|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
13-349 |
1.17e-168 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 473.56 E-value: 1.17e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 13 AQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSIAWADGEKST 92
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 93 AKAAQKANICYVISSYASYTVEDIVAAApGGLHWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVLGNRRGNKRSL 172
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 173 LDLEANIKLK----DLRSPGESKSGLPTPLSMPSS---------SSCWNDLPLLQSMTRLPIILKGILTKEDAELAVKHN 239
Cdd:pfam01070 160 FTLPPRLTPRnlldLALHPRWALGVLRRGGAGGAAafvgsqfdpALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 240 IRGIIVSNHGGRQLDEVPASIDALREVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFLGRPIIWGLACKGEDGVKE 319
Cdd:pfam01070 240 VDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAH 319
|
330 340 350
....*....|....*....|....*....|
gi 254281176 320 VLDILKEELHTCMALSGCRSVAEISPDLIQ 349
Cdd:pfam01070 320 ALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
7-345 |
2.15e-164 |
|
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: 460.76 E-value: 2.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 7 ADFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSIAWA 86
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 87 DGEKSTAKAAQKANICYVISSYASYTVEDIVAAAPGGLhWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVLGNRR 166
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPR-WFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 167 gnkrslldleaniklkdlrspgesksglptplsmpssssCWNDLPLLQSMTRLPIILKGILTKEDAELAVKHNIRGIIVS 246
Cdd:cd02809 160 ---------------------------------------TWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 247 NHGGRQLDEVPASIDALREVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFLGRPIIWGLACKGEDGVKEVLDILKE 326
Cdd:cd02809 201 NHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRD 280
|
330
....*....|....*....
gi 254281176 327 ELHTCMALSGCRSVAEISP 345
Cdd:cd02809 281 ELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
4-348 |
7.68e-151 |
|
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: 428.78 E-value: 7.68e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 4 LCLADFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSI 83
Cdd:COG1304 5 LSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 84 AWADGEKSTAKAAQKANICYVISSYASYTVEDIVAAAPGGLhWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVLG 163
Cdd:COG1304 85 AHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPL-WFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 164 NRRGNKRSLLDLEANIKLK---DLRSPGESKSGLPTPLSMP----SSSSCWNDLPLLQSMTRLPIILKGILTKEDAELAV 236
Cdd:COG1304 164 RRERDLREGFSQPPRLTPRnllEAATHPRWALGLASLAAWLdtnfDPSLTWDDIAWLRERWPGPLIVKGVLSPEDARRAV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 237 KHNIRGIIVSNHGGRQLDEVPASIDALREVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFLGRPIIWGLACKGEDG 316
Cdd:COG1304 244 DAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAG 323
|
330 340 350
....*....|....*....|....*....|..
gi 254281176 317 VKEVLDILKEELHTCMALSGCRSVAEISPDLI 348
Cdd:COG1304 324 VARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
8-345 |
1.25e-129 |
|
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: 374.63 E-value: 1.25e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 8 DFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSIAWAD 87
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 88 GEKSTAKAAQKANICYVISSYASYTVEDIVAAAPGGL-HWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVLGNRR 166
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQpLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 167 GNKRSLLDLEANIKLKDLRSPGESKSGLPTPLSMPSSSSCWNDLPLLQSMTRLPIILKGILTKEDAELAVKHNIRGIIVS 246
Cdd:cd02922 162 RDERLKAEEAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 247 NHGGRQLDEVPASIDALREVV---AAVNGKIEVYMDGGVRTGNDVLKALALGARCIFLGRPIIWGLACKGEDGVKEVLDI 323
Cdd:cd02922 242 NHGGRQLDTAPAPIEVLLEIRkhcPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQI 321
|
330 340
....*....|....*....|..
