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Conserved domains on  [gi|504205390|ref|WP_014392492|]
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type 2 isopentenyl-diphosphate Delta-isomerase [Rickettsia amblyommatis]

Protein Classification

isopentenyl-diphosphate delta-isomerase( domain architecture ID 10120281)

isopentenyl-diphosphate delta-isomerase catalyzes the isomerization of isopentenyl pyrophosphate to dimethylallyl diphosphate in the mevalonate pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 11-337 2.85e-172

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


:

Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 481.23  E-value: 2.85e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  11 RKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:cd02811    1 RKDEHLELCLEENVESGGSTGFDDVRLVHNALPELDLDDIDLSTEFLGKRLSAPLLISAMTGGSEKAKEINRNLAEAAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  91 AGIAMGLGSMRVLLTEPDTIKTFAVRHIA-PDIPLLANIGAIQLNyGVTPKECQYLVDAIKADALILHLNVLQELTQPEG 169
Cdd:cd02811   81 LGIAMGVGSQRAALEDPELAESFTVVREApPNGPLIANLGAVQLN-GYGVEEARRAVEMIEADALAIHLNPLQEAVQPEG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 170 NRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSlQNRIASSFINW 249
Cdd:cd02811  160 DRDFRGWLERIEELVKALSVPVIVKEVGFGISRETAKRLADAGVKAIDVAGAGGTSWARVENYRAKDS-DQRLAEYFADW 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 250 GIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAADTSERLLSEEIQLIIEQLKITMLCTGS 329
Cdd:cd02811  239 GIPTAASLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALEGEEAVIETIEQIIEELRTAMFLTGA 318


                 ....*...
gi 504205390 330 RTLKDLAK 337
Cdd:cd02811  319 KNLAELKQ 326
 
Name Accession Description Interval E-value
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 11-337 2.85e-172

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 481.23  E-value: 2.85e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  11 RKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:cd02811    1 RKDEHLELCLEENVESGGSTGFDDVRLVHNALPELDLDDIDLSTEFLGKRLSAPLLISAMTGGSEKAKEINRNLAEAAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  91 AGIAMGLGSMRVLLTEPDTIKTFAVRHIA-PDIPLLANIGAIQLNyGVTPKECQYLVDAIKADALILHLNVLQELTQPEG 169
Cdd:cd02811   81 LGIAMGVGSQRAALEDPELAESFTVVREApPNGPLIANLGAVQLN-GYGVEEARRAVEMIEADALAIHLNPLQEAVQPEG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 170 NRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSlQNRIASSFINW 249
Cdd:cd02811  160 DRDFRGWLERIEELVKALSVPVIVKEVGFGISRETAKRLADAGVKAIDVAGAGGTSWARVENYRAKDS-DQRLAEYFADW 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 250 GIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAADTSERLLSEEIQLIIEQLKITMLCTGS 329
Cdd:cd02811  239 GIPTAASLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALEGEEAVIETIEQIIEELRTAMFLTGA 318


                 ....*...
gi 504205390 330 RTLKDLAK 337
Cdd:cd02811  319 KNLAELKQ 326
IPP_isom_2 TIGR02151
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP ...
 10-340 4.86e-163

isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP isomerase) interconverts isopentenyl diphosphate and dimethylallyl diphosphate. This model represents the type 2 enzyme. FMN, NADPH, and Mg2+ are required by this form, which lacks homology to the type 1 enzyme (TIGR02150). IPP is precursor to many compounds, including enzyme cofactors, sterols, and isoprenoids. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273999  Cd Length: 333  Bit Score: 458.27  E-value: 4.86e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390   10 ERKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQ 89
Cdd:TIGR02151   1 ERKDEHIELCLKQNVEYGGSTGFDDITLIHNALPEINLDDIDLTTEFLGKRLKAPFYINAMTGGSEEAGKINRNLARAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390   90 KAGIAMGLGSMRVLLTEPDTIKTF-AVRHIAPDIPLLANIGAIQLNYGVtPKECQYLVDAIKADALILHLNVLQELTQPE 168
Cdd:TIGR02151  81 ELGIPMGVGSQRAALKDPETADTFeVVREEAPNGPLIANIGAPQLVEGG-PEEAQEAIDMIEADALAIHLNVLQELVQPE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  169 GNRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSLQnriASSFIN 248
Cdd:TIGR02151 160 GDRNFKGWLEKIAEICSQLSVPVIVKEVGFGISKEVAKLLADAGVSAIDVAGAGGTSWAQVENYRAKGSNL---ASFFND 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  249 WGIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAA-DTSERLLSEEIQLIIEQLKITMLCT 327
Cdd:TIGR02151 237 WGIPTAASLLEVRSDAPDAPIIASGGLRTGLDVAKAIALGADAVGMARPFLKAAlDEGEEAVIEEIELIIEELKVAMFLT 316

                         330
                  ....*....|...
gi 504205390  328 GSRTLKDLAKAEI 340
Cdd:TIGR02151 317 GAKTIAELKKVPL 329
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 14-342 2.53e-68

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 218.08  E-value: 2.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  14 DHIEINLtkNVESTLK---SGFESIQFIHNALpeINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:COG1304   24 DYIDGGA--GDEVTLRrnrAAFDRVRLRPRVL--EDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  91 AGIAMGLGSMRVlltepDTIKTfaVRHIAPDIPLlanigaIQLN----YGVTpKECQYLVDAIKADALILHLNV------ 160
Cdd:COG1304  100 AGIPMGLSTQST-----TSLEE--VAAAAPAPLW------FQLYvpkdRGFT-DDLLRRAEAAGADALVLTVDTpvlgrr 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 161 ---LQE-LTQPEGNR--------------------------------NWEKllpkIREVVNYLSIPVIVKEVgygLSKKV 204
Cdd:COG1304  166 erdLREgFSQPPRLTprnlleaathprwalglaslaawldtnfdpslTWDD----IAWLRERWPGPLIVKGV---LSPED 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 205 AESLIDAGVKVLDIAGSGGTswsQVEAyratnslqnriassfinwGIPTLDSLKMVRE-VSKDIPIITSGGLKSGIDGAK 283
Cdd:COG1304  239 ARRAVDAGVDGIDVSNHGGR---QLDG------------------GPPTIDALPEIRAaVGGRIPVIADGGIRRGLDVAK 297

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 284 AIRIGANIFGLAGQFLKA-ADTSERLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEIRL 342
Cdd:COG1304  298 ALALGADAVGLGRPFLYGlAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
FMN_dh pfam01070
FMN-dependent dehydrogenase;
25-342 1.18e-13

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 71.02  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390   25 ESTLK---SGFESIQFIHNALPEINydSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQKAGIAMGLGSM- 100
Cdd:pfam01070  20 EVTLRrnrAAFDRIRLRPRVLRDVS--NRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVLSTVs 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  101 -----RV-------------LLTEPDTIKTFAVRHIAP---------DIPLLAN-----IGAIQLNYGVTPKE------- 141
Cdd:pfam01070  98 stsleEVaaaaggplwfqlyVPRDRELTEDLLERAEAAgykalvltvDTPVLGRrerdlRNGFTLPPRLTPRNlldlalh 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  142 CQYLVDAIKADALILHLNVLQEltQPEGNRNWEkllpKIREVVNYLSIPVIVKEVgygLSKKVAESLIDAGVKVLDIAGS 221
Cdd:pfam01070 178 PRWALGVLRRGGAGGAAAFVGS--QFDPALTWD----DLAWLRERWKGPLVVKGI---LSPEDAKRAVEAGVDGIVVSNH 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  222 GGtswsqveayRATNSlqnriassfinwGIPTLDSL-KMVREVSKDIPIITSGGLKSGIDGAKAIRIGAN--------IF 292
Cdd:pfam01070 249 GG---------RQLDG------------APATIDALpEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADavllgrpfLY 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 504205390  293 GLAgqfLKAADTSERLLseeiQLIIEQLKITMLCTGSRTLKDLAKAEIRL 342
Cdd:pfam01070 308 GLA---AGGEAGVAHAL----EILRDELERTMALLGCKSIADLTPSLLRR 350
PLN02535 PLN02535
glycolate oxidase
 258-341 2.64e-04

