|
Name |
Accession |
Description |
Interval |
E-value |
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
1-377 |
0e+00 |
|
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: 531.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 1 MSVITDIEDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTG 80
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 81 LAGMQHADGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQ 160
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 161 IIGQRHKDLKNGLSAPPRPTLANLLNIATKPRWALGmlgtrrrgfgnivghvkgvddMGSLSEWTARQFDPRLNWGDVEW 240
Cdd:COG1304 161 VLGRRERDLREGFSQPPRLTPRNLLEAATHPRWALG---------------------LASLAAWLDTNFDPSLTWDDIAW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 241 IKRRWGGKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDVLKAI 320
Cdd:COG1304 220 LRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKAL 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15597578 321 ALGARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGRDILL 377
Cdd:COG1304 300 ALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
14-376 |
6.58e-179 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 500.91 E-value: 6.58e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 14 ARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLAGMQHADGEILA 93
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 94 ARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQIIGQRHKDLKNGL 173
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 174 SAPPRPTLANLLNIATKPRWALGMLGTRRrgfgnivghvkgvddMGSLSEWTARQFDPRLNWGDVEWIKRRWGGKLVLKG 253
Cdd:pfam01070 161 TLPPRLTPRNLLDLALHPRWALGVLRRGG---------------AGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 254 ILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDVLKAIALGARGTMIGRPY 333
Cdd:pfam01070 226 ILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPF 305
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15597578 334 LYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGRDIL 376
Cdd:pfam01070 306 LYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLL 348
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
8-373 |
6.24e-156 |
|
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: 440.73 E-value: 6.24e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 8 EDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLAGMQHA 87
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 88 DGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQIIGQRhk 167
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 168 dlknglsapprptlanllniatkprwalgmlgtrrrgfgnivghvkgvddmgslsewtarqfdprLNWGDVEWIKRRWGG 247
Cdd:cd02809 159 -----------------------------------------------------------------LTWDDLAWLRSQWKG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 248 KLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDVLKAIALGARGT 327
Cdd:cd02809 174 PLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAV 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15597578 328 MIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGR 373
Cdd:cd02809 254 LIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
3-376 |
1.64e-146 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 419.81 E-value: 1.64e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 3 VITDIEDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLA 82
Cdd:PRK11197 2 IISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 83 GMQHADGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQII 162
Cdd:PRK11197 82 GMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 163 GQRHKDLKNGLSAPPRPtLANLLNIATKPRWA--LGMLGtRRRGFGNI---VGHVKGVDD-MGslseWTARQFDPRLNWG 236
Cdd:PRK11197 162 GARYRDAHSGMSGPNAA-MRRYLQAVTHPQWAwdVGLNG-RPHDLGNIsayLGKPTGLEDyIG----WLGNNFDPSISWK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 237 DVEWIKRRWGGKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDV 316
Cdd:PRK11197 236 DLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 317 LKAIALGARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGRDIL 376
Cdd:PRK11197 316 VRMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| L_lactate_LldD |
NF033901 |
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ... |
3-378 |
2.51e-124 |
|
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. It occurs in E. coli, Salmonella, and as one of two L-lactate dehydrogenases in Pseudomonas aeruginosa. It is unrelated to the NAD-dependent enzyme.
