|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
16-379 |
8.22e-170 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 477.79 E-value: 8.22e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 16 AKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHHQGERAV 95
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 96 AAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNRERDKRTGF 175
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 176 AIPFKLNLAGMTQFAIKPSWAIDWLTHerfrlpqlenhvkmdGGALSISRYFTEMLDPSMSWDDVAEMVREWGGPFCLKG 255
Cdd:pfam01070 161 TLPPRLTPRNLLDLALHPRWALGVLRR---------------GGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 256 IMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLGAKAVGLGRYY 335
Cdd:pfam01070 226 ILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPF 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 517055726 336 LFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNLR 379
Cdd:pfam01070 306 LYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
3-380 |
1.37e-165 |
|
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: 467.30 E-value: 1.37e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 3 LTDCYNFHDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTA 82
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 83 LQRLFHHQGERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSI 162
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 163 TGGNRERDKRTGFAIPFKLNLAGMTQFAIKPSWAIdwltherfrlpqlenhvkmdgGALSISRYFTEMLDPSMSWDDVAE 242
Cdd:COG1304 161 VLGRRERDLREGFSQPPRLTPRNLLEAATHPRWAL---------------------GLASLAAWLDTNFDPSLTWDDIAW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 243 MVREWGGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKAL 322
Cdd:COG1304 220 LRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKAL 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 517055726 323 SLGAKAVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNLRF 380
Cdd:COG1304 300 ALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
10-375 |
1.15e-147 |
|
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: 419.54 E-value: 1.15e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 10 HDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHH 89
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 90 QGERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNRer 169
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 170 dkrtgfaipfklnlagmtqfaikpswaidwltherfrlpqlenhvkmdggalsisryftemldpsMSWDDVAEMVREWGG 249
Cdd:cd02809 159 -----------------------------------------------------------------LTWDDLAWLRSQWKG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 250 PFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLGAKAV 329
Cdd:cd02809 174 PLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAV 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 517055726 330 GLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSR 375
Cdd:cd02809 254 LIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
11-378 |
8.63e-97 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 293.47 E-value: 8.63e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 11 DFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHHQ 90
Cdd:PRK11197 8 DYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYARR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 91 GERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNRERD 170
Cdd:PRK11197 88 GEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGARYRD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 171 KRTGFAIPFKlNLAGMTQFAIKPSWAIDWLTHERfrlP-QLENHVKMDGGALSISRYF---TEMLDPSMSWDDVaEMVRE 246
Cdd:PRK11197 168 AHSGMSGPNA-AMRRYLQAVTHPQWAWDVGLNGR---PhDLGNISAYLGKPTGLEDYIgwlGNNFDPSISWKDL-EWIRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 247 -WGGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLG 325
Cdd:PRK11197 243 fWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIALG 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 517055726 326 AKAVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNL 378
Cdd:PRK11197 323 ADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
16-379 |
8.22e-170 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 477.79 E-value: 8.22e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 16 AKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHHQGERAV 95
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 96 AAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNRERDKRTGF 175
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 176 AIPFKLNLAGMTQFAIKPSWAIDWLTHerfrlpqlenhvkmdGGALSISRYFTEMLDPSMSWDDVAEMVREWGGPFCLKG 255
Cdd:pfam01070 161 TLPPRLTPRNLLDLALHPRWALGVLRR---------------GGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 256 IMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLGAKAVGLGRYY 335
Cdd:pfam01070 226 ILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPF 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 517055726 336 LFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNLR 379
Cdd:pfam01070 306 LYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
3-380 |
1.37e-165 |
|
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: 467.30 E-value: 1.37e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 3 LTDCYNFHDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTA 82
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 83 LQRLFHHQGERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSI 162
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 163 TGGNRERDKRTGFAIPFKLNLAGMTQFAIKPSWAIdwltherfrlpqlenhvkmdgGALSISRYFTEMLDPSMSWDDVAE 242