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 42.52  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 258 KMVREVSKDIPIITSGGLKSGIDGAKAIRIGAN--------IFGLAGqflKAADTSERLlseeIQLIIEQLKITMLCTGS 329
Cdd:PLN02535 270 EVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQavlvgrpvIYGLAA---KGEDGVRKV----IEMLKDELEITMALSGC 342

                         90
                 ....*....|..
gi 504205390 330 RTLKDLAKAEIR 341
Cdd:PLN02535 343 PSVKDITRSHVR 354
 
Name Accession Description Interval E-value
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 11-337 2.85e-172

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 481.23  E-value: 2.85e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  11 RKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:cd02811    1 RKDEHLELCLEENVESGGSTGFDDVRLVHNALPELDLDDIDLSTEFLGKRLSAPLLISAMTGGSEKAKEINRNLAEAAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  91 AGIAMGLGSMRVLLTEPDTIKTFAVRHIA-PDIPLLANIGAIQLNyGVTPKECQYLVDAIKADALILHLNVLQELTQPEG 169
Cdd:cd02811   81 LGIAMGVGSQRAALEDPELAESFTVVREApPNGPLIANLGAVQLN-GYGVEEARRAVEMIEADALAIHLNPLQEAVQPEG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 170 NRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSlQNRIASSFINW 249
Cdd:cd02811  160 DRDFRGWLERIEELVKALSVPVIVKEVGFGISRETAKRLADAGVKAIDVAGAGGTSWARVENYRAKDS-DQRLAEYFADW 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 250 GIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAADTSERLLSEEIQLIIEQLKITMLCTGS 329
Cdd:cd02811  239 GIPTAASLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALEGEEAVIETIEQIIEELRTAMFLTGA 318


                 ....*...
gi 504205390 330 RTLKDLAK 337
Cdd:cd02811  319 KNLAELKQ 326
IPP_isom_2 TIGR02151
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP ...
 10-340 4.86e-163

isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP isomerase) interconverts isopentenyl diphosphate and dimethylallyl diphosphate. This model represents the type 2 enzyme. FMN, NADPH, and Mg2+ are required by this form, which lacks homology to the type 1 enzyme (TIGR02150). IPP is precursor to many compounds, including enzyme cofactors, sterols, and isoprenoids. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273999  Cd Length: 333  Bit Score: 458.27  E-value: 4.86e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390   10 ERKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQ 89
Cdd:TIGR02151   1 ERKDEHIELCLKQNVEYGGSTGFDDITLIHNALPEINLDDIDLTTEFLGKRLKAPFYINAMTGGSEEAGKINRNLARAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390   90 KAGIAMGLGSMRVLLTEPDTIKTF-AVRHIAPDIPLLANIGAIQLNYGVtPKECQYLVDAIKADALILHLNVLQELTQPE 168
Cdd:TIGR02151  81 ELGIPMGVGSQRAALKDPETADTFeVVREEAPNGPLIANIGAPQLVEGG-PEEAQEAIDMIEADALAIHLNVLQELVQPE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  169 GNRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSLQnriASSFIN 248
Cdd:TIGR02151 160 GDRNFKGWLEKIAEICSQLSVPVIVKEVGFGISKEVAKLLADAGVSAIDVAGAGGTSWAQVENYRAKGSNL---ASFFND 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  249 WGIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAA-DTSERLLSEEIQLIIEQLKITMLCT 327
Cdd:TIGR02151 237 WGIPTAASLLEVRSDAPDAPIIASGGLRTGLDVAKAIALGADAVGMARPFLKAAlDEGEEAVIEEIELIIEELKVAMFLT 316

