|
Name |
Accession |
Description |
Interval |
E-value |
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
117-460 |
0e+00 |
|
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: 524.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 117 SDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGgrIKSSLPIYITPTGLSRYA 196
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILG--HKVSLPFFISPAALAKLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 197 HQDGDQCLARACGHEGIVYCMPTTA--AHEAVFGARTtPNQPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSPVI 274
Cdd:cd02922 79 HPDGELNLARAAGKHGILQMISTNAscSLEEIVDARP-PDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 275 GRRERDDRIKAADGEDPLFAAGVAKSGS-------MTLLNPTLTWDDLDWLRAATSLPLVLKGVQTVEDAVLAHRAGVDG 347
Cdd:cd02922 158 GKRERDERLKAEEAVSDGPAGKKTKAKGggagramSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 348 IVLSNHGGRSQDTAQAPMLTLLEIRRHAPHLLapetrSRFEVFLDGGVRRGTDVLKALALGASAVGVGRPALYSMTnGWG 427
Cdd:cd02922 238 IVLSNHGGRQLDTAPAPIEVLLEIRKHCPEVF-----DKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALS-AYG 311
|
330 340 350
....*....|....*....|....*....|...
gi 2286884698 428 EAGVRRLIMMLRMEIETNMALAGATRLGEVVPE 460
Cdd:cd02922 312 EEGVEKAIQILKDEIETTMRLLGVTSLDQLGPS 344
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
123-464 |
2.64e-128 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 376.10 E-value: 2.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 123 AKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLSRYAHQDGDQ 202
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRL--SLPFGIAPVGMQGLAHPDGEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 203 CLARACGHEGIVYCMPT--TAAHEAVFGARttpNQPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSPVIGRRERD 280
Cdd:pfam01070 79 ALARAAAAAGIPFVLSTvsSTSLEEVAAAA---GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 281 DR--------IKAADGEDPLF----AAGVAKSGSM--------TLLNPTLTWDDLDWLRAATSLPLVLKGVQTVEDAVLA 340
Cdd:pfam01070 156 LRngftlpprLTPRNLLDLALhprwALGVLRRGGAggaaafvgSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 341 HRAGVDGIVLSNHGGRSQDTAQAPMLTLLEIRRHAPHllapetrsRFEVFLDGGVRRGTDVLKALALGASAVGVGRPALY 420
Cdd:pfam01070 236 VEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGG--------RIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLY 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2286884698 421 SMTNGwGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPEMVNT 464
Cdd:pfam01070 308 GLAAG-GEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
110-462 |
3.16e-119 |
|
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: 353.28 E-value: 3.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 110 LTSMLNVSDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITP 189
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRL--AAPFLIAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 190 TGLSRYAHQDGDQCLARACGHEGIVYCMPTTAAH--EAVfgARTTPNQPLcFQLYTGRDYDRTRALLRKVERLGAAAIFV 267
Cdd:COG1304 79 MGGGGLAHPDGELALARAAAAAGIPMGLSTQSTTslEEV--AAAAPAPLW-FQLYVPKDRGFTDDLLRRAEAAGADALVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 268 TVDSPVIGRRERDDR-----------IKAADGE-DPLFAAGVAKSGSM--TLLNPTLTWDDLDWLRAATSLPLVLKGVQT 333
Cdd:COG1304 156 TVDTPVLGRRERDLRegfsqpprltpRNLLEAAtHPRWALGLASLAAWldTNFDPSLTWDDIAWLRERWPGPLIVKGVLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 334 VEDAVLAHRAGVDGIVLSNHGGRSQDTAQAPMLTLLEIRRhaphllapETRSRFEVFLDGGVRRGTDVLKALALGASAVG 413
Cdd:COG1304 236 PEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRA--------AVGGRIPVIADGGIRRGLDVAKALALGADAVG 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2286884698 414 VGRPALYSMTNGwGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPEMV 462
