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Conserved domains on  [gi|767920255|ref|XP_011510343|]
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alkyldihydroxyacetonephosphate synthase, peroxisomal isoform X1 [Homo sapiens]

Protein Classification

FAD-binding oxidoreductase( domain architecture ID 11416043)

FAD-binding oxidoreductase catalyzes the oxidation or reduction of a specific substrate using flavin adenine dinucleotide (FAD) as a cofactor

CATH:  3.30.465.50|3.40.462.20
EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
110-562 1.66e-102

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


:

Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 317.22  E-value: 1.66e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 110 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVE 189
Cdd:COG0277   34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 190 AGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRG-IIEKSCQGPRMSTGP 268
Cdd:COG0277  110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGeVVRTGGRVPKNVTGY 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 269 DIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPqvss 348
Cdd:COG0277  190 DLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPP---- 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 349 iftsfldglkkfyitkfKGFDPNQLSVATLLFEGDREKVLQHE-KQVYDIAAKFGGLAAG--EDNGQRGYL---LTYVIA 422
Cdd:COG0277  266 -----------------LGLPEDGGALLLVEFDGDDAEEVEAQlARLRAILEAGGATDVRvaADGAERERLwkaRKAALP 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 423 YIRDLALEYYVLgesFETSAPWDRVVDLCRnvkeRITRECKEKGVQFAPFStcrvtqtyDAG-ACIYFYFAFNyRGISDP 501
Cdd:COG0277  329 ALGRLDGGAKLL---EDVAVPPSRLPELLR----ELGALAAKYGLRATAFG--------HAGdGNLHVRILFD-PADPEE 392

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920255 502 LTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIF 562
Cdd:COG0277  393 VERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGIL 453
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
110-562 1.66e-102

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 317.22  E-value: 1.66e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 110 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVE 189
Cdd:COG0277   34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 190 AGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRG-IIEKSCQGPRMSTGP 268
Cdd:COG0277  110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGeVVRTGGRVPKNVTGY 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 269 DIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPqvss 348
Cdd:COG0277  190 DLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPP---- 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 349 iftsfldglkkfyitkfKGFDPNQLSVATLLFEGDREKVLQHE-KQVYDIAAKFGGLAAG--EDNGQRGYL---LTYVIA 422
Cdd:COG0277  266 -----------------LGLPEDGGALLLVEFDGDDAEEVEAQlARLRAILEAGGATDVRvaADGAERERLwkaRKAALP 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 423 YIRDLALEYYVLgesFETSAPWDRVVDLCRnvkeRITRECKEKGVQFAPFStcrvtqtyDAG-ACIYFYFAFNyRGISDP 501
Cdd:COG0277  329 ALGRLDGGAKLL---EDVAVPPSRLPELLR----ELGALAAKYGLRATAFG--------HAGdGNLHVRILFD-PADPEE 392

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920255 502 LTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIF 562
Cdd:COG0277  393 VERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGIL 453
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
 295-567 1.39e-56

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 190.22  E-value: 1.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  295 PEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVssiftsfldglkkfyitkfKGFDPNQLS 374
Cdd:pfam02913   2 PEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP-------------------KGLPRDAAA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  375 VATLLFEGDREKVLQHEKQVydIAAKFGGLAAGEDNG--------QRGYLLTYVIAyIRDLALEYYVLGESFETSAPWDR 446
Cdd:pfam02913  63 LLLVEFEGDDEETAEEELEA--VEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  447 VVDLCRNVKERITRECkekgvqfapFSTCRVTQTYDAGACIYFYFAFNYRGISDPL-TVFEQTeaaaREEILANGGSLSH 525
Cdd:pfam02913 140 LADLVRDIKELLDKYG---------LVVCLFGHAGDGNLHLYILFDFRDPEQEERAeKLFDEI----MDLALELGGSISG 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767920255  526 HHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNL 567
Cdd:pfam02913 207 EHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
 115-561 1.90e-29