                         330
                  ....*....|...
gi 504205390  328 GSRTLKDLAKAEI 340
Cdd:TIGR02151 317 GAKTIAELKKVPL 329
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 14-342 2.53e-68

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 218.08  E-value: 2.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  14 DHIEINLtkNVESTLK---SGFESIQFIHNALpeINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:COG1304   24 DYIDGGA--GDEVTLRrnrAAFDRVRLRPRVL--EDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  91 AGIAMGLGSMRVlltepDTIKTfaVRHIAPDIPLlanigaIQLN----YGVTpKECQYLVDAIKADALILHLNV------ 160
Cdd:COG1304  100 AGIPMGLSTQST-----TSLEE--VAAAAPAPLW------FQLYvpkdRGFT-DDLLRRAEAAGADALVLTVDTpvlgrr 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 161 ---LQE-LTQPEGNR--------------------------------NWEKllpkIREVVNYLSIPVIVKEVgygLSKKV 204
Cdd:COG1304  166 erdLREgFSQPPRLTprnlleaathprwalglaslaawldtnfdpslTWDD----IAWLRERWPGPLIVKGV---LSPED 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 205 AESLIDAGVKVLDIAGSGGTswsQVEAyratnslqnriassfinwGIPTLDSLKMVRE-VSKDIPIITSGGLKSGIDGAK 283
Cdd:COG1304  239 ARRAVDAGVDGIDVSNHGGR---QLDG------------------GPPTIDALPEIRAaVGGRIPVIADGGIRRGLDVAK 297

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 284 AIRIGANIFGLAGQFLKA-ADTSERLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEIRL 342
Cdd:COG1304  298 ALALGADAVGLGRPFLYGlAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
FMN_dh pfam01070
FMN-dependent dehydrogenase;
25-342 1.18e-13

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 71.02  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390   25 ESTLK---SGFESIQFIHNALPEINydSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQKAGIAMGLGSM- 100
Cdd:pfam01070  20 EVTLRrnrAAFDRIRLRPRVLRDVS--NRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVLSTVs 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  101 -----RV-------------LLTEPDTIKTFAVRHIAP---------DIPLLAN-----IGAIQLNYGVTPKE------- 141
Cdd:pfam01070  98 stsleEVaaaaggplwfqlyVPRDRELTEDLLERAEAAgykalvltvDTPVLGRrerdlRNGFTLPPRLTPRNlldlalh 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  142 CQYLVDAIKADALILHLNVLQEltQPEGNRNWEkllpKIREVVNYLSIPVIVKEVgygLSKKVAESLIDAGVKVLDIAGS 221
Cdd:pfam01070 178 PRWALGVLRRGGAGGAAAFVGS--QFDPALTWD----DLAWLRERWKGPLVVKGI---LSPEDAKRAVEAGVDGIVVSNH 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  222 GGtswsqveayRATNSlqnriassfinwGIPTLDSL-KMVREVSKDIPIITSGGLKSGIDGAKAIRIGAN--------IF 292
Cdd:pfam01070 249 GG---------RQLDG------------APATIDALpEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADavllgrpfLY 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 504205390  293 GLAgqfLKAADTSERLLseeiQLIIEQLKITMLCTGSRTLKDLAKAEIRL 342
Cdd:pfam01070 308 GLA---AGGEAGVAHAL----EILRDELERTMALLGCKSIADLTPSLLRR 350
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 25-335 7.59e-10

