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Conserved domains on  [gi|1002583046|ref|XP_015670460|]
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alkyldihydroxyacetonephosphate synthase, peroxisomal [Protobothrops mucrosquamatus]

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];
175-633 9.18e-100

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


:

Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 312.21  E-value: 9.18e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 175 GMFKRVPDVVVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGLQCPPDEkrtiVSLDTSQMNRIHWIDEKNLTAHVD 254
Cdd:COG0277    34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 255 AGIVGQDLEKQLGESGYCTGHEPDSMEFSTLGGWVATRASGMKKNVYGNIEDLVVHIKMVTPKGVIQKNcqGPRM---ST 331
Cdd:COG0277   110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGEVVRT--GGRVpknVT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 332 GPDIHHFILGSEGILGVITEVTIKIRPVPEYQKYGSVVFPNFEKGVACLREIAKQRCAPASIRLMDNVQFQFGHALKPqv 411
Cdd:COG0277   188 GYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPP-- 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 412 asiftslldglkkvyitkfKGFDPNVLCVATLVFEGAREKVLQHE-KQVYDIAAKFGG----LAAGEDNGQRGYMMTF-I 485
Cdd:COG0277   266 -------------------LGLPEDGGALLLVEFDGDDAEEVEAQlARLRAILEAGGAtdvrVAADGAERERLWKARKaA 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 486 IAYIRDFGMDYYIVgesFETSVPWDRVLDLCknvkERMTRECKEKGVQFPLFAtcrvtqmyDSG-ACVYFYLGFNYRGIS 564
Cdd:COG0277   327 LPALGRLDGGAKLL---EDVAVPPSRLPELL----RELGALAAKYGLRATAFG--------HAGdGNLHVRILFDPADPE 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002583046 565 DPTRViEEIEAAARDEILANGGSLSHHHGVGKLRKHWMKECVSDVGLGMLKSMKQFVDPDNIFGNGNLL 633
Cdd:COG0277   392 EVERA-RAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKIL 459
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
175-633 9.18e-100

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 312.21  E-value: 9.18e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 175 GMFKRVPDVVVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGLQCPPDEkrtiVSLDTSQMNRIHWIDEKNLTAHVD 254
Cdd:COG0277    34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 255 AGIVGQDLEKQLGESGYCTGHEPDSMEFSTLGGWVATRASGMKKNVYGNIEDLVVHIKMVTPKGVIQKNcqGPRM---ST 331
Cdd:COG0277   110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGEVVRT--GGRVpknVT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 332 GPDIHHFILGSEGILGVITEVTIKIRPVPEYQKYGSVVFPNFEKGVACLREIAKQRCAPASIRLMDNVQFQFGHALKPqv 411
Cdd:COG0277   188 GYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPP-- 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 412 asiftslldglkkvyitkfKGFDPNVLCVATLVFEGAREKVLQHE-KQVYDIAAKFGG----LAAGEDNGQRGYMMTF-I 485
Cdd:COG0277   266 -------------------LGLPEDGGALLLVEFDGDDAEEVEAQlARLRAILEAGGAtdvrVAADGAERERLWKARKaA 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 486 IAYIRDFGMDYYIVgesFETSVPWDRVLDLCknvkERMTRECKEKGVQFPLFAtcrvtqmyDSG-ACVYFYLGFNYRGIS 564
Cdd:COG0277   327 LPALGRLDGGAKLL---EDVAVPPSRLPELL----RELGALAAKYGLRATAFG--------HAGdGNLHVRILFDPADPE 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002583046 565 DPTRViEEIEAAARDEILANGGSLSHHHGVGKLRKHWMKECVSDVGLGMLKSMKQFVDPDNIFGNGNLL 633
Cdd:COG0277   392 EVERA-RAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKIL 459
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
 360-632 1.08e-55

