|
Name |
Accession |
Description |
Interval |
E-value |
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
116-461 |
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: 582.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFSDVGSNVQAtGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVL 355
Cdd:cd02922 162 RDERLKAEEAVSDGPA-GKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 356 SNHGGRQLDTAPSGIEVLAQVMPILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRA 435
Cdd:cd02922 241 SNHGGRQLDTAPAPIEVLLEIRKHCPEVF--DKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKA 318
|
330 340
....*....|....*....|....*.
gi 2301322313 436 MQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:cd02922 319 IQILKDEIETTMRLLGVTSLDQLGPS 344
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
121-464 |
9.55e-157 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 449.29 E-value: 9.55e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 121 ARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPEGEVVL 200
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 201 TRAAHDHDVIQMIPTLASCSFDEIVDARRGDqvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRREKDMRS 280
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGP--LWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 281 KFS------------DVGSNVQATGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEA 348
Cdd:pfam01070 159 GFTlpprltprnlldLALHPRWALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 349 GVQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRergweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYG 428
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVG-----GRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGG 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 2301322313 429 QPGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMVD 464
Cdd:pfam01070 314 EAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
108-463 |
4.75e-126 |
|
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: 371.39 E-value: 4.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 108 LSACYNLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATA 187
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 188 LGKLGNPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDqvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVD 267
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAP--LWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 268 APQLGRREKDMRSKFS----DVGSNVQ--ATGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVED 341
Cdd:COG1304 159 TPVLGRRERDLREGFSqpprLTPRNLLeaATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSPED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 342 VLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQvmpILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFL 421
Cdd:COG1304 239 ARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPE---IRAAVG--GRIPVIADGGIRRGLDVAKALALGADAVGLGRPFL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2301322313 422 FAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMV 463
Cdd:COG1304 314 YGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
113-463 |
2.02e-106 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 321.78 E-value: 2.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 113 NLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLG 192
Cdd:PLN02535 7 NVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 193 NPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLG 272
Cdd:PLN02535 87 HPEGEIATARAAAACNTIMVLSFMASCTVEEV--ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 273 RREKDMRSK-FSDVGSNVQATGGDEV--DRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAG 349
Cdd:PLN02535 165 RREADIKNKmISPQLKNFEGLLSTEVvsDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVEVG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 350 VQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRErgwenRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQ 429
Cdd:PLN02535 245 VAGIIVSNHGARQLDYSPATISVLEEVVQAVGG-----RVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGE 319
|
330 340 350
....*....|....*....|....*....|....
gi 2301322313 430 PGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMV 463
Cdd:PLN02535 320 DGVRKVIEMLKDELEITMALSGCPSVKDITRSHV 353
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
9-80 |
1.03e-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: 1.03e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301322313 9 ADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEF-DPIHPPDTLDKYLDSSkHLGEVD 80
Cdd:pfam00173 3 EELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKY-RIGELA 74
|
|
| CYB5 |
COG5274 |
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ... |
3-62 |
8.25e-24 |
|
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];
Pssm-ID: 444085 [Multi-domain] Cd Length: 93 Bit Score: 95.10 E-value: 8.25e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 3 NNKLTGADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEFDPIHP 62
Cdd:COG5274 15 EKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHP 74
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
7-97 |
1.59e-21 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 98.21 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 7 TGADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEFDPIHPP---DTLDKYldsskHLGEVDMAT 83
Cdd:PLN02252 521 TMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDkakKMLEDY-----RIGELVTTG 595
|
90
....*....|....
gi 2301322313 84 VEQEEKAHDPEEDA 97
Cdd:PLN02252 596 AAASSSASSHPLSA 609
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
116-461 |
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: 582.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFSDVGSNVQAtGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVL 355
Cdd:cd02922 162 RDERLKAEEAVSDGPA-GKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 356 SNHGGRQLDTAPSGIEVLAQVMPILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRA 435
Cdd:cd02922 241 SNHGGRQLDTAPAPIEVLLEIRKHCPEVF--DKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKA 318
|
330 340
....*....|....*....|....*.
