|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
1-367 |
0e+00 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 721.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 1 MEITNVTEYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAF 80
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPR 160
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 161 LGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDIQWLQTITNMPILVKGVLTGEDARI 240
Cdd:PLN02493 161 LGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 241 AIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFALAAEGE 320
Cdd:PLN02493 241 AIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15229497 321 AGVKKVLQMLRDEFELTMALSGCRSLSEITRNHIVTEWDTPRHLPRL 367
Cdd:PLN02493 321 AGVRKVLQMLRDEFELTMALSGCRSLKEISRNHITTEWDTPRPSARL 367
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
47-367 |
0e+00 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 599.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 47 FRPRILIDVNKIDMATTVLGFKISMPIMVAPTAFQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFF 126
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 127 QLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQ 206
Cdd:PLN02979 126 QLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 207 IDRTLSWKDIQWLQTITNMPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDG 286
Cdd:PLN02979 206 IDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 287 GVRRGTDVFKALALGASGIFIGRPVVFALAAEGEAGVKKVLQMLRDEFELTMALSGCRSLSEITRNHIVTEWDTPRHLPR 366
Cdd:PLN02979 286 GVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHITTEWDTPRPSAR 365
|
.
gi 15229497 367 L 367
Cdd:PLN02979 366 L 366
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
2-359 |
0e+00 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 508.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 2 EITNVTEYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAFQ 81
Cdd:PLN02535 4 EIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 82 KMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPRL 161
Cdd:PLN02535 84 KLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 162 GRRESDIKNRFTLPpnlTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDIQWLQTITNMPILVKGVLTGEDARIA 241
Cdd:PLN02535 164 GRREADIKNKMISP---QLKNFEGLLSTEVVSDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 242 IQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFALAAEGEA 321
Cdd:PLN02535 241 VEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGED 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 15229497 322 GVKKVLQMLRDEFELTMALSGCRSLSEITRNHIVTEWD 359
Cdd:PLN02535 321 GVRKVIEMLKDELEITMALSGCPSVKDITRSHVRTERE 358
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
13-356 |
4.26e-180 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 503.22 E-value: 4.26e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 13 AKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAFQKMAHPDGEYAT 92
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 93 ARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPRLGRRESDIKNRF 172
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 173 TLPPNLTLKNFE------GLDLGKMDEANDSGLASYVAGQIDRTLSWKDIQWLQTITNMPILVKGVLTGEDARIAIQAGA 246
Cdd:pfam01070 161 TLPPRLTPRNLLdlalhpRWALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 247 AGIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFALAAEGEAGVKKV 326
Cdd:pfam01070 241 DGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHA 320
|
330 340 350
....*....|....*....|....*....|
gi 15229497 327 LQMLRDEFELTMALSGCRSLSEITRNHIVT 356
Cdd:pfam01070 321 LEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
8-351 |
2.77e-162 |
|
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: 456.14 E-value: 2.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 8 EYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAFQKMAHPD 87
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 88 GEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPRLGRResd 167
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 168 iknrftlppnltlknfegldlgkmdeandsglasyvagqidrtLSWKDIQWLQTITNMPILVKGVLTGEDARIAIQAGAA 247
Cdd:cd02809 159 -------------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGAD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 248 GIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFALAAEGEAGVKKVL 327
Cdd:cd02809 196 GIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVL 275
|
330 340
....*....|....*....|....
gi 15229497 328 QMLRDEFELTMALSGCRSLSEITR 351
Cdd:cd02809 276 EILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
3-356 |
4.13e-160 |
|
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: 452.66 E-value: 4.13e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 3 ITNVTEYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAFQK 82
Cdd:COG1304 4 ILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 83 MAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPRLG 162
Cdd:COG1304 84 LAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 163 RRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDIQWLQTITNMPILVKGVLTGEDARIAI 242
Cdd:COG1304 164 RRERDLREGFSQPPRLTPRNLLEAATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSPEDARRAV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 243 QAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFALAAEGEAG 322
Cdd:COG1304 244 DAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAG 323
|
330 340 350
....*....|....*....|....*....|....