Cdd:COG1304 308 LGRPFLYGLAAG-GEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
114-466 |
1.08e-74 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 239.35 E-value: 1.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 114 LNVSDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLS 193
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTI--SAPIMIAPTAMH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 194 RYAHQDGDQCLARA---CGHEGIVYCMPTTAAHEAVfgarTTPNQPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVD 270
Cdd:PLN02535 84 KLAHPEGEIATARAaaaCNTIMVLSFMASCTVEEVA----SSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 271 SPVIGRRERD-------DRIKAADGEDPLFAAGVAKSG----SMTLLNPTLTWDDLDWLRAATSLPLVLKGVQTVEDAVL 339
Cdd:PLN02535 160 VPRLGRREADiknkmisPQLKNFEGLLSTEVVSDKGSGleafASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 340 AHRAGVDGIVLSNHGGRSQDTAQApMLTLLEIRRHAphllapeTRSRFEVFLDGGVRRGTDVLKALALGASAVGVGRPAL 419
Cdd:PLN02535 240 AVEVGVAGIIVSNHGARQLDYSPA-TISVLEEVVQA-------VGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVI 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2286884698 420 YSMTnGWGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPEMVNTER 466
Cdd:PLN02535 312 YGLA-AKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVRTER 357
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
6-78 |
2.61e-22 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 90.37 E-value: 2.61e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2286884698 6 DAAELSRHNSKSSCWIVIHGQVWDVTEFLELHPGGDRIILKSAGRDATPSYESVHDPDLVANTLAPSCLVGTI 78
Cdd:pfam00173 1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGEL 73
|
|
| CYB5 |
COG5274 |
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ... |
8-77 |
1.92e-19 |
|
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];
Pssm-ID: 444085 [Multi-domain] Cd Length: 93 Bit Score: 82.78 E-value: 1.92e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 8 AELSRHNSKSSCWIVIHGQVWDVTEFLELHPGGDRIILKSAGRDATPSYESVHDPDLVANTLAPSCLVGT 77
Cdd:COG5274 21 AEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPHSPKAERLLESYRIGR 90
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
4-109 |
1.44e-15 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 79.72 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 4 YIDAAELSRHNSKSSCWIVIHGQVWDVTEFLELHPGGDRIILKSAGRDATPSYESVHDPDlvANTLAPSCLVGTINPQST 83
Cdd:PLN02252 519 QYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDK--AKKMLEDYRIGELVTTGA 596
|
90 100
....*....|....*....|....*.
gi 2286884698 84 TLVPTAEEVPSPATDDSRSAQPIHPP 109
Cdd:PLN02252 597 AASSSASSHPLSAISTASALAAASPA 622
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
117-460 |
0e+00 |
|
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: 524.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 117 SDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGgrIKSSLPIYITPTGLSRYA 196
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILG--HKVSLPFFISPAALAKLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 197 HQDGDQCLARACGHEGIVYCMPTTA--AHEAVFGARTtPNQPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSPVI 274
Cdd:cd02922 79 HPDGELNLARAAGKHGILQMISTNAscSLEEIVDARP-PDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 275 GRRERDDRIKAADGEDPLFAAGVAKSGS-------MTLLNPTLTWDDLDWLRAATSLPLVLKGVQTVEDAVLAHRAGVDG 347
Cdd:cd02922 158 GKRERDERLKAEEAVSDGPAGKKTKAKGggagramSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 348 IVLSNHGGRSQDTAQAPMLTLLEIRRHAPHLLapetrSRFEVFLDGGVRRGTDVLKALALGASAVGVGRPALYSMTnGWG 427
Cdd:cd02922 238 IVLSNHGGRQLDTAPAPIEVLLEIRKHCPEVF-----DKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALS-AYG 311
|
330 340 350
....*....|....*....|....*....|...
