|
Name |
Accession |
Description |
Interval |
E-value |
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
189-532 |
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: 568.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 189 QDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGNP 268
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 269 LGEVNLTRGAGACGIVQGISINASCSLDEIMTARKEGQPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSKR 348
Cdd:cd02922 81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 349 TMDVRAKAHVAPPPSSSGQQKSASPLGVSQAISGYQDTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAKAGVQGVIL 428
Cdd:cd02922 161 ERDERLKAEEAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 429 SNHGGRQCDYAPAPIDLLYELRCKRPDLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEEGVVRLCQ 508
Cdd:cd02922 241 SNHGGRQLDTAPAPIEVLLEIRKHCPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQ 320
|
330 340
....*....|....*....|....
gi 58266812 509 ILAEEITNTMRNIGAPRLEDLKPE 532
Cdd:cd02922 321 ILKDEIETTMRLLGVTSLDQLGPS 344
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
195-536 |
2.07e-142 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 415.01 E-value: 2.07e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 195 AEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGNPLGEVNL 274
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 275 TRGAGACGIVQGISINASCSLDEIMTARkeGQPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSKRTMDVRA 354
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAA--GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 355 KAHV-------------APPPSSSGQQKSASPLGVSQAISGYQDTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAKA 421
Cdd:pfam01070 159 GFTLpprltprnlldlaLHPRWALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 422 GVQGVILSNHGGRQCDYAPAPIDLLYELRCKRPdlfDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEE 501
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVG---GRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEA 315
|
330 340 350
....*....|....*....|....*....|....*
gi 58266812 502 GVVRLCQILAEEITNTMRNIGAPRLEDLKPEMVGP 536
Cdd:pfam01070 316 GVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
183-534 |
2.42e-112 |
|
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: 338.26 E-value: 2.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 183 DGMLLVQDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAM 262
Cdd:COG1304 2 SRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 263 AKLGNPLGEVNLTRGAGACGIVQGISINASCSLDEImtARKEGQPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDT 342
Cdd:COG1304 82 GGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEV--AAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 343 AWRSKRTMDVRAkAHVAPPPSS--------SGQQKSASPLGVSQAISGYQDTNLTWKDIDFIREHTNLPIIVKGVQCVED 414
Cdd:COG1304 160 PVLGRRERDLRE-GFSQPPRLTprnlleaaTHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSPED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 415 VDLCAKAGVQGVILSNHGGRQCDYAPAPIDLLYELRCKrpdLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYA 494
Cdd:COG1304 239 ARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAA---VGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYG 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 58266812 495 NGTHGEEGVVRLCQILAEEITNTMRNIGAPRLEDLKPEMV 534
Cdd:COG1304 316 LAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
188-529 |
1.86e-70 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 230.49 E-value: 1.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 188 VQDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGN 267
Cdd:PLN02535 8 VNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLAH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 268 PLGEVNLTRGAGACGIVQGISINASCSLDEIMTARKEGQpvMFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSK 347
Cdd:PLN02535 88 PEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVR--FLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 348 RTMDVRAKAHVappPSSSGQQKSASPLGVSQAISGYQ-------DTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAK 420
Cdd:PLN02535 166 READIKNKMIS---PQLKNFEGLLSTEVVSDKGSGLEafasetfDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 421 AGVQGVILSNHGGRQCDYAPAPIDLLYELRCKrpdLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGE 500
Cdd:PLN02535 243 VGVAGIIVSNHGARQLDYSPATISVLEEVVQA---VGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGE 319
|
330 340
....*....|....*....|....*....