gi 15229497 323 VKKVLQMLRDEFELTMALSGCRSLSEITRNHIVT 356
Cdd:COG1304 324 VARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
8-349 |
3.77e-133 |
|
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: 383.87 E-value: 3.77e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 8 EYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAFQKMAHPD 87
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 88 GEYATARAASAAGTIMTLSSWATSSVEEV--ASTGPGIRFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPRLGRRE 165
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIvdARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 166 SDIKNRFTLPPnltlknfEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDIQWLQTITNMPILVKGVLTGEDARIAIQAG 245
Cdd:cd02922 162 RDERLKAEEAV-------SDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 246 AAGIIVSNHGARQLDYVPATISALEEVVK-ATQ--GRVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFALAAEGEAG 322
Cdd:cd02922 235 VDGIVLSNHGGRQLDTAPAPIEVLLEIRKhCPEvfDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEG 314
|
330 340
....*....|....*....|....*..
gi 15229497 323 VKKVLQMLRDEFELTMALSGCRSLSEI 349
Cdd:cd02922 315 VEKAIQILKDEIETTMRLLGVTSLDQL 341
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
1-354 |
1.96e-116 |
|
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: 341.73 E-value: 1.96e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 1 MEITNVTEYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAF 80
Cdd:cd04737 3 LDIINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGI-RFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTP 159
Cdd:cd04737 83 HGLAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGpKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 160 RLGRRESDIKNRFTLP---PNLTlKNFEGLDLGKMDeandsglaSYVAGQIDRTLSWKDIQWLQTITNMPILVKGVLTGE 236
Cdd:cd04737 163 VGGNREADIRNKFQFPfgmPNLN-HFSEGTGKGKGI--------SEIYAAAKQKLSPADIEFIAKISGLPVIVKGIQSPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 237 DARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFALA 316
Cdd:cd04737 234 DADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLA 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 15229497 317 AEGEAGVKKVLQMLRDEFELTMALSGCRSLSEITRNHI 354
Cdd:cd04737 314 LGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRTFL 351
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
4-354 |
5.10e-109 |
|
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: 323.85 E-value: 5.10e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 4 TNVTEYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAFQKM 83
Cdd:cd03332 19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 84 AHPDGEYATARAASAAGTIMTLSSWATSSVEEVA-STGPGIRFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPRLG 162
Cdd:cd03332 99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAaAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 163 RRESD-------------IKNRFTLPpnLTLKNFEGlDLGKMDEANDSGLAS---YVAGQIDRTLSWKDIQWLQTITNMP 226
Cdd:cd03332 179 WRPRDldlgylpflrgigIANYFSDP--VFRKKLAE-PVGEDPEAPPPMEAAvarFVSVFSGPSLTWEDLAFLREWTDLP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 227 ILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIF 306
Cdd:cd03332 256 IVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVL 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15229497 307 IGRPVVFALAAEGEAGVKKVLQMLRDEFELTMALSGCRSLSEITRNHI 354
Cdd:cd03332 336 IGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
8-351 |
1.19e-100 |
|
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: 301.75 E-value: 1.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 8 EYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAFQKMAHPD 87
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 88 GEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYkNRKVVEQLVRRAEKAGFKAIALTVDTPRLGRRESD 167
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVV-HRELAELLVKRALAAGYTTLVLTTDVAVNGYRERD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 168 IKNRFTLP--------------PNLTLKNFEGLDLGK----MDEANDSGL-ASYVAGQIDRTLSWKDIQWLQTITNMPIL 228
Cdd:cd04736 161 LRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPQLanfaSDDAIDVEVqAALMSRQMDASFNWQDLRWLRDLWPHKLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 229 VKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQgrVPVFLDGGVRRGTDVFKALALGASGIFIG 308
Cdd:cd04736 241 VKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATY--KPVLIDSGIRRGSDIVKALALGANAVLLG 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15229497 309 RPVVFALAAEGEAGVKKVLQMLRDEFELTMALSGCRSLSEITR 351
Cdd:cd04736 319 RATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
1-355 |
3.86e-83 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 257.64 E-value: 3.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 1 MEITNVTEYDAIAKAKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVNKIDMATTVLGFKISMPIMVAPTAF 80
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRKVVEQLVRRAEKAGFKAIALTVDTPR 160
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 161 LGRRESDIKNRFTLPPNLTLKNFEGL-------DLGKMDEAND-----------SGLASYVA---GQIDRTLSWKDIQWL 219
Cdd:PRK11197 161 PGARYRDAHSGMSGPNAAMRRYLQAVthpqwawDVGLNGRPHDlgnisaylgkpTGLEDYIGwlgNNFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 220 QTITNMPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRVPVFLDGGVRRGTDVFKALA 299
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15229497 300 LGASGIFIGRPVVFALAAEGEAGVKKVLQMLRDEFELTMALSGCRSLSEITRNHIV 355
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLV 376
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
226-351 |
6.43e-14 |
|
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.