gi 2286884698 428 EAGVRRLIMMLRMEIETNMALAGATRLGEVVPE 460
Cdd:cd02922 312 EEGVEKAIQILKDEIETTMRLLGVTSLDQLGPS 344
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
123-464 |
2.64e-128 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 376.10 E-value: 2.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 123 AKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLSRYAHQDGDQ 202
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRL--SLPFGIAPVGMQGLAHPDGEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 203 CLARACGHEGIVYCMPT--TAAHEAVFGARttpNQPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSPVIGRRERD 280
Cdd:pfam01070 79 ALARAAAAAGIPFVLSTvsSTSLEEVAAAA---GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 281 DR--------IKAADGEDPLF----AAGVAKSGSM--------TLLNPTLTWDDLDWLRAATSLPLVLKGVQTVEDAVLA 340
Cdd:pfam01070 156 LRngftlpprLTPRNLLDLALhprwALGVLRRGGAggaaafvgSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 341 HRAGVDGIVLSNHGGRSQDTAQAPMLTLLEIRRHAPHllapetrsRFEVFLDGGVRRGTDVLKALALGASAVGVGRPALY 420
Cdd:pfam01070 236 VEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGG--------RIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLY 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2286884698 421 SMTNGwGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPEMVNT 464
Cdd:pfam01070 308 GLAAG-GEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
110-462 |
3.16e-119 |
|
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: 353.28 E-value: 3.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 110 LTSMLNVSDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITP 189
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRL--AAPFLIAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 190 TGLSRYAHQDGDQCLARACGHEGIVYCMPTTAAH--EAVfgARTTPNQPLcFQLYTGRDYDRTRALLRKVERLGAAAIFV 267
Cdd:COG1304 79 MGGGGLAHPDGELALARAAAAAGIPMGLSTQSTTslEEV--AAAAPAPLW-FQLYVPKDRGFTDDLLRRAEAAGADALVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 268 TVDSPVIGRRERDDR-----------IKAADGE-DPLFAAGVAKSGSM--TLLNPTLTWDDLDWLRAATSLPLVLKGVQT 333
Cdd:COG1304 156 TVDTPVLGRRERDLRegfsqpprltpRNLLEAAtHPRWALGLASLAAWldTNFDPSLTWDDIAWLRERWPGPLIVKGVLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 334 VEDAVLAHRAGVDGIVLSNHGGRSQDTAQAPMLTLLEIRRhaphllapETRSRFEVFLDGGVRRGTDVLKALALGASAVG 413
Cdd:COG1304 236 PEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRA--------AVGGRIPVIADGGIRRGLDVAKALALGADAVG 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2286884698 414 VGRPALYSMTNGwGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPEMV 462
Cdd:COG1304 308 LGRPFLYGLAAG-GEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
117-457 |
3.13e-113 |
|
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: 335.57 E-value: 3.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 117 SDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLSRYA 196
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKL--AMPFGIAPTGLQGLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 197 HQDGDQCLARACGHEGIVYCMPTTAAH--EAVfgARTTPNqPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSPVI 274
Cdd:cd02809 79 HPDGELATARAAAAAGIPFTLSTVSTTslEEV--AAAAPG-PRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 275 GRRerddrikaadgedplfaagvaksgsmtllnptLTWDDLDWLRAATSLPLVLKGVQTVEDAVLAHRAGVDGIVLSNHG 354
Cdd:cd02809 156 GRR--------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 355 GRSQDTAQAPMLTLLEIRRHAphllapetRSRFEVFLDGGVRRGTDVLKALALGASAVGVGRPALYSMTNGwGEAGVRRL 434
Cdd:cd02809 204 GRQLDGAPATIDALPEIVAAV--------GGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAG-GEAGVAHV 274
|
330 340
....*....|....*....|...