gi 58266812 501 EGVVRLCQILAEEITNTMRNIGAPRLEDL 529
Cdd:PLN02535 320 DGVRKVIEMLKDELEITMALSGCPSVKDI 348
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
81-153 |
1.58e-26 |
|
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: 102.70 E-value: 1.58e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58266812 81 SFEEVQKHNKREDCWVIIDGKIYDVTDFLENHPGGAEIIIANAGKDATKIF-KPLHPPDALDMLDPSQHIGPVD 153
Cdd:pfam00173 1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKYRIGELA 74
|
|
| CYB5 |
COG5274 |
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ... |
67-152 |
1.35e-21 |
|
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];
Pssm-ID: 444085 [Multi-domain] Cd Length: 93 Bit Score: 89.33 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 67 PGVSTVQPSGQKLVSFEEVQKHNKREDCWVIIDGKIYDVTDFLENHPGGAEIIIANAGKDATKIF--KPLHPPDALDMLd 144
Cdd:COG5274 5 TTPATDAAAPEKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFntKHPHSPKAERLL- 83
|
....*...
gi 58266812 145 PSQHIGPV 152
Cdd:COG5274 84 ESYRIGRL 91
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
65-156 |
3.59e-21 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 97.83 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 65 QAPGVSTVQPSGQKLVSFEEVQKHNKREDCWVIIDGKIYDVTDFLENHPGGAEIIIANAGKDATKIFKPLHPPDALDMLD 144
Cdd:PLN02252 505 SVSTPFMNTNTGSKQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDKAKKMLE 584
|
90
....*....|..
gi 58266812 145 PsQHIGPVDPAT 156
Cdd:PLN02252 585 D-YRIGELVTTG 595
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
189-532 |
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: 568.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 189 QDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGNP 268
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 269 LGEVNLTRGAGACGIVQGISINASCSLDEIMTARKEGQPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSKR 348
Cdd:cd02922 81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 349 TMDVRAKAHVAPPPSSSGQQKSASPLGVSQAISGYQDTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAKAGVQGVIL 428
Cdd:cd02922 161 ERDERLKAEEAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 429 SNHGGRQCDYAPAPIDLLYELRCKRPDLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEEGVVRLCQ 508
Cdd:cd02922 241 SNHGGRQLDTAPAPIEVLLEIRKHCPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQ 320
|
330 340
....*....|....*....|....
gi 58266812 509 ILAEEITNTMRNIGAPRLEDLKPE 532
Cdd:cd02922 321 ILKDEIETTMRLLGVTSLDQLGPS 344
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
195-536 |
2.07e-142 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 415.01 E-value: 2.07e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 195 AEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGNPLGEVNL 274
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 275 TRGAGACGIVQGISINASCSLDEIMTARkeGQPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSKRTMDVRA 354
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAA--GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 355 KAHV-------------APPPSSSGQQKSASPLGVSQAISGYQDTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAKA 421
Cdd:pfam01070 159 GFTLpprltprnlldlaLHPRWALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 422 GVQGVILSNHGGRQCDYAPAPIDLLYELRCKRPdlfDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEE 501
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVG---GRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEA 315
|
330 340 350
....*....|....*....|....*....|....*
gi 58266812 502 GVVRLCQILAEEITNTMRNIGAPRLEDLKPEMVGP 536
Cdd:pfam01070 316 GVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
189-531 |
8.47e-114 |
|
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: 339.81 E-value: 8.47e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 189 QDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGNP 268
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 269 LGEVNLTRGAGACGIVQGISINASCSLDEIMTARkeGQPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSKR 348
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAA--PGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 349 tmdvrakahvapppsssgqqksasplgvsqaisgyqdtnLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAKAGVQGVIL 428
Cdd:cd02809 159 ---------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 429 SNHGGRQCDYAPAPIDLLYELRcKRPDlfDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEEGVVRLCQ 508
Cdd:cd02809 200 SNHGGRQLDGAPATIDALPEIV-AAVG--GRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLE 276
|
330 340
....*....|....*....|...