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 122.42  E-value: 1.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 115 IPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVEAGITG 194
Cdd:PLN02805 133 IPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGG----VCIDMSLMKSVKALHVEDMDVVVEPGIGW 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 195 QELERQLKESGYCTGHEPDSleFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMST-GPDIHHF 273
Cdd:PLN02805 209 LELNEYLEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAaGYDLTRL 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 274 IMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGvaclreiakqrcAPASIRLMDNkqfqfghalKPQVSSIftSF 353
Cdd:PLN02805 287 VIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDA------------ADVAIATMLS---------GIQVSRV--EL 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 354 LDGLKKFYITKFKGfdPNQLSVATLLFE--GDREKVLQHEKQVYDIAAKFGG--LAAGEDNGQRGYLLTyviayIRDLAL 429
Cdd:PLN02805 344 LDEVQIRAINMANG--KNLPEAPTLMFEfiGTEAYAREQTLIVQKIASKHNGsdFVFAEEPEAKKELWK-----IRKEAL 416

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 430 -EYYVLGESFETsapwdRVVDLC---RNVKERITRECKEkgVQFAPFsTCRVTQTYDAG---ACIYFyfafnyrgisDPL 502
Cdd:PLN02805 417 wACFAMEPKYEA-----MITDVCvplSHLAELISRSKKE--LDASPL-VCTVIAHAGDGnfhTIILF----------DPS 478

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920255 503 TVFEQTEAAAREEILANG-----GSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNI 561
Cdd:PLN02805 479 QEDQRREAERLNHFMVHTalsmeGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNI 542
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 119-293 2.03e-11

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 66.42  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  119 VLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPAD-ETRTIISldTSQMNRILWVDENNLTAHVEAGITGQEL 197
Cdd:TIGR01677  35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGsDGALLIS--TKRLNHVVAVDATAMTVTVESGMSLREL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  198 ERQLKESGYCTGHEPdSLEFSTVGGWVSTRASGmkKNIYGN---IEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHF- 273
Cdd:TIGR01677 113 IVEAEKAGLALPYAP-YWWGLTVGGMMGTGAHG--SSLWGKgsaVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFn 189

                         170       180
                  ....*....|....*....|.
gi 767920255  274 -IMGSEGTLGVITEATIKIRP 293
Cdd:TIGR01677 190 aAKVSLGVLGVISQVTLALQP 210
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
110-562 1.66e-102

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 317.22  E-value: 1.66e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 110 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVE 189
Cdd:COG0277   34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 190 AGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRG-IIEKSCQGPRMSTGP 268
Cdd:COG0277  110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGeVVRTGGRVPKNVTGY 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 269 DIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPqvss 348
Cdd:COG0277  190 DLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPP---- 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 349 iftsfldglkkfyitkfKGFDPNQLSVATLLFEGDREKVLQHE-KQVYDIAAKFGGLAAG--EDNGQRGYL---LTYVIA 422
Cdd:COG0277  266 -----------------LGLPEDGGALLLVEFDGDDAEEVEAQlARLRAILEAGGATDVRvaADGAERERLwkaRKAALP 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 423 YIRDLALEYYVLgesFETSAPWDRVVDLCRnvkeRITRECKEKGVQFAPFStcrvtqtyDAG-ACIYFYFAFNyRGISDP 501
Cdd:COG0277  329 ALGRLDGGAKLL---EDVAVPPSRLPELLR----ELGALAAKYGLRATAFG--------HAGdGNLHVRILFD-PADPEE 392

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767920255 502 LTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIF 562
Cdd:COG0277  393 VERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGIL 453
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
 295-567 1.39e-56

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 190.22  E-value: 1.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  295 PEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVssiftsfldglkkfyitkfKGFDPNQLS 374
Cdd:pfam02913   2 PEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP-------------------KGLPRDAAA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  375 VATLLFEGDREKVLQHEKQVydIAAKFGGLAAGEDNG--------QRGYLLTYVIAyIRDLALEYYVLGESFETSAPWDR 446
Cdd:pfam02913  63 LLLVEFEGDDEETAEEELEA--VEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  447 VVDLCRNVKERITRECkekgvqfapFSTCRVTQTYDAGACIYFYFAFNYRGISDPL-TVFEQTeaaaREEILANGGSLSH 525
Cdd:pfam02913 140 LADLVRDIKELLDKYG---------LVVCLFGHAGDGNLHLYILFDFRDPEQEERAeKLFDEI----MDLALELGGSISG 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767920255  526 HHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNL 567
Cdd:pfam02913 207 EHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 116-257 3.55e-43

