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Conserved domains on  [gi|17565764|ref|NP_503730|]
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L-2-hydroxyglutarate dehydrogenase, mitochondrial [Caenorhabditis elegans]

Protein Classification

FAD dependent oxidoreductase family protein( domain architecture ID 1750071)

FAD dependent oxidoreductase family protein may catalyze the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Gene Ontology:  GO:0071949|GO:0016491
PubMed:  27714222

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAO super family cl40741
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 24-427 0e+00

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


The actual alignment was detected with superfamily member PRK11728:

Pssm-ID: 477422 [Multi-domain]  Cd Length: 393  Bit Score: 563.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   24 PKYDLVIVGGGIVGCATARQLLIEKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDK 103
Cdd:PRK11728   1 AMYDFVIIGGGIVGLSTAMQLQERYPGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRGNEATKAFCDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  104 EKVPYKKTGKLIVAVEPEEVPRLDALFSRAQTNGCrDIEMIDSSKITELEPHCRGLKALWSPHTGIVDWGYVTKRFGEDF 183
Cdd:PRK11728  81 HGIPYEECGKLLVATSELELERMEALYERARANGI-EVERLDAEELREREPNIRGLGAIFVPSTGIVDYRAVAEAMAELI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  184 EKRGGKIYTSYPLEKIsDNHDPGYPIRVSSGpalaEFETKNLITCAGLQSDRVAALSGCSTDPKIVPFRGEYLLLKPEKR 263
Cdd:PRK11728 160 QARGGEIRLGAEVTAL-DEHANGVVVRTTQG----EYEARTLINCAGLMSDRLAKMAGLEPDFRIVPFRGEYYRLAPEKN 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  264 HLVKTNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLAYKREGYSYFSISPSDLLESLSYSGMQKLVKKHFTFGIKELY 343
Cdd:PRK11728 235 QLVNHLIYPVPDPAFPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLRDLLEILTYPGFWKLAQKHWRSGLGEMK 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  344 RGVWIAAQVKQLQRFIPELKLSDVTRGPAGVRAQAMDSAGNLVDDFVFDSGtgklsPLLMHVRNAPSPAATSSLAIAKMI 423
Cdd:PRK11728 315 NSLSKSGYLRLVQKYCPSLTLSDLQPYPAGVRAQAVSRDGKLVDDFLFVET-----PRSLHVCNAPSPAATSSLPIGEHI 389


                 ....
gi 17565764  424 TSEA 427
Cdd:PRK11728 390 VSKV 393
 
Name Accession Description Interval E-value
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
24-427 0e+00

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 563.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   24 PKYDLVIVGGGIVGCATARQLLIEKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDK 103
Cdd:PRK11728   1 AMYDFVIIGGGIVGLSTAMQLQERYPGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRGNEATKAFCDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  104 EKVPYKKTGKLIVAVEPEEVPRLDALFSRAQTNGCrDIEMIDSSKITELEPHCRGLKALWSPHTGIVDWGYVTKRFGEDF 183
Cdd:PRK11728  81 HGIPYEECGKLLVATSELELERMEALYERARANGI-EVERLDAEELREREPNIRGLGAIFVPSTGIVDYRAVAEAMAELI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  184 EKRGGKIYTSYPLEKIsDNHDPGYPIRVSSGpalaEFETKNLITCAGLQSDRVAALSGCSTDPKIVPFRGEYLLLKPEKR 263
Cdd:PRK11728 160 QARGGEIRLGAEVTAL-DEHANGVVVRTTQG----EYEARTLINCAGLMSDRLAKMAGLEPDFRIVPFRGEYYRLAPEKN 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  264 HLVKTNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLAYKREGYSYFSISPSDLLESLSYSGMQKLVKKHFTFGIKELY 343
Cdd:PRK11728 235 QLVNHLIYPVPDPAFPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLRDLLEILTYPGFWKLAQKHWRSGLGEMK 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  344 RGVWIAAQVKQLQRFIPELKLSDVTRGPAGVRAQAMDSAGNLVDDFVFDSGtgklsPLLMHVRNAPSPAATSSLAIAKMI 423
Cdd:PRK11728 315 NSLSKSGYLRLVQKYCPSLTLSDLQPYPAGVRAQAVSRDGKLVDDFLFVET-----PRSLHVCNAPSPAATSSLPIGEHI 389


