|
Name |
Accession |
Description |
Interval |
E-value |
| bact_FAD_ox |
TIGR01679 |
FAD-linked oxidoreductase; This model represents a family of bacterial oxidoreductases with ... |
19-440 |
1.95e-153 |
|
FAD-linked oxidoreductase; This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, 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.
Pssm-ID: 130740 [Multi-domain] Cd Length: 419 Bit Score: 441.25 E-value: 1.95e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 19 WRNWSGAQSCLPLAREAPKDLDELVRIIRQASGRIRPVGSGHSFSALVPTDGTLLSLAYFSGLLSHDSVTLQAEFGGGTP 98
Cdd:TIGR01679 1 WSNWSGEQVAAPSAIVRPTDEGELADVIAQAAKPVRAVGSGHSFTDLACTDGTMISLTGLQGVVDVDQPTGLATVEAGTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 99 MSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGTGVGFGSYSAQVRGLQLVTASGEVLECDAKRNVEVFDAARVSLG 178
Cdd:TIGR01679 81 LGALGPQLAQRGLGLENQGDIDPQSIGGALGTATHGTGVRFQALHARIVSLRLVTAGGKVLDLSEGDDQDMYLAARVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 179 ALGVVTRVRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPKTPpldPAKEGGNE 258
Cdd:TIGR01679 161 ALGVISQVTLQTVALFRLRRRDWRRPLAQTLERLDEFVDGHRHFEFYVFPFAGKALTITMDRSDEQPKP---RQRDVDEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 259 FVGLIEGLDKYLSDFPETRRTLLNSLRHFARFDERVDDSYAVYANVRNVRFNEMEYSVPAEHGPACLREILALIRDKDLR 338
Cdd:TIGR01679 238 FLGGLRLLRQTLRRFPSLRPRLNRLMTNMMSSETVVDRAYKVFATQRKVRFNEMEYHLPRENGRKALQEVIDLVERRSPP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 339 TWFPIEYRYVKADDIPLSMFEGRDSCSISVHQHYSMDHHNFFAAVEPIFWKYAGRPHWGKLHGLNAHQLQGLYPRWKAFA 418
Cdd:TIGR01679 318 VMFPIEVRFSAPDDSWLSPFYGRPTCSIAVHQYAGMDFESYFRAVEPIFRRYAGRPHWGKRHYLTAATLRERYPRWDDFA 397
|
410 420
....*....|....*....|..
gi 15600520 419 EVRQALDPRGRFLNAHLSSILG 440
Cdd:TIGR01679 398 AVRDDLDPDRRFLNPYTRGLFG 419
|
|
| ALO |
pfam04030 |
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC: ... |
186-438 |
2.26e-104 |
|
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.
Pssm-ID: 427663 [Multi-domain] Cd Length: 258 Bit Score: 310.35 E-value: 2.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 186 VRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPktPPLDPAKEGGNEFVG--LI 263
Cdd:pfam04030 1 VTLRVVPAFTLTSTQEVISFDTLLENWDELLTSSEHFRFWWFPYTDKAVVWRANKTDEP--EQSRPRKSLYGEWLGngVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 264 EGLDKYLSDFPETRRTLLNSLRHFARF-DERVDDSYAVYANVRNVRFNEMEYSVPAEHGPACLREILALIRDKDLRTWFP 342
Cdd:pfam04030 79 EALLWLSRIFPSLTPWVERFVFKLQYGgDEAVDDSYKVFNMDCLVSQFVMEWAIPLENGPEALRELRAWIRRAALRVHFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 343 IEYRYVKADDIPLSMFEGRDSCSISVHQHYSMD----HHNFFAAVEPIFWKYAGRPHWGKLHGLNAHQLQGLYPRWKAFA 418
Cdd:pfam04030 159 IEVRCSAADDIYLSTAYGRDTCYINAHMYRPYGrnvpYHKYFRAFEDIMKKYGGRPHWAKNHTLTAEDLEEWYPDWDRFL 238
|
250 260
....*....|....*....|
gi 15600520 419 EVRQALDPRGRFLNAHLSSI 438
Cdd:pfam04030 239 QVRKKLDPEGVFLNEYLRRV 258
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
21-442 |
3.38e-38 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 145.76 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 21 NWSGAQSCLPLAREAPKDLDELVRIIRQASG---RIRPVGSGHSFSALVPTDGTLLSLAYFSGLLSHD----SVTLQAef 93