gi 2301322313 436 MQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:cd02922 319 IQILKDEIETTMRLLGVTSLDQLGPS 344
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
121-464 |
9.55e-157 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 449.29 E-value: 9.55e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 121 ARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPEGEVVL 200
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 201 TRAAHDHDVIQMIPTLASCSFDEIVDARRGDqvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRREKDMRS 280
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGP--LWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 281 KFS------------DVGSNVQATGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEA 348
Cdd:pfam01070 159 GFTlpprltprnlldLALHPRWALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 349 GVQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRergweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYG 428
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVG-----GRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGG 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 2301322313 429 QPGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMVD 464
Cdd:pfam01070 314 EAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
116-460 |
9.36e-132 |
|
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: 383.72 E-value: 9.36e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQvqWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRe 275
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPR--WFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 kdmrskfsdvgsnvqatggdevdrsqgaaraissfidpsLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVL 355
Cdd:cd02809 159 ---------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 356 SNHGGRQLDTAPSGIEVLAQVMPILRergweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRA 435
Cdd:cd02809 200 SNHGGRQLDGAPATIDALPEIVAAVG-----GRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHV 274
|
330 340
....*....|....*....|....*
gi 2301322313 436 MQLLKDELEMNMRLIGAQKIADLNP 460
Cdd:cd02809 275 LEILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
108-463 |
4.75e-126 |
|
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: 371.39 E-value: 4.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 108 LSACYNLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATA 187
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 188 LGKLGNPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDqvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVD 267
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAP--LWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 268 APQLGRREKDMRSKFS----DVGSNVQ--ATGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVED 341
Cdd:COG1304 159 TPVLGRRERDLREGFSqpprLTPRNLLeaATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSPED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 342 VLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQvmpILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFL 421
Cdd:COG1304 239 ARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPE---IRAAVG--GRIPVIADGGIRRGLDVAKALALGADAVGLGRPFL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2301322313 422 FAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMV 463
Cdd:COG1304 314 YGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
113-463 |
2.02e-106 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 321.78 E-value: 2.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 113 NLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLG 192
Cdd:PLN02535 7 NVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 193 NPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLG 272
Cdd:PLN02535 87 HPEGEIATARAAAACNTIMVLSFMASCTVEEV--ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 273 RREKDMRSK-FSDVGSNVQATGGDEV--DRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAG 349
Cdd:PLN02535 165 RREADIKNKmISPQLKNFEGLLSTEVvsDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVEVG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 350 VQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRErgwenRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQ 429
Cdd:PLN02535 245 VAGIIVSNHGARQLDYSPATISVLEEVVQAVGG-----RVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGE 319
|
330 340 350
....*....|....*....|....*....|....
gi 2301322313 430 PGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMV 463
Cdd:PLN02535 320 DGVRKVIEMLKDELEITMALSGCPSVKDITRSHV 353
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
113-458 |
8.65e-95 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 292.02 E-value: 8.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 113 NLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLG 192
Cdd:PLN02493 5 NVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 193 NPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLG 272
Cdd:PLN02493 85 HPDGEYATARAASAAGTIMTLSSWATSSVEEV--ASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 273 RREKDMRSKFSdVGSNVQATGGDEVD-------RSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRA 345
Cdd:PLN02493 163 RRESDIKNRFT-LPPNLTLKNFEGLDlgkmdeaNDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 346 VEAGVQGVVLSNHGGRQLDTAPSGIEVLAQVMpilreRGWENRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMS 425
Cdd:PLN02493 242 IQAGAAGIIVSNHGARQLDYVPATISALEEVV-----KATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLA 316
|
330 340 350
....*....|....*....|....*....|...