                 ....
gi 17565764  424 TSEA 427
Cdd:PRK11728 390 VSKV 393
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
25-432 3.98e-161

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 460.38  E-value: 3.98e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  25 KYDLVIVGGGIVGCATARQLLiEKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDKE 104
Cdd:COG0579   4 MYDVVIIGAGIVGLALARELS-RYEDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYTPGSLKARLCVEGNELFYELCREL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 105 KVPYKKTGKLIVAVEPEEVPRLDALFSRAQTNGCRDIEMIDSSKITELEPHCR--GLKALWSPHTGIVDWGYVTKRFGED 182
Cdd:COG0579  83 GIPFKRCGKLVVATGEEEVAFLEKLYERGKANGVPGLEILDREELRELEPLLSdeGVAALYSPSTGIVDPGALTRALAEN 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 183 FEKRGGKIYTSYPLEKISDNHDpGYPIRVSSGpalaEFETKNLITCAGLQSDRVAALSGCSTDPKIVPFRGEYLLLKPEK 262
Cdd:COG0579 163 AEANGVELLLNTEVTGIEREGD-GWEVTTNGG----TIRARFVINAAGLYADRLAQMAGIGKDFGIFPVKGEYLVLDKPA 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 263 rHLVKTNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLAYKREGysyfsiSPSDLLESLSYSGMQKLVKKHFTFGIKEL 342
Cdd:COG0579 238 -ELVNAKVYPVPDPGAPFLGVHLTRTIDGNLLFGPNAVFVPKKED------SLLDLFESLRFPNFWPMLAKNLLTKYLES 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 343 YRGVWIAAQVKQLQRFIPELKLSDVTRGPAGVRAQAMDSAGnlvdDFVFDSGTGKLSpllMHVRNAPSPAATSSLAIAKM 422
Cdd:COG0579 311 VTSLSKEAFLEALRKYVPELPDEDLIPAFAGIRAQIIKPDG----DFVIEEADDPGS---IHVLGIESPGATSALAIAEH 383

                       410
                ....*....|
gi 17565764 423 ITSEAINRFK 432
Cdd:COG0579 384 VAELLPEKLE 393
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 27-424 4.59e-57

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 191.07  E-value: 4.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764    27 DLVIVGGGIVGCATARQLLieKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDK--E 104
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELA--RRGLSVTLLERGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALDLWEELEEElgI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   105 KVPYKKTGKLIVAVEPEEvPRLDALFSRAQTNGCrDIEMIDSSKITELEPHCRGLK-ALWSPHTGIVDWGYVTKRFGEDF 183
Cdd:pfam01266  79 DCGFRRCGVLVLARDEEE-EALEKLLAALRRLGV-PAELLDAEELRELEPLLPGLRgGLFYPDGGHVDPARLLRALARAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   184 EKRGGKIYTSYPLEKISDnHDPGYPIRVSSgpalaefETKNLITCAGLQSDRVAALsgcSTDPKIVPFRGEYLLLKPEKR 263
Cdd:pfam01266 157 EALGVRIIEGTEVTGIEE-EGGVWGVVTTG-------EADAVVNAAGAWADLLALP---GLRLPVRPVRGQVLVLEPLPE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   264 HLvktNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLaykrEGYSYFSISPSDlleslsysgmqklvkkhftfgikely 343
Cdd:pfam01266 226 AL---LILPVPITVDPGRGVYLRPRADGRLLLGGTDEE----DGFDDPTPDPEE-------------------------- 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   344 rgvwIAAQVKQLQRFIPELKlsDVTRGPAGVRAqamdsagnlVDDFVFDSGTGkLSPLLMHVRNAPSPAATSSLAIAKMI 423
Cdd:pfam01266 273 ----IEELLEAARRLFPALA--DIERAWAGLRP---------LPDGLPIIGRP-GSPGLYLATGHGGHGLTLAPGIGKLL 336


