|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
26-326 |
4.62e-151 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 431.96 E-value: 4.62e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 26 AREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMST 105
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 106 ARAAQAAGICYITSTFASCSLEDIViAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQ 185
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVA-AAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 186 LRRNLTLTD----------------LQSPKKGNAIPYFQMTpISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKH 249
Cdd:pfam01070 160 FTLPPRLTPrnlldlalhprwalgvLRRGGAGGAAAFVGSQ-FDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453353 250 NVQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAckAAG 326
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLA--AGG 313
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
21-326 |
8.83e-151 |
|
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: 429.17 E-value: 8.83e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRrh 180
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 181 dirnqlrrnltltdlqspkkgnaipyfqmtpistsLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQGIIVSNHG 260
Cdd:cd02809 159 -----------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHG 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453353 261 GRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAckAAG 326
Cdd:cd02809 204 GRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLA--AGG 267
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
17-327 |
3.48e-135 |
|
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: 391.80 E-value: 3.48e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:COG1304 5 LSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:COG1304 85 AHPDGELALARAAAAAGIPMGLSTQSTTSLEE-VAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 177 NRRHDIRNQLR-------RNLT--LTDLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAV 247
Cdd:COG1304 164 RRERDLREGFSqpprltpRNLLeaATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSPEDARRAV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 248 KHNVQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAckAAGR 327
Cdd:COG1304 244 DAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLA--AGGE 321
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
21-322 |
6.38e-116 |
|
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.
Pssm-ID: 239238 [Multi-domain] Cd Length: 344 Bit Score: 342.27 E-value: 6.38e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGL-RWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR 179
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQpLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 180 HDIRnqLRRNLTLTDLQSPKKGNAIPYFQMTP----ISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQGII 255
Cdd:cd02922 162 RDER--LKAEEAVSDGPAGKKTKAKGGGAGRAmsgfIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 256 VSNHGGRQLDEVLASIDALTEVV---AAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAC 322
Cdd:cd02922 240 LSNHGGRQLDTAPAPIEVLLEIRkhcPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSA 309
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
17-323 |
8.33e-106 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 317.16 E-value: 8.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:PLN02535 86 AHPEGEIATARAAAACNTIMVLSFMASCTVEE-VASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 177 NRRHDIRNQL----RRNLT--LTDLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHN 250
Cdd:PLN02535 165 RREADIKNKMispqLKNFEglLSTEVVSDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVEVG 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370453353 251 VQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACK 323
Cdd:PLN02535 245 VAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAK 317
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
17-321 |
1.13e-105 |
|
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: 317.30 E-value: 1.13e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:cd03332 19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:cd03332 99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 177 NRRHDIRN----QLR-RNLT--LTD------LQSPKKGN---------AIPYFQMTPISTSLCWNDLSWFQSITRLPIIL 234
Cdd:cd03332 179 WRPRDLDLgylpFLRgIGIAnyFSDpvfrkkLAEPVGEDpeapppmeaAVARFVSVFSGPSLTWEDLAFLREWTDLPIVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 235 KGILTKEDAELAVKHNVQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 314
Cdd:cd03332 259 KGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGR 338
|
....*..
gi 1370453353 315 PILWGLA 321
Cdd:cd03332 339 PYAYGLA 345
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
14-349 |
1.75e-95 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 290.86 E-value: 1.75e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 14 MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGF 93
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 94 HCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTP 173
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 174 VCGNRRHDIRNQ--LRRNLTLTDLQSPKKG-------NAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAE 244
Cdd:PLN02493 160 RLGRRESDIKNRftLPPNLTLKNFEGLDLGkmdeandSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 245 LAVKHNVQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKA 324
Cdd:PLN02493 240 IAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEG 319
|
330 340 350
....*....|....*....|....*....|..