gi 58266812 509 ILAEEITNTMRNIGAPRLEDLKP 531
Cdd:cd02809 277 ILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
183-534 |
2.42e-112 |
|
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: 338.26 E-value: 2.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 183 DGMLLVQDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAM 262
Cdd:COG1304 2 SRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 263 AKLGNPLGEVNLTRGAGACGIVQGISINASCSLDEImtARKEGQPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDT 342
Cdd:COG1304 82 GGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEV--AAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 343 AWRSKRTMDVRAkAHVAPPPSS--------SGQQKSASPLGVSQAISGYQDTNLTWKDIDFIREHTNLPIIVKGVQCVED 414
Cdd:COG1304 160 PVLGRRERDLRE-GFSQPPRLTprnlleaaTHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSPED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 415 VDLCAKAGVQGVILSNHGGRQCDYAPAPIDLLYELRCKrpdLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYA 494
Cdd:COG1304 239 ARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAA---VGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYG 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 58266812 495 NGTHGEEGVVRLCQILAEEITNTMRNIGAPRLEDLKPEMV 534
Cdd:COG1304 316 LAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
185-530 |
8.22e-78 |
|
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: 248.90 E-value: 8.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 185 MLLVQDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAK 264
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 265 LGNPLGEVNLTRGAGACGIVQGISINASCSLDEIMTARKEGqPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAW 344
Cdd:cd04737 85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGG-PKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 345 RSKRTMDVRAKaHVAPPPSSSGQqKSASPLGVSQAIS---GYQDTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAKA 421
Cdd:cd04737 164 GGNREADIRNK-FQFPFGMPNLN-HFSEGTGKGKGISeiyAAAKQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAINA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 422 GVQGVILSNHGGRQCDYAPAPIDLLYELrCKRPDlfDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEE 501
Cdd:cd04737 242 GADGIWVSNHGGRQLDGGPASFDSLPEI-AEAVN--HRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQ 318
|
330 340
....*....|....*....|....*....
gi 58266812 502 GVVRLCQILAEEITNTMRNIGAPRLEDLK 530
Cdd:cd04737 319 GVASVLEHLNKELKIVMQLAGTRTIEDVK 347
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
190-532 |
8.52e-76 |
|
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: 244.88 E-value: 8.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 190 DFEDW---AEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLG 266
Cdd:cd03332 20 DPERLealAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 267 NPLGEVNLTRGAGACGIVQGISINASCSLDEIMTARKEGqPVMFQIYLNKDRAASIALLKRVTALGANAIIFTVDT---A 343
Cdd:cd03332 100 HPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDA-PRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTwslG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 344 WRSKR-----------------TMDVRAKAHVAPPPSSSGQQKSASPLGVSQAISGYQDTNLTWKDIDFIREHTNLPIIV 406
Cdd:cd03332 179 WRPRDldlgylpflrgigianyFSDPVFRKKLAEPVGEDPEAPPPMEAAVARFVSVFSGPSLTWEDLAFLREWTDLPIVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 407 KGVQCVEDVDLCAKAGVQGVILSNHGGRQCDYAPAPIDLLYELrckRPDLFDKIEVMMDGGVRSGADVVKAIALGAKAVG 486
Cdd:cd03332 259 KGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEI---VEAVGDRLTVLFDSGVRTGADIMKALALGAKAVL 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 58266812 487 IGRSFLYANGTHGEEGVVRLCQILAEEITNTMRNIGAPRLEDLKPE 532
Cdd:cd03332 336 IGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRD 381
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
188-529 |
1.86e-70 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 230.49 E-value: 1.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 188 VQDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGN 267
Cdd:PLN02535 8 VNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLAH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 268 PLGEVNLTRGAGACGIVQGISINASCSLDEIMTARKEGQpvMFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSK 347
Cdd:PLN02535 88 PEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVR--FLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 348 RTMDVRAKAHVappPSSSGQQKSASPLGVSQAISGYQ-------DTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAK 420
Cdd:PLN02535 166 READIKNKMIS---PQLKNFEGLLSTEVVSDKGSGLEafasetfDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 421 AGVQGVILSNHGGRQCDYAPAPIDLLYELRCKrpdLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGE 500
Cdd:PLN02535 243 VGVAGIIVSNHGARQLDYSPATISVLEEVVQA---VGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGE 319
|
330 340
....*....|....*....|....*....