gi 254281176 324 LKEELHTCMALSGCRSVAEISP 345
Cdd:cd02922 322 LKDEIETTMRLLGVTSLDQLGP 343
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
8-344 |
2.87e-112 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 331.03 E-value: 2.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 8 DFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSIAWAD 87
Cdd:PLN02535 10 EFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLAHPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 88 GEKSTAKAAQKANICYVISSYASYTVEDiVAAAPGGLHWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVLGNRrg 167
Cdd:PLN02535 90 GEIATARAAAACNTIMVLSFMASCTVEE-VASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGRR-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 168 nkrslldlEANIKLKDLRSPGESKSGLPTPLSMPS--------------SSSCWNDLPLLQSMTRLPIILKGILTKEDAE 233
Cdd:PLN02535 167 --------EADIKNKMISPQLKNFEGLLSTEVVSDkgsgleafasetfdASLSWKDIEWLRSITNLPILIKGVLTREDAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 234 LAVKHNIRGIIVSNHGGRQLDEVPASIDALREVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFLGRPIIWGLACKG 313
Cdd:PLN02535 239 KAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKG 318
|
330 340 350
....*....|....*....|....*....|.
gi 254281176 314 EDGVKEVLDILKEELHTCMALSGCRSVAEIS 344
Cdd:PLN02535 319 EDGVRKVIEMLKDELEITMALSGCPSVKDIT 349
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
6-348 |
1.09e-110 |
|
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: 327.70 E-value: 1.09e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 6 LADFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSIAW 85
Cdd:cd03332 21 PERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 86 ADGEKSTAKAAQKANICYVISSYASYTVEDIVAAAPGGLHWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVLGNR 165
Cdd:cd03332 101 PDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 166 --------------RGNKRSLLDLEANIKLKdlRSPGESKSGLPTP----------LSMPSSSscWNDLPLLQSMTRLPI 221
Cdd:cd03332 181 prdldlgylpflrgIGIANYFSDPVFRKKLA--EPVGEDPEAPPPMeaavarfvsvFSGPSLT--WEDLAFLREWTDLPI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 222 ILKGILTKEDAELAVKHNIRGIIVSNHGGRQLDEVPASIDALREVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFL 301
Cdd:cd03332 257 VLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLI 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 254281176 302 GRPIIWGLACKGEDGVKEVLDILKEELHTCMALSGCRSVAEISPDLI 348
Cdd:cd03332 337 GRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
1-348 |
2.18e-101 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 303.58 E-value: 2.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 1 MSLLCLADFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAF 80
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 81 HSIAWADGEKSTAKAAQKANICYVISSYASYTVEDIVAAAPGgLHWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAP 160
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPG-IRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 161 VLGNRRGNKRSLLDLEANIKLK-----DLRSPGESK-SGLPTPLS-MPSSSSCWNDLPLLQSMTRLPIILKGILTKEDAE 233
Cdd:PLN02493 160 RLGRRESDIKNRFTLPPNLTLKnfeglDLGKMDEANdSGLASYVAgQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 234 LAVKHNIRGIIVSNHGGRQLDEVPASIDALREVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFLGRPIIWGLACKG 313
Cdd:PLN02493 240 IAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEG 319
|
330 340 350
....*....|....*....|....*....|....*
gi 254281176 314 EDGVKEVLDILKEELHTCMALSGCRSVAEISPDLI 348
Cdd:PLN02493 320 EAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 354
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
6-344 |
2.69e-101 |
|
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: 302.82 E-value: 2.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 6 LADFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSIAW 85
Cdd:cd04737 8 LYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 86 ADGEKSTAKAAQKANICYVISSYASYTVEDIVAAAPGGLHWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVLGNR 165
Cdd:cd04737 88 ATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGGNR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 166 RGNKR--SLLDLEANIKLKDLRSPGESKsGLPTPLSMPSSSSCWNDLPLLQSMTRLPIILKGILTKEDAELAVKHNIRGI 243
Cdd:cd04737 168 EADIRnkFQFPFGMPNLNHFSEGTGKGK-GISEIYAAAKQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAINAGADGI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 244 IVSNHGGRQLDEVPASIDALREVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFLGRPIIWGLACKGEDGVKEVLDI 323
Cdd:cd04737 247 WVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVLEH 326
|
330 340
....*....|....*....|.