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


Pssm-ID: 397178  Cd Length: 248  Bit Score: 189.45  E-value: 1.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 360 PEYQKYGSVVFPNFEKGVACLREIAKQRCAPASIRLMDNVQFQFGHALKPQVasiftslldglkkvyitkfKGFDPNVLC 439
Cdd:pfam02913   2 PEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP-------------------KGLPRDAAA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 440 VATLVFEGAREKVLQHEKQVydIAAKFGGLAAGEDNG--------QRGYMMTFIIAyIRDFGMDYYIVGESFETSVPWDR 511
Cdd:pfam02913  63 LLLVEFEGDDEETAEEELEA--VEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 512 VLDLCKNVKERMTRECkekgvqfplFATCRVTQMYDSGACVYFYLGFNYRGISDPtrvIEEIEAAARDEILANGGSLSHH 591
Cdd:pfam02913 140 LADLVRDIKELLDKYG---------LVVCLFGHAGDGNLHLYILFDFRDPEQEER---AEKLFDEIMDLALELGGSISGE 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1002583046 592 HGVGKLRKHWMKECVSDVGLGMLKSMKQFVDPDNIFGNGNL 632
Cdd:pfam02913 208 HGVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
 180-633 4.68e-29

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 122.04  E-value: 4.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 180 VPDVVVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGLQCPpdekRTIVSLDTSQMNRIHWIDEKNLTAHVDAGIVG 259
Cdd:PLN02805  133 IPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAP----HGGVCIDMSLMKSVKALHVEDMDVVVEPGIGW 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 260 QDLEKQLGESGYCTGHEPDSMefSTLGGWVATRASGMKKNVYGNIEDLVVHIKMVTPKGVIQKNCQGPRMS-TGPDIHHF 338
Cdd:PLN02805  209 LELNEYLEPYGLFFPLDPGPG--ATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSaAGYDLTRL 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 339 ILGSEGILGVITEVTIKIRPVPEYQKYGSVVFPNFEKGVACLREIAKQRCAPASIRLMDNVQfqfghalkpqvasiftsl 418
Cdd:PLN02805  287 VIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATMLSGIQVSRVELLDEVQ------------------ 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 419 ldgLKKVYITKFKgfdpNVLCVATLVFE--GAREKVLQHEKQVYDIAAKFGG---LAAGEDNGQRGYMMTFIIAYIRDFG 493
Cdd:PLN02805  349 ---IRAINMANGK----NLPEAPTLMFEfiGTEAYAREQTLIVQKIASKHNGsdfVFAEEPEAKKELWKIRKEALWACFA 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 494 MDYYIVGESFETSVPWDRVLDLCKNVKERMTREckekgvqfPLfaTCRVTQMYDSG---ACVYFylgfnyrgisDPT--- 567
Cdd:PLN02805  422 MEPKYEAMITDVCVPLSHLAELISRSKKELDAS--------PL--VCTVIAHAGDGnfhTIILF----------DPSqed 481

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002583046 568 --RVIEEIEAAARDEILANGGSLSHHHGVGKLRkhwMKECVSDVGLGMLKSMKQF---VDPDNIFGNGNLL 633
Cdd:PLN02805  482 qrREAERLNHFMVHTALSMEGTCTGEHGVGTGK---MKYLEKELGIEALQTMKRIkkaLDPNNIMNPGKLI 549
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 184-358 9.89e-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: 64.50  E-value: 9.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 184 VVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGLQCPPDEKRTIVsLDTSQMNRIHWIDEKNLTAHVDAGIVGQDLE 263
Cdd:TIGR01677  35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGSDGALL-ISTKRLNHVVAVDATAMTVTVESGMSLRELI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 264 KQLGESGYCTGHEPdSMEFSTLGGWVATRASGMKKNVYGN-IEDLVVHIKMVTPKGVIQKNCQGPRMSTGPDIHHF--IL 340
Cdd:TIGR01677 114 VEAEKAGLALPYAP-YWWGLTVGGMMGTGAHGSSLWGKGSaVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFnaAK 192

                         170
                  ....*....|....*...
gi 1002583046 341 GSEGILGVITEVTIKIRP 358
Cdd:TIGR01677 193 VSLGVLGVISQVTLALQP 210
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
175-633 9.18e-100

