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Conserved domains on  [gi|328758689|gb|EGF72305|]
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inositol 2-dehydrogenase [Cutibacterium acnes HL020PA1]

Protein Classification

myo_inos_iolG superfamily protein( domain architecture ID 1904337)

myo_inos_iolG superfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
myo_inos_iolG super family cl44365
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 1-327 5.65e-127

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]


The actual alignment was detected with superfamily member TIGR04380:

Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 366.16  E-value: 5.65e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689    1 MIRIAIIGAGRIGHVHARAIQGRN-DVTLALVCDPFEQNARALAGEYDVRYCL-DPDEVFDDSTIDAVVIGSPTQFHVDH 78
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVpGARLKAIVDPFADAAAELAEKLGIEPVTqDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   79 ILKAVNGGKRVMCEKPIALDVESAKRCINELGDRADQVMMGFNRRFDPTFSALKSRLDDGEIGSLQQLTVISRDPAAPSA 158
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDPAPPPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  159 SYIAGSGGIFKDMTIHDFDMVRHFLGD-IAEVNAVGTN-VSPEIAEQGDFDQVIVTLKSRDGKLATIINSRTCAFGYDQR 236
Cdd:TIGR04380 161 AYVKVSGGLFLDMTIHDFDMARFLLGSeVEEVYAQGSVlVDPAIGEAGDVDTAVITLKFENGAIAVIDNSRRAAYGYDQR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  237 LEAFGADGMLSADNLTDAAVRMATSTQTDAKTAImDFFLERYEDAYRIELETFLDSIAIGGAVSPSVRDGYEALVLADAA 316
Cdd:TIGR04380 241 VEVFGSKGMLRAENDTESTVILYDAEGVRGDKPL-NFFLERYRDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLALAA 319

                         330
                  ....*....|.
gi 328758689  317 TRSAQEHRVVA 327
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 ...
 1-327 5.65e-127

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: 366.16  E-value: 5.65e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689    1 MIRIAIIGAGRIGHVHARAIQGRN-DVTLALVCDPFEQNARALAGEYDVRYCL-DPDEVFDDSTIDAVVIGSPTQFHVDH 78
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVpGARLKAIVDPFADAAAELAEKLGIEPVTqDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   79 ILKAVNGGKRVMCEKPIALDVESAKRCINELGDRADQVMMGFNRRFDPTFSALKSRLDDGEIGSLQQLTVISRDPAAPSA 158
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDPAPPPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  159 SYIAGSGGIFKDMTIHDFDMVRHFLGD-IAEVNAVGTN-VSPEIAEQGDFDQVIVTLKSRDGKLATIINSRTCAFGYDQR 236
Cdd:TIGR04380 161 AYVKVSGGLFLDMTIHDFDMARFLLGSeVEEVYAQGSVlVDPAIGEAGDVDTAVITLKFENGAIAVIDNSRRAAYGYDQR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  237 LEAFGADGMLSADNLTDAAVRMATSTQTDAKTAImDFFLERYEDAYRIELETFLDSIAIGGAVSPSVRDGYEALVLADAA 316
Cdd:TIGR04380 241 VEVFGSKGMLRAENDTESTVILYDAEGVRGDKPL-NFFLERYRDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLALAA 319

                         330
                  ....*....|.
gi 328758689  317 TRSAQEHRVVA 327
Cdd:TIGR04380 320 KRSLEEGRPVK 330
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-328 6.62e-71

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 222.11  E-value: 6.62e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   1 MIRIAIIGAGRIGHVHARAIQGRNDVTLALVCDPFEQNARALAGEYDVRYCLDPDEVFDDSTIDAVVIGSPTQFHVDHIL 80
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  81 KAVNGGKRVMCEKPIALDVESAKRCInELGDRAD-QVMMGFNRRFDPTFSALKSRLDDGEIGSLQQLTV-ISRDPAAPSA 158
Cdd:COG0673   83 AALEAGKHVLCEKPLALTLEEARELV-AAAEEAGvVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRArFGHPRPAGPA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689 159 SYIA----GSGGIFKDMTIHDFDMVRHFLG-DIAEVNAVGTNVSPEiaEQGDFDQVIVTLKSRDGKLATIINSRTCAFG- 232
Cdd:COG0673  162 DWRFdpelAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPD--RVEVDDTAAATLRFANGAVATLEASWVAPGGe 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689 233 YDQRLEAFGADGMLsadnltdaavrmatstqtdaktaimdffleryedayrieletFLDSIAIGGAVSPSVRDGYEALVL 312
Cdd:COG0673  240 RDERLEVYGTKGTL------------------------------------------FVDAIRGGEPPPVSLEDGLRALEL 277

                        330
                 ....*....|....*.
gi 328758689 313 ADAATRSAQEHRVVAL 328
Cdd:COG0673  278 AEAAYESARTGRRVEL 293
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 2-120 3.75e-30