Pssm-ID: 239205 [Multi-domain] Cd Length: 326 Bit Score: 71.76 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 226 PILVKGV---LTGEDARIAIQAGAAGIIVS----------------NHGARQLDY-----VPATISALEevVKATQGRVP 281
Cdd:cd02811 180 PVIVKEVgfgISRETAKRLADAGVKAIDVAgaggtswarvenyrakDSDQRLAEYfadwgIPTAASLLE--VRSALPDLP 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 282 VFLDGGVRRGTDVFKALALGASGIFIGRPVVFAlAAEGEAGVKKVLQMLRDEFELTMALSGCRSLSEITR 351
Cdd:cd02811 258 LIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEELRTAMFLTGAKNLAELKQ 326
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
193-309 |
4.78e-11 |
|
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: 61.45 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 193 EANDSGLASYVAGQIDRTLSWKDIQWL-QTITNMPILVKGVLTGEDARI-AIQAGAAGIIVSNHGARQL--DYVPATISA 268
Cdd:cd04722 82 AAGADGVEIHGAVGYLAREDLELIRELrEAVPDVKVVVKLSPTGELAAAaAEEAGVDEVGLGNGGGGGGgrDAVPIADLL 161
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15229497 269 LEEVVKATqgRVPVFLDGGVRRGTDVFKALALGASGIFIGR 309
Cdd:cd04722 162 LILAKRGS--KVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
216-356 |
5.75e-10 |
|
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: 60.25 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 216 IQWLQTITNM-PILVK---GVLTGEDARIAIQAGAAGIIVSNH----GARQL---DYV--PaTISALEEVVKATQG---- 278
Cdd:cd02808 205 IEDLREATGGkPIGVKlvaGHGEGDIAAGVAAAGADFITIDGAeggtGAAPLtfiDHVglP-TELGLARAHQALVKnglr 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 279 -RVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFALAA-----------------------------EGEAGVKKVLQ 328
Cdd:cd02808 284 dRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCiqarkchtntcpvgvatqdpelrrrldveGKAERVANYLK 363
|
170 180
....*....|....*....|....*...
gi 15229497 329 MLRDEFELTMALSGCRSLSEITRNHIVT 356
Cdd:cd02808 364 SLAEELRELAAALGKRSLELLGRSDLLA 391
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
216-318 |
5.62e-08 |
|
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: 53.68 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 216 IQWL-QTITNMPILVKGVLTGEDARIAIQAGAAGIIV-----SNHGAR--------QLdyvpatiSALEEVVKATQGR-V 280
Cdd:cd00381 126 IKFIkKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRivtgvgvpQA-------TAVADVAAAARDYgV 198
|
90 100 110
....*....|....*....|....*....|....*...