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 312.21  E-value: 9.18e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 175 GMFKRVPDVVVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGLQCPPDEkrtiVSLDTSQMNRIHWIDEKNLTAHVD 254
Cdd:COG0277    34 SLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDGG----VVLDLSRMNRILEVDPEDRTATVE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 255 AGIVGQDLEKQLGESGYCTGHEPDSMEFSTLGGWVATRASGMKKNVYGNIEDLVVHIKMVTPKGVIQKNcqGPRM---ST 331
Cdd:COG0277   110 AGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVLGLEVVLADGEVVRT--GGRVpknVT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 332 GPDIHHFILGSEGILGVITEVTIKIRPVPEYQKYGSVVFPNFEKGVACLREIAKQRCAPASIRLMDNVQFQFGHALKPqv 411
Cdd:COG0277   188 GYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAGIAPAALELMDRAALALVEAAPP-- 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 412 asiftslldglkkvyitkfKGFDPNVLCVATLVFEGAREKVLQHE-KQVYDIAAKFGG----LAAGEDNGQRGYMMTF-I 485
Cdd:COG0277   266 -------------------LGLPEDGGALLLVEFDGDDAEEVEAQlARLRAILEAGGAtdvrVAADGAERERLWKARKaA 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 486 IAYIRDFGMDYYIVgesFETSVPWDRVLDLCknvkERMTRECKEKGVQFPLFAtcrvtqmyDSG-ACVYFYLGFNYRGIS 564
Cdd:COG0277   327 LPALGRLDGGAKLL---EDVAVPPSRLPELL----RELGALAAKYGLRATAFG--------HAGdGNLHVRILFDPADPE 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002583046 565 DPTRViEEIEAAARDEILANGGSLSHHHGVGKLRKHWMKECVSDVGLGMLKSMKQFVDPDNIFGNGNLL 633
Cdd:COG0277   392 EVERA-RAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKIL 459
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
 360-632 1.08e-55

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


Pssm-ID: 397178  Cd Length: 248  Bit Score: 189.45  E-value: 1.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 360 PEYQKYGSVVFPNFEKGVACLREIAKQRCAPASIRLMDNVQFQFGHALKPQVasiftslldglkkvyitkfKGFDPNVLC 439
Cdd:pfam02913   2 PEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFP-------------------KGLPRDAAA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 440 VATLVFEGAREKVLQHEKQVydIAAKFGGLAAGEDNG--------QRGYMMTFIIAyIRDFGMDYYIVGESFETSVPWDR 511
Cdd:pfam02913  63 LLLVEFEGDDEETAEEELEA--VEAILEAGGAGDVVVatdeaeaeRLWAARKYALP-LRDALGGAGPAVFSEDVSVPRSR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 512 VLDLCKNVKERMTRECkekgvqfplFATCRVTQMYDSGACVYFYLGFNYRGISDPtrvIEEIEAAARDEILANGGSLSHH 591
Cdd:pfam02913 140 LADLVRDIKELLDKYG---------LVVCLFGHAGDGNLHLYILFDFRDPEQEER---AEKLFDEIMDLALELGGSISGE 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1002583046 592 HGVGKLRKHWMKECVSDVGLGMLKSMKQFVDPDNIFGNGNL 632
Cdd:pfam02913 208 HGVGRDKKPYLEREFGEEGLALMRRIKAAFDPKGILNPGKV 248
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 181-322 2.32e-41

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: 146.58  E-value: 2.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 181 PDVVVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGLQCPPDekrtiVSLDTSQMNRIHWIDEKNLTAHVDAGIVGQ 260
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGG-----IVLDLSRLNGILEIDPEDGTATVEAGVTLG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002583046 261 DLEKQLGESGYCTGHEPDSMEFSTLGGWVATRASGMKKNVYGNIEDLVVHIKMVTPKGVIQK 322
Cdd:pfam01565  76 DLVRALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVR 137
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
 180-633 4.68e-29

