|
Name |
Accession |
Description |
Interval |
E-value |
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
9-326 |
6.31e-158 |
|
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.
Pssm-ID: 239205 [Multi-domain] Cd Length: 326 Bit Score: 445.40 E-value: 6.31e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 9 RKNEHVEIAMAQ--QDAPASDFDRVRFVHHSIPHIDVAQVNLSTHTSNFKLDYPLYINAMTGGSEWTKQINEKLATVARE 86
Cdd:cd02811 1 RKDEHLELCLEEnvESGGSTGFDDVRLVHNALPELDLDDIDLSTEFLGKRLSAPLLISAMTGGSEKAKEINRNLAEAAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 87 TGLAMAVGSTHAALRNPDMIESFRIARQVNPEGVIFSNVGA----DVPVERAVEAVELMEAQALQIHVNAPQELVMPEGN 162
Cdd:cd02811 81 LGIAMGVGSQRAALEDPELAESFTVVREAPPNGPLIANLGAvqlnGYGVEEARRAVEMIEADALAIHLNPLQEAVQPEGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 163 RTFASWMDNIAKMINHVPVPVIIKEVGFGFSKETFKALKDIGVTYVDVSGRGGTNFVSIENERRSNKDM---NYLANWGQ 239
Cdd:cd02811 161 RDFRGWLERIEELVKALSVPVIVKEVGFGISRETAKRLADAGVKAIDVAGAGGTSWARVENYRAKDSDQrlaEYFADWGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 240 STVESLLESQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVEnEGVEQTITFVAQFTTQMQQIMTMLNAP 319
Cdd:cd02811 241 PTAASLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAAL-EGEEAVIETIEQIIEELRTAMFLTGAK 319
|
....*..
gi 488390773 320 DIEALKQ 326
Cdd:cd02811 320 NLAELKQ 326
|
|
| IPP_isom_2 |
TIGR02151 |
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP ... |
8-331 |
8.03e-149 |
|
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP isomerase) interconverts isopentenyl diphosphate and dimethylallyl diphosphate. This model represents the type 2 enzyme. FMN, NADPH, and Mg2+ are required by this form, which lacks homology to the type 1 enzyme (TIGR02150). IPP is precursor to many compounds, including enzyme cofactors, sterols, and isoprenoids. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273999 Cd Length: 333 Bit Score: 422.45 E-value: 8.03e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 8 QRKNEHVEIAMAQQDA--PASDFDRVRFVHHSIPHIDVAQVNLSTHTSNFKLDYPLYINAMTGGSEWTKQINEKLATVAR 85
Cdd:TIGR02151 1 ERKDEHIELCLKQNVEygGSTGFDDITLIHNALPEINLDDIDLTTEFLGKRLKAPFYINAMTGGSEEAGKINRNLARAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 86 ETGLAMAVGSTHAALRNPDMIESFRIARQVNPEGVIFSNVGADVPVER----AVEAVELMEAQALQIHVNAPQELVMPEG 161
Cdd:TIGR02151 81 ELGIPMGVGSQRAALKDPETADTFEVVREEAPNGPLIANIGAPQLVEGgpeeAQEAIDMIEADALAIHLNVLQELVQPEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 162 NRTFASWMDNIAKMINHVPVPVIIKEVGFGFSKETFKALKDIGVTYVDVSGRGGTNFVSIENERRsNKDMN--YLANWGQ 239
Cdd:TIGR02151 161 DRNFKGWLEKIAEICSQLSVPVIVKEVGFGISKEVAKLLADAGVSAIDVAGAGGTSWAQVENYRA-KGSNLasFFNDWGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 240 STVESLLESQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVENEGVEQTITFVAQFTTQMQQIMTMLNAP 319
Cdd:TIGR02151 240 PTAASLLEVRSDAPDAPIIASGGLRTGLDVAKAIALGADAVGMARPFLKAALDEGEEAVIEEIELIIEELKVAMFLTGAK 319
|
330
....*....|..