                  .
gi 17565764   424 T 424
Cdd:pfam01266 337 A 337
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 26-82 6.50e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 41.54  E-value: 6.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17565764    26 YDLVIVGGGIVGCATARQLLieKPQLKVALIEKEKELAVHQSGhnSGVIHAGIYYTP 82
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLA--DKGLRVLLLEKKSFPRYKPCG--GALSPRALEELD 53
 
Name Accession Description Interval E-value
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
24-427 0e+00

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 563.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   24 PKYDLVIVGGGIVGCATARQLLIEKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDK 103
Cdd:PRK11728   1 AMYDFVIIGGGIVGLSTAMQLQERYPGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRGNEATKAFCDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  104 EKVPYKKTGKLIVAVEPEEVPRLDALFSRAQTNGCrDIEMIDSSKITELEPHCRGLKALWSPHTGIVDWGYVTKRFGEDF 183
Cdd:PRK11728  81 HGIPYEECGKLLVATSELELERMEALYERARANGI-EVERLDAEELREREPNIRGLGAIFVPSTGIVDYRAVAEAMAELI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  184 EKRGGKIYTSYPLEKIsDNHDPGYPIRVSSGpalaEFETKNLITCAGLQSDRVAALSGCSTDPKIVPFRGEYLLLKPEKR 263
Cdd:PRK11728 160 QARGGEIRLGAEVTAL-DEHANGVVVRTTQG----EYEARTLINCAGLMSDRLAKMAGLEPDFRIVPFRGEYYRLAPEKN 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  264 HLVKTNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLAYKREGYSYFSISPSDLLESLSYSGMQKLVKKHFTFGIKELY 343
Cdd:PRK11728 235 QLVNHLIYPVPDPAFPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLRDLLEILTYPGFWKLAQKHWRSGLGEMK 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  344 RGVWIAAQVKQLQRFIPELKLSDVTRGPAGVRAQAMDSAGNLVDDFVFDSGtgklsPLLMHVRNAPSPAATSSLAIAKMI 423
Cdd:PRK11728 315 NSLSKSGYLRLVQKYCPSLTLSDLQPYPAGVRAQAVSRDGKLVDDFLFVET-----PRSLHVCNAPSPAATSSLPIGEHI 389


                 ....
gi 17565764  424 TSEA 427
Cdd:PRK11728 390 VSKV 393
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
25-432 3.98e-161

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 460.38  E-value: 3.98e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  25 KYDLVIVGGGIVGCATARQLLiEKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDKE 104
Cdd:COG0579   4 MYDVVIIGAGIVGLALARELS-RYEDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYTPGSLKARLCVEGNELFYELCREL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 105 KVPYKKTGKLIVAVEPEEVPRLDALFSRAQTNGCRDIEMIDSSKITELEPHCR--GLKALWSPHTGIVDWGYVTKRFGED 182
Cdd:COG0579  83 GIPFKRCGKLVVATGEEEVAFLEKLYERGKANGVPGLEILDREELRELEPLLSdeGVAALYSPSTGIVDPGALTRALAEN 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 183 FEKRGGKIYTSYPLEKISDNHDpGYPIRVSSGpalaEFETKNLITCAGLQSDRVAALSGCSTDPKIVPFRGEYLLLKPEK 262
Cdd:COG0579 163 AEANGVELLLNTEVTGIEREGD-GWEVTTNGG----TIRARFVINAAGLYADRLAQMAGIGKDFGIFPVKGEYLVLDKPA 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 263 rHLVKTNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLAYKREGysyfsiSPSDLLESLSYSGMQKLVKKHFTFGIKEL 342
Cdd:COG0579 238 -ELVNAKVYPVPDPGAPFLGVHLTRTIDGNLLFGPNAVFVPKKED------SLLDLFESLRFPNFWPMLAKNLLTKYLES 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 343 YRGVWIAAQVKQLQRFIPELKLSDVTRGPAGVRAQAMDSAGnlvdDFVFDSGTGKLSpllMHVRNAPSPAATSSLAIAKM 422
Cdd:COG0579 311 VTSLSKEAFLEALRKYVPELPDEDLIPAFAGIRAQIIKPDG----DFVIEEADDPGS---IHVLGIESPGATSALAIAEH 383