gi 2301322313 426 AYGQPGVNRAMQLLKDELEMNMRLIGAQKIADL 458
Cdd:PLN02493 317 AEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 349
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
98-461 |
8.34e-92 |
|
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: 284.56 E-value: 8.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 98 RQERIERMPPLSAcyNLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKC 177
Cdd:cd03332 7 LAGLLGRRPDLPV--DPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 178 SIPFYVTATALGKLGNPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARrGDQVQWLQLYVNKDRAITKRIIEHAEAR 257
Cdd:cd03332 85 AAPLLLAPIGVQELFHPDAELATARAAAELGVPYILSTASSSSIEDVAAAA-GDAPRWFQLYWPKDDDLTESLLRRAEKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 258 GCKGLFITVDAPQLGRREKDMRSK-------------FSD------VGSNVQATGGDEVDRSQGAARAISSFIDPSLSWK 318
Cdd:cd03332 164 GYRVLVVTLDTWSLGWRPRDLDLGylpflrgigianyFSDpvfrkkLAEPVGEDPEAPPPMEAAVARFVSVFSGPSLTWE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 319 DIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRergweNRIEIFIDGGIR 398
Cdd:cd03332 244 DLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVG-----DRLTVLFDSGVR 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301322313 399 RATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:cd03332 319 TGADIMKALALGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRD 381
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
113-458 |
3.27e-82 |
|
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: 258.91 E-value: 3.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 113 NLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLG 192
Cdd:cd04737 7 NLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 193 NPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLG 272
Cdd:cd04737 87 HATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGP-KWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 273 RREKDMRSKFSdvgSNVQATGGDEVDRSQGAARAIsSFIDPS----LSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEA 348
Cdd:cd04737 166 NREADIRNKFQ---FPFGMPNLNHFSEGTGKGKGI-SEIYAAakqkLSPADIEFIAKISGLPVIVKGIQSPEDADVAINA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 349 GVQGVVLSNHGGRQLDTAPSGIEVLAQVMPILrergwENRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYG 428
Cdd:cd04737 242 GADGIWVSNHGGRQLDGGPASFDSLPEIAEAV-----NHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGG 316
|
330 340 350
....*....|....*....|....*....|
gi 2301322313 429 QPGVNRAMQLLKDELEMNMRLIGAQKIADL 458
Cdd:cd04737 317 AQGVASVLEHLNKELKIVMQLAGTRTIEDV 346
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
155-459 |
1.36e-78 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 250.02 E-value: 1.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 155 FRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQ 234
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEV--ASTGPGIR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 235 WLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRREKDMRSKFSdVGSNVQATGGDEVD-------RSQGAARAI 307
Cdd:PLN02979 124 FFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFT-LPPNLTLKNFEGLDlgkmdeaNDSGLASYV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 308 SSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQVMpilreRGWEN 387
Cdd:PLN02979 203 AGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVV-----KATQG 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301322313 388 RIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLN 459
Cdd:PLN02979 278 RIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEIS 349
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
116-461 |
3.66e-66 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 217.97 E-value: 3.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:PRK11197 8 DYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYARR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:PRK11197 88 GEVQAARAADAKGIPFTLSTVSVCPIEEV--APAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGARY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFS--------------------DVGSNVQATGGDEVDRSQGAARAISSFI-------DPSLSWKDIPWFQSVTK 328
Cdd:PRK11197 166 RDAHSGMSgpnaamrrylqavthpqwawDVGLNGRPHDLGNISAYLGKPTGLEDYIgwlgnnfDPSISWKDLEWIRDFWD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 329 MPIVLKGVQCVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGievlAQVMPILRErGWENRIEIFIDGGIRRATDILKALC 408
Cdd:PRK11197 246 GPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSS----ARALPAIAD-AVKGDITILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2301322313 409 LGAKGVGIGRPFLFAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRD 373
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
116-460 |
3.83e-66 |
|
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: 217.39 E-value: 3.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKdRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDV--ARQADGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFSDVGSNVQATGGDEV-----------------------DRSQGAARA--ISSFIDPSLSWKDIPWFQSVTKMP 330
Cdd:cd04736 159 RDLRNGFAIPFRYTPRVLLDGIlhprwllrflrngmpqlanfasdDAIDVEVQAalMSRQMDASFNWQDLRWLRDLWPHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 331 IVLKGVQCVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQV-----MPILrergwenrieifIDGGIRRATDILK 405
Cdd:cd04736 239 LLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIvaatyKPVL------------IDSGIRRGSDIVK 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2301322313 406 ALCLGAKGVGIGRPFLFAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNP 460
Cdd:cd04736 307 ALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
9-80 |
1.03e-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: 1.03e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301322313 9 ADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEF-DPIHPPDTLDKYLDSSkHLGEVD 80
Cdd:pfam00173 3 EELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKY-RIGELA 74
|
|
| CYB5 |
COG5274 |
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ... |
3-62 |
8.25e-24 |
|
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];
Pssm-ID: 444085 [Multi-domain] Cd Length: 93 Bit Score: 95.10 E-value: 8.25e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 3 NNKLTGADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEFDPIHP 62
Cdd:COG5274 15 EKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHP 74
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
7-97 |
1.59e-21 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 98.21 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 7 TGADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEFDPIHPP---DTLDKYldsskHLGEVDMAT 83
Cdd:PLN02252 521 TMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDkakKMLEDY-----RIGELVTTG 595
|
90
....*....|....