gi 488390773 320 DIEALKQSQLIF 331
Cdd:TIGR02151 320 TIAELKKVPLVI 331
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
26-331 |
2.20e-46 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 161.07 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 26 SDFDRVRFVHHSIphIDVAQVNLSTHTSNFKLDYPLYINAMTGGSEWTKQINEKLATVARETGLAMAVGSthaaLRnpdm 105
Cdd:COG1304 41 AAFDRVRLRPRVL--EDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAAAGIPMGLST----QS---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 106 IESFRIARQVNPEGVIFS-NVGADVP-VERAVEAVELMEAQALQIHVNAP---------QE-LVMP-------------- 159
Cdd:COG1304 111 TTSLEEVAAAAPAPLWFQlYVPKDRGfTDDLLRRAEAAGADALVLTVDTPvlgrrerdlREgFSQPprltprnlleaath 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 160 ----EGNRTFASWMDN----------IAKMINHVPVPVIIKEVgfgFSKETFKALKDIGVTYVDVSGRGGTNFvsienER 225
Cdd:COG1304 191 prwaLGLASLAAWLDTnfdpsltwddIAWLRERWPGPLIVKGV---LSPEDARRAVDAGVDGIDVSNHGGRQL-----DG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 226 rsnkdmnylanwGQSTVESLLE-SQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVEN---EGVEQTItf 301
Cdd:COG1304 263 ------------GPPTIDALPEiRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAggeAGVARVL-- 328
|
330 340 350
....*....|....*....|....*....|
gi 488390773 302 vAQFTTQMQQIMTMLNAPDIEALKQSQLIF 331
Cdd:COG1304 329 -ELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
26-329 |
8.26e-15 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 74.49 E-value: 8.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 26 SDFDRVRFVHHSIPhiDVAQVNLSTHTSNFKLDYPLYINAMTGGSEWTKQINEKLATVARETGLAMAVgSTHA------- 98
Cdd:pfam01070 28 AAFDRIRLRPRVLR--DVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVL-STVSstsleev 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 99 -------------ALRNPDMIESF-RIARQVNPEGVIfsnVGADVPV----ERAVEAVELMEAQALQihVNAPQELVMPE 160
Cdd:pfam01070 105 aaaaggplwfqlyVPRDRELTEDLlERAEAAGYKALV---LTVDTPVlgrrERDLRNGFTLPPRLTP--RNLLDLALHPR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 161 GNRTFA--------------------SWmDNIAKMINHVPVPVIIKEVgfgFSKETFKALKDIGVTYVDVSGRGGTNFVS 220
Cdd:pfam01070 180 WALGVLrrggaggaaafvgsqfdpalTW-DDLAWLRERWKGPLVVKGI---LSPEDAKRAVEAGVDGIVVSNHGGRQLDG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 221 ienerrsnkdmnylanwGQSTVESLLE-SQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHV----EnEGV 295
Cdd:pfam01070 256 -----------------APATIDALPEiVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLaaggE-AGV 317
|
330 340 350
....*....|....*....|....*....|....
gi 488390773 296 EQTItfvAQFTTQMQQIMTMLNAPDIEALKQSQL 329
Cdd:pfam01070 318 AHAL---EILRDELERTMALLGCKSIADLTPSLL 348
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
249-330 |
6.19e-06 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 47.71 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 249 QAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPF---LNHVENEGVEQTITFVAQfttQMQQIMTMLNAPDIEALK 325
Cdd:PRK11197 295 DAVKGDITILADSGIRNGLDVVRMIALGADTVLLGRAFvyaLAAAGQAGVANLLDLIEK---EMRVAMTLTGAKSISEIT 371
|
....*
gi 488390773 326 QSQLI 330
Cdd:PRK11197 372 RDSLV 376
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
9-326 |
6.31e-158 |
|
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.
Pssm-ID: 239205 [Multi-domain] Cd Length: 326 Bit Score: 445.40 E-value: 6.31e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 9 RKNEHVEIAMAQ--QDAPASDFDRVRFVHHSIPHIDVAQVNLSTHTSNFKLDYPLYINAMTGGSEWTKQINEKLATVARE 86
Cdd:cd02811 1 RKDEHLELCLEEnvESGGSTGFDDVRLVHNALPELDLDDIDLSTEFLGKRLSAPLLISAMTGGSEKAKEINRNLAEAAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 87 TGLAMAVGSTHAALRNPDMIESFRIARQVNPEGVIFSNVGA----DVPVERAVEAVELMEAQALQIHVNAPQELVMPEGN 162
Cdd:cd02811 81 LGIAMGVGSQRAALEDPELAESFTVVREAPPNGPLIANLGAvqlnGYGVEEARRAVEMIEADALAIHLNPLQEAVQPEGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 163 RTFASWMDNIAKMINHVPVPVIIKEVGFGFSKETFKALKDIGVTYVDVSGRGGTNFVSIENERRSNKDM---NYLANWGQ 239
Cdd:cd02811 161 RDFRGWLERIEELVKALSVPVIVKEVGFGISRETAKRLADAGVKAIDVAGAGGTSWARVENYRAKDSDQrlaEYFADWGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 240 STVESLLESQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVEnEGVEQTITFVAQFTTQMQQIMTMLNAP 319
Cdd:cd02811 241 PTAASLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAAL-EGEEAVIETIEQIIEELRTAMFLTGAK 319
|
....*..