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: 110.76  E-value: 3.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689    2 IRIAIIGAGRIGHVHARAIQ-GRNDVTLALVCDPFEQNARALAGEYDVRYCLDPDEVFDDSTIDAVVIGSPTQFHVDHIL 80
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNaSQPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 328758689   81 KAVNGGKRVMCEKPIALDVESAKRCINELGDRADQVMMGF 120
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
 2-143 8.32e-12

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 65.12  E-value: 8.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   2 IRIAIIGAGRIGHV-HARAIQGRNDVTLALVCDPFEQNARAlageyD---VRYCLDPDEVFDDSTIDAVVIGSPTQFHVD 77
Cdd:PRK11579   5 IRVGLIGYGYASKTfHAPLIAGTPGLELAAVSSSDATKVKA-----DwptVTVVSEPQHLFNDPNIDLIVIPTPNDTHFP 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 328758689  78 HILKAVNGGKRVMCEKPIALDVESAkRCINELGDRADQVMMGF-NRRFDPTFSALKSRLDDGEIGSL 143
Cdd:PRK11579  80 LAKAALEAGKHVVVDKPFTVTLSQA-RELDALAKSAGRVLSVFhNRRWDSDFLTLKALLAEGVLGEV 145
 
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 ...
 1-327 5.65e-127

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: 366.16  E-value: 5.65e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689    1 MIRIAIIGAGRIGHVHARAIQGRN-DVTLALVCDPFEQNARALAGEYDVRYCL-DPDEVFDDSTIDAVVIGSPTQFHVDH 78
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVpGARLKAIVDPFADAAAELAEKLGIEPVTqDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   79 ILKAVNGGKRVMCEKPIALDVESAKRCINELGDRADQVMMGFNRRFDPTFSALKSRLDDGEIGSLQQLTVISRDPAAPSA 158
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDPAPPPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  159 SYIAGSGGIFKDMTIHDFDMVRHFLGD-IAEVNAVGTN-VSPEIAEQGDFDQVIVTLKSRDGKLATIINSRTCAFGYDQR 236
Cdd:TIGR04380 161 AYVKVSGGLFLDMTIHDFDMARFLLGSeVEEVYAQGSVlVDPAIGEAGDVDTAVITLKFENGAIAVIDNSRRAAYGYDQR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  237 LEAFGADGMLSADNLTDAAVRMATSTQTDAKTAImDFFLERYEDAYRIELETFLDSIAIGGAVSPSVRDGYEALVLADAA 316
Cdd:TIGR04380 241 VEVFGSKGMLRAENDTESTVILYDAEGVRGDKPL-NFFLERYRDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLALAA 319

                         330
                  ....*....|.
gi 328758689  317 TRSAQEHRVVA 327
Cdd:TIGR04380 320 KRSLEEGRPVK 330
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-328 6.62e-71

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 222.11  E-value: 6.62e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   1 MIRIAIIGAGRIGHVHARAIQGRNDVTLALVCDPFEQNARALAGEYDVRYCLDPDEVFDDSTIDAVVIGSPTQFHVDHIL 80
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  81 KAVNGGKRVMCEKPIALDVESAKRCInELGDRAD-QVMMGFNRRFDPTFSALKSRLDDGEIGSLQQLTV-ISRDPAAPSA 158
Cdd:COG0673   83 AALEAGKHVLCEKPLALTLEEARELV-AAAEEAGvVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRArFGHPRPAGPA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689 159 SYIA----GSGGIFKDMTIHDFDMVRHFLG-DIAEVNAVGTNVSPEiaEQGDFDQVIVTLKSRDGKLATIINSRTCAFG- 232
Cdd:COG0673  162 DWRFdpelAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPD--RVEVDDTAAATLRFANGAVATLEASWVAPGGe 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689 233 YDQRLEAFGADGMLsadnltdaavrmatstqtdaktaimdffleryedayrieletFLDSIAIGGAVSPSVRDGYEALVL 312
Cdd:COG0673  240 RDERLEVYGTKGTL------------------------------------------FVDAIRGGEPPPVSLEDGLRALEL 277

                        330
                 ....*....|....*.
gi 328758689 313 ADAATRSAQEHRVVAL 328
Cdd:COG0673  278 AEAAYESARTGRRVEL 293
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 2-120 3.75e-30

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: 110.76  E-value: 3.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689    2 IRIAIIGAGRIGHVHARAIQ-GRNDVTLALVCDPFEQNARALAGEYDVRYCLDPDEVFDDSTIDAVVIGSPTQFHVDHIL 80
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNaSQPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 328758689   81 KAVNGGKRVMCEKPIALDVESAKRCINELGDRADQVMMGF 120
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 132-328 4.54e-19