Cdd:PLN02465 88 NWSGTHEVQTRRYHQPESLEELEDIVKEAHEkgrRIRPVGSGLSPNGLAFSREGMVNLALMDKVLEVDkekkRVTVQA-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 94 ggGTPMSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGTGVGFGSYSAQVRGLQLVTASGEVLECDAKRNVEVFDAA 173
Cdd:PLN02465 166 --GARVQQVVEALRPHGLTLQNYASIREQQIGGFIQVGAHGTGARIPPIDEQVVSMKLVTPAKGTIELSKEDDPELFRLA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 174 RVSLGALGVVTRVRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPKTPPLDPAK 253
Cdd:PLN02465 244 RCGLGGLGVVAEVTLQCVPAHRLVEHTFVSNRKEIKKNHKKWLSENKHIRYMWIPYTDTVVVVTCNPLSKWKEPPKIKPK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 254 EGGNEFVGLIEGLDKYLSD---------------FPETRRTLLN----SLRHFARFDE------------RVDDSYAVYA 302
Cdd:PLN02465 324 YSEDERVQPLRDLYKESAGtkssenpepdiqemgFGELRDKLLAldplDPDHVKRVNAaeaefwrrsegyRVGWSDEILG 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 303 -------NVRNVRFNEMEYSVPAEHGPACLREILALIRDKDLRTWFPIEYRYVKADDIPLSmfEGRDSCSISVHQH---- 371
Cdd:PLN02465 404 fdcggqqWVSEVCFPAGTLAKPSMKDLEFMEELLALIEKEGIPAPAPIEQRWTASSSSPMS--PASSPSPDDLHSWvgii 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 372 -Y--SMDHHN-------FFA---AVEPIFW-KYAGRPHWGKLH-GLNAHQLQGLYPRWK------AFAEVRQALDPRGRF 430
Cdd:PLN02465 482 mYlpTEDERQrkeiteeFFHyrkKTQRNLWdKYSAYEHWAKIEvPKDKEELEALRERLRkrfpvdAFNKARKELDPKGIL 561
|
490
....*....|..
gi 15600520 431 LNAHLSSILGVT 442
Cdd:PLN02465 562 SNNLLEKLFPKS 573
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
22-338 |
9.16e-14 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 73.00 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 22 WSGAQSCLPLAREAPKDLDELVRIIRQASGR---IRPVGSGHSFS--ALVPTDGTLLSLAYFSGLLSHDSVTLQAEFGGG 96
Cdd:COG0277 32 GNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHgvpVVPRGGGTGLAggAVPLDGGVVLDLSRMNRILEVDPEDRTATVEAG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 97 TPMSQMGAPLKEIGQAL-VNMADIDYQTLAGAIATSTHGTG-VGFGSYSAQVRGLQLVTASGEVLECDAK--RNVEVFDA 172
Cdd:COG0277 112 VTLADLNAALAPHGLFFpPDPSSQGTATIGGNIATNAGGPRsLKYGLTRDNVLGLEVVLADGEVVRTGGRvpKNVTGYDL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 173 ARV---SLGALGVVTRVRLqnRAAYRLRERQWIARTEELLEDVEKNTRE--NQHWEMLVVTHSDyALSIALNETDEPKTP 247
Cdd:COG0277 192 FWLlvgSEGTLGVITEATL--RLHPLPEAVATALVAFPDLEAAAAAVRAllAAGIAPAALELMD-RAALALVEAAPPLGL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 248 PLDPA------KEGGNEFVG--LIEGLDKYLSDFPETRRTLLNSLRHFARFDERVDDSYAVYANVRNVRFNEMEYSVPAE 319
Cdd:COG0277 269 PEDGGalllveFDGDDAEEVeaQLARLRAILEAGGATDVRVAADGAERERLWKARKAALPALGRLDGGAKLLEDVAVPPS 348
|
330
....*....|....*....
gi 15600520 320 HGPACLREILALIRDKDLR 338
Cdd:COG0277 349 RLPELLRELGALAAKYGLR 367
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| bact_FAD_ox |
TIGR01679 |
FAD-linked oxidoreductase; This model represents a family of bacterial oxidoreductases with ... |
19-440 |
1.95e-153 |
|
FAD-linked oxidoreductase; This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, 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.