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 150.81  E-value: 3.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  116 PDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSyglmcPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQ 195
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLL-----GGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767920255  196 ELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEK 257
Cdd:pfam01565  76 DLVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVR 137
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
 115-561 1.90e-29

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 122.42  E-value: 1.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 115 IPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADEtrtiISLDTSQMNRILWVDENNLTAHVEAGITG 194
Cdd:PLN02805 133 IPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGG----VCIDMSLMKSVKALHVEDMDVVVEPGIGW 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 195 QELERQLKESGYCTGHEPDSleFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMST-GPDIHHF 273
Cdd:PLN02805 209 LELNEYLEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAaGYDLTRL 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 274 IMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGvaclreiakqrcAPASIRLMDNkqfqfghalKPQVSSIftSF 353
Cdd:PLN02805 287 VIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDA------------ADVAIATMLS---------GIQVSRV--EL 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 354 LDGLKKFYITKFKGfdPNQLSVATLLFE--GDREKVLQHEKQVYDIAAKFGG--LAAGEDNGQRGYLLTyviayIRDLAL 429
Cdd:PLN02805 344 LDEVQIRAINMANG--KNLPEAPTLMFEfiGTEAYAREQTLIVQKIASKHNGsdFVFAEEPEAKKELWK-----IRKEAL 416

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 430 -EYYVLGESFETsapwdRVVDLC---RNVKERITRECKEkgVQFAPFsTCRVTQTYDAG---ACIYFyfafnyrgisDPL 502
Cdd:PLN02805 417 wACFAMEPKYEA-----MITDVCvplSHLAELISRSKKE--LDASPL-VCTVIAHAGDGnfhTIILF----------DPS 478

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767920255 503 TVFEQTEAAAREEILANG-----GSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNI 561
Cdd:PLN02805 479 QEDQRREAERLNHFMVHTalsmeGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNI 542
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
 115-358 1.05e-11

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 67.11  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 115 IPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMcPADETrtiISLDTSQMNRILWVDENNLTAHVEAGITG 194
Cdd:PRK11230  55 RPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGAL-PLEKG---VLLVMARFNRILDINPVGRRARVQPGVRN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 195 QELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGniedLVVH----IKMVTPRGiiEKSCQGPRM--STGP 268
Cdd:PRK11230 131 LAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYG----LTVHnllkVEILTLDG--EALTLGSDAldSPGF 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 269 DIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQ----FGHALKP 344
Cdd:PRK11230 205 DLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDNLSIRaaedFIHAGYP 284

                        250
                 ....*....|....*
gi 767920255 345 -QVSSIFTSFLDGLK 358
Cdd:PRK11230 285 vDAEAILLCELDGVE 299
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 119-293 2.03e-11

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 66.42  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  119 VLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPAD-ETRTIISldTSQMNRILWVDENNLTAHVEAGITGQEL 197
Cdd:TIGR01677  35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGsDGALLIS--TKRLNHVVAVDATAMTVTVESGMSLREL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  198 ERQLKESGYCTGHEPdSLEFSTVGGWVSTRASGmkKNIYGN---IEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHF- 273
Cdd:TIGR01677 113 IVEAEKAGLALPYAP-YWWGLTVGGMMGTGAHG--SSLWGKgsaVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFn 189

                         170       180
                  ....*....|....*....|.
gi 767920255  274 -IMGSEGTLGVITEATIKIRP 293
Cdd:TIGR01677 190 aAKVSLGVLGVISQVTLALQP 210
PLN02465 PLN02465
L-galactono-1,4-lactone dehydrogenase
 122-293 9.74e-10