Cdd:COG1304 161 VLGRRERDLREGFSQPPRLTPRNLLEAATHPRWAL---------------------GLASLAAWLDTNFDPSLTWDDIAW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 243 MVREWGGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKAL 322
Cdd:COG1304 220 LRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKAL 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 517055726 323 SLGAKAVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNLRF 380
Cdd:COG1304 300 ALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
10-375 |
1.15e-147 |
|
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: 419.54 E-value: 1.15e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 10 HDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHH 89
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 90 QGERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNRer 169
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 170 dkrtgfaipfklnlagmtqfaikpswaidwltherfrlpqlenhvkmdggalsisryftemldpsMSWDDVAEMVREWGG 249
Cdd:cd02809 159 -----------------------------------------------------------------LTWDDLAWLRSQWKG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 250 PFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLGAKAV 329
Cdd:cd02809 174 PLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAV 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 517055726 330 GLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSR 375
Cdd:cd02809 254 LIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
10-373 |
4.63e-116 |
|
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: 341.11 E-value: 4.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 10 HDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHH 89
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 90 QGERAVAAAAAKHGTMFGVSSLGTISLEE--ARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNR 167
Cdd:cd02922 81 DGELNLARAAGKHGILQMISTNASCSLEEivDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 168 ERDKRtgfaipFKLNLAGMTQFAIKpswaidwltherfrlpqlenhvKMDGGALSISRYFTEMLDPSMSWDDVAEMVREW 247
Cdd:cd02922 161 ERDER------LKAEEAVSDGPAGK----------------------KTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 248 GGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVD---AVGDRIDVMMDGGVQRGTHVLKALSL 324
Cdd:cd02922 213 KLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVYVDGGVRRGTDVLKALCL 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 517055726 325 GAKAVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQL 373
Cdd:cd02922 293 GAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQL 341
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
5-378 |
4.33e-100 |
|
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: 300.51 E-value: 4.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 5 DCYNFHDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQ 84
Cdd:cd04737 4 DIINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 85 RLFHHQGERAVAAAAAKHGTMFGVSSLGTISLEEARRIS-NGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSIT 163
Cdd:cd04737 84 GLAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASnGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 164 GGNRERDKRTGFAIPFklnlaGMtqfaikpswaidwltherfrlPQLENHVKMDGGALSISrYFTEMLDPSMSWDDVAEM 243
Cdd:cd04737 164 GGNREADIRNKFQFPF-----GM---------------------PNLNHFSEGTGKGKGIS-EIYAAAKQKLSPADIEFI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 244 VREWGGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALS 323
Cdd:cd04737 217 AKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALA 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 517055726 324 LGAKAVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNL 378
Cdd:cd04737 297 SGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRTFL 351
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
8-375 |
1.23e-98 |
|
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: 298.04 E-value: 1.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 8 NFHDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLF 87
Cdd:cd03332 20 DPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 88 HHQGERAVAAAAAKHGTMFGVSSLGTISLEE-ARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGN 166
Cdd:cd03332 100 HPDAELATARAAAELGVPYILSTASSSSIEDvAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 167 RERDKRTGFaIPFkLNLAGMTQFAIKPSWaidwltHERFRLPQLENHVKMDGGALSISRYFTEMLDPSMSWDDVAEMVRE 246
Cdd:cd03332 180 RPRDLDLGY-LPF-LRGIGIANYFSDPVF------RKKLAEPVGEDPEAPPPMEAAVARFVSVFSGPSLTWEDLAFLREW 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 247 WGGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLGA 326
Cdd:cd03332 252 TDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGA 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 517055726 327 KAVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSR 375
Cdd:cd03332 332 KAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTR 380
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
11-378 |
8.63e-97 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 293.47 E-value: 8.63e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 11 DFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHHQ 90
Cdd:PRK11197 8 DYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYARR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 91 GERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNRERD 170
Cdd:PRK11197 88 GEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGARYRD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 171 KRTGFAIPFKlNLAGMTQFAIKPSWAIDWLTHERfrlP-QLENHVKMDGGALSISRYF---TEMLDPSMSWDDVaEMVRE 246