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 122.04  E-value: 4.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 180 VPDVVVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGLQCPpdekRTIVSLDTSQMNRIHWIDEKNLTAHVDAGIVG 259
Cdd:PLN02805  133 IPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAP----HGGVCIDMSLMKSVKALHVEDMDVVVEPGIGW 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 260 QDLEKQLGESGYCTGHEPDSMefSTLGGWVATRASGMKKNVYGNIEDLVVHIKMVTPKGVIQKNCQGPRMS-TGPDIHHF 338
Cdd:PLN02805  209 LELNEYLEPYGLFFPLDPGPG--ATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSaAGYDLTRL 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 339 ILGSEGILGVITEVTIKIRPVPEYQKYGSVVFPNFEKGVACLREIAKQRCAPASIRLMDNVQfqfghalkpqvasiftsl 418
Cdd:PLN02805  287 VIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATMLSGIQVSRVELLDEVQ------------------ 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 419 ldgLKKVYITKFKgfdpNVLCVATLVFE--GAREKVLQHEKQVYDIAAKFGG---LAAGEDNGQRGYMMTFIIAYIRDFG 493
Cdd:PLN02805  349 ---IRAINMANGK----NLPEAPTLMFEfiGTEAYAREQTLIVQKIASKHNGsdfVFAEEPEAKKELWKIRKEALWACFA 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 494 MDYYIVGESFETSVPWDRVLDLCKNVKERMTREckekgvqfPLfaTCRVTQMYDSG---ACVYFylgfnyrgisDPT--- 567
Cdd:PLN02805  422 MEPKYEAMITDVCVPLSHLAELISRSKKELDAS--------PL--VCTVIAHAGDGnfhTIILF----------DPSqed 481

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002583046 568 --RVIEEIEAAARDEILANGGSLSHHHGVGKLRkhwMKECVSDVGLGMLKSMKQF---VDPDNIFGNGNLL 633
Cdd:PLN02805  482 qrREAERLNHFMVHTALSMEGTCTGEHGVGTGK---MKYLEKELGIEALQTMKRIkkaLDPNNIMNPGKLI 549
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
 177-423 1.37e-15

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 79.82  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 177 FKRVPDVVVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGlqCPPDEKRtiVSLDTSQMNRIHWIDEKNLTAHVDAG 256
Cdd:PRK11230   52 YRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGG--ALPLEKG--VLLVMARFNRILDINPVGRRARVQPG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 257 IVGQDLEKQLGESGYCTGHEPDSMEFSTLGGWVATRASGMKKNVYGniedLVVH----IKMVTpkgviqknCQGPRM--- 329
Cdd:PRK11230  128 VRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYG----LTVHnllkVEILT--------LDGEALtlg 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 330 -----STGPDIHHFILGSEGILGVITEVTIKIRPVPEYQKYGSVVFPNFEKGVACLREIAKQRCAPASIRLMDNVQFQ-- 402
Cdd:PRK11230  196 sdaldSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDNLSIRaa 275

                         250       260
                  ....*....|....*....|....
gi 1002583046 403 --FGHALKP-QVASIFTSLLDGLK 423
Cdd:PRK11230  276 edFIHAGYPvDAEAILLCELDGVE 299
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 184-358 9.89e-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: 64.50  E-value: 9.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 184 VVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSGLQCPPDEKRTIVsLDTSQMNRIHWIDEKNLTAHVDAGIVGQDLE 263
Cdd:TIGR01677  35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYSHSIPKLACPDGSDGALL-ISTKRLNHVVAVDATAMTVTVESGMSLRELI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 264 KQLGESGYCTGHEPdSMEFSTLGGWVATRASGMKKNVYGN-IEDLVVHIKMVTPKGVIQKNCQGPRMSTGPDIHHF--IL 340
Cdd:TIGR01677 114 VEAEKAGLALPYAP-YWWGLTVGGMMGTGAHGSSLWGKGSaVHDYVVGIRLVVPASAAEGFAKVRILSEGDTPNEFnaAK 192

                         170
                  ....*....|....*...
gi 1002583046 341 GSEGILGVITEVTIKIRP 358
Cdd:TIGR01677 193 VSLGVLGVISQVTLALQP 210
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
 175-358 3.44e-07