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 59.00  E-value: 7.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  25 ESTLK---SGFESIQFIHNALPEInyDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQKAGIAMGLGSMr 101
Cdd:cd02809   26 EVTLRrnrAAFDRIRLRPRVLRDV--SKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPDGELATARAAAAAGIPFTLSTV- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 102 vlltepdtiKTFAVRHIAPDIPLLANIgaiQLNYGVTPKECQYLVD---AIKADALILHLNvlqelTQPEGNR-NWEKll 177
Cdd:cd02809  103 ---------STTSLEEVAAAAPGPRWF---QLYVPRDREITEDLLRraeAAGYKALVLTVD-----TPVLGRRlTWDD-- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 178 pkIREVVNYLSIPVIVKEVgygLSKKVAESLIDAGVK----------VLDIAgsggtswsqveayratnslqnriassfi 247
Cdd:cd02809  164 --LAWLRSQWKGPLILKGI---LTPEDALRAVDAGADgivvsnhggrQLDGA---------------------------- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 248 nwgIPTLDSLKMVRE-VSKDIPIITSGGLKSGIDGAKAIRIGAN--------IFGLAGQflkAADTSERLLseeiQLIIE 318
Cdd:cd02809  211 ---PATIDALPEIVAaVGGRIEVLLDGGIRRGTDVLKALALGADavligrpfLYGLAAG---GEAGVAHVL----EILRD 280

                        330
                 ....*....|....*..
gi 504205390 319 QLKITMLCTGSRTLKDL 335
Cdd:cd02809  281 ELERAMALLGCASLADL 297
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 46-340 1.83e-08

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 55.14  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  46 NYDSVNTTTTFLGKSLQAPILISSMTGgttrardinYRLAHVAQKAGIAMGLGSMRVLLTepdtIKTFAVRHIaPDIPLL 125
Cdd:cd04737   56 GVESPDTSTELLGIKLKTPIIMAPIAA---------HGLAHATGEVATARGMAEVGSLFS----ISTYSNTSL-EEIAKA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 126 ANIGA--IQLNYGVTPKECQYLVDAIKAD---ALILH----------------------LNVLQELTQPEG-----NRNW 173
Cdd:cd04737  122 SNGGPkwFQLYMSKDDGFNRSLLDRAKAAgakAIILTadatvggnreadirnkfqfpfgMPNLNHFSEGTGkgkgiSEIY 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 174 E----KLLPK-IREVVNYLSIPVIVKEVgygLSKKVAESLIDAGVKVLDIAGSGGTSwsqveayratnslqnriassfIN 248
Cdd:cd04737  202 AaakqKLSPAdIEFIAKISGLPVIVKGI---QSPEDADVAINAGADGIWVSNHGGRQ---------------------LD 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 249 WGIPTLDSLKMVRE-VSKDIPIITSGGLKSGIDGAKAIRIGAN--------IFGLA-GQFLKAADTSERLLSEeiqliie 318
Cdd:cd04737  258 GGPASFDSLPEIAEaVNHRVPIIFDSGVRRGEHVFKALASGADavavgrpvLYGLAlGGAQGVASVLEHLNKE------- 330

                        330       340
                 ....*....|....*....|..
gi 504205390 319 qLKITMLCTGSRTLKDLAKAEI 340
Cdd:cd04737  331 -LKIVMQLAGTRTIEDVKRTFL 351
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 119-296 2.73e-08

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 53.36  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 119 APDIPLLANIGAIqlNYGVTPKECQYLVDAIKADALILHLNVLQELtqpegnRNWEKLLPKIREVvnYLSIPVIVKEVGY 198
Cdd:cd04722   55 ETDLPLGVQLAIN--DAAAAVDIAAAAARAAGADGVEIHGAVGYLA------REDLELIRELREA--VPDVKVVVKLSPT 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 199 GlsKKVAESLIDAGVKVLDIAGSGGTSWSQVEAyratnslqnriassfinwgiPTLDSLKMVREVSKDIPIITSGGLKSG 278
Cdd:cd04722  125 G--ELAAAAAEEAGVDEVGLGNGGGGGGGRDAV--------------------PIADLLLILAKRGSKVPVIAGGGINDP 182

                        170
                 ....*....|....*...
gi 504205390 279 IDGAKAIRIGANIFGLAG 296
Cdd:cd04722  183 EDAAEALALGADGVIVGS 200
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 179-301 1.73e-06