gi 2286884698 435 IMMLRMEIETNMALAGATRLGEV 457
Cdd:cd02809 275 LEILRDELERAMALLGCASLADL 297
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
108-460 |
3.25e-81 |
|
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: 256.44 E-value: 3.25e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 108 PPLTSMlNVSDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIKSslPIYI 187
Cdd:cd03332 14 RPDLPV-DPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAA--PLLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 188 TPTGLSRYAHQDGDQCLARACGHEGIVYCMPTTAAH--EAVfgARTTPNQPLCFQLYTGRDYDRTRALLRKVERLGAAAI 265
Cdd:cd03332 91 APIGVQELFHPDAELATARAAAELGVPYILSTASSSsiEDV--AAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 266 FVTVDSPVIGRRERD---------------------------DRIKAADGEDPLFAAGVAKSGSMTLLNPTLTWDDLDWL 318
Cdd:cd03332 169 VVTLDTWSLGWRPRDldlgylpflrgigianyfsdpvfrkklAEPVGEDPEAPPPMEAAVARFVSVFSGPSLTWEDLAFL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 319 RAATSLPLVLKGVQTVEDAVLAHRAGVDGIVLSNHGGRSQDTAQAPMLTLLEIrrhaphllAPETRSRFEVFLDGGVRRG 398
Cdd:cd03332 249 REWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEI--------VEAVGDRLTVLFDSGVRTG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2286884698 399 TDVLKALALGASAVGVGRPALYSMTNGwGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPE 460
Cdd:cd03332 321 ADIMKALALGAKAVLIGRPYAYGLALG-GEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRD 381
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
114-466 |
1.08e-74 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 239.35 E-value: 1.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 114 LNVSDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLS 193
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTI--SAPIMIAPTAMH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 194 RYAHQDGDQCLARA---CGHEGIVYCMPTTAAHEAVfgarTTPNQPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVD 270
Cdd:PLN02535 84 KLAHPEGEIATARAaaaCNTIMVLSFMASCTVEEVA----SSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 271 SPVIGRRERD-------DRIKAADGEDPLFAAGVAKSG----SMTLLNPTLTWDDLDWLRAATSLPLVLKGVQTVEDAVL 339
Cdd:PLN02535 160 VPRLGRREADiknkmisPQLKNFEGLLSTEVVSDKGSGleafASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 340 AHRAGVDGIVLSNHGGRSQDTAQApMLTLLEIRRHAphllapeTRSRFEVFLDGGVRRGTDVLKALALGASAVGVGRPAL 419
Cdd:PLN02535 240 AVEVGVAGIIVSNHGARQLDYSPA-TISVLEEVVQA-------VGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVI 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2286884698 420 YSMTnGWGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPEMVNTER 466
Cdd:PLN02535 312 YGLA-AKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVRTER 357
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
115-465 |
9.38e-74 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 236.94 E-value: 9.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 115 NVSDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLSR 194
Cdd:PLN02493 5 NVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKI--SMPIMVAPTAMQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 195 YAHQDGDQCLARACGHEGIVYCMPTTAAHEAVFGARTTPNQPLcFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSPVI 274
Cdd:PLN02493 83 MAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRF-FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 275 GRRERD-------------------DRIKAADGEDPLFAAGVAKSgsmtlLNPTLTWDDLDWLRAATSLPLVLKGVQTVE 335
Cdd:PLN02493 162 GRRESDiknrftlppnltlknfeglDLGKMDEANDSGLASYVAGQ-----IDRTLSWKDVQWLQTITKLPILVKGVLTGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 336 DAVLAHRAGVDGIVLSNHGGRSQDTAQAPMLTLLEIRRhaphllapETRSRFEVFLDGGVRRGTDVLKALALGASAVGVG 415
Cdd:PLN02493 237 DARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVK--------ATQGRIPVFLDGGVRRGTDVFKALALGASGIFIG 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2286884698 416 RPALYSMTnGWGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPEMVNTE 465
Cdd:PLN02493 309 RPVVFSLA-AEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHITTE 357
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
113-457 |
6.56e-71 |
|
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: 228.87 E-value: 6.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 113 MLNVSDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIKSslPIYITPTGL 192
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKT--PIIMAPIAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 193 SRYAHQDGDQCLARACGHEGIVYCMPTTAAHEAVFGARTTPNQPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSP 272
Cdd:cd04737 83 HGLAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 273 VIGRRERDDRIK------AADGEDPLFAAGVAKSGS--MTLLNPTLTWDDLDWLRAATSLPLVLKGVQTVEDAVLAHRAG 344
Cdd:cd04737 163 VGGNREADIRNKfqfpfgMPNLNHFSEGTGKGKGISeiYAAAKQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAINAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 345 VDGIVLSNHGGRSQDTAQAPMLTLLEIrrhaphllAPETRSRFEVFLDGGVRRGTDVLKALALGASAVGVGRPALYSMTN 424
Cdd:cd04737 243 ADGIWVSNHGGRQLDGGPASFDSLPEI--------AEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLAL 314
|
330 340 350
....*....|....*....|....*....|...