Cdd:PRK11197 168 AHSGMSGPNA-AMRRYLQAVTHPQWAWDVGLNGR---PhDLGNISAYLGKPTGLEDYIgwlGNNFDPSISWKDL-EWIRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 247 -WGGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLG 325
Cdd:PRK11197 243 fWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIALG 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 517055726 326 AKAVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNL 378
Cdd:PRK11197 323 ADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
11-375 |
6.90e-92 |
|
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: 280.18 E-value: 6.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 11 DFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHHQ 90
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 91 GERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFY-FHKDrgLNREMMARAKNAGVQAMMLTVDSITGGNRER 169
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYvVHRE--LAELLVKRALAAGYTTLVLTTDVAVNGYRER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 170 DKRTGFAIPFKLNLAGMTQFAIKPSWAIDWLTHErfrLPQLENHVKMDGGALSI-SRYFTEMLDPSMSWDDVAEMVREWG 248
Cdd:cd04736 160 DLRNGFAIPFRYTPRVLLDGILHPRWLLRFLRNG---MPQLANFASDDAIDVEVqAALMSRQMDASFNWQDLRWLRDLWP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 249 GPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDriDVMMDGGVQRGTHVLKALSLGAKA 328
Cdd:cd04736 237 HKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYK--PVLIDSGIRRGSDIVKALALGANA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 517055726 329 VGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSR 375
Cdd:cd04736 315 VLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
8-379 |
1.44e-81 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 253.60 E-value: 1.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 8 NFHDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLF 87
Cdd:PLN02535 7 NVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 88 HHQGERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNR 167
Cdd:PLN02535 87 HPEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGRR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 168 ERDKRTGFAIPFKLNLAGMtqfaikpswaidwltherfrlpqLENHVKMDGGAlSISRYFTEMLDPSMSWDDVAEMVREW 247
Cdd:PLN02535 167 EADIKNKMISPQLKNFEGL-----------------------LSTEVVSDKGS-GLEAFASETFDASLSWKDIEWLRSIT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 248 GGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLGAK 327
Cdd:PLN02535 223 NLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQ 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 517055726 328 AVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNLR 379
Cdd:PLN02535 303 AVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVR 354
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
8-378 |
2.63e-74 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 235.40 E-value: 2.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 8 NFHDFRRMAKRRLPGPIFDYIDGGADDEVTYRRNTAAFEACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLF 87
Cdd:PLN02493 5 NVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 88 HHQGERAVAAAAAKHGTMFGVSSLGTISLEEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNR 167
Cdd:PLN02493 85 HPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 168 ERDKRTGFAIPFKLNLAGMTQFAIKpswaidwltherfrlpqlenhvKMDGGALS-ISRYFTEMLDPSMSWDDVAEMVRE 246
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLG----------------------KMDEANDSgLASYVAGQIDRTLSWKDVQWLQTI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 247 WGGPFCLKGIMSVEDAKRAAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLGA 326
Cdd:PLN02493 223 TKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGA 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 517055726 327 KAVGLGRYYLFPLAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNL 378
Cdd:PLN02493 303 SGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 354
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
38-378 |
2.64e-64 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 209.19 E-value: 2.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 38 YRRNTAAFE-ACDLVPDVLRGVAEVDMSVTVMGQKLAMPVYCSPTALQRLFHHQGERAVAAAAAKHGTMFGVSSLGTISL 116
Cdd:PLN02979 33 FKRCDALLGgFCDFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 117 EEARRISNGPQVYQFYFHKDRGLNREMMARAKNAGVQAMMLTVDSITGGNRERDKRTGFAIPFKLNLAGMTQFAIKpswa 196
Cdd:PLN02979 113 EEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLG---- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 197 idwltherfrlpqlenhvKMDGGALS-ISRYFTEMLDPSMSWDDVAEMVREWGGPFCLKGIMSVEDAKRAAEIGCSGIVL 275
Cdd:PLN02979 189 ------------------KMDEANDSgLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 276 SNHGGRQLDGSRSAFDQLAEIVDAVGDRIDVMMDGGVQRGTHVLKALSLGAKAVGLGRYYLFPLAAAGQPGVERALETMR 355
Cdd:PLN02979 251 SNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLR 330
|
330 340
....*....|....*....|...
gi 517055726 356 TEIERGMKLMGCTSVSQLSRRNL 378
Cdd:PLN02979 331 DEFELTMALSGCRSLKEISRNHI 353
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
237-375 |
6.91e-11 |
|
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: 62.90 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 237 WDDVAEMVREWGGPFCLKGI---MSVEDAKRAAEIGCSGIVLSNHGG---------RQLDGSRSAFDQLAEI-------- 296
Cdd:cd02811 167 LERIEELVKALSVPVIVKEVgfgISRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSDQRLAEYFADWgiptaasl 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 297 --VDAVGDRIDVMMDGGVQRGTHVLKALSLGAKAVGLGRYYLFPlAAAGQPGVERALETMRTEIERGMKLMGCTSVSQLS 374
Cdd:cd02811 247 leVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEELRTAMFLTGAKNLAELK 325
|
.