                       410
                ....*....|
gi 17565764 423 ITSEAINRFK 432
Cdd:COG0579 384 VAELLPEKLE 393
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 27-424 4.59e-57

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 191.07  E-value: 4.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764    27 DLVIVGGGIVGCATARQLLieKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDK--E 104
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELA--RRGLSVTLLERGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALDLWEELEEElgI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   105 KVPYKKTGKLIVAVEPEEvPRLDALFSRAQTNGCrDIEMIDSSKITELEPHCRGLK-ALWSPHTGIVDWGYVTKRFGEDF 183
Cdd:pfam01266  79 DCGFRRCGVLVLARDEEE-EALEKLLAALRRLGV-PAELLDAEELRELEPLLPGLRgGLFYPDGGHVDPARLLRALARAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   184 EKRGGKIYTSYPLEKISDnHDPGYPIRVSSgpalaefETKNLITCAGLQSDRVAALsgcSTDPKIVPFRGEYLLLKPEKR 263
Cdd:pfam01266 157 EALGVRIIEGTEVTGIEE-EGGVWGVVTTG-------EADAVVNAAGAWADLLALP---GLRLPVRPVRGQVLVLEPLPE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   264 HLvktNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLaykrEGYSYFSISPSDlleslsysgmqklvkkhftfgikely 343
Cdd:pfam01266 226 AL---LILPVPITVDPGRGVYLRPRADGRLLLGGTDEE----DGFDDPTPDPEE-------------------------- 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   344 rgvwIAAQVKQLQRFIPELKlsDVTRGPAGVRAqamdsagnlVDDFVFDSGTGkLSPLLMHVRNAPSPAATSSLAIAKMI 423
Cdd:pfam01266 273 ----IEELLEAARRLFPALA--DIERAWAGLRP---------LPDGLPIIGRP-GSPGLYLATGHGGHGLTLAPGIGKLL 336


                  .
gi 17565764   424 T 424
Cdd:pfam01266 337 A 337
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
25-296 2.76e-32

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 125.79  E-value: 2.76e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  25 KYDLVIVGGGIVGCATARQLLieKPQLKVALIEKEkELAVHQSGHNSGVIHAGiYYTPGSLK-AKLCVEGLDLsYEFFDK 103
Cdd:COG0665   2 TADVVVIGGGIAGLSTAYHLA--RRGLDVTVLERG-RPGSGASGRNAGQLRPG-LAALADRAlVRLAREALDL-WRELAA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 104 E---KVPYKKTGKLIVAVEPEEVPRLDALFSRAQTNGCrDIEMIDSSKITELEPHCRG---LKALWSPHTGIVDWGYVTK 177
Cdd:COG0665  77 ElgiDCDFRRTGVLYLARTEAELAALRAEAEALRALGL-PVELLDAAELREREPGLGSpdyAGGLYDPDDGHVDPAKLVR 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764 178 RFGEDFEKRGGKIYTSYPLEKISDNHDPGYPIRVSSGpalaEFETKNLITCAGLQSDRVAALSGcsTDPKIVPFRGEYLL 257
Cdd:COG0665 156 ALARAARAAGVRIREGTPVTGLEREGGRVTGVRTERG----TVRADAVVLAAGAWSARLLPMLG--LRLPLRPVRGYVLV 229