gi 2286884698 425 GwGEAGVRRLIMMLRMEIETNMALAGATRLGEV 457
Cdd:cd04737 315 G-GAQGVASVLEHLNKELKIVMQLAGTRTIEDV 346
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
157-465 |
2.51e-61 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 204.57 E-value: 2.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 157 LRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLSRYAHQDGDQCLARACGHEGIVYCMPTTAAHEAVFGARTTPNQP 236
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKI--SMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 237 LcFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSPVIGRRERD-------------------DRIKAADGEDPLFAAGV 297
Cdd:PLN02979 124 F-FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDiknrftlppnltlknfeglDLGKMDEANDSGLASYV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 298 AKSgsmtlLNPTLTWDDLDWLRAATSLPLVLKGVQTVEDAVLAHRAGVDGIVLSNHGGRSQDTAQAPMLTLLEIRRhaph 377
Cdd:PLN02979 203 AGQ-----IDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVK---- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 378 llapETRSRFEVFLDGGVRRGTDVLKALALGASAVGVGRPALYSMTnGWGEAGVRRLIMMLRMEIETNMALAGATRLGEV 457
Cdd:PLN02979 274 ----ATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLA-AEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 348
|
....*...
gi 2286884698 458 VPEMVNTE 465
Cdd:PLN02979 349 SRNHITTE 356
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
118-459 |
2.74e-56 |
|
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: 191.20 E-value: 2.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 118 DFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLSRYAH 197
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVW--SAPLVIAPTGLNGAFW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 198 QDGDQCLARACGHEGIVYCMpTTAAHEAVFGARTTPNQPLCFQLYTGRDyDRTRALLRKVERLGAAAIFVTVDSPVIGRR 277
Cdd:cd04736 80 PNGDLALARAAAKAGIPFVL-STASNMSIEDVARQADGDLWFQLYVVHR-ELAELLVKRALAAGYTTLVLTTDVAVNGYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 278 ERDDR-----------IKAADG-EDPLFAAGVAKSGSMTLLNPTLT---------------------WDDLDWLRAATSL 324
Cdd:cd04736 158 ERDLRngfaipfrytpRVLLDGiLHPRWLLRFLRNGMPQLANFASDdaidvevqaalmsrqmdasfnWQDLRWLRDLWPH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 325 PLVLKGVQTVEDAVLAHRAGVDGIVLSNHGGRSQDTAQAPMLTLLEIRRHAPHllapetrsrfEVFLDGGVRRGTDVLKA 404
Cdd:cd04736 238 KLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYK----------PVLIDSGIRRGSDIVKA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2286884698 405 LALGASAVGVGRPALYSMTNGwGEAGVRRLIMMLRMEIETNMALAGATRLGEVVP 459
Cdd:cd04736 308 LALGANAVLLGRATLYGLAAR-GEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
117-460 |
1.13e-48 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 171.36 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 117 SDFERAAKKYLSDIGWAYYSSGAEDEISMQDPRRIFNRIALRPRILRHVETIDTSCSFFGGRIksSLPIYITPTGLSRYA 196
Cdd:PRK11197 7 SDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKL--SMPVALAPVGLTGMY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 197 HQDGDQCLARACGHEGIVYCMPTTAAH--EAVFGArttPNQPLCFQLYTGRDYDRTRALLRKVERLGAAAIFVTVDSPVI 274