gi 254281176 324 LKEELHTCMALSGCRSVAEIS 344
Cdd:cd04737 327 LNKELKIVMQLAGTRTIEDVK 347
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
47-348 |
2.78e-91 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 277.76 E-value: 2.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 47 LRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSIAWADGEKSTAKAAQKANICYVISSYASYTVEDIVAAAPGgLHW 126
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPG-IRF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 127 FQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVLGNRRGNKRSLLDLEANIKLK-----DLRSPGESK-SGLPTPLS- 199
Cdd:PLN02979 125 FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKnfeglDLGKMDEANdSGLASYVAg 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 200 MPSSSSCWNDLPLLQSMTRLPIILKGILTKEDAELAVKHNIRGIIVSNHGGRQLDEVPASIDALREVVAAVNGKIEVYMD 279
Cdd:PLN02979 205 QIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLD 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254281176 280 GGVRTGNDVLKALALGARCIFLGRPIIWGLACKGEDGVKEVLDILKEELHTCMALSGCRSVAEISPDLI 348
Cdd:PLN02979 285 GGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 353
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
7-345 |
9.81e-86 |
|
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: 263.23 E-value: 9.81e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 7 ADFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAFHSIAWA 86
Cdd:cd04736 1 EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 87 DGEKSTAKAAQKANICYVISSYASYTVEDIVAAAPGGLhWFQLYV-QPDwdINKQMVQRIEALGFKALVVTVDAPVLGNR 165
Cdd:cd04736 81 NGDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDL-WFQLYVvHRE--LAELLVKRALAAGYTTLVLTTDVAVNGYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 166 ------------RGNKRSLLD--LEANIKLKDLRS--PG------ESKSGLPTPLSMPS----SSSCWNDLPLLQSMTRL 219
Cdd:cd04736 158 erdlrngfaipfRYTPRVLLDgiLHPRWLLRFLRNgmPQlanfasDDAIDVEVQAALMSrqmdASFNWQDLRWLRDLWPH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 220 PIILKGILTKEDAELAVKHNIRGIIVSNHGGRQLDEVPASIDALREVVAAvNGKiEVYMDGGVRTGNDVLKALALGARCI 299
Cdd:cd04736 238 KLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAA-TYK-PVLIDSGIRRGSDIVKALALGANAV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 254281176 300 FLGRPIIWGLACKGEDGVKEVLDILKEELHTCMALSGCRSVAEISP 345
Cdd:cd04736 316 LLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
1-348 |
1.55e-75 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 237.61 E-value: 1.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 1 MSLLCLADFKAQAQKQLSKTSWDFIEGEADDGITYNDNLAAFRRIRLRPRYLRDVSKIDTRTTIQGQEINAPICISPTAF 80
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 81 HSIAWADGEKSTAKAAQKANICYVISSYASYTVEDiVAAAPGGLHWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAP 160
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEE-VAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 161 VLGNRRGNKRSLL---------------------DLEANIKLKDLrspGESKSGLPTPLSM------------PSSSscW 207
Cdd:PRK11197 160 VPGARYRDAHSGMsgpnaamrrylqavthpqwawDVGLNGRPHDL---GNISAYLGKPTGLedyigwlgnnfdPSIS--W 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 208 NDLPLLQSMTRLPIILKGILTKEDAELAVKHNIRGIIVSNHGGRQLDEVPASIDALREVVAAVNGKIEVYMDGGVRTGND 287
Cdd:PRK11197 235 KDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLD 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254281176 288 VLKALALGARCIFLGRPIIWGLACKGEDGVKEVLDILKEELHTCMALSGCRSVAEISPDLI 348
Cdd:PRK11197 315 VVRMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
220-342 |
9.71e-16 |
|
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: 76.77 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 220 PIILK----GIlTKEDAELAVKHNIRGIIVSNHGG---------RQLDEVPASIDALREV----------VAAVNGKIEV 276
Cdd:cd02811 180 PVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSDQRLAEYFADWgiptaaslleVRSALPDLPL 258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254281176 277 YMDGGVRTGNDVLKALALGARCIFLGRPIIwGLACKGEDGVKEVLDILKEELHTCMALSGCRSVAE 342