gi 58266812 501 EGVVRLCQILAEEITNTMRNIGAPRLEDL 529
Cdd:PLN02535 320 DGVRKVIEMLKDELEITMALSGCPSVKDI 348
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
188-529 |
3.34e-63 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 211.51 E-value: 3.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 188 VQDFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGN 267
Cdd:PLN02493 6 VTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 268 PLGEVNLTRGAGACGIVQGISINASCSLDEIMTArkeGQPV-MFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRS 346
Cdd:PLN02493 86 PDGEYATARAASAAGTIMTLSSWATSSVEEVAST---GPGIrFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 347 KRTMDVRAKAHVAPPPSSS-------GQQKSASPLGVSQAISGYQDTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCA 419
Cdd:PLN02493 163 RRESDIKNRFTLPPNLTLKnfegldlGKMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 420 KAGVQGVILSNHGGRQCDYAPAPIDLLYELRCKRPdlfDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHG 499
Cdd:PLN02493 243 QAGAAGIIVSNHGARQLDYVPATISALEEVVKATQ---GRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEG 319
|
330 340 350
....*....|....*....|....*....|
gi 58266812 500 EEGVVRLCQILAEEITNTMRNIGAPRLEDL 529
Cdd:PLN02493 320 EAGVRKVLQMLRDEFELTMALSGCRSLKEI 349
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
229-529 |
1.08e-53 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 186.08 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 229 FRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGNPLGEVNLTRGAGACGIVQGISINASCSLDEIMTArkeGQPV 308
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVAST---GPGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 309 -MFQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSKRTMDVRAKAHVAPPPSSS-------GQQKSASPLGVSQAI 380
Cdd:PLN02979 123 rFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKnfegldlGKMDEANDSGLASYV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 381 SGYQDTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAKAGVQGVILSNHGGRQCDYAPAPIDLLYELRCKRPdlfDKI 460
Cdd:PLN02979 203 AGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQ---GRI 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58266812 461 EVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEEGVVRLCQILAEEITNTMRNIGAPRLEDL 529
Cdd:PLN02979 280 PVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 348
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
190-531 |
5.88e-53 |
|
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: 183.88 E-value: 5.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 190 DFEDWAEKVMSGTAWNYYKSAADREKTAAENEKAFDRYFFRPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGNPL 269
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 270 GEVNLTRGAGACGIVQGISINASCSLDEImtARKEGQPVMFQIYLNKDRAASiALLKRVTALGANAIIFTVDTAWRSKRT 349
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDV--ARQADGDLWFQLYVVHRELAE-LLVKRALAAGYTTLVLTTDVAVNGYRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 350 MDVR-------------AKAHVAPPPSSSGQQKSASPLGVSQAISGYQDTNL-------------TWKDIDFIREHTNLP 403
Cdd:cd04736 159 RDLRngfaipfrytprvLLDGILHPRWLLRFLRNGMPQLANFASDDAIDVEVqaalmsrqmdasfNWQDLRWLRDLWPHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 404 IIVKGVQCVEDVDLCAKAGVQGVILSNHGGRQCDYAPAPIDLLYELRCKRPDlfdkiEVMMDGGVRSGADVVKAIALGAK 483
Cdd:cd04736 239 LLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYK-----PVLIDSGIRRGSDIVKALALGAN 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 58266812 484 AVGIGRSFLYANGTHGEEGVVRLCQILAEEITNTMRNIGAPRLEDLKP 531
Cdd:cd04736 314 AVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
230-532 |