L-galactono-1,4-lactone dehydrogenase


Pssm-ID: 215258 [Multi-domain]  Cd Length: 573  Bit Score: 61.02  E-value: 9.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 122 PTCHDDVVKIVNLACKYNLCIIPIGGGTSVSyGLmcpADETRTIISLdtSQMNRILWVDENNLTAHVEAGITGQELERQL 201
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRRIRPVGSGLSPN-GL---AFSREGMVNL--ALMDKVLEVDKEKKRVTVQAGARVQQVVEAL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 202 KESGYcTGHEPDSLEFSTVGGWVSTRASGMKKNIyGNIEDLVVHIKMVTP-RGIIEKSCQgprmsTGPDIHHFIMGSEGT 280
Cdd:PLN02465 177 RPHGL-TLQNYASIREQQIGGFIQVGAHGTGARI-PPIDEQVVSMKLVTPaKGTIELSKE-----DDPELFRLARCGLGG 249

                        170
                 ....*....|...
gi 767920255 281 LGVITEATIKIRP 293
Cdd:PLN02465 250 LGVVAEVTLQCVP 262
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
 110-293 2.61e-09

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 59.53  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  110 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYglMCPADETrtIISLDtsQMNRILWVDENNLTAHVE 189
Cdd:TIGR01678   9 KTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSD--IACTDGF--LIHLD--KMNKVLQFDKEKKQITVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  190 AGITGQELERQLKESGYCTGHePDSLEFSTVGGWVS--TRASGMKkniYGNIEDLVVHIKMVTPRGIIeKSCQGPRmstG 267
Cdd:TIGR01678  83 AGIRLYQLHEQLDEHGYSMSN-LGSISEVSVAGIIStgTHGSSIK---HGILATQVVALTIMTADGEV-LECSEER---N 154

                         170       180
                  ....*....|....*....|....*.
gi 767920255  268 PDIHHFIMGSEGTLGVITEATIKIRP 293
Cdd:TIGR01678 155 ADVFQAARVSLGCLGIIVTVTIQVVP 180
GLDHase TIGR01676
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ...
 110-290 3.34e-07

galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD.


Pssm-ID: 130737 [Multi-domain]  Cd Length: 541  Bit Score: 53.14  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  110 GMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVS-YGLmcpadeTRTIIsLDTSQMNRILWVDENNLTAHV 188
Cdd:TIGR01676  56 GTHEVLTRTFHQPEAIEELEGIVKQANEKKARIRPVGSGLSPNgIGL------SRAGM-VNLALMDKVLEVDEEKKRVRV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255  189 EAGITGQELERQLKESGYcTGHEPDSLEFSTVGGWVSTRASGMKKNIyGNIEDLVVHIKMVTP-RGIIEKSCQgprmsTG 267
Cdd:TIGR01676 129 QAGIRVQQLVDAIKEYGI-TLQNFASIREQQIGGIIQVGAHGTGAKL-PPIDEQVIAMKLVTPaKGTIEISKD-----KD 201

                         170       180
                  ....*....|....*....|...
gi 767920255  268 PDIHHFIMGSEGTLGVITEATIK 290
Cdd:TIGR01676 202 PELFFLARCGLGGLGVVAEVTLQ 224
glcE PRK11282
glycolate oxidase FAD binding subunit; Provisional
 140-321 9.33e-06

glycolate oxidase FAD binding subunit; Provisional


Pssm-ID: 236893 [Multi-domain]  Cd Length: 352  Bit Score: 47.91  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 140 LCIIpiGGGTSVSYGlMCPADETrtiisLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDslEF-- 217
Cdd:PRK11282  21 LRIR--GGGSKDFYG-RALAGEV-----LDTRAHRGIVSYDPTELVITARAGTPLAELEAALAEAGQMLPFEPP--HFgg 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767920255 218 -STVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIeKSCQGPRMST--GPDIHHFIMGSEGTLGVITEATIKIRPV 294
Cdd:PRK11282  91 gATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEH-LRFGGQVMKNvaGYDVSRLMAGSLGTLGVLLEVSLKVLPR 169

                        170       180
                 ....*....|....*....|....*...
gi 767920255 295 PEYQkyGSVAFP-NFEQGVACLREIAKQ 321
Cdd:PRK11282 170 PRAE--LTLRLEmDAAEALRKLNEWGGQ 195
 
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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