Pssm-ID: 411463 Cd Length: 377 Bit Score: 363.37 E-value: 2.51e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 3 VITDIEDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLA 82
Cdd:NF033901 2 IISASTDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 83 GMQHADGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQII 162
Cdd:NF033901 82 GMYARRGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPTP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 163 GQRHKDLKNGLSAPPRPtLANLLNIATKPRWA--LGMLGtRRRGFGNI---VGHVKGVDD-MGslseWTARQFDPRLNWG 236
Cdd:NF033901 162 GARYRDAHSGMSGPNAA-LRRMLQAVTHPQWAwdVGLLG-RPHDLGNIsayRGKPTGLEDyIG----WLGNNFDPSISWK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 237 DVEWIKRRWGGKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDV 316
Cdd:NF033901 236 DLEWIREFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597578 317 LKAIALGARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGRDILLP 378
Cdd:NF033901 316 VRMIALGADSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLVQ 377
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
5-376 |
4.49e-111 |
|
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: 330.01 E-value: 4.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 5 TDIEDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLAGM 84
Cdd:cd03332 19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 85 QHADGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQ-PFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQIIG 163
Cdd:cd03332 99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDaPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 164 QRHKDLKNGLSapPRPTLANLLNIATKPRWalgmlgtrRRGFGNIVGH-VKGVDDMGSLSEWTARQF-DPRLNWGDVEWI 241
Cdd:cd03332 179 WRPRDLDLGYL--PFLRGIGIANYFSDPVF--------RKKLAEPVGEdPEAPPPMEAAVARFVSVFsGPSLTWEDLAFL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 242 KRRWGGKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDVLKAIA 321
Cdd:cd03332 249 REWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALA 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15597578 322 LGARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGRDIL 376
Cdd:cd03332 329 LGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
9-372 |
1.33e-109 |
|
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: 324.55 E-value: 1.33e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 9 DLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLAGMQHAD 88
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 89 GEILAARAAAEFGVRYTLSTMSICSLEDIATEV--GQPFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQIIGQRH 166
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARppDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 167 KDLKNGLSAPPRPTLAnllniATKPRWALGMLGTRRRGFGnivghvkgvddmgslsewtarqfDPRLNWGDVEWIKRRWG 246
Cdd:cd02922 162 RDERLKAEEAVSDGPA-----GKKTKAKGGGAGRAMSGFI-----------------------DPTLTWDDIKWLRKHTK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 247 GKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVE---AVGERIEVWLDSGIRSGQDVLKAIALG 323
Cdd:cd02922 214 LPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVYVDGGVRRGTDVLKALCLG 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15597578 324 ARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVG 372
Cdd:cd02922 294 AKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQLG 342
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
8-373 |
2.43e-102 |
|
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: 306.76 E-value: 2.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 8 EDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLAGMQHA 87
Cdd:cd04736 1 EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 88 DGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWFQLYVMRdRDFIERLIDRAKAAGCDALVLTLDLQIIGQRHK 167
Cdd:cd04736 81 NGDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 168 DLKNGLSAPPRPTLANLLNIATKPRWALGMLGTRRRGFGNIVG-HVKGVDDMGSLsewTARQFDPRLNWGDVEWIKRRWG 246
Cdd:cd04736 160 DLRNGFAIPFRYTPRVLLDGILHPRWLLRFLRNGMPQLANFASdDAIDVEVQAAL---MSRQMDASFNWQDLRWLRDLWP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 247 GKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGEriEVWLDSGIRSGQDVLKAIALGARG 326
Cdd:cd04736 237 HKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYK--PVLIDSGIRRGSDIVKALALGANA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15597578 327 TMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGR 373
Cdd:cd04736 315 VLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
4-373 |
1.67e-90 |
|
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: 276.25 E-value: 1.67e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 4 ITDIEDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLAG 83
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 84 MQHADGEILAARAAAEFGVRYTLSTMSICSLEDIAtEVGQ--PFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQI 161
Cdd:cd04737 85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIA-KASNggPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 162 IGQRHKDLKNGLsapPRPTLANLLNIATKPRWAlGMlgtrrrgfgnivghvkgvddmgSLSEWTArQFDPRLNWGDVEWI 241
Cdd:cd04737 164 GGNREADIRNKF---QFPFGMPNLNHFSEGTGK-GK----------------------GISEIYA-AAKQKLSPADIEFI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 242 KRRWGGKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDVLKAIA 321