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202 [Multi-domain]  Cd Length: 392  Bit Score: 49.08  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 179 KIREVVNYlsIPVIVKEVGYGLskkvaESLIDAGVK-----VLDIAGS-GGTSWSQVEayratnslqnriassFIN-WGI 251
Cdd:cd02808  207 DLREATGG--KPIGVKLVAGHG-----EGDIAAGVAaagadFITIDGAeGGTGAAPLT---------------FIDhVGL 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504205390 252 PTLDSLKMVRE------VSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKA 301
Cdd:cd02808  265 PTELGLARAHQalvkngLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIA 320
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 119-295 1.25e-04

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 43.11  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 119 APDIPLLANIGAIQLNYGVtpkECQYLVDAIKADALILHLNVLQELTQPEGNRNWEKLLPKIREVVNYLSIPVIVKeVGY 198
Cdd:cd02810   96 FPGQPLIASVGGSSKEDYV---ELARKIERAGAKALELNLSCPNVGGGRQLGQDPEAVANLLKAVKAAVDIPLLVK-LSP 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 199 GLSKKVAESLidagVKVLDIAGsggtswsqVEAYRATNSLQNRIASSfINWGIPTLD-------------SLKMVREVS- 264
Cdd:cd02810  172 YFDLEDIVEL----AKAAERAG--------ADGLTAINTISGRVVDL-KTVGPGPKRgtgglsgapirplALRWVARLAa 238

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504205390 265 ---KDIPIITSGGLKSGIDGAKAIRIGANIFGLA 295
Cdd:cd02810  239 rlqLDIPIIGVGGIDSGEDVLEMLMAGASAVQVA 272
PLN02535 PLN02535
glycolate oxidase
 258-341 2.64e-04

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 42.52  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 258 KMVREVSKDIPIITSGGLKSGIDGAKAIRIGAN--------IFGLAGqflKAADTSERLlseeIQLIIEQLKITMLCTGS 329
Cdd:PLN02535 270 EVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQavlvgrpvIYGLAA---KGEDGVRKV----IEMLKDELEITMALSGC 342

                         90
                 ....*....|..
gi 504205390 330 RTLKDLAKAEIR 341
Cdd:PLN02535 343 PSVKDITRSHVR 354
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 190-295 9.40e-04

Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 396287 [Multi-domain]  Cd Length: 367  Bit Score: 40.78  E-value: 9.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  190 PVIVK---EVGYGLskkVAESLIDAGVKVLDIAG-SGGTSWSQVeayratnslqnriaSSFINWGIPTLDSLKMVREVSK 265
Cdd:pfam01645 204 PISVKlvsGHGVGT---IAAGVAKAGADIILIDGyDGGTGASPK--------------TSIKHAGLPWELALAEAHQTLK 266

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 504205390  266 D------IPIITSGGLKSGIDGAKAIRIGANIFGLA 295
Cdd:pfam01645 267 EnglrdrVSLIADGGLRTGADVAKAAALGADAVYIG 302
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
 66-293 1.24e-03

Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.


Pssm-ID: 188634 [Multi-domain]  Cd Length: 201  Bit Score: 39.62  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390  66 LISSMTGGTTRARDINyRLAHVAQKAGIAmglgsmrVLLTEPDTIKTfAVRHIAP-DIPLLANIGAiqlNYGVTPKEC-- 142
Cdd:cd00945    1 IDLTLLHPDATLEDIA-KLCDEAIEYGFA-------AVCVNPGYVRL-AADALAGsDVPVIVVVGF---PTGLTTTEVkv 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 143 QYLVDAIK--ADALILHLNVLQELtqpegNRNWEKLLPKIREVVNYLSIPVIVK---EVGYGLSK----KVAESLIDAG- 212
Cdd:cd00945   69 AEVEEAIDlgADEIDVVINIGSLK-----EGDWEEVLEEIAAVVEAADGGLPLKvilETRGLKTAdeiaKAARIAAEAGa 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 213 --VKVldiagsgGTSWSQVEAyratnslqnriassfinwgipTLDSLK-MVREVSKDIPIITSGGLKSGIDGAKAIRIGA 289
Cdd:cd00945  144 dfIKT-------STGFGGGGA---------------------TVEDVKlMKEAVGGRVGVKAAGGIKTLEDALAAIEAGA 195