5.85e-50 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 176.37 E-value: 5.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 230 RPRILRDATTGSTETEFMGMKTTMPVFISPAAMAKLGNPLGEVNLTRGAGACGIVQGISINASCSLDEImtARKEGQPVM 309
Cdd:PRK11197 48 RQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEV--APAIKRPMW 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 310 FQIYLNKDRAASIALLKRVTALGANAIIFTVDTAWRSKRTMDVRAkahvapppSSSGqqKSASPLGVSQA---------- 379
Cdd:PRK11197 126 FQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGARYRDAHS--------GMSG--PNAAMRRYLQAvthpqwawdv 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 380 -----------ISGYQ-----------------DTNLTWKDIDFIREHTNLPIIVKGVQCVEDVDLCAKAGVQGVILSNH 431
Cdd:PRK11197 196 glngrphdlgnISAYLgkptgledyigwlgnnfDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 432 GGRQCDYAPAPIDLLyelrckrPDLFD----KIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEEGVVRLC 507
Cdd:PRK11197 276 GGRQLDGVLSSARAL-------PAIADavkgDITILADSGIRNGLDVVRMIALGADTVLLGRAFVYALAAAGQAGVANLL 348
|
330 340
....*....|....*....|....*
gi 58266812 508 QILAEEITNTMRNIGAPRLEDLKPE 532
Cdd:PRK11197 349 DLIEKEMRVAMTLTGAKSISEITRD 373
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
81-153 |
1.58e-26 |
|
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: 102.70 E-value: 1.58e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58266812 81 SFEEVQKHNKREDCWVIIDGKIYDVTDFLENHPGGAEIIIANAGKDATKIF-KPLHPPDALDMLDPSQHIGPVD 153
Cdd:pfam00173 1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKYRIGELA 74
|
|
| CYB5 |
COG5274 |
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ... |
67-152 |
1.35e-21 |
|
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];
Pssm-ID: 444085 [Multi-domain] Cd Length: 93 Bit Score: 89.33 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 67 PGVSTVQPSGQKLVSFEEVQKHNKREDCWVIIDGKIYDVTDFLENHPGGAEIIIANAGKDATKIF--KPLHPPDALDMLd 144
Cdd:COG5274 5 TTPATDAAAPEKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFntKHPHSPKAERLL- 83
|
....*...
gi 58266812 145 PSQHIGPV 152
Cdd:COG5274 84 ESYRIGRL 91
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
65-156 |
3.59e-21 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 97.83 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 65 QAPGVSTVQPSGQKLVSFEEVQKHNKREDCWVIIDGKIYDVTDFLENHPGGAEIIIANAGKDATKIFKPLHPPDALDMLD 144
Cdd:PLN02252 505 SVSTPFMNTNTGSKQYTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDKAKKMLE 584
|
90
....*....|..
gi 58266812 145 PsQHIGPVDPAT 156
Cdd:PLN02252 585 D-YRIGELVTTG 595
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
224-530 |
5.26e-14 |
|
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: 73.30 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 224 FDRYFFR----PRILRDATtgSTETEFMGMKTTMPVFISpaAMAKLGNPLGEVN--LTRGAGACGIV-----QGISINAS 292
Cdd:cd02811 22 FDDVRLVhnalPELDLDDI--DLSTEFLGKRLSAPLLIS--AMTGGSEKAKEINrnLAEAAEELGIAmgvgsQRAALEDP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 293 cSLDEIMTARKEGQPVMFqIYLN----KDRAASIALLKR-VTALGANAIIFtvdtawrskrtmdvrakaHVAPPpsssgq 367
Cdd:cd02811 98 -ELAESFTVVREAPPNGP-LIANlgavQLNGYGVEEARRaVEMIEADALAI------------------HLNPL------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 368 QKSASPLGvsqaisgyqDTNLT-WKD-IDFIREHTNLPIIVKGVQC---VEDVDLCAKAGVQGVILSNHGG--------- 433
Cdd:cd02811 152 QEAVQPEG---------DRDFRgWLErIEELVKALSVPVIVKEVGFgisRETAKRLADAGVKAIDVAGAGGtswarveny 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 434 ----RQCDYAPAPIDL-------LYELRckrpDLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYAnGTHGEEG 502
Cdd:cd02811 223 rakdSDQRLAEYFADWgiptaasLLEVR----SALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEA 297
|
330 340
....*....|....*....|....*...