Cdd:cd04737 217 AKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALA 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15597578 322 LGARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGR 373
Cdd:cd04737 297 SGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKR 348
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
1-373 |
1.29e-88 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 271.71 E-value: 1.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 1 MSVITDIEDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTG 80
Cdd:PLN02535 2 ADEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 81 LAGMQHADGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQ 160
Cdd:PLN02535 82 MHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 161 IIGQRHKDLKNGLSAPPRPTLANLLNIATKPrwalgmlgtrrrgfgnivghvkgvDDMGSLSEWTARQFDPRLNWGDVEW 240
Cdd:PLN02535 162 RLGRREADIKNKMISPQLKNFEGLLSTEVVS------------------------DKGSGLEAFASETFDASLSWKDIEW 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 241 IKRRWGGKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDVLKAI 320
Cdd:PLN02535 218 LRSITNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKAL 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15597578 321 ALGARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGR 373
Cdd:PLN02535 298 ALGAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITR 350
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
4-374 |
3.87e-85 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 263.13 E-value: 3.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 4 ITDIEDLRRLARKRVPRMFYDYADSGSWSEGTYRANQDDFAAIKLRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLAG 83
Cdd:PLN02493 3 ITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 84 MQHADGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWFQLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQIIG 163
Cdd:PLN02493 83 MAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 164 QRHKDLKNGLSAPPRPTLANLLNIAtkprwalgmlgtrrrgfgniVGHVKGVDDMGsLSEWTARQFDPRLNWGDVEWIKR 243
Cdd:PLN02493 163 RRESDIKNRFTLPPNLTLKNFEGLD--------------------LGKMDEANDSG-LASYVAGQIDRTLSWKDVQWLQT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 244 RWGGKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDSGIRSGQDVLKAIALG 323
Cdd:PLN02493 222 ITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALG 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15597578 324 ARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTDIREVGRD 374
Cdd:PLN02493 302 ASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRN 352
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
48-374 |
6.54e-73 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 231.53 E-value: 6.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 48 LRQRVARNIENRSLRTRMLGQEMAMPVAIAPTGLAGMQHADGEILAARAAAEFGVRYTLSTMSICSLEDIATEVGQPFWF 127
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 128 QLYVMRDRDFIERLIDRAKAAGCDALVLTLDLQIIGQRHKDLKNGLSAPPRPTLANLLNIAtkprwalgmlgtrrrgfgn 207
Cdd:PLN02979 126 QLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLD------------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 208 iVGHVKGVDDMGsLSEWTARQFDPRLNWGDVEWIKRRWGGKLVLKGILDAEDARLAADSGADALVVSNHGGRQLDGAPST 287
Cdd:PLN02979 187 -LGKMDEANDSG-LASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPAT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 288 ISALPAIVEAVGERIEVWLDSGIRSGQDVLKAIALGARGTMIGRPYLYGLGALGQAGVTRALEIIARELDLTMAFCGHTD 367
Cdd:PLN02979 265 ISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRS 344
|
....*..
gi 15597578 368 IREVGRD 374
Cdd:PLN02979 345 LKEISRN 351
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
231-331 |
4.13e-08 |
|
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: 52.97 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 231 PRLNWGDVEWIKRRWGGKLVLKGI--LDAEDARLAADSGADALVVSNHGGRQLDGAPSTISALPAIVEAVGERIEVWLDS 308
Cdd:cd04722 98 AREDLELIRELREAVPDVKVVVKLspTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGG 177
|
90 100
....*....|....*....|...
gi 15597578 309 GIRSGQDVLKAIALGARGTMIGR 331
Cdd:cd04722 178 GINDPEDAAEALALGADGVIVGS 200
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
236-370 |
1.22e-07 |
|
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: 52.89 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 236 GDVEW---------IKRRWGGKLVLK----GIlDAEDARLAADSGADALVVSNHGG-------------RQLDGAP---- 285
Cdd:cd02811 159 GDRDFrgwlerieeLVKALSVPVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGtswarvenyrakdSDQRLAEyfad 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 286 ---STISALPAIVEAVGErIEVWLDSGIRSGQDVLKAIALGARGTMIGRPYLYGLGAlGQAGVTRALEIIARELDLTMAF 362
Cdd:cd02811 238 wgiPTAASLLEVRSALPD-LPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALE-GEEAVIETIEQIIEELRTAMFL 315
|
....*...
gi 15597578 363 CGHTDIRE 370
Cdd:cd02811 316 TGAKNLAE 323
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
239-330 |
3.92e-07 |
|
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: 50.56 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 239 EWIKR--RWGGKLVLKgILDAEDARLAADSGADALVVSN-----HGGRQLDGapsTISALPAIVEAVGerIEVWLDSGIR 311
Cdd:cd04730 93 EVVERlkAAGIKVIPT-VTSVEEARKAEAAGADALVAQGaeaggHRGTFDIG---TFALVPEVRDAVD--IPVIAAGGIA 166
|
90
....*....|....*....