Cdd:PRK11197 85 ARRGEVQAARAADAKGIPFTLSTVSVCpiEEVAPA---IKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 275 GRRERDDR--IKAADGE---------DPLFAAGV-------------AKSGSMTLL-----------NPTLTWDDLDWLR 319
Cdd:PRK11197 162 GARYRDAHsgMSGPNAAmrrylqavtHPQWAWDVglngrphdlgnisAYLGKPTGLedyigwlgnnfDPSISWKDLEWIR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 320 AATSLPLVLKGVQTVEDAVLAHRAGVDGIVLSNHGGRSQD----TAQApmltLLEIrrhaphllAPETRSRFEVFLDGGV 395
Cdd:PRK11197 242 DFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDgvlsSARA----LPAI--------ADAVKGDITILADSGI 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2286884698 396 RRGTDVLKALALGASAVGVGRPALYSMTNGwGEAGVRRLIMMLRMEIETNMALAGATRLGEVVPE 460
Cdd:PRK11197 310 RNGLDVVRMIALGADTVLLGRAFVYALAAA-GQAGVANLLDLIEKEMRVAMTLTGAKSISEITRD 373
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
6-78 |
2.61e-22 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 90.37 E-value: 2.61e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2286884698 6 DAAELSRHNSKSSCWIVIHGQVWDVTEFLELHPGGDRIILKSAGRDATPSYESVHDPDLVANTLAPSCLVGTI 78
Cdd:pfam00173 1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEAIGHSEDAAEKLLKKYRIGEL 73
|
|
| CYB5 |
COG5274 |
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ... |
8-77 |
1.92e-19 |
|
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];
Pssm-ID: 444085 [Multi-domain] Cd Length: 93 Bit Score: 82.78 E-value: 1.92e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 8 AELSRHNSKSSCWIVIHGQVWDVTEFLELHPGGDRIILKSAGRDATPSYESVHDPDLVANTLAPSCLVGT 77
Cdd:COG5274 21 AEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPHSPKAERLLESYRIGR 90
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
4-109 |
1.44e-15 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 79.72 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 4 YIDAAELSRHNSKSSCWIVIHGQVWDVTEFLELHPGGDRIILKSAGRDATPSYESVHDPDlvANTLAPSCLVGTINPQST 83
Cdd:PLN02252 519 QYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDK--AKKMLEDYRIGELVTTGA 596
|
90 100
....*....|....*....|....*.
gi 2286884698 84 TLVPTAEEVPSPATDDSRSAQPIHPP 109
Cdd:PLN02252 597 AASSSASSHPLSAISTASALAAASPA 622
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
165-456 |
2.04e-13 |
|
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: 70.99 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 165 VETIDTSCSFFGGRIKSslPIYITP-TGlsryAHQDGD---QCLARACGHEGIVYC------MPTTAAHEAVFGAR--TT 232
Cdd:cd02811 37 LDDIDLSTEFLGKRLSA--PLLISAmTG----GSEKAKeinRNLAEAAEELGIAMGvgsqraALEDPELAESFTVVreAP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 233 PNQPLC-----FQLyTGRDYDRTRALlrkVERLGAAAIFVTVDSP---VIGRRERD-----DRIKAadgedplfaagvak 299
Cdd:cd02811 111 PNGPLIanlgaVQL-NGYGVEEARRA---VEMIEADALAIHLNPLqeaVQPEGDRDfrgwlERIEE-------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 300 sgsmtllnptltwddldwLRAATSLPLVLKGVQ---TVEDAVLAHRAGVDGIVLSNHGGRS------------------- 357
Cdd:cd02811 173 ------------------LVKALSVPVIVKEVGfgiSRETAKRLADAGVKAIDVAGAGGTSwarvenyrakdsdqrlaey 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 358 -----QDTAQApmltLLEIRRHAPHLlapetrsrfEVFLDGGVRRGTDVLKALALGASAVGVGRPALYSMTNgwGEAGVR 432
Cdd:cd02811 235 fadwgIPTAAS----LLEVRSALPDL---------PLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALE--GEEAVI 299
|
330 340
....*....|....*....|....