gi 15229497 281 PVFLDGGVRRGTDVFKALALGASGIFIGRPvvFALAAE 318
Cdd:cd00381 199 PVIADGGIRTSGDIVKALAAGADAVMLGSL--LAGTDE 234
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
232-308 |
9.03e-08 |
|
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: 52.49 E-value: 9.03e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229497 232 VLTGEDARIAIQAGAAGIIVSNHGA--RQLDYVPATISALEEVVKATqgRVPVFLDGGVRRGTDVFKALALGASGIFIG 308
Cdd:cd04730 109 VTSVEEARKAEAAGADALVAQGAEAggHRGTFDIGTFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
234-361 |
1.72e-07 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 52.04 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 234 TGEDARIAIQAGAAGIIVSNHGA---RQLDYVPaTISALEEVVKATqgRVPVFLDGGVRRGTDVFKALALGASGIFIGrp 310
Cdd:COG2070 113 SVREARKAEKAGADAVVAEGAEAgghRGADEVS-TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG-- 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15229497 311 VVFALAAEGEA--GVKkvlQMLRDEFE----LTMALSG--CRSLseitRNHIVTEWDTP 361
Cdd:COG2070 188 TRFLATEESPAheAYK---QALVDAKEedtvLTRSFTGrpARAL----RNSFTREGLDL 239
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
216-321 |
5.18e-07 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 51.12 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 216 IQWLQTIT-NMPILVKGVLTGEDARIAIQAGAAGI-------------IVSNHGARQLdyvpatiSALEEVVK-ATQGRV 280
Cdd:PTZ00314 273 IKKLKSNYpHVDIIAGNVVTADQAKNLIDAGADGLrigmgsgsicitqEVCAVGRPQA-------SAVYHVARyARERGV 345
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15229497 281 PVFLDGGVRRGTDVFKALALGASGIFIGRpvvfALAAEGEA 321
Cdd:PTZ00314 346 PCIADGGIKNSGDICKALALGADCVMLGS----LLAGTEEA 382
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
204-309 |
6.44e-06 |
|
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: 47.77 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 204 AGQIDRtlswkdIQWL-QTITNMPILVKGVLTGEDARIAIQAGAAGI-------------IVSNHGARQldyvpatISAL 269
Cdd:pfam00478 246 KGVIDT------VKWIkKKYPDVQVIAGNVATAEGAKALIEAGADAVkvgigpgsicttrVVAGVGVPQ-------LTAI 312
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15229497 270 EEVVKATQGR-VPVFLDGGVRRGTDVFKALALGASGIFIGR 309
Cdd:pfam00478 313 YDVAEAAKKYgVPVIADGGIKYSGDIVKALAAGADAVMLGS 353
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
214-315 |
2.72e-05 |
|
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: 45.79 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 214 KDIQWlqtitNMPILVKgvLTGEDARIAIQAGAAG-----IIVSNH----GARQL---DYV--PaTISALEEVVKAT--- 276
Cdd:pfam01645 197 KEINP-----KAPISVK--LVSGHGVGTIAAGVAKagadiILIDGYdggtGASPKtsiKHAglP-WELALAEAHQTLken 268
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15229497 277 --QGRVPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFAL 315
Cdd:pfam01645 269 glRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIAL 309
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
227-342 |
5.76e-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: 44.43 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 227 ILVKGVLTGEDARIAIQAGAAGIIVS------NHGARQLDYVpATISALEEVVKATQgrVPVFLDGGVRRGTDVFKALAL 300
Cdd:pfam03060 138 ALIPTISSAKEARIAEARGADALIVQgpeaggHQGTPEYGDK-GLFRLVPQVPDAVD--IPVIAAGGIWDRRGVAAALAL 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15229497 301 GASGIFIGrpVVFALAAEGEAGV---KKVLQMLRDEFELTMALSG 342
Cdd:pfam03060 215 GASGVQMG--TRFLLTKESGAHDahkQKITEAGEDDTLVTSPFSG 257
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
216-326 |
6.77e-05 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 44.29 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 216 IQWLQTITNMPILVKgvLT------GEDARIAIQAGAAGIIVSN----------HGARQLDYVPATIS-------ALE-- 270