Pssm-ID: 130740 [Multi-domain] Cd Length: 419 Bit Score: 441.25 E-value: 1.95e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 19 WRNWSGAQSCLPLAREAPKDLDELVRIIRQASGRIRPVGSGHSFSALVPTDGTLLSLAYFSGLLSHDSVTLQAEFGGGTP 98
Cdd:TIGR01679 1 WSNWSGEQVAAPSAIVRPTDEGELADVIAQAAKPVRAVGSGHSFTDLACTDGTMISLTGLQGVVDVDQPTGLATVEAGTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 99 MSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGTGVGFGSYSAQVRGLQLVTASGEVLECDAKRNVEVFDAARVSLG 178
Cdd:TIGR01679 81 LGALGPQLAQRGLGLENQGDIDPQSIGGALGTATHGTGVRFQALHARIVSLRLVTAGGKVLDLSEGDDQDMYLAARVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 179 ALGVVTRVRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPKTPpldPAKEGGNE 258
Cdd:TIGR01679 161 ALGVISQVTLQTVALFRLRRRDWRRPLAQTLERLDEFVDGHRHFEFYVFPFAGKALTITMDRSDEQPKP---RQRDVDEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 259 FVGLIEGLDKYLSDFPETRRTLLNSLRHFARFDERVDDSYAVYANVRNVRFNEMEYSVPAEHGPACLREILALIRDKDLR 338
Cdd:TIGR01679 238 FLGGLRLLRQTLRRFPSLRPRLNRLMTNMMSSETVVDRAYKVFATQRKVRFNEMEYHLPRENGRKALQEVIDLVERRSPP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 339 TWFPIEYRYVKADDIPLSMFEGRDSCSISVHQHYSMDHHNFFAAVEPIFWKYAGRPHWGKLHGLNAHQLQGLYPRWKAFA 418
Cdd:TIGR01679 318 VMFPIEVRFSAPDDSWLSPFYGRPTCSIAVHQYAGMDFESYFRAVEPIFRRYAGRPHWGKRHYLTAATLRERYPRWDDFA 397
|
410 420
....*....|....*....|..
gi 15600520 419 EVRQALDPRGRFLNAHLSSILG 440
Cdd:TIGR01679 398 AVRDDLDPDRRFLNPYTRGLFG 419
|
|
| ALO |
pfam04030 |
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC: ... |
186-438 |
2.26e-104 |
|
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.
Pssm-ID: 427663 [Multi-domain] Cd Length: 258 Bit Score: 310.35 E-value: 2.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 186 VRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPktPPLDPAKEGGNEFVG--LI 263
Cdd:pfam04030 1 VTLRVVPAFTLTSTQEVISFDTLLENWDELLTSSEHFRFWWFPYTDKAVVWRANKTDEP--EQSRPRKSLYGEWLGngVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 264 EGLDKYLSDFPETRRTLLNSLRHFARF-DERVDDSYAVYANVRNVRFNEMEYSVPAEHGPACLREILALIRDKDLRTWFP 342
Cdd:pfam04030 79 EALLWLSRIFPSLTPWVERFVFKLQYGgDEAVDDSYKVFNMDCLVSQFVMEWAIPLENGPEALRELRAWIRRAALRVHFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 343 IEYRYVKADDIPLSMFEGRDSCSISVHQHYSMD----HHNFFAAVEPIFWKYAGRPHWGKLHGLNAHQLQGLYPRWKAFA 418
Cdd:pfam04030 159 IEVRCSAADDIYLSTAYGRDTCYINAHMYRPYGrnvpYHKYFRAFEDIMKKYGGRPHWAKNHTLTAEDLEEWYPDWDRFL 238
|
250 260
....*....|....*....|
gi 15600520 419 EVRQALDPRGRFLNAHLSSI 438
Cdd:pfam04030 239 QVRKKLDPEGVFLNEYLRRV 258
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
19-432 |
8.51e-62 |
|
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: 206.67 E-value: 8.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 19 WRNWSGAQSCLPLAREAPKDLDELVRII---RQASGRIRPVGSGHSFSALVPTDGTLLSLAYFSGLLSHDSVTLQAEFGG 95