gi 2286884698 433 RLIMMLRMEIETNMALAGATRLGE 456
Cdd:cd02811 300 ETIEQIIEELRTAMFLTGAKNLAE 323
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
313-422 |
1.30e-10 |
|
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: 62.94 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 313 DDL----DWLRAAT-SLPLVLK-----GVQTVEDAVlaHRAGVDGIVLSNHGGrsqDTAQAPmltlLEIRRHA--PHLLA 380
Cdd:cd02808 199 EDLaqliEDLREATgGKPIGVKlvaghGEGDIAAGV--AAAGADFITIDGAEG---GTGAAP----LTFIDHVglPTELG 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2286884698 381 -PET---------RSRFEVFLDGGVRRGTDVLKALALGASAVGVGRPALYSM 422
Cdd:cd02808 270 lARAhqalvknglRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIAL 321
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
330-422 |
4.74e-10 |
|
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: 61.19 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 330 GVQTVEDAVLahRAGVDGIVLSNHGGrsqDTAQAPmltlLEIRRHA--PHLLA-PET---------RSRFEVFLDGGVRR 397
Cdd:pfam01645 214 GVGTIAAGVA--KAGADIILIDGYDG---GTGASP----KTSIKHAglPWELAlAEAhqtlkenglRDRVSLIADGGLRT 284
|
90 100
....*....|....*....|....*
gi 2286884698 398 GTDVLKALALGASAVGVGRPALYSM 422
Cdd:pfam01645 285 GADVAKAAALGADAVYIGTAALIAL 309
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
268-416 |
5.58e-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: 58.75 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 268 TVDSPVIGRRERDDRIKAADGEDPLFAAGVAKSGSMTLLNPTL---TWDDLDWLRAAT-SLPLVLKGVQTVEDAV-LAHR 342
Cdd:cd04722 55 ETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYLareDLELIRELREAVpDVKVVVKLSPTGELAAaAAEE 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2286884698 343 AGVDGIVLSNHGGRSQDTAQAPMLTLLEIRRHAphllapetRSRFEVFLDGGVRRGTDVLKALALGASAVGVGR 416
Cdd:cd04722 135 AGVDEVGLGNGGGGGGGRDAVPIADLLLILAKR--------GSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PLN03198 |
PLN03198 |
delta6-acyl-lipid desaturase; Provisional |
8-60 |
2.07e-08 |
|
delta6-acyl-lipid desaturase; Provisional
Pssm-ID: 178739 [Multi-domain] Cd Length: 526 Bit Score: 56.62 E-value: 2.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2286884698 8 AELSRHNSKSSCWIVIHGQVWDVTEFLELHPGGDrIILKSAGRDATPSYESVH 60
Cdd:PLN03198 109 SEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFH 160
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
331-415 |
1.15e-05 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 46.71 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 331 VQTVEDAVLAHRAGVDGIVLSN-----HGGrsqdTAQAPMLTLLeirrhaphllaPETRSRFE--VFLDGGVRRGTDVLK 403
Cdd:cd04730 109 VTSVEEARKAEAAGADALVAQGaeaggHRG----TFDIGTFALV-----------PEVRDAVDipVIAAGGIADGRGIAA 173
|
90
....*....|..
