2 LKVGIIGAGRIGRVHSESISKYVKGAEIKAISDIKVTDELTAwAKSMGIPnVYDDYKKILQDPEIDAVLVCSSTNTHAPI 81
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEAV-AESFGVE-VYSDLEELLNDPEIDAVIVATPNGLHYDL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 544677873   82 SIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGF 123
Cdd:pfam01408  79 AIAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
135-332 2.24e-20

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 87.47  E-value: 2.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  135 KNRVANGDIGDPHLIRVTSRDPDAPPIEYV------KVSGGMFFDMTIHDFDMVRYLSGSEVVEVFAAGGvlvnpeigka 208
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHTRDPFRPPQEFKrwrvdpEKSGGALYDLGIHTIDLLIYLFGEPPSVVAVYAS---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  209 gdIDTAVITLKLANGAIAVIDNSR-KAVYGYDQRAEVFGSKGAV-----QTRNDTDST-----AVYSCEAGVIAEKPKYF 277
Cdd:pfam02894  71 --EDTAFATLEFKNGAVGTLETSGgSIVEANGHRISIHGTKGSIeldgiDDGLLSVTVvgepgWATDDPMVRKGGDEVPE 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 544677873  278 FLERYMQSFADEMACFIDSVVNNKPTLVNGNDGLQPVLIALAAKKSLEENRPVKL 332
Cdd:pfam02894 149 FLGSFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
PRK11579 PRK11579
putative oxidoreductase; Provisional
2-145 3.52e-12

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 66.28  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873   2 LKVGIIGAGRIGRV-HSESISKyVKGAEIKAISDikvTDELTAWAKSMGIPnVYDDYKKILQDPEIDAVLVCSSTNTHAP 80
Cdd:PRK11579   5 IRVGLIGYGYASKTfHAPLIAG-TPGLELAAVSS---SDATKVKADWPTVT-VVSEPQHLFNDPNIDLIVIPTPNDTHFP 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544677873  81 ISIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGFNRRFDHNFKAIKNRVANGDIGD 145
Cdd:PRK11579  80 LAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGE 144
PRK10206 PRK10206
putative oxidoreductase; Provisional
56-187 3.88e-09

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 57.14  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544677873  56 DYKKILQDPEIDAVLVCSSTNTHAPISIEAAQAGKHIFCEKPIDADVGRIHEVLSAVEKAGVKFQVGFNRRFDHNFKAIK 135
Cdd:PRK10206  55 DLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAK 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 544677873 136 NRVANGDIGDphLIRVTSRDPDAPPIEYVKVSG---GMFFDMTIHDFDMVRYLSG 187
Cdd:PRK10206 135 KAIESGKLGE--IVEVESHFDYYRPVAETKPGLpqdGAFYGLGVHTMDQIISLFG 187
 
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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