                 ....
gi 504205390 290 NIFG 293
Cdd:cd00945  196 DGIG 199
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 257-320 1.55e-03

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091 [Multi-domain]  Cd Length: 296  Bit Score: 39.84  E-value: 1.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504205390 257 LKMVREVSK--DIPIITSGGLKSGID-------GAKAIRIGANIFGLAGQFLKAADTSERLLSEEIQLIIEQL 320
Cdd:cd04740  220 LRMVYQVYKavEIPIIGVGGIASGEDaleflmaGASAVQVGTANFVDPEAFKEIIEGLEAYLDEEGIKSIEEL 292
PLN02979 PLN02979
glycolate oxidase
 189-340 1.90e-03

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 39.71  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 189 IPVIVKEVGYGLSKKVAeslIDAGVKVLDIAGSGGTSWSQVEAyratnslqnriassfinwgipTLDSLK-MVREVSKDI 267
Cdd:PLN02979 224 LPILVKGVLTGEDARIA---IQAGAAGIIVSNHGARQLDYVPA---------------------TISALEeVVKATQGRI 279

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504205390 268 PIITSGGLKSGIDGAKAIRIGAN-IFGLAGQFLKAADTSERLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEI 340
Cdd:PLN02979 280 PVFLDGGVRRGTDVFKALALGASgIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 353
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 180-299 3.17e-03

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 39.09  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 180 IREVVNyLSIPVIVK-----EVGYGL----SKKVAESLIDAGVKVLDIagSGGTSWSQVEAYRATNSLQNRIassfinwg 250
Cdd:cd02803  201 VREAVG-PDFPVGVRlsaddFVPGGLtleeAIEIAKALEEAGVDALHV--SGGSYESPPPIIPPPYVPEGYF-------- 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504205390 251 iptLDSLKMVREVSkDIPIITSGGLKSGIDGAKAIRIG-ANIFGLAGQFL 299
Cdd:cd02803  270 ---LELAEKIKKAV-KIPVIAVGGIRDPEVAEEILAEGkADLVALGRALL 315
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 188-340 4.49e-03

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 38.56  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 188 SIPVIVKEVGYGLSKKVAeslIDAGVKVLDIAGSGGTSWSQVEAyratnslqnriassfinwgipTLDSLK-MVREVSKD 266
Cdd:PLN02493 224 KLPILVKGVLTGEDARIA---IQAGAAGIIVSNHGARQLDYVPA---------------------TISALEeVVKATQGR 279

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504205390 267 IPIITSGGLKSGIDGAKAIRIGAN-IF-GLAGQFLKAADtSERLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEI 340
Cdd:PLN02493 280 IPVFLDGGVRRGTDVFKALALGASgIFiGRPVVFSLAAE-GEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 354
PRK07259 PRK07259
dihydroorotate dehydrogenase;
257-292 5.10e-03

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 38.21  E-value: 5.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 504205390 257 LKMVREVSK--DIPIITSGGLKSGID-------GAKAIRIGANIF 292
Cdd:PRK07259 223 LRMVYQVYQavDIPIIGMGGISSAEDaiefimaGASAVQVGTANF 267
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 185-290 8.96e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 37.64  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 185 NYLSIPVIVKEVgygLSKKVAESLIDAGVKVLDIA-GSGGTSWSQVeayratnslqnrIASSfinwGIPTLDSLKMVREV 263
Cdd:PTZ00314 279 NYPHVDIIAGNV---VTADQAKNLIDAGADGLRIGmGSGSICITQE------------VCAV----GRPQASAVYHVARY 339

                         90       100
                 ....*....|....*....|....*....
gi 504205390 264 SKD--IPIITSGGLKSGIDGAKAIRIGAN 290
Cdd:PTZ00314 340 ARErgVPCIADGGIKNSGDICKALALGAD 368
 
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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