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: 52.98  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 175 GMFKRVPDVVVWPECHDDVVKIVEIACKHNICIIPYGGGTSVSSglQCPPDEkrTIVSLDtsQMNRIHWIDEKNLTAHVD 254
Cdd:TIGR01678   9 KTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSD--IACTDG--FLIHLD--KMNKVLQFDKEKKQITVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 255 AGIVGQDLEKQLGESGYCTGHePDSMEFSTLGGWVA--TRASGMKknvYGNIEDLVVHIKMVTPKGVIqKNCQGPRmstG 332
Cdd:TIGR01678  83 AGIRLYQLHEQLDEHGYSMSN-LGSISEVSVAGIIStgTHGSSIK---HGILATQVVALTIMTADGEV-LECSEER---N 154

                         170       180
                  ....*....|....*....|....*.
gi 1002583046 333 PDIHHFILGSEGILGVITEVTIKIRP 358
Cdd:TIGR01678 155 ADVFQAARVSLGCLGIIVTVTIQVVP 180
PLN02465 PLN02465
L-galactono-1,4-lactone dehydrogenase
 187-358 1.30e-05

L-galactono-1,4-lactone dehydrogenase


Pssm-ID: 215258 [Multi-domain]  Cd Length: 573  Bit Score: 48.31  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 187 PECHDDVVKIVEIACKHNICIIPYGGGTSvSSGLQCppdEKRTIVSLdtSQMNRIHWIDEKNLTAHVDAGIVGQDLEKQL 266
Cdd:PLN02465  103 PESLEELEDIVKEAHEKGRRIRPVGSGLS-PNGLAF---SREGMVNL--ALMDKVLEVDKEKKRVTVQAGARVQQVVEAL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 267 GESGYcTGHEPDSMEFSTLGGWVATRASGMKKNVyGNIEDLVVHIKMVTP-KGVIQKNCQgprmsTGPDIHHFILGSEGI 345
Cdd:PLN02465  177 RPHGL-TLQNYASIREQQIGGFIQVGAHGTGARI-PPIDEQVVSMKLVTPaKGTIELSKE-----DDPELFRLARCGLGG 249

                         170
                  ....*....|...
gi 1002583046 346 LGVITEVTIKIRP 358
Cdd:PLN02465  250 LGVVAEVTLQCVP 262
glcE PRK11282
glycolate oxidase FAD binding subunit; Provisional
 260-361 4.79e-05

glycolate oxidase FAD binding subunit; Provisional


Pssm-ID: 236893 [Multi-domain]  Cd Length: 352  Bit Score: 45.98  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 260 QDLEKQLGESGYCTGHEPDsmEF---STLGGWVATRASGMKKNVYGNIEDLVVHIKMVTPK-------GVIQKNCqgprm 329
Cdd:PRK11282   68 AELEAALAEAGQMLPFEPP--HFgggATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRgehlrfgGQVMKNV----- 140

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1002583046 330 sTGPDIHHFILGSEGILGVITEVTIKIRPVPE 361
Cdd:PRK11282  141 -AGYDVSRLMAGSLGTLGVLLEVSLKVLPRPR 171
GLDHase TIGR01676
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ...
 187-355 7.24e-05

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: 45.82  E-value: 7.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 187 PECHDDVVKIVEIACKHNICIIPYGGGTSVSS-GLQcppdeKRTIVSLdtSQMNRIHWIDEKNLTAHVDAGIVGQDLEKQ 265
Cdd:TIGR01676  68 PEAIEELEGIVKQANEKKARIRPVGSGLSPNGiGLS-----RAGMVNL--ALMDKVLEVDEEKKRVRVQAGIRVQQLVDA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002583046 266 LGESGYcTGHEPDSMEFSTLGGWVATRASGMKKNVyGNIEDLVVHIKMVTP-KGVIQkncqgprMSTGPDIHHFILGSEG 344
Cdd:TIGR01676 141 IKEYGI-TLQNFASIREQQIGGIIQVGAHGTGAKL-PPIDEQVIAMKLVTPaKGTIE-------ISKDKDPELFFLARCG 211

                         170
                  ....*....|...
gi 1002583046 345 I--LGVITEVTIK 355
Cdd:TIGR01676 212 LggLGVVAEVTLQ 224
 
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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