Cdd:cd02811 259 IASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVIETIEQIIEELRTAMFLTGAKNLAE 323
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
93-303 |
3.28e-06 |
|
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: 47.20 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 93 AKAAQKANICYVISSYAS----------YTVEDIVAAAPGGLHWFQLYVQPDWDINKQMVQRIEALGFKALVVTVDAPVL 162
Cdd:cd04722 18 AKAAAEAGADAIIVGTRSsdpeeaetddKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 163 gnrrgnkrsllDLEANIKLKDLRSPgesksglptplsmpsssscWNDLPLlqsmtrlpIILKGILTKEDAELAVKHNIRG 242
Cdd:cd04722 98 -----------AREDLELIRELREA-------------------VPDVKV--------VVKLSPTGELAAAAAEEAGVDE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254281176 243 IIVSNHGGRQL--DEVPASIDALREVVAAVNGKIEVymDGGVRTGNDVLKALALGARCIFLGR 303
Cdd:cd04722 140 VGLGNGGGGGGgrDAVPIADLLLILAKRGSKVPVIA--GGGINDPEDAAEALALGADGVIVGS 200
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
218-342 |
3.98e-05 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 45.11 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 218 RLPIILK--GILTKED----AELAVKHNIRGIIVSNHGGRQLDEVPA------------------SIDALREVVAAVNGK 273
Cdd:PLN02826 262 PPPLLVKiaPDLSKEDlediAAVALALGIDGLIISNTTISRPDSVLGhphadeagglsgkplfdlSTEVLREMYRLTRGK 341
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254281176 274 IEVYMDGGVRTGNDVLKALALGARCIFLGRpiiwGLACKGedgvKEVLDILKEELHTCMALSGCRSVAE 342
Cdd:PLN02826 342 IPLVGCGGVSSGEDAYKKIRAGASLVQLYT----AFAYEG----PALIPRIKAELAACLERDGFKSIQE 402
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
260-303 |
1.78e-04 |
|
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: 42.91 E-value: 1.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 254281176 260 IDALREVVAAVNG-----KIEVYMDGGVRTGNDVLKALALGARCIFLGR 303
Cdd:cd02808 267 ELGLARAHQALVKnglrdRVSLIASGGLRTGADVAKALALGADAVGIGT 315
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
262-304 |
4.19e-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: 41.73 E-value: 4.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 254281176 262 ALREVVAAVNG-KIEVYMDGGVRTGNDVLKALALGARCIFLGRP 304
Cdd:cd00381 185 AVADVAAAARDyGVPVIADGGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
220-296 |
9.76e-04 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 40.56 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281176 220 PIILKgI---LTKED----AELAVKHNIRGIIVSN--------HGGRQLDEV---------PASIDALREVVAAVNGKIE 275
Cdd:cd04738 204 PLLVK-IapdLSDEElediADVALEHGVDGIIATNttisrpglLRSPLANETgglsgaplkERSTEVLRELYKLTGGKIP 282
|
90 100
....*....|....*....|.
gi 254281176 276 VYMDGGVRTGNDVLKALALGA 296
Cdd:cd04738 283 IIGVGGISSGEDAYEKIRAGA 303
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
262-312 |
1.24e-03 |
|
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: 40.39 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 254281176 262 ALREVVAAV--NG---KIEVYMDGGVRTGNDVLKALALGARCIFLGRPIIWGLACK 312
Cdd:pfam01645 257 ALAEAHQTLkeNGlrdRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCI 312
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
279-303 |
1.29e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 40.34 E-value: 1.29e-03
10 20
....*....|....*....|....*
gi 254281176 279 DGGVRTGNDVLKALALGARCIFLGR 303
Cdd:PTZ00314 350 DGGIKNSGDICKALALGADCVMLGS 374
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
256-302 |
1.88e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 38.85 E-value: 1.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 254281176 256 VPASIDALREVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFLG 302
Cdd:cd00945 155 GGATVEDVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
265-301 |
6.04e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 37.54 E-value: 6.04e-03
10 20 30
....*....|....*....|....*....|....*..
gi 254281176 265 EVVAAVNGKIEVYMDGGVRTGNDVLKALALGARCIFL 301
Cdd:PRK04302 165 EAVKKVNPDVKVLCGAGISTGEDVKAALELGADGVLL 201
|
|
| |