gi 58266812 503 VVRLCQILAEEITNTMRNIGAPRLEDLK 530
Cdd:cd02811 298 VIETIEQIIEELRTAMFLTGAKNLAELK 325
|
|
| PLN03198 |
PLN03198 |
delta6-acyl-lipid desaturase; Provisional |
62-153 |
6.97e-11 |
|
delta6-acyl-lipid desaturase; Provisional
Pssm-ID: 178739 [Multi-domain] Cd Length: 526 Bit Score: 64.71 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 62 SNAQAPGV----STVQPSGQKLVSFE--------EVQKHNKREDCWVIIDGKIYDVTDFLENHPGGAeIIIANAGKDATK 129
Cdd:PLN03198 76 SNSQEAAEalaeSVVKPTRRRSSKEKkskshllsEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTD 154
|
90 100
....*....|....*....|....
gi 58266812 130 IFKPLHPPDALDMLDpSQHIGPVD 153
Cdd:PLN03198 155 AFSSFHAASTWKILQ-DFYIGDVD 177
|
|
| PLN03199 |
PLN03199 |
delta6-acyl-lipid desaturase-like protein; Provisional |
59-156 |
1.55e-10 |
|
delta6-acyl-lipid desaturase-like protein; Provisional
Pssm-ID: 178740 [Multi-domain] Cd Length: 485 Bit Score: 63.52 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 59 DELSNAQAPGVSTVQPSGQKlVSFEEVQKHNKREDCWVIIDGKIYDVTDFLEnHPGGAeIIIANAGKDATKIFKPLHPPD 138
Cdd:PLN03199 6 DAAAAKGRSAALKLAEKPQK-ISWQEVKKHASPDDAWIIHQNKVYDVSNWHD-HPGGA-VIFTHAGDDMTDIFAAFHAPG 82
|
90
....*....|....*...
gi 58266812 139 ALDMLDpSQHIGPVDPAT 156
Cdd:PLN03199 83 SQALMK-KFYIGDLIPES 99
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
301-489 |
4.59e-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: 59.52 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 301 ARKEGQPVMFQIYLNKDRAASIALLKRVTALGANAIIFtvdtawrskrtmdvrakaHVAPPPSSSGqqksasplgvsqai 380
Cdd:cd04722 53 AAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEI------------------HGAVGYLARE-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 381 sgyqdtnlTWKDIDFIREHT-NLPIIVKGVQCVEDVD-LCAKAGVQGVILSNHGGRQCDYAPAPIDLLyelRCKRPDLFD 458
Cdd:cd04722 101 --------DLELIRELREAVpDVKVVVKLSPTGELAAaAAEEAGVDEVGLGNGGGGGGGRDAVPIADL---LLILAKRGS 169
|
170 180 190
....*....|....*....|....*....|.
gi 58266812 459 KIEVMMDGGVRSGADVVKAIALGAKAVGIGR 489
Cdd:cd04722 170 KVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
393-494 |
1.21e-08 |
|
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: 57.17 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 393 IDFIREHTNL-PIIVK---GVQcVEDVD-LCAKAGVQGVILSNHGG-------RQCDYAPAPIDL-LYELR--CKRPDLF 457
Cdd:cd02808 205 IEDLREATGGkPIGVKlvaGHG-EGDIAaGVAAAGADFITIDGAEGgtgaaplTFIDHVGLPTELgLARAHqaLVKNGLR 283
|
90 100 110
....*....|....*....|....*....|....*..