gi 488390773 320 DIEALKQ 326
Cdd:cd02811 320 NLAELKQ 326
|
|
| IPP_isom_2 |
TIGR02151 |
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP ... |
8-331 |
8.03e-149 |
|
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP isomerase) interconverts isopentenyl diphosphate and dimethylallyl diphosphate. This model represents the type 2 enzyme. FMN, NADPH, and Mg2+ are required by this form, which lacks homology to the type 1 enzyme (TIGR02150). IPP is precursor to many compounds, including enzyme cofactors, sterols, and isoprenoids. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273999 Cd Length: 333 Bit Score: 422.45 E-value: 8.03e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 8 QRKNEHVEIAMAQQDA--PASDFDRVRFVHHSIPHIDVAQVNLSTHTSNFKLDYPLYINAMTGGSEWTKQINEKLATVAR 85
Cdd:TIGR02151 1 ERKDEHIELCLKQNVEygGSTGFDDITLIHNALPEINLDDIDLTTEFLGKRLKAPFYINAMTGGSEEAGKINRNLARAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 86 ETGLAMAVGSTHAALRNPDMIESFRIARQVNPEGVIFSNVGADVPVER----AVEAVELMEAQALQIHVNAPQELVMPEG 161
Cdd:TIGR02151 81 ELGIPMGVGSQRAALKDPETADTFEVVREEAPNGPLIANIGAPQLVEGgpeeAQEAIDMIEADALAIHLNVLQELVQPEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 162 NRTFASWMDNIAKMINHVPVPVIIKEVGFGFSKETFKALKDIGVTYVDVSGRGGTNFVSIENERRsNKDMN--YLANWGQ 239
Cdd:TIGR02151 161 DRNFKGWLEKIAEICSQLSVPVIVKEVGFGISKEVAKLLADAGVSAIDVAGAGGTSWAQVENYRA-KGSNLasFFNDWGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 240 STVESLLESQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVENEGVEQTITFVAQFTTQMQQIMTMLNAP 319
Cdd:TIGR02151 240 PTAASLLEVRSDAPDAPIIASGGLRTGLDVAKAIALGADAVGMARPFLKAALDEGEEAVIEEIELIIEELKVAMFLTGAK 319
|
330
....*....|..
gi 488390773 320 DIEALKQSQLIF 331
Cdd:TIGR02151 320 TIAELKKVPLVI 331
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
26-331 |
2.20e-46 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 161.07 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 26 SDFDRVRFVHHSIphIDVAQVNLSTHTSNFKLDYPLYINAMTGGSEWTKQINEKLATVARETGLAMAVGSthaaLRnpdm 105
Cdd:COG1304 41 AAFDRVRLRPRVL--EDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAAAGIPMGLST----QS---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 106 IESFRIARQVNPEGVIFS-NVGADVP-VERAVEAVELMEAQALQIHVNAP---------QE-LVMP-------------- 159
Cdd:COG1304 111 TTSLEEVAAAAPAPLWFQlYVPKDRGfTDDLLRRAEAAGADALVLTVDTPvlgrrerdlREgFSQPprltprnlleaath 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 160 ----EGNRTFASWMDN----------IAKMINHVPVPVIIKEVgfgFSKETFKALKDIGVTYVDVSGRGGTNFvsienER 225
Cdd:COG1304 191 prwaLGLASLAAWLDTnfdpsltwddIAWLRERWPGPLIVKGV---LSPEDARRAVDAGVDGIDVSNHGGRQL-----DG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 226 rsnkdmnylanwGQSTVESLLE-SQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVEN---EGVEQTItf 301
Cdd:COG1304 263 ------------GPPTIDALPEiRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAggeAGVARVL-- 328
|
330 340 350
....*....|....*....|....*....|
gi 488390773 302 vAQFTTQMQQIMTMLNAPDIEALKQSQLIF 331
Cdd:COG1304 329 -ELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
26-327 |
3.77e-17 |
|
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.