Cdd:TIGR01678 4 FQNWAKTYSASPEVYYQPTSVEEVREVLalaREQKKKVKVVGGGHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQITVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 96 GTPMSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGTGVGFGSYSAQVRGLQLVTASGEVLECDAKRNVEVFDAARV 175
Cdd:TIGR01678 84 GIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGSSIKHGILATQVVALTIMTADGEVLECSEERNADVFQAARV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 176 SLGALGVVTRVRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNET-DEPKTPpldpake 254
Cdd:TIGR01678 164 SLGCLGIIVTVTIQVVPQFHLQETSFVSTLKELLDNWDSHWKSSEFFRVLWFPYTENVVIWRQNKTnKAPSSP------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 255 gGNEFVGLieGLDKYLSDFPETRRTLLNSLRHFA-RF-------------DERVDDSYAVYAnvRNVRFNEM--EYSVPA 318
Cdd:TIGR01678 237 -SNSFWDY--KLGFFLYEFLLWTSKYLPCLTPWIeRFffwmlygeksstkKESSNLSHKIFT--MECRFSQHvqEWGIPR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 319 EHGPACLREILALIRD----KDLRTWFPIEYRYVKA---DDIPLSMFEGRDSCSIS--VHQHYSMD--HHNFFAAVEPIF 387
Cdd:TIGR01678 312 EKTKEALLELKAMLEAhaknKEVYAHYPVEVRFTRGtlpDECLLSPCFQVDTCYINaiMYRPFGKDvpRLDYFLAYETIM 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15600520 388 WKYAGRPHWGKLHGLNAHQ-LQGLYPRWKAFAEVRQALDPRGRFLN 432
Cdd:TIGR01678 392 KKFGGKPHWAKAHNVCKQKdFEEMYPTLHKFCDIRKKLDPTGVFLN 437
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
21-442 |
3.38e-38 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 145.76 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 21 NWSGAQSCLPLAREAPKDLDELVRIIRQASG---RIRPVGSGHSFSALVPTDGTLLSLAYFSGLLSHD----SVTLQAef 93
Cdd:PLN02465 88 NWSGTHEVQTRRYHQPESLEELEDIVKEAHEkgrRIRPVGSGLSPNGLAFSREGMVNLALMDKVLEVDkekkRVTVQA-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 94 ggGTPMSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGTGVGFGSYSAQVRGLQLVTASGEVLECDAKRNVEVFDAA 173
Cdd:PLN02465 166 --GARVQQVVEALRPHGLTLQNYASIREQQIGGFIQVGAHGTGARIPPIDEQVVSMKLVTPAKGTIELSKEDDPELFRLA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 174 RVSLGALGVVTRVRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPKTPPLDPAK 253
Cdd:PLN02465 244 RCGLGGLGVVAEVTLQCVPAHRLVEHTFVSNRKEIKKNHKKWLSENKHIRYMWIPYTDTVVVVTCNPLSKWKEPPKIKPK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 254 EGGNEFVGLIEGLDKYLSD---------------FPETRRTLLN----SLRHFARFDE------------RVDDSYAVYA 302
Cdd:PLN02465 324 YSEDERVQPLRDLYKESAGtkssenpepdiqemgFGELRDKLLAldplDPDHVKRVNAaeaefwrrsegyRVGWSDEILG 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 303 -------NVRNVRFNEMEYSVPAEHGPACLREILALIRDKDLRTWFPIEYRYVKADDIPLSmfEGRDSCSISVHQH---- 371
Cdd:PLN02465 404 fdcggqqWVSEVCFPAGTLAKPSMKDLEFMEELLALIEKEGIPAPAPIEQRWTASSSSPMS--PASSPSPDDLHSWvgii 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 372 -Y--SMDHHN-------FFA---AVEPIFW-KYAGRPHWGKLH-GLNAHQLQGLYPRWK------AFAEVRQALDPRGRF 430
Cdd:PLN02465 482 mYlpTEDERQrkeiteeFFHyrkKTQRNLWdKYSAYEHWAKIEvPKDKEELEALRERLRkrfpvdAFNKARKELDPKGIL 561
|
490
....*....|..