Cdd:COG0167 149 LAAVKAATDKPVLVK--LApdltdiVEIARAAEEAGADGVIAINttlgraidleTRRPVLANEAGGLSgpalkpiALRmv 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229497 271 -EVVKATQGRVPVFLDGGVRRGTDVFKALALGAS------GIFIGRPVVFALAAEG------EAGVKKV 326
Cdd:COG0167 227 rEVAQAVGGDIPIIGVGGISTAEDALEFILAGASavqvgtALFYEGPGLVRRIIRGleayleEKGFSSI 295
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
226-348 |
5.52e-04 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 41.65 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 226 PILVKGV--LTGED----ARIAIQAGAAGIIVSNHGARQLDYVPATISA------------------LEEVVKATQGRVP 281
Cdd:PLN02826 264 PLLVKIApdLSKEDlediAAVALALGIDGLIISNTTISRPDSVLGHPHAdeagglsgkplfdlstevLREMYRLTRGKIP 343
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229497 282 VFLDGGVRRGTDVFKALALGASGIfigrPVVFALAAEGEAgvkkVLQMLRDEFELTMALSGCRSLSE 348
Cdd:PLN02826 344 LVGCGGVSSGEDAYKKIRAGASLV----QLYTAFAYEGPA----LIPRIKAELAACLERDGFKSIQE 402
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
137-308 |
6.99e-04 |
|
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: 40.39 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 137 VEQLVRRAEKAGFKAIALTVDTPRLGRRE---SDIK-----NRFTLPPNLTLKNFEgldlgkMDEANDSGlASYVA---- 204
Cdd:cd00945 15 IAKLCDEAIEYGFAAVCVNPGYVRLAADAlagSDVPvivvvGFPTGLTTTEVKVAE------VEEAIDLG-ADEIDvvin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 205 -GQIDRTLSWKDIQWLQTITN--------MPILVKGVLTGED-----ARIAIQAGAAGIIVSNHGArqldYVPATISALE 270
Cdd:cd00945 88 iGSLKEGDWEEVLEEIAAVVEaadgglplKVILETRGLKTADeiakaARIAAEAGADFIKTSTGFG----GGGATVEDVK 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 15229497 271 EVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIFIG 308
Cdd:cd00945 164 LMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
238-309 |
1.97e-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: 39.40 E-value: 1.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229497 238 ARIAIQAGAAGIIVsnHG-ARQLDYV-PATISALEEVVKATqgRVPVFLDGGVRRGTDVFKALAL-GASGIFIGR 309
Cdd:cd02801 144 AKALEDAGASALTV--HGrTREQRYSgPADWDYIAEIKEAV--SIPVIANGDIFSLEDALRCLEQtGVDGVMIGR 214
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
238-354 |
2.84e-03 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 39.31 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229497 238 ARIAIQAGAAGIIVsnHG--ARQLDYVPATISALEEVVKATqgRVPVFLDGGVRRGTDVFKALAL-GASGIFIGR----- 309
Cdd:COG0042 152 ARIAEDAGAAALTV--HGrtREQRYKGPADWDAIARVKEAV--SIPVIGNGDIFSPEDAKRMLEEtGCDGVMIGRgalgn 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15229497 310 PVVFALAAEGEAG-------VKKVLQMLRDEFELTMALSGCR-SLSEITRnHI 354
Cdd:COG0042 228 PWLFREIDAYLAGgeapppsLEEVLELLLEHLELLLEFYGERrGLRRMRK-HL 279
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
232-305 |
3.98e-03 |
|
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway
Pssm-ID: 440563 Cd Length: 213 Bit Score: 38.14 E-value: 3.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229497 232 VLTGEDARIAIQAGAAgIIVSnhgarqldyvPATIsalEEVVKATQGR-VPVFLdgGVRRGTDVFKALALGASGI 305
Cdd:COG0800 72 VLTPEQARAAIAAGAR-FIVS----------PGLD---PEVIKAANRAgLPVLP--GVATPTEIMAALEAGADAV 130
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
266-309 |
4.84e-03 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 38.65 E-value: 4.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15229497 266 ISALEEVVKATQGRVPVFLDGGVRRGTDVFKALALGASGIFIGR 309
Cdd:COG0516 184 LSAAMDTVTEARMAIAIAADGGIGYIHDNAKALAAGADAVMLGS 227
|
|
| |