gi 2301322313 84 VEQEEKAHDPEEDA 97
Cdd:PLN02252 596 AAASSSASSHPLSA 609
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
330-458 |
3.81e-12 |
|
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: 67.14 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 330 PIVLKGVQC---VEDVLRAVEAGVQGVVLSNHGG-------------RQLDTAPS----GI---EVLAQVMPILRErgwe 386
Cdd:cd02811 180 PVIVKEVGFgisRETAKRLADAGVKAIDVAGAGGtswarvenyrakdSDQRLAEYfadwGIptaASLLEVRSALPD---- 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301322313 387 nrIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAmSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADL 458
Cdd:cd02811 256 --LPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEELRTAMFLTGAKNLAEL 324
|
|
| PLN03198 |
PLN03198 |
delta6-acyl-lipid desaturase; Provisional |
9-101 |
5.26e-10 |
|
delta6-acyl-lipid desaturase; Provisional
Pssm-ID: 178739 [Multi-domain] Cd Length: 526 Bit Score: 61.63 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 9 ADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQkIILKYAGKDATEEFDPIHPPDTLdkyldssKHLGEVDMATVEQEE 88
Cdd:PLN03198 109 SEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFHAASTW-------KILQDFYIGDVDNVE 180
|
90
....*....|...
gi 2301322313 89 KAHDPEEDARQER 101
Cdd:PLN03198 181 PTPELLKDFRDLR 193
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
370-424 |
1.42e-09 |
|
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: 59.86 E-value: 1.42e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2301322313 370 IEVLAQVMPILRERGWENRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAM 424
Cdd:cd02808 267 ELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIAL 321
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
318-424 |
8.54e-09 |
|
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: 57.34 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 318 KDIPWfqsvtKMPIVLKGV--QCVEDV-LRAVEAGVQGVVLSNHGG-------RQLDTAPSGIEV-LAQVMPILRERGWE 386
Cdd:pfam01645 197 KEINP-----KAPISVKLVsgHGVGTIaAGVAKAGADIILIDGYDGgtgaspkTSIKHAGLPWELaLAEAHQTLKENGLR 271
|
90 100 110
....*....|....*....|....*....|....*...
gi 2301322313 387 NRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAM 424
Cdd:pfam01645 272 DRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIAL 309
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
313-418 |
3.06e-07 |
|
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: 51.05 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 313 PSLSWKDIPWF-QSVTKMPIVLKGVQ-CVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQvmpILRERGWenRIE 390
Cdd:cd04722 98 AREDLELIRELrEAVPDVKVVVKLSPtGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLL---ILAKRGS--KVP 172
|
90 100
....*....|....*....|....*...
gi 2301322313 391 IFIDGGIRRATDILKALCLGAKGVGIGR 418
Cdd:cd04722 173 VIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PLN03199 |
PLN03199 |
delta6-acyl-lipid desaturase-like protein; Provisional |
5-89 |
4.72e-07 |
|
delta6-acyl-lipid desaturase-like protein; Provisional
Pssm-ID: 178740 [Multi-domain] Cd Length: 485 Bit Score: 52.35 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 5 KLTGADVAKHNSKDSCWVIVHGKAYDVTEFLpEHPGGqKIILKYAGKDATEEFDPIHPPDTldKYLDSSKHLGEVDMATV 84
Cdd:PLN03199 25 KISWQEVKKHASPDDAWIIHQNKVYDVSNWH-DHPGG-AVIFTHAGDDMTDIFAAFHAPGS--QALMKKFYIGDLIPEST 100
|
....*
gi 2301322313 85 EQEEK 89
Cdd:PLN03199 101 EHKDP 105
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
371-424 |
1.34e-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: 47.94 E-value: 1.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2301322313 371 EVLAQVMPILRERGWENRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAM 424
Cdd:COG0069 423 LGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVAL 476
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
336-423 |
3.75e-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: 39.00 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 336 VQCVEDVLRAVEAGVQGVVLSNH--GGRQLDTAPSGIEVLAQVMPILRergwenrIEIFIDGGIRRATDILKALCLGAKG 413
Cdd:cd04730 109 VTSVEEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVD-------IPVIAAGGIADGRGIAAALALGADG 181
|
90
....*....|
gi 2301322313 414 VGIGRPFLFA 423
Cdd:cd04730 182 VQMGTRFLAT 191
|
|
|