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: 83.62  E-value: 4.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  132 KSRLDDGEIGSLQQLTVISRDPAAPSASYI------AGSGGIFKDMTIHDFDMVRHFLGDIAEVNAVgtnvspeIAEQgd 205
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHTRDPFRPPQEFKrwrvdpEKSGGALYDLGIHTIDLLIYLFGEPPSVVAV-------YASE-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  206 fDQVIVTLKSRDGKLATIINSRTCAFGY-DQRLEAFGADGMLSADNLTDA----AVRMAT------STQTDAKTAIMDFf 274
Cdd:pfam02894  72 -DTAFATLEFKNGAVGTLETSGGSIVEAnGHRISIHGTKGSIELDGIDDGllsvTVVGEPgwatddPMVRKGGDEVPEF- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 328758689  275 LERYEDAYRIELETFLDSIAIGGAVSPSVRDGYEALVLADAATRSAQEHRVVAL 328
Cdd:pfam02894 150 LGSFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
PRK11579 PRK11579
putative oxidoreductase; Provisional
 2-143 8.32e-12

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 65.12  E-value: 8.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   2 IRIAIIGAGRIGHV-HARAIQGRNDVTLALVCDPFEQNARAlageyD---VRYCLDPDEVFDDSTIDAVVIGSPTQFHVD 77
Cdd:PRK11579   5 IRVGLIGYGYASKTfHAPLIAGTPGLELAAVSSSDATKVKA-----DwptVTVVSEPQHLFNDPNIDLIVIPTPNDTHFP 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 328758689  78 HILKAVNGGKRVMCEKPIALDVESAkRCINELGDRADQVMMGF-NRRFDPTFSALKSRLDDGEIGSL 143
Cdd:PRK11579  80 LAKAALEAGKHVVVDKPFTVTLSQA-RELDALAKSAGRVLSVFhNRRWDSDFLTLKALLAEGVLGEV 145
PRK10206 PRK10206
putative oxidoreductase; Provisional
 53-184 7.38e-09

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 56.37  E-value: 7.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689  53 DPDEVFDDSTIDAVVIGSPTQFHVDHILKAVNGGKRVMCEKPIALDVESAKRCINELGDRADQVMMGFNRRFDPTFSALK 132
Cdd:PRK10206  55 DLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAK 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 328758689 133 SRLDDGEIGSLQQLTViSRDPAAPSASYIAGS--GGIFKDMTIHDFDMVRHFLG 184
Cdd:PRK10206 135 KAIESGKLGEIVEVES-HFDYYRPVAETKPGLpqDGAFYGLGVHTMDQIISLFG 187
AspD COG1712
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
2-90 7.14e-05

L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];


Pssm-ID: 441318 [Multi-domain]  Cd Length: 263  Bit Score: 43.64  E-value: 7.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   2 IRIAIIGAGRIGHVHARAIQGRNdVTLALVCDPFEQNARALAGEYDVRYCLDPDEvFDDSTIDAVV-IGSPTQFHvDHIL 80
Cdd:COG1712    1 MRIGLIGCGAIGSEVAEALADAG-VELVAVYDRDPERAEALLASLGARVVSDVDE-LLAADPDLVVeAASQAAVR-EHGP 77

                         90
                 ....*....|
gi 328758689  81 KAVNGGKRVM 90
Cdd:COG1712   78 AVLEAGKDLM 87
PRK13304 PRK13304
aspartate dehydrogenase;
1-90 8.47e-05

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 43.44  E-value: 8.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328758689   1 MIRIAIIGAGRIGHVHARAI-QGRNDVTLALVCDPFEQNARALAGEYDVRYCLDPDEVFDDstIDaVVIGSPTQFHV-DH 78
Cdd:PRK13304   1 MLKIGIVGCGAIASLITKAIlSGRINAELYAFYDRNLEKAENLASKTGAKACLSIDELVED--VD-LVVECASVNAVeEV 77

                         90
                 ....*....|..
gi 328758689  79 ILKAVNGGKRVM 90
Cdd:PRK13304  78 VPKSLENGKDVI 89
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-71 1.03e-04

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 43.26  E-value: 1.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 328758689   1 MIRIAIIGAGRIGHVHARAIQgRNDVTLALVCDPFEQNARALAGEYDVRYCLDPDEVFDDStiDAVVIGSP 71
Cdd:COG5495    3 RMKIGIIGAGRVGTALAAALR-AAGHEVVGVYSRSPASAERAAALLGAVPALDLEELAAEA--DLVLLAVP 70
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-69 2.49e-03

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 38.89  E-value: 2.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 328758689   1 MIRIAIIGAGRIGHVHARAIQGR----NDVTlalVCDPFEQNARALAGEYDVRYCLDPDEVFDDStiDAVVIG 69
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKGLLKSgvppEDII---VSDRSPERLEALAERYGVRVTTDNAEAAAQA--DVVVLA 69
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 2-67 5.38e-03

Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 36.44  E-value: 5.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 328758689    2 IRIAIIGA-GRIGHVHARAIQGRNDVTLALV----CDPFEQNARALAGEYDVRYCLDPDEVFDDStiDAVV 67
Cdd:pfam01113   1 IKIAVAGAsGRMGRELIKAVLEAPDLELVAAvdrpGSSLLGSDAGELAPLGVPVTDDLEEVLADA--DVLI 69
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 2-35 8.98e-03

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 37.39  E-value: 8.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 328758689   2 IRIAIIGAGRIGHVHARAIQGRNDVTLALVCDPF 35
Cdd:PLN02358   6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPF 39
 
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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