Pssm-ID: 239238 [Multi-domain] Cd Length: 344 Bit Score: 81.10 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 26 SDFDRVRFVhhsiPHI--DVAQVNLSTHTSNFKLDYPLYINAMTGGsewtkqineKLATVARETGLAMAVG--------S 95
Cdd:cd02922 34 EAFQRIRFR----PRVlrDVEKVDTSTTILGHKVSLPFFISPAALA---------KLAHPDGELNLARAAGkhgilqmiS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 96 THAALRNPDMIESF--------------------RIARQVNPEGV--IFSNVgaDVPV-------ERAVEAVELMEAQAL 146
Cdd:cd02922 101 TNASCSLEEIVDARppdqplffqlyvnkdrtkteELLKRAEKLGAkaIFLTV--DAPVlgkrerdERLKAEEAVSDGPAG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 147 QIHVNAPQEL--VMPEGNRTFASWmDNIAKMINHVPVPVIIKEVGfgfSKETFKALKDIGVTYVDVSGRGGTNFvsiene 224
Cdd:cd02922 179 KKTKAKGGGAgrAMSGFIDPTLTW-DDIKWLRKHTKLPIVLKGVQ---TVEDAVLAAEYGVDGIVLSNHGGRQL------ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 225 rrsnkdmnylaNWGQSTVESLLESQAYQSSLN----IFASGGIRTPLDAIKSLALGAKAVGMSRPFL---NHVENEGVEQ 297
Cdd:cd02922 249 -----------DTAPAPIEVLLEIRKHCPEVFdkieVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLyalSAYGEEGVEK 317
|
330 340 350
....*....|....*....|....*....|
gi 488390773 298 TITFVAQfttQMQQIMTMLNAPDIEALKQS 327
Cdd:cd02922 318 AIQILKD---EIETTMRLLGVTSLDQLGPS 344
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
26-329 |
8.26e-15 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 74.49 E-value: 8.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 26 SDFDRVRFVHHSIPhiDVAQVNLSTHTSNFKLDYPLYINAMTGGSEWTKQINEKLATVARETGLAMAVgSTHA------- 98
Cdd:pfam01070 28 AAFDRIRLRPRVLR--DVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVL-STVSstsleev 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 99 -------------ALRNPDMIESF-RIARQVNPEGVIfsnVGADVPV----ERAVEAVELMEAQALQihVNAPQELVMPE 160
Cdd:pfam01070 105 aaaaggplwfqlyVPRDRELTEDLlERAEAAGYKALV---LTVDTPVlgrrERDLRNGFTLPPRLTP--RNLLDLALHPR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 161 GNRTFA--------------------SWmDNIAKMINHVPVPVIIKEVgfgFSKETFKALKDIGVTYVDVSGRGGTNFVS 220
Cdd:pfam01070 180 WALGVLrrggaggaaafvgsqfdpalTW-DDLAWLRERWKGPLVVKGI---LSPEDAKRAVEAGVDGIVVSNHGGRQLDG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 221 ienerrsnkdmnylanwGQSTVESLLE-SQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHV----EnEGV 295
Cdd:pfam01070 256 -----------------APATIDALPEiVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLaaggE-AGV 317
|
330 340 350
....*....|....*....|....*....|....
gi 488390773 296 EQTItfvAQFTTQMQQIMTMLNAPDIEALKQSQL 329
Cdd:pfam01070 318 AHAL---EILRDELERTMALLGCKSIADLTPSLL 348
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
26-326 |
5.65e-14 |
|
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.
Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 71.32 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 26 SDFDRVRFVhhsiPHI--DVAQVNLSTHTSNFKLDYPLYInAMTGGS-------EwtkqinEKLATVARETGLAMAVGST 96
Cdd:cd02809 34 AAFDRIRLR----PRVlrDVSKRDTSTTLLGQKLAMPFGI-APTGLQglahpdgE------LATARAAAAAGIPFTLSTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 97 --------HAALRNPDMiesFRIARQVNPEGVifsnvgADVpVERAVEAvelmEAQALQIHVNAPqelVMpeGNRTfasW 168
Cdd:cd02809 103 sttsleevAAAAPGPRW---FQLYVPRDREIT------EDL-LRRAEAA----GYKALVLTVDTP---VL--GRRL---T 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 169 MDNIAKMINHVPVPVIIKEVgfgFSKETFKALKDIGVTYVDVSGRGGTNFVSienerrsnkdmnylanwGQSTVESLLE- 247
Cdd:cd02809 161 WDDLAWLRSQWKGPLILKGI---LTPEDALRAVDAGADGIVVSNHGGRQLDG-----------------APATIDALPEi 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 248 SQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHV----EnEGVEQTITfvaQFTTQMQQIMTMLNAPDIEA 323
Cdd:cd02809 221 VAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLaaggE-AGVAHVLE---ILRDELERAMALLGCASLAD 296
|
...