gi 517055726 375 R 375
Cdd:cd02811 326 Q 326
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
230-333 |
1.89e-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: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 230 MLDPSMSWDDVAEMVRE-----WGGPFCLKGIMSVEDAKR-AAEIGCSGIVLSNHGGRQLDGSRSAFDQLAEIVDAVGDR 303
Cdd:cd04722 91 HGAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAaAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSK 170
|
90 100 110
....*....|....*....|....*....|
gi 517055726 304 IDVMMDGGVQRGTHVLKALSLGAKAVGLGR 333
Cdd:cd04722 171 VPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
239-332 |
1.17e-06 |
|
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: 49.02 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 239 DVAEMVREWGGPFCLKgIMSVEDAKRAAEIGCSGIVLSN-----HGGRQLDGSrsaFDQLAEIVDAVGdrIDVMMDGGVQ 313
Cdd:cd04730 93 EVVERLKAAGIKVIPT-VTSVEEARKAEAAGADALVAQGaeaggHRGTFDIGT---FALVPEVRDAVD--IPVIAAGGIA 166
|
90
....*....|....*....
gi 517055726 314 RGTHVLKALSLGAKAVGLG 332
Cdd:cd04730 167 DGRGIAAALALGADGVQMG 185
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
293-381 |
2.34e-06 |
|
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: 49.08 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 293 LAEIVDA-----VGDRIDVMMDGGVQRGTHVLKALSLGAKAVGLGRYYLFPLAAA------------------------- 342
Cdd:cd02808 270 LARAHQAlvkngLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCIqarkchtntcpvgvatqdpelrrrl 349
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 517055726 343 ----GQPGVERALETMRTEIERGMKLMGCTSVSQLSRRNLRFR 381
Cdd:cd02808 350 dvegKAERVANYLKSLAEELRELAAALGKRSLELLGRSDLLAL 392
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
239-332 |
1.39e-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: 46.26 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 239 DVAEMVREWGGPfclkgIM----SVEDAKRAAEIGCSGIVLSN-----HGGRQLdgsRSAFDQLAEIVDAVgdRIDVMMD 309
Cdd:COG2070 95 DLIERLKEAGIK-----VIpivtSVREARKAEKAGADAVVAEGaeaggHRGADE---VSTFALVPEVRDAV--DIPVIAA 164
|
90 100
....*....|....*....|...
gi 517055726 310 GGVQRGTHVLKALSLGAKAVGLG 332
Cdd:COG2070 165 GGIADGRGIAAALALGADGVQMG 187
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
238-332 |
9.33e-04 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 40.25 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 238 DDVAEMVREWGGPFCLKGIMSVEDAKRAAEIGCS--GIVLSNHGGRQLDGSRSAFDQLAEIVDAVGdrIDVMMDGGVQRG 315
Cdd:cd04729 112 AELIKRIHEEYNCLLMADISTLEEALNAAKLGFDiiGTTLSGYTEETAKTEDPDFELLKELRKALG--IPVIAEGRINSP 189
|
90
....*....|....*..
gi 517055726 316 THVLKALSLGAKAVGLG 332
Cdd:cd04729 190 EQAAKALELGADAVVVG 206
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
178-336 |
1.65e-03 |
|
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.
Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 40.19 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 178 PFKLNLagmtqFAIKPSwAIDWLTHERFRLPQLENH------VKMDGGALSISRYFTEMLdpSMSWDDVAEMV---REWG 248
Cdd:pfam03060 64 PFGANL-----FLPKPD-LADPAANYAKILGNNALGynieegVPDYGKVLVDLDEGVNVV--SFGFGLPPNDVvfrLHFA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 249 GPFCLKGIMSVEDAKRAAEIGCSGIVLSN-----HGGRQLDGSRSAFDQLAEIVDAVGdrIDVMMDGGVQRGTHVLKALS 323
Cdd:pfam03060 136 GVALIPTISSAKEARIAEARGADALIVQGpeaggHQGTPEYGDKGLFRLVPQVPDAVD--IPVIAAGGIWDRRGVAAALA 213
|
170
....*....|...
gi 517055726 324 LGAKAVGLGRYYL 336
Cdd:pfam03060 214 LGASGVQMGTRFL 226
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
304-362 |
9.05e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 38.03 E-value: 9.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517055726 304 IDVMMDGGVQRGTHVLKALSLGAKAVGLGRYylfpLAAAGQ-PGVERALETMRTEIERGM 362
Cdd:PTZ00314 345 VPCIADGGIKNSGDICKALALGADCVMLGSL----LAGTEEaPGEYFFKDGVRLKVYRGM 400
|
|
| |