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 17565764 258 LKPEKRHLVKTNIYPVpdprfpflGVHFTPRMNGDIWLG 296
Cdd:COG0665 230 TEPLPDLPLRPVLDDT--------GVYLRPTADGRLLVG 260
PTZ00383 PTZ00383
malate:quinone oxidoreductase; Provisional
 26-420 2.26e-14

malate:quinone oxidoreductase; Provisional


Pssm-ID: 240393 [Multi-domain]  Cd Length: 497  Bit Score: 74.77  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   26 YDLVIVGGGIVGCATARQLLIEKPQLKVALIEKEKELAVHQS--GHNSGVIHAGIYYTPGSL-KAKLCVEGLDLSYEF-- 100
Cdd:PTZ00383  46 YDVVIVGGGVTGTALFYTLSKFTNLKKIALIERRSDFALVAShgKNNSQTIHCGDIETNYTLeKARKVKRQADMLRNYlt 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  101 -FDKEKVP--YKKTGKLIVAVEPEEV-------PRLDALFSRAQtngcrdieMIDSSKITELEPhCRGLK---------- 160
Cdd:PTZ00383 126 kLPPSERDsiIFKMQKMVLGVGEKECeflekryPVFKELFPSMQ--------LLDKKEIHRVEP-RVVLKnnhtlreepl 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  161 -ALWSP--HTGiVDWGYVTKRFGE----DFEKRGGKIYTSYPLEKISDNHDPGYPIRVSSGPalAEFETKNLITCAGLQS 233
Cdd:PTZ00383 197 aALYVPneLTT-VDYQKLSESFVKharrDALVPGKKISINLNTEVLNIERSNDSLYKIHTNR--GEIRARFVVVSACGYS 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  234 DRVAALSGCSTDPKIVPFRGEYLLLKpekrHLVKTNIYPVPDPRFPFLGVHFTPR--MNGDIWLGPNAVLAYKREGYS-- 309
Cdd:PTZ00383 274 LLFAQKMGYGLEYSCLPVAGSFYFSG----NILNGKVYTVQNPALPFAAVHGDPDiiAKGKTRFGPTALPLPLLERYNms 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764  310 ----YFSISPSDLLESLSY------SGMQKLVKKHFTFGIKELYRGVWIaaqvKQLQRFIPELKLSDVTRGPA--GVRAQ 377
Cdd:PTZ00383 350 slpdFLKVWNPDLNLLAVYfdlfkdSTMRKYVLRNFLFEVPLLNKYLFL----KDARKIVPSLTRKDLRYCVGygGVRPQ 425

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 17565764  378 AMDSAGNlvddfVFDSGTGKLSPLLMHVRN-APSPAATSSLAIA 420
Cdd:PTZ00383 426 LIDKVSK-----KLLLGEGKIDPGKGIIFNiTPSPGATTCLGNA 464
PRK07364 PRK07364
FAD-dependent hydroxylase;
16-78 2.07e-04

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 43.47  E-value: 2.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17565764   16 PPKKSVDLPKYDLVIVGGGIVGCATARQLliEKPQLKVALIE---------KEKELAVHQSghnSGVIHAGI 78
Cdd:PRK07364   9 PTLPSTRSLTYDVAIVGGGIVGLTLAAAL--KDSGLRIALIEaqpaeaaaaKGQAYALSLL---SARIFEGI 75
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 23-57 4.58e-04

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 42.51  E-value: 4.58e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17565764  23 LPKYDLVIVGGGIVGCATARQlLIEKPQLKVALIE 57
Cdd:COG2303   2 LEEYDYVIVGAGSAGCVLANR-LSEDAGLRVLLLE 35
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 27-75 6.43e-04

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 42.14  E-value: 6.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 17565764   27 DLVIVGGGIVGCATARQLLieKPQLKVALIEKEKELAVHQSGHNSGVIH 75
Cdd:PRK01747 262 DAAIIGGGIAGAALALALA--RRGWQVTLYEADEAPAQGASGNRQGALY 308
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 26-82 6.50e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 41.54  E-value: 6.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17565764    26 YDLVIVGGGIVGCATARQLLieKPQLKVALIEKEKELAVHQSGhnSGVIHAGIYYTP 82
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLA--DKGLRVLLLEKKSFPRYKPCG--GALSPRALEELD 53
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 24-77 7.89e-04

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 41.46  E-value: 7.89e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 17565764  24 PKYDLVIVGGGIVGCATARQLLieKPQLKVALIEKEKELAVHQSGHnsgVIHAG 77
Cdd:COG0654   2 MRTDVLIVGGGPAGLALALALA--RAGIRVTVVERAPPPRPDGRGI---ALSPR 50
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
 26-80 1.28e-03