gi 15600520 431 LNAHLSSILGVT 442
Cdd:PLN02465 562 SNNLLEKLFPKS 573
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
30-162 |
1.81e-29 |
|
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: 111.91 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 30 PLAREAPKDLDELVRIIRQASGR---IRPVGSGHSFS-ALVPTDGTLLSLAYFSGLLSHDSVTLQAEFGGGTPMSQMGAP 105
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENglpVLPRGGGSSLLgGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600520 106 LKEIGQAL-VNMADIDYQTLAGAIATSTHGTGVGF-GSYSAQVRGLQLVTASGEVLECD 162
Cdd:pfam01565 81 LAAKGLLLgLDPGSGIPGTVGGAIATNAGGYGSEKyGLTRDNVLGLEVVLADGEVVRLG 139
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
21-269 |
7.72e-28 |
|
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: 115.93 E-value: 7.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 21 NWSGAQSCLPLAREAPKDLDELVRIIRQAS---GRIRPVGSGHSFSALVPTDGTLLSLAYFSGLLSHD----SVTLQAef 93
Cdd:TIGR01676 53 NWSGTHEVLTRTFHQPEAIEELEGIVKQANekkARIRPVGSGLSPNGIGLSRAGMVNLALMDKVLEVDeekkRVRVQA-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 94 ggGTPMSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGTGVGFGSYSAQVRGLQLVTASGEVLECDAKRNVEVFDAA 173
Cdd:TIGR01676 131 --GIRVQQLVDAIKEYGITLQNFASIREQQIGGIIQVGAHGTGAKLPPIDEQVIAMKLVTPAKGTIEISKDKDPELFFLA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 174 RVSLGALGVVTRVRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPKTPPLDPAK 253
Cdd:TIGR01676 209 RCGLGGLGVVAEVTLQCVERQELVEHTFISNMKDIKKNHKKFLADNKHVKYLHIPYTDAIVVVTCNPISKSRGPPKFKPK 288
|
250 260
....*....|....*....|.
gi 15600520 254 EGGNEFVG-----LIEGLDKY 269
Cdd:TIGR01676 289 YTSEEAIQhvrdlYRESLKKY 309
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
22-442 |
4.16e-16 |
|
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: 80.29 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 22 WSGAQSCLPLAREAPKDLDELVRIIRQASGRIRPV----GSGHSFSALVPTDGT----LLSLAYFSGLLSHDSVTLQAEF 93
Cdd:TIGR01677 24 FPDRSTCRAANVAYPKTEAELVSVVAAATAAGRKMkvvtRYSHSIPKLACPDGSdgalLISTKRLNHVVAVDATAMTVTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 94 GGGTPMSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGT---GVGfGSYSAQVRGLQLVTASG------EVLECDAK 164
Cdd:TIGR01677 104 ESGMSLRELIVEAEKAGLALPYAPYWWGLTVGGMMGTGAHGSslwGKG-SAVHDYVVGIRLVVPASaaegfaKVRILSEG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 165 RNVEVFDAARVSLGALGVVTRVRLQNRAAYRlRERQWIARTEELLEDveKNTRENQHWEMLVVThsdYALSI--ALNETD 242
Cdd:TIGR01677 183 DTPNEFNAAKVSLGVLGVISQVTLALQPMFK-RSVTYTMRDDSDFED--QFVTFGKKHEFADIT---WYPSQgkAVYRRD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 243 EpkTPPLDPAKEGGNEFVGL----------IEGLDKYLSDFPE------TRRTLLNSLRH----FARFDERVDDSYAVY- 301
Cdd:TIGR01677 257 D--RVPVNASGNGVNDFLGFrstliaaiagIRALEETFERSRNangkcvTATITSAALFLpgygLTNSGGIIFTGYPVVg 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 302 ---------------------ANVRNVRFNEMEY------SVPAEHGPACLREILALiRDKD------LRTWFPIEYRYV 348
Cdd:TIGR01677 335 sqgrmqtsgscldspqdglltACAWDPRYKGLFFfhqttlSVPVSRFRDFVLDVKRL-RDMEpkslcgVELYNGILIRYV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 349 KADDIPLSMFEgrDSCSISVHQHYSMD------HHNFFAAVEPI-FWKYAGRPHWGKLHGLNAHQLQGLYPRWKAFAEVR 421
Cdd:TIGR01677 414 KASPAYLGKEE--DAVDFDFTYYRAKDpltprlYEDVIEEIEQMaFFKYGALPHWGKNRNLAFDGVIRKYPNADKFLKVK 491
|
490 500
....*....|....*....|.