gi 2286884698 404 ALALGASAVGVG 415
Cdd:cd04730 174 ALALGADGVQMG 185
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
326-477 |
1.40e-05 |
|
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: 47.55 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 326 LVL-KGVQTVE--DAVLAHRAGVDGIVLSNH-GGrsqdTAQAPmLTLLeirRHA--PHLLA-PET---------RSRFEV 389
Cdd:COG0069 372 LVSgAGVGTIAacKGVAKTGAYADFITIDGGeGG----TGAAP-LESI---KHAglPWELGlAEVhqtlvgnglRDRIRL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 390 FLDGGVRRGTDVLKALALGASAVGVGRPALYSM---------TN---------------GWGEAG----VRRLIMMLRME 441
Cdd:COG0069 444 IADGKLKTGRDVAIAAALGADEFGFARAFMVALgcimarkchLNtcpvgvatqdpelrkGFVVEGkperVVNYFRFTAEE 523
|
170 180 190
....*....|....*....|....*....|....*.
gi 2286884698 442 IETNMALAGATRLGEVVPEMVNTERVEHEVFRRVKL 477
Cdd:COG0069 524 VREILAALGVRSPDELIGRHDLLRVRDGEHWKAKGL 559
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
252-415 |
2.23e-05 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 46.19 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 252 ALLRKVERLGAAAIFVTVDSPVIGrrerddrikaadgedplfaagvakSGSMTLLNPTLTWDDLDWLRAATSLPLVLK-- 329
Cdd:cd02810 115 ELARKIERAGAKALELNLSCPNVG------------------------GGRQLGQDPEAVANLLKAVKAAVDIPLLVKls 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 330 ---GVQTVEDAVLA-HRAGVDGIVLSNH-GGRS--QDTAQAPM--------------LTLLEIRRhaphlLAPETRSRFE 388
Cdd:cd02810 171 pyfDLEDIVELAKAaERAGADGLTAINTiSGRVvdLKTVGPGPkrgtgglsgapirpLALRWVAR-----LAARLQLDIP 245
|
170 180
....*....|....*....|....*..
gi 2286884698 389 VFLDGGVRRGTDVLKALALGASAVGVG 415
Cdd:cd02810 246 IIGVGGIDSGEDVLEMLMAGASAVQVA 272
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
331-415 |
4.06e-05 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 45.49 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 331 VQTVEDAVLAHRAGVDGIVLSN-----HGGRSQdtaqapmltlleirrHAPHLLAPETRSRFE--VFLDGGVRRGTDVLK 403
Cdd:COG2070 111 VTSVREARKAEKAGADAVVAEGaeaggHRGADE---------------VSTFALVPEVRDAVDipVIAAGGIADGRGIAA 175
|
90
....*....|..
gi 2286884698 404 ALALGASAVGVG 415
Cdd:COG2070 176 ALALGADGVQMG 187
|
|
| PLN03199 |
PLN03199 |
delta6-acyl-lipid desaturase-like protein; Provisional |
9-83 |
6.70e-04 |
|
delta6-acyl-lipid desaturase-like protein; Provisional
Pssm-ID: 178740 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 6.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2286884698 9 ELSRHNSKSSCWIVIHGQVWDVTEFLElHPGGdRIILKSAGRDATPSYESVHDPDlvANTLAPSCLVGTINPQST 83
Cdd:PLN03199 30 EVKKHASPDDAWIIHQNKVYDVSNWHD-HPGG-AVIFTHAGDDMTDIFAAFHAPG--SQALMKKFYIGDLIPEST 100
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
323-417 |
5.37e-03 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 39.04 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286884698 323 SLPLVLKGVQTVEDAVLAHRAGVDGiVLSNHGGRSQDTAQA------PMLTLLeirrhaphLLAPETRSRFEVFL--DGG 394
Cdd:cd00381 135 NVDVIAGNVVTAEAARDLIDAGADG-VKVGIGPGSICTTRIvtgvgvPQATAV--------ADVAAAARDYGVPViaDGG 205
|
90 100
....*....|....*....|...
gi 2286884698 395 VRRGTDVLKALALGASAVGVGRP 417
Cdd:cd00381 206 IRTSGDIVKALAAGADAVMLGSL 228
|
|
| |