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 41.11  E-value: 1.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17565764   26 YDLVIVGGGIVGCATARQLLIEKpqLKVALIEKEkELAVHQSGHNSGVIHAGIYY 80
Cdd:PRK13369   7 YDLFVIGGGINGAGIARDAAGRG--LKVLLCEKD-DLAQGTSSRSGKLVHGGLRY 58
trkA PRK09496
Trk system potassium transporter TrkA;
10-63 1.80e-03

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 40.49  E-value: 1.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17565764   10 FRGISGPPKKSVDlpkyDLVIVGGGIVGCATARQLliEKPQLKVALIEKEKELA 63
Cdd:PRK09496 220 VMSEFGRLEKPVK----RVMIVGGGNIGYYLAKLL--EKEGYSVKLIERDPERA 267
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
25-57 2.12e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 39.94  E-value: 2.12e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 17565764   25 KYDLVIVGGGIVGCATArqLLIEKPQLKVALIE 57
Cdd:PRK07608   5 KFDVVVVGGGLVGASLA--LALAQSGLRVALLA 35
Lycopene_cycl pfam05834
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. ...
 27-57 2.56e-03

Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. Carotenoids with cyclic end groups are essential components of the photosynthetic membranes in all plants, algae, and cyanobacteria. These lipid-soluble compounds protect against photo-oxidation, harvest light for photosynthesis, and dissipate excess light energy absorbed by the antenna pigments. The cyclization of lycopene (psi, psi-carotene) is a key branch point in the pathway of carotenoid biosynthesis. Two types of cyclic end groups are found in higher plant carotenoids: the beta and epsilon rings. Carotenoids with two beta rings are ubiquitous, and those with one beta and one epsilon ring are common; however, carotenoids with two epsilon rings are rare.


Pssm-ID: 310433 [Multi-domain]  Cd Length: 380  Bit Score: 39.71  E-value: 2.56e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 17565764    27 DLVIVGGGIVGCATARQLLIEKPQLKVALIE 57
Cdd:pfam05834   1 DVVIIGAGPAGLSLAARLAAAKPGLSVVLIE 31
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
24-63 4.03e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 39.17  E-value: 4.03e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17565764  24 PKYDLVIVGGGIVGCATARQLLIE-KPQLKVALIEKEKELA 63
Cdd:COG4529   4 ARKRIAIIGGGASGTALAIHLLRRaPEPLRITLFEPRPELG 44
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
 26-80 4.08e-03

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 39.36  E-value: 4.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565764   26 YDLVIVGGGIVGC-----ATARqlliekpQLKVALIEKEkELAVHQSGHNSGVIHAGIYY 80
Cdd:PRK12266   7 YDLLVIGGGINGAgiardAAGR-------GLSVLLCEQD-DLASATSSASTKLIHGGLRY 58
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 24-59 6.64e-03

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 38.43  E-value: 6.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 17565764   24 PKYDLVIVGGGIVGCATArqLLIEKPQLKVALIEKE 59
Cdd:PRK08020   4 QPTDIAIVGGGMVGAALA--LGLAQHGFSVAVLEHA 37
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 25-60 7.22e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 38.53  E-value: 7.22e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 17565764  25 KYDLVIVGGGIVGCATARQLliEKPQLKVALIEKEK 60
Cdd:COG1249   3 DYDLVVIGAGPGGYVAAIRA--AQLGLKVALVEKGR 36
sdhA PRK05945
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
25-58 7.64e-03

succinate dehydrogenase/fumarate reductase flavoprotein subunit;


Pssm-ID: 180319 [Multi-domain]  Cd Length: 575  Bit Score: 38.56  E-value: 7.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 17565764   25 KYDLVIVGGGIVGCATARQLLIEKPQLKVALIEK 58
Cdd:PRK05945   3 EHDVVIVGGGLAGCRAALEIKRLDPSLDVAVVAK 36
 
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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