gi 15597578 312 SGQDVLKAIALGARGTMIG 330
Cdd:cd04730 167 DGRGIAAALALGADGVQMG 185
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
263-338 |
7.73e-07 |
|
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: 50.41 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 263 AADSGADALVVSNHGG---------RQLDGAPsTISALPAIVEAV-----GERIEVWLDSGIRSGQDVLKAIALGARGTM 328
Cdd:pfam01645 222 VAKAGADIILIDGYDGgtgaspktsIKHAGLP-WELALAEAHQTLkenglRDRVSLIADGGLRTGADVAKAAALGADAVY 300
|
90
....*....|
gi 15597578 329 IGRPYLYGLG 338
Cdd:pfam01645 301 IGTAALIALG 310
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
260-377 |
7.90e-07 |
|
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: 50.62 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 260 ARLAADSGADALVVSNHGGrqldG---APSTIS------ALPAIVEAV--------GERIEVWLDSGIRSGQDVLKAIAL 322
Cdd:cd02808 231 AAGVAAAGADFITIDGAEG----GtgaAPLTFIdhvglpTELGLARAHqalvknglRDRVSLIASGGLRTGADVAKALAL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 323 GARGTMIGRPYLYGLGA-------LGQ--AGVT-------RALEI-------------IARELDLTMAFCGHTDIREVGR 373
Cdd:cd02808 307 GADAVGIGTAALIALGCiqarkchTNTcpVGVAtqdpelrRRLDVegkaervanylksLAEELRELAAALGKRSLELLGR 386
|
....
gi 15597578 374 DILL 377
Cdd:cd02808 387 SDLL 390
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
239-330 |
1.16e-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: 46.64 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 239 EWIKR--RWGGKLVLKGIlDAEDARLAADSGADALVVSNH--GGRQLDGAPSTISALPAIVEAVgeRIEVWLDSGIRSGQ 314
Cdd:COG2070 95 DLIERlkEAGIKVIPIVT-SVREARKAEKAGADAVVAEGAeaGGHRGADEVSTFALVPEVRDAV--DIPVIAAGGIADGR 171
|
90
....*....|....*.
gi 15597578 315 DVLKAIALGARGTMIG 330
Cdd:COG2070 172 GIAAALALGADGVQMG 187
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
246-334 |
2.34e-05 |
|
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: 45.97 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 246 GGKLVLKGILDAEDARLAADSGADALVVS-----NHGGRQLDGAPSTISALPAIVEAVGerIEVWLDSGIRSGQDVLKAI 320
Cdd:pfam03060 135 AGVALIPTISSAKEARIAEARGADALIVQgpeagGHQGTPEYGDKGLFRLVPQVPDAVD--IPVIAAGGIWDRRGVAAAL 212
|
90
....*....|....
gi 15597578 321 ALGARGTMIGRPYL 334
Cdd:pfam03060 213 ALGASGVQMGTRFL 226
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
238-332 |
1.19e-04 |
|
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: 43.66 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 238 VEWIKRRWGG-KLVLKGILDAEDARLAADSGADALVV-----SNHGGRQLDGA--PsTISALPAIVEAVGER-IEVWLDS 308
Cdd:cd00381 126 IKFIKKKYPNvDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgvP-QATAVADVAAAARDYgVPVIADG 204
|
90 100
....*....|....*....|....
gi 15597578 309 GIRSGQDVLKAIALGARGTMIGRP 332
Cdd:cd00381 205 GIRTSGDIVKALAAGADAVMLGSL 228
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
238-331 |
9.23e-04 |
|
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: 41.22 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 238 VEWIKRRWGGKLVLKG-ILDAEDARLAADSGADAL-------------VVSNHGGRQldgapstISALPAIVEAVGER-I 302
Cdd:pfam00478 252 VKWIKKKYPDVQVIAGnVATAEGAKALIEAGADAVkvgigpgsicttrVVAGVGVPQ-------LTAIYDVAEAAKKYgV 324
|
90 100 110
....*....|....*....|....*....|
gi 15597578 303 EVWLDSGIR-SGqDVLKAIALGARGTMIGR 331
Cdd:pfam00478 325 PVIADGGIKySG-DIVKALAAGADAVMLGS 353
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
285-327 |
1.09e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 40.24 E-value: 1.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15597578 285 PSTISALPAIVEAVGERIEVWLDSGIRSGQDVLKAIALGARGT 327
Cdd:PRK04302 157 PEVVEDAVEAVKKVNPDVKVLCGAGISTGEDVKAALELGADGV 199
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
260-341 |
1.46e-03 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 39.79 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597578 260 ARLAADSGADALVVsnHG--GRQLDGAPSTISALPAIVEAVgeRIEVWLDSGIRSGQDVLKAIAL-GARGTMIGRpylyg 336
Cdd:cd02801 144 AKALEDAGASALTV--HGrtREQRYSGPADWDYIAEIKEAV--SIPVIANGDIFSLEDALRCLEQtGVDGVMIGR----- 214
|
....*
gi 15597578 337 lGALG 341
Cdd:cd02801 215 -GALG 218
|
|
|