gi 488390773 324 LKQ 326
Cdd:cd02809 297 LDP 299
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
61-284 |
8.11e-10 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 57.98 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 61 LYINAMTGG-SEWTKQINEKLAtvaRETGLAMAVGSTHAALRNPDMIESFRIARQVN----PEGVIFSNVGADVPVERAV 135
Cdd:cd04722 1 VILALLAGGpSGDPVELAKAAA---EAGADAIIVGTRSSDPEEAETDDKEVLKEVAAetdlPLGVQLAINDAAAAVDIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 136 EAVELMEAQALQIHVNAPQElvmPEGNRTFASWmdnIAKMINHVPVpvIIKEVGFGFSKEtfKALKDIGVTYVDVSGRGG 215
Cdd:cd04722 78 AAARAAGADGVEIHGAVGYL---AREDLELIRE---LREAVPDVKV--VVKLSPTGELAA--AAAEEAGVDEVGLGNGGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 216 TNFVSIENErrsnkdmnylanwgqstVESLLESQAY-QSSLNIFASGGIRTPLDAIKSLALGAKAVGMSR 284
Cdd:cd04722 148 GGGGRDAVP-----------------IADLLLILAKrGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
257-309 |
7.83e-07 |
|
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.
Pssm-ID: 239448 [Multi-domain] Cd Length: 383 Bit Score: 50.36 E-value: 7.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488390773 257 IFASGgIRTPLDAIKSLALGAKAVGMSRPF---LNHVENEGVEQTI-TFVAQFTTQM 309
Cdd:cd03332 312 LFDSG-VRTGADIMKALALGAKAVLIGRPYaygLALGGEDGVEHVLrNLLAELDLTM 367
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
249-330 |
6.19e-06 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 47.71 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 249 QAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPF---LNHVENEGVEQTITFVAQfttQMQQIMTMLNAPDIEALK 325
Cdd:PRK11197 295 DAVKGDITILADSGIRNGLDVVRMIALGADTVLLGRAFvyaLAAAGQAGVANLLDLIEK---EMRVAMTLTGAKSISEIT 371
|
....*
gi 488390773 326 QSQLI 330
Cdd:PRK11197 372 RDSLV 376
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
131-287 |
6.97e-06 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240086 [Multi-domain] Cd Length: 353 Bit Score: 47.21 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 131 VERAVEA----VELMEAQALQIhvnapQELVMPEGNRTFASW--------------MDNIAKMIN-HVPVPVIIkevGFG 191
Cdd:cd04735 150 TRRAIEAgfdgVEIHGANGYLI-----QQFFSPHSNRRTDEWggslenrmrfplavVKAVQEVIDkHADKDFIL---GYR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 192 FSKE-------TFK-------ALKDIGVTYVDVSGRGGTNFvsieneRRSNKDMNylanwgQSTVESLLEsqAYQSSLNI 257
Cdd:cd04735 222 FSPEepeepgiRMEdtlalvdKLADKGLDYLHISLWDFDRK------SRRGRDDN------QTIMELVKE--RIAGRLPL 287
|
170 180 190
....*....|....*....|....*....|
gi 488390773 258 FASGGIRTPLDAIKSLALGAKAVGMSRPFL 287
Cdd:cd04735 288 IAVGSINTPDDALEALETGADLVAIGRGLL 317
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
181-287 |
1.16e-05 |
|
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.
Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 46.77 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 181 VPVIIKeVGFGFSKETFK-ALKDIGVTYVDVSGR-GGTN---FVSIENerrsnkdmnylanWGQSTVESLLEsqAYQ--- 252
Cdd:cd02808 215 KPIGVK-LVAGHGEGDIAaGVAAAGADFITIDGAeGGTGaapLTFIDH-------------VGLPTELGLAR--AHQalv 278
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 488390773 253 -----SSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFL 287
Cdd:cd02808 279 knglrDRVSLIASGGLRTGADVAKALALGADAVGIGTAAL 318
|
|
| deoC |
TIGR00126 |
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ... |
126-284 |
4.67e-05 |
|
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism of nucleotides and deoxyriibonucleotides. The catalytic process is as follows: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. It is found in both gram-postive and gram-negative bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
Pssm-ID: 272921 Cd Length: 211 Bit Score: 43.99 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 126 GADVPVERAVEAVELMEAQALQIHVNAPQELVMPEGNRTFASWMDNIAKMINHVPVPVIIkEVGFGFSKETFKAL---KD 202
Cdd:TIGR00126 65 GASTTDVKLYETKEAIKYGADEVDMVINIGALKDGNEEVVYDDIRAVVEACAGVLLKVII-ETGLLTDEEIRKACeicID 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 203 IGVTYVDVSgrggTNFVSienerrsnkdmnylanwGQSTVESL-LESQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVG 281
Cdd:TIGR00126 144 AGADFVKTS----TGFGA-----------------GGATVEDVrLMRNTVGDTIGVKASGGVRTAEDAIAMIEAGASRIG 202
|
...