gi 1370453353 325 -AG-----RSLR-SIETWSSFPGCKKKGPITR 349
Cdd:PLN02493 320 eAGvrkvlQMLRdEFELTMALSGCRSLKEISR 351
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
16-326 |
2.14e-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: 277.40 E-value: 2.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 16 LVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHC 95
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 96 LVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVC 175
Cdd:cd04737 85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 176 GNRRHDIRNQLRRNLTLTDLQSPKKGNAIP---YFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQ 252
Cdd:cd04737 165 GNREADIRNKFQFPFGMPNLNHFSEGTGKGkgiSEIYAAAKQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAINAGAD 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370453353 253 GIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKAAG 326
Cdd:cd04737 245 GIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQ 318
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
60-349 |
3.78e-81 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 254.26 E-value: 3.78e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 60 LRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRW 139
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 140 FQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQ--LRRNLTLTDLQSPKKG-------NAIPYFQMT 210
Cdd:PLN02979 125 FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRftLPPNLTLKNFEGLDLGkmdeandSGLASYVAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 211 PISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLD 290
Cdd:PLN02979 205 QIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLD 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453353 291 GGVRTGNDVLKALALGAKCIFLGRPILWGLACKA-AG-----RSLR-SIETWSSFPGCKKKGPITR 349
Cdd:PLN02979 285 GGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGeAGvrkvlQMLRdEFELTMALSGCRSLKEISR 350
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
21-323 |
1.53e-78 |
|
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: 247.05 E-value: 1.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAApEGLRWFQLYV-HPDLQlnKQLIQRVESLGFKALVITLDTPVCGNRR 179
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQA-DGDLWFQLYVvHRELA--ELLVKRALAAGYTTLVLTTDVAVNGYRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 180 HDIRNQ---------------------LRRNLTLTDLQ-----SPKKGN-----AIPYFQMtpiSTSLCWNDLSWFQSIT 228
Cdd:cd04736 159 RDLRNGfaipfrytprvlldgilhprwLLRFLRNGMPQlanfaSDDAIDvevqaALMSRQM---DASFNWQDLRWLRDLW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 229 RLPIILKGILTKEDAELAVKHNVQGIIVSNHGGRQLDEVLASIDALTEVVAAVkgKIEVYLDGGVRTGNDVLKALALGAK 308
Cdd:cd04736 236 PHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGAN 313
|
330
....*....|....*
gi 1370453353 309 CIFLGRPILWGLACK 323
Cdd:cd04736 314 AVLLGRATLYGLAAR 328
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
14-327 |
2.58e-75 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 239.54 E-value: 2.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 14 MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGF 93
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 94 HCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTP 173
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEE-VAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 174 VCGNRRHDIRN-------QLRRNLtltdlQSPKK----------------GNAIPYFQmTPIS-------------TSLC 217
Cdd:PRK11197 160 VPGARYRDAHSgmsgpnaAMRRYL-----QAVTHpqwawdvglngrphdlGNISAYLG-KPTGledyigwlgnnfdPSIS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 218 WNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGN 297
Cdd:PRK11197 234 WKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGL 313
|
330 340 350
....*....|....*....|....*....|
gi 1370453353 298 DVLKALALGAKCIFLGRPILWGLAckAAGR 327
Cdd:PRK11197 314 DVVRMIALGADTVLLGRAFVYALA--AAGQ 341
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
95-314 |
1.04e-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: 63.76 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 95 CLVWPDGEMS---TARAAQAAGICYITSTFASCSLEDI---------VIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLG 162
Cdd:cd04722 5 LLAGGPSGDPvelAKAAAEAGADAIIVGTRSSDPEEAEtddkevlkeVAAETDLPLGVQLAINDAAAAVDIAAAAARAAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 163 FKALVITLDtpvCGNRRHDIRNQLRRnltltdlqspkkgnaipyfqmtpistsLCwndlswfQSITRLPIILKGILT-KE 241
Cdd:cd04722 85 ADGVEIHGA---VGYLAREDLELIRE---------------------------LR-------EAVPDVKVVVKLSPTgEL 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370453353 242 DAELAVKHNVQGIIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 314
Cdd:cd04722 128 AAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
55-335 |
1.29e-09 |
|
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: 59.05 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 55 FKRIRLRPRYLR--DVSEVDTRTTIQGEEISAPICI-APTGFHclvwPDGE---MSTARAAQAAGIcyitsTFASCS--- 125
Cdd:cd02811 22 FDDVRLVHNALPelDLDDIDLSTEFLGKRLSAPLLIsAMTGGS----EKAKeinRNLAEAAEELGI-----AMGVGSqra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 126 -LEDiviaaPEGLRWFQL--YVHPDL---------QLNK---QLIQR-VESLGFKALVITLDTP-----VCGNRrhDIRN 184
Cdd:cd02811 93 aLED-----PELAESFTVvrEAPPNGplianlgavQLNGygvEEARRaVEMIEADALAIHLNPLqeavqPEGDR--DFRG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 185 QLRRnltLTDLQSpkkgnAIPYfqmtpistslcwndlswfqsitrlPIILK----GIlTKEDAELAVKHNVQGIIVSNHG 260
Cdd:cd02811 166 WLER---IEELVK-----ALSV------------------------PVIVKevgfGI-SRETAKRLADAGVKAIDVAGAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 261 G-----------RQLDEVLASI---------DALTEVVAAVKgKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILwgl 320
Cdd:cd02811 213 GtswarvenyraKDSDQRLAEYfadwgiptaASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL--- 288
|
330
....*....|....*....