gi 58266812 458 DKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYA 494
Cdd:cd02808 284 DRVSLIASGGLRTGADVAKALALGADAVGIGTAALIA 320
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
403-496 |
9.11e-08 |
|
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: 54.26 E-value: 9.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 403 PIIVKGV--QCVEDVDLC-AKAGVQGVILSNHGG-------RQCDYAPAPIDL-LYEL--RCKRPDLFDKIEVMMDGGVR 469
Cdd:pfam01645 204 PISVKLVsgHGVGTIAAGvAKAGADIILIDGYDGgtgaspkTSIKHAGLPWELaLAEAhqTLKENGLRDRVSLIADGGLR 283
|
90 100
....*....|....*....|....*..
gi 58266812 470 SGADVVKAIALGAKAVGIGRSFLYANG 496
Cdd:pfam01645 284 TGADVAKAAALGADAVYIGTAALIALG 310
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
455-496 |
3.73e-06 |
|
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: 49.86 E-value: 3.73e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 58266812 455 DLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANG 496
Cdd:COG0069 436 GLRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVALG 477
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
446-501 |
5.01e-04 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 42.72 E-value: 5.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 58266812 446 LYELrCKRPDlfdkIEVMMDGGVRSGADVVKAIALGAKAVGIGRSFLYANGTHGEE 501
Cdd:PRK06843 248 VYEV-CKNTN----ICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEE 298
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
460-491 |
1.20e-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: 41.35 E-value: 1.20e-03
10 20 30
....*....|....*....|....*....|..
gi 58266812 460 IEVMMDGGVRSGADVVKAIALGAKAVGIGRSF 491
Cdd:cd00381 198 VPVIADGGIRTSGDIVKALAAGADAVMLGSLL 229
|
|
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
455-488 |
1.52e-03 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 41.40 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|....
gi 58266812 455 DLFDKIEVMMDGGVRSGADVVKAIALGAKAVGIG 488
Cdd:PRK11750 1063 GLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFG 1096
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
396-529 |
1.86e-03 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B 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.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 40.61 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 396 IREHTNLPIIVKGVQCVEDVDLCAKA----GVQGV------------------ILSN-HGGRqcdYAPA--PIdllyELR 450
Cdd:cd04740 149 VKKATDVPVIVKLTPNVTDIVEIARAaeeaGADGLtlintlkgmaidietrkpILGNvTGGL---SGPAikPI----ALR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 451 CKRpDLFD--KIEVMMDGGVRSGADVVKAIALGAKAVGIGrSFLYANGTHGEEgvvrlcqiLAEEITNTMRNIGAPRLED 528
Cdd:cd04740 222 MVY-QVYKavEIPIIGVGGIASGEDALEFLMAGASAVQVG-TANFVDPEAFKE--------IIEGLEAYLDEEGIKSIEE 291
|
.
gi 58266812 529 L 529
Cdd:cd04740 292 L 292
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
393-492 |
2.05e-03 |
|
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: 40.16 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58266812 393 IDFIREHtNLPIIVKgVQCVEDVDLCAKAGVQGVILSN-----HGGRQCDyapAPIDLLYELRckrpDLFDkIEVMMDGG 467
Cdd:cd04730 95 VERLKAA-GIKVIPT-VTSVEEARKAEAAGADALVAQGaeaggHRGTFDI---GTFALVPEVR----DAVD-IPVIAAGG 164
|
90 100
....*....|....*....|....*
gi 58266812 468 VRSGADVVKAIALGAKAVGIGRSFL 492
Cdd:cd04730 165 IADGRGIAAALALGADGVQMGTRFL 189
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
465-491 |
2.76e-03 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 40.45 E-value: 2.76e-03
10 20
....*....|....*....|....*..
gi 58266812 465 DGGVRSGADVVKAIALGAKAVGIGRSF 491
Cdd:pfam00478 329 DGGIKYSGDIVKALAAGADAVMLGSLL 355
|
|
| |