gi 488390773 282 MSR 284
Cdd:TIGR00126 203 ASA 205
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
257-287 |
1.31e-03 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 40.39 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|.
gi 488390773 257 IFASGGIRTPLDAIKSLALGAKAVGMSRPFL 287
Cdd:pfam01645 276 LIADGGLRTGADVAKAAALGADAVYIGTAAL 306
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
193-289 |
1.33e-03 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 40.25 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 193 SKETFKALKDIGVTYVDVSgrGGTNFVSIENERRSNKDMNYLANWgqstveslleSQAYQSSLNI--FASGGIRTPLDAI 270
Cdd:cd02803 230 AIEIAKALEEAGVDALHVS--GGSYESPPPIIPPPYVPEGYFLEL----------AEKIKKAVKIpvIAVGGIRDPEVAE 297
|
90 100
....*....|....*....|
gi 488390773 271 KSLALG-AKAVGMSRPFLNH 289
Cdd:cd02803 298 EILAEGkADLVALGRALLAD 317
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
257-287 |
3.46e-03 |
|
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439839 Cd Length: 728 Bit Score: 39.46 E-value: 3.46e-03
10 20 30
....*....|....*....|....*....|.
gi 488390773 257 IFASGGIRTPLDAIKSLALGAKAVGMSRPFL 287
Cdd:COG0069 443 LIADGKLKTGRDVAIAAALGADEFGFARAFM 473
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
102-283 |
4.10e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 38.08 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 102 NPDMIEsfRIARQVNPEGVIFSNVG----ADVPVERAVEAVEL---MEAQALQIHVNAPQELvmpEGNRTFAswMDNIAK 174
Cdd:cd00945 33 NPGYVR--LAADALAGSDVPVIVVVgfptGLTTTEVKVAEVEEaidLGADEIDVVINIGSLK---EGDWEEV--LEEIAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 175 MINHVPVPVIIK---EVGFGFSKETF----KALKDIGVTYVDVSgrggTNFVSienerrsnkdmnylanwGQSTVESLLE 247
Cdd:cd00945 106 VVEAADGGLPLKvilETRGLKTADEIakaaRIAAEAGADFIKTS----TGFGG-----------------GGATVEDVKL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 488390773 248 -SQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMS 283
Cdd:cd00945 165 mKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
239-324 |
4.39e-03 |
|
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240087 Cd Length: 361 Bit Score: 38.66 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 239 QSTVESLLESQAyQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVENEGVEQTITFVAQFTTQMQQIMTMLNA 318
Cdd:cd04736 275 IAPIEALAEIVA-ATYKPVLIDSGIRRGSDIVKALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGC 353
|
....*.
gi 488390773 319 PDIEAL 324
Cdd:cd04736 354 PDIASL 359
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
238-329 |
5.46e-03 |
|
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240088 [Multi-domain] Cd Length: 351 Bit Score: 38.19 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 238 GQSTVESLLE-SQAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVENEGVEQTITFVAQFTTQMQQIMTML 316
Cdd:cd04737 259 GPASFDSLPEiAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLA 338
|
90
....*....|...
gi 488390773 317 NAPDIEALKQSQL 329
Cdd:cd04737 339 GTRTIEDVKRTFL 351
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
240-344 |
5.51e-03 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 38.17 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390773 240 STVESLLES-QAYQSSLNIFASGGIRTPLDAIKSLALGAKAVGMSRPFLNHVENEGVEQTITFVAQFTTQMQQIMTMLNA 318
Cdd:PLN02493 264 ATISALEEVvKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGC 343
|
90 100
....*....|....*....|....*.
gi 488390773 319 PDIEALKQSQLIFDqqllsWMEQRHI 344
Cdd:PLN02493 344 RSLKEISRNHITTE-----WDTPRPS 364
|
|
| |