gi 1370453353 321 acKAAGRS----LRSIETW 335
Cdd:cd02811 289 --KAALEGeeavIETIEQI 305
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
231-327 |
4.61e-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: 51.39 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 231 PIILK---GILTKEDAELAVKHNVQGIIVSNHGG-------RQLDEV-LASIDALTEVV-----AAVKGKIEVYLDGGVR 294
Cdd:cd02808 216 PIGVKlvaGHGEGDIAAGVAAAGADFITIDGAEGgtgaaplTFIDHVgLPTELGLARAHqalvkNGLRDRVSLIASGGLR 295
|
90 100 110
....*....|....*....|....*....|...
gi 1370453353 295 TGNDVLKALALGAKCIFLGRPILWGLACKAAGR 327
Cdd:cd02808 296 TGADVAKALALGADAVGIGTAALIALGCIQARK 328
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
246-327 |
1.19e-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: 46.94 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 246 AVKHNVQGIIVSNHGGRQLDEVLASID--------ALTEVVAAVK-----GKIEVYLDGGVRTGNDVLKALALGAKCIFL 312
Cdd:pfam01645 222 VAKAGADIILIDGYDGGTGASPKTSIKhaglpwelALAEAHQTLKenglrDRVSLIADGGLRTGADVAKAAALGADAVYI 301
|
90
....*....|....*
gi 1370453353 313 GRPILWGLACKAAGR 327
Cdd:pfam01645 302 GTAALIALGCIMCRV 316
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
229-315 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453353 229 RLPIILKGILTKEDAELAVKHNVQGIIV-----SNHGGRqldEVLAS----IDALTEVVAAVKG-KIEVYLDGGVRTGND 298
Cdd:cd00381 135 NVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTR---IVTGVgvpqATAVADVAAAARDyGVPVIADGGIRTSGD 211
|
90
....*....|....*..
gi 1370453353 299 VLKALALGAKCIFLGRP 315
Cdd:cd00381 212 IVKALAAGADAVMLGSL 228
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
290-314 |
1.14e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 41.11 E-value: 1.14e-03
10 20
....*....|....*....|....*
gi 1370453353 290 DGGVRTGNDVLKALALGAKCIFLGR 314
Cdd:PTZ00314 350 DGGIKNSGDICKALALGADCVMLGS 374
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
239-307 |
2.32e-03 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 39.39 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370453353 239 TKEDAELAVKHNVQGIIVSNH--GGRQLDEVLASIDALTEVVAAVKgkIEVYLDGGVRTGNDVLKALALGA 307
Cdd:cd04730 111 SVEEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGA 179
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
273-314 |
3.42e-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: 39.42 E-value: 3.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1370453353 273 ALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 314
Cdd:COG0516 186 AAMDTVTEARMAIAIAADGGIGYIHDNAKALAAGADAVMLGS 227
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
268-307 |
5.05e-03 |
|
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439839 Cd Length: 728 Bit Score: 39.08 E-value: 5.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1370453353 268 LASID--------ALTEVVAA-----VKGKIEVYLDGGVRTGNDVLKALALGA 307
Cdd:COG0069 411 LESIKhaglpwelGLAEVHQTlvgngLRDRIRLIADGKLKTGRDVAIAAALGA 463
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
273-314 |
5.37e-03 |
|
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: 38.91 E-value: 5.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1370453353 273 ALTEVVAAVKG-KIEVYLDGGVRTGNDVLKALALGAKCIFLGR 314
Cdd:pfam00478 311 AIYDVAEAAKKyGVPVIADGGIKYSGDIVKALAAGADAVMLGS 353
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
267-313 |
7.18e-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: 37.69 E-value: 7.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1370453353 267 VLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLG 313
Cdd:cd00945 155 GGATVEDVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| |