gi 15600520 422 QALDPRGRFLNAHLSSILGVT 442
Cdd:TIGR01677 492 DSYDPKGLFSSEWSDEILGIK 512
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
22-338 |
9.16e-14 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 73.00 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 22 WSGAQSCLPLAREAPKDLDELVRIIRQASGR---IRPVGSGHSFS--ALVPTDGTLLSLAYFSGLLSHDSVTLQAEFGGG 96
Cdd:COG0277 32 GNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHgvpVVPRGGGTGLAggAVPLDGGVVLDLSRMNRILEVDPEDRTATVEAG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 97 TPMSQMGAPLKEIGQAL-VNMADIDYQTLAGAIATSTHGTG-VGFGSYSAQVRGLQLVTASGEVLECDAK--RNVEVFDA 172
Cdd:COG0277 112 VTLADLNAALAPHGLFFpPDPSSQGTATIGGNIATNAGGPRsLKYGLTRDNVLGLEVVLADGEVVRTGGRvpKNVTGYDL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 173 ARV---SLGALGVVTRVRLqnRAAYRLRERQWIARTEELLEDVEKNTRE--NQHWEMLVVTHSDyALSIALNETDEPKTP 247
Cdd:COG0277 192 FWLlvgSEGTLGVITEATL--RLHPLPEAVATALVAFPDLEAAAAAVRAllAAGIAPAALELMD-RAALALVEAAPPLGL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 248 PLDPA------KEGGNEFVG--LIEGLDKYLSDFPETRRTLLNSLRHFARFDERVDDSYAVYANVRNVRFNEMEYSVPAE 319
Cdd:COG0277 269 PEDGGalllveFDGDDAEEVeaQLARLRAILEAGGATDVRVAADGAERERLWKARKAALPALGRLDGGAKLLEDVAVPPS 348
|
330
....*....|....*....
gi 15600520 320 HGPACLREILALIRDKDLR 338
Cdd:COG0277 349 RLPELLRELGALAAKYGLR 367
|
|
| PLN00107 |
PLN00107 |
FAD-dependent oxidoreductase; Provisional |
307-441 |
1.38e-06 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 165679 Cd Length: 257 Bit Score: 49.59 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 307 VRFNEMEY----SVPAEHGPACLREILALIRDK-----DLRTWFPIEYRYVKADdiPLSMFEGRDSCSISVHQHYSMD-- 375
Cdd:PLN00107 56 IKHGEFFFqsaiSVPLSGAAAFINDIKALRDIEpdalcGLELNYGVLLRYVRAS--PAHLGKEEDALDFDLTYYRSKDdp 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600520 376 -----HHNFFAAVEPI-FWKYAGRPHWGKLHGLNAHQLQGLYPRWKAFAEVRQALDPRGRFLNAHLSSILGV 441
Cdd:PLN00107 134 aaprlHEDAMEEIEQMaILKYGALPHWGKNRNAAFDGAIAKYKKAGEFLKVKERLDPEGLFSSEWSDKILGL 205
|
|
| PLN02441 |
PLN02441 |
cytokinin dehydrogenase |
149-251 |
1.92e-03 |
|
cytokinin dehydrogenase
Pssm-ID: 215242 [Multi-domain] Cd Length: 525 Bit Score: 40.67 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 149 LQLVTASGEVLECDAKRNVEVFDAARVSLGALGVVTRVR--LQnRAAYRLRerqWIaRTeeLLEDVEKNTRENqhwEMLV 226
Cdd:PLN02441 197 LDVVTGKGEVVTCSPTQNSDLFFAVLGGLGQFGIITRARiaLE-PAPKRVR---WI-RV--LYSDFSTFTRDQ---ERLI 266
|
90 100 110
....*....|....*....|....*....|...
gi 15600520 227 VTHSDYAL-----SIALNETDEP---KTPPLDP 251
Cdd:PLN02441 267 SRPPENSFdyvegFVIVNRNGLInnwRSSFFSP 299
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
38-188 |
4.84e-03 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 39.05 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 38 DLDELVRIIRQASG-----RIRPVGSGHSFSAlvPTDGTLLSLAYFSGLLSHDS----VTLQAefggGTPMSQMGAPLKE 108
Cdd:PRK11282 3 ISAALLERVRQAAAdgtplRIRGGGSKDFYGR--ALAGEVLDTRAHRGIVSYDPtelvITARA----GTPLAELEAALAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600520 109 IGQALV-------NMAdidyqTLAGAIATSTHGTGVGF-GSYSAQVRGLQLVTASGEVLECDAK--RNVEVFDAARV--- 175
Cdd:PRK11282 77 AGQMLPfepphfgGGA-----TLGGMVAAGLSGPRRPWaGAVRDFVLGTRLINGRGEHLRFGGQvmKNVAGYDVSRLmag 151
|
170
....*....|...
gi 15600520 176 SLGALGVVTRVRL 188
Cdd:PRK11282 152 SLGTLGVLLEVSL 164
|
|
| |
