|
Name |
Accession |
Description |
Interval |
E-value |
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
21-286 |
6.91e-131 |
|
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: 373.32 E-value: 6.91e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR- 179
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRLt 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 180 -HDIRnQLRRnltLTDLQ-----------------------------------SPKKIDALTEVVAAVKGKIEVYLDGGV 223
Cdd:cd02809 161 wDDLA-WLRS---QWKGPlilkgiltpedalravdagadgivvsnhggrqldgAPATIDALPEIVAAVGGRIEVLLDGGI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796958726 224 RTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINR 286
Cdd:cd02809 237 RRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
26-290 |
4.97e-122 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 352.99 E-value: 4.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 26 AREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMST 105
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 106 ARAAQAAGICYITSTFASCSLEDIViAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN- 184
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVA-AAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 185 ----------------------------------------QLRRNLTLTDLQ---------------------------- 196
Cdd:pfam01070 160 ftlpprltprnlldlalhprwalgvlrrggaggaaafvgsQFDPALTWDDLAwlrerwkgplvvkgilspedakraveag 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 197 ----------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKE 260
Cdd:pfam01070 240 vdgivvsnhggrqldgAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAH 319
|
330 340 350
....*....|....*....|....*....|
gi 1796958726 261 VLNILTNEFHTSMALTGCRSVAEINRNLVQ 290
Cdd:pfam01070 320 ALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
17-289 |
2.01e-109 |
|
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: 321.31 E-value: 2.01e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:COG1304 5 LSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:COG1304 85 AHPDGELALARAAAAAGIPMGLSTQSTTSLEE-VAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 177 NRRHDIRN-----------------------------------QLRRNLTLTDL-----QSPKK---------------- 200
Cdd:COG1304 164 RRERDLREgfsqpprltprnlleaathprwalglaslaawldtNFDPSLTWDDIawlreRWPGPlivkgvlspedarrav 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 201 -----------------------IDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHG 257
Cdd:COG1304 244 dagvdgidvsnhggrqldggpptIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAG 323
|
330 340 350
....*....|....*....|....*....|..
gi 1796958726 258 VKEVLNILTNEFHTSMALTGCRSVAEINRNLV 289
Cdd:COG1304 324 VARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
17-293 |
3.50e-82 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 252.06 E-value: 3.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:PLN02535 86 AHPEGEIATARAAAACNTIMVLSFMASCTVEE-VASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 177 NRRHDIRNQL----RRNL-------------------------------------TLTDLQ------------------- 196
Cdd:PLN02535 165 RREADIKNKMispqLKNFegllstevvsdkgsgleafasetfdaslswkdiewlrSITNLPilikgvltredaikavevg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 197 ----------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKE 260
Cdd:PLN02535 245 vagiivsnhgarqldySPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRK 324
|
330 340 350
....*....|....*....|....*....|...
gi 1796958726 261 VLNILTNEFHTSMALTGCRSVAEINRNLVQFSR 293
Cdd:PLN02535 325 VIEMLKDELEITMALSGCPSVKDITRSHVRTER 357
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
21-286 |
6.91e-131 |
|
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: 373.32 E-value: 6.91e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR- 179
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRLt 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 180 -HDIRnQLRRnltLTDLQ-----------------------------------SPKKIDALTEVVAAVKGKIEVYLDGGV 223
Cdd:cd02809 161 wDDLA-WLRS---QWKGPlilkgiltpedalravdagadgivvsnhggrqldgAPATIDALPEIVAAVGGRIEVLLDGGI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796958726 224 RTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINR 286
Cdd:cd02809 237 RRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
26-290 |
4.97e-122 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 352.99 E-value: 4.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 26 AREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMST 105
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 106 ARAAQAAGICYITSTFASCSLEDIViAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN- 184
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVA-AAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 185 ----------------------------------------QLRRNLTLTDLQ---------------------------- 196
Cdd:pfam01070 160 ftlpprltprnlldlalhprwalgvlrrggaggaaafvgsQFDPALTWDDLAwlrerwkgplvvkgilspedakraveag 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 197 ----------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKE 260
Cdd:pfam01070 240 vdgivvsnhggrqldgAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAH 319
|
330 340 350
....*....|....*....|....*....|
gi 1796958726 261 VLNILTNEFHTSMALTGCRSVAEINRNLVQ 290
Cdd:pfam01070 320 ALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
17-289 |
2.01e-109 |
|
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: 321.31 E-value: 2.01e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:COG1304 5 LSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:COG1304 85 AHPDGELALARAAAAAGIPMGLSTQSTTSLEE-VAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 177 NRRHDIRN-----------------------------------QLRRNLTLTDL-----QSPKK---------------- 200
Cdd:COG1304 164 RRERDLREgfsqpprltprnlleaathprwalglaslaawldtNFDPSLTWDDIawlreRWPGPlivkgvlspedarrav 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 201 -----------------------IDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHG 257
Cdd:COG1304 244 dagvdgidvsnhggrqldggpptIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAG 323
|
330 340 350
....*....|....*....|....*....|..
gi 1796958726 258 VKEVLNILTNEFHTSMALTGCRSVAEINRNLV 289
Cdd:COG1304 324 VARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
21-285 |
1.08e-85 |
|
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: 260.22 E-value: 1.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGL-RWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR 179
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQpLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 180 HDIRNQLRR----------------------------NLTLTDLQ----------------------------------- 196
Cdd:cd02922 162 RDERLKAEEavsdgpagkktkakgggagramsgfidpTLTWDDIKwlrkhtklpivlkgvqtvedavlaaeygvdgivls 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 197 ---------SPKKIDALTEVV---AAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNI 264
Cdd:cd02922 242 nhggrqldtAPAPIEVLLEIRkhcPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQI 321
|
330 340
....*....|....*....|.
gi 1796958726 265 LTNEFHTSMALTGCRSVAEIN 285
Cdd:cd02922 322 LKDEIETTMRLLGVTSLDQLG 342
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
17-293 |
3.50e-82 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 252.06 E-value: 3.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:PLN02535 86 AHPEGEIATARAAAACNTIMVLSFMASCTVEE-VASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 177 NRRHDIRNQL----RRNL-------------------------------------TLTDLQ------------------- 196
Cdd:PLN02535 165 RREADIKNKMispqLKNFegllstevvsdkgsgleafasetfdaslswkdiewlrSITNLPilikgvltredaikavevg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 197 ----------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKE 260
Cdd:PLN02535 245 vagiivsnhgarqldySPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRK 324
|
330 340 350
....*....|....*....|....*....|...
gi 1796958726 261 VLNILTNEFHTSMALTGCRSVAEINRNLVQFSR 293
Cdd:PLN02535 325 VIEMLKDELEITMALSGCPSVKDITRSHVRTER 357
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
17-289 |
5.58e-77 |
|
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: 239.11 E-value: 5.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:cd03332 19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:cd03332 99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 177 NRRHDIRN---------------------------------------------------------QLRRNLTLTDL---- 195
Cdd:cd03332 179 WRPRDLDLgylpflrgigianyfsdpvfrkklaepvgedpeapppmeaavarfvsvfsgpsltweDLAFLREWTDLpivl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 196 ---QSPK----------------------------KIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:cd03332 259 kgiLHPDdarraveagvdgvvvsnhggrqvdgsiaALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGR 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1796958726 245 PILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLV 289
Cdd:cd03332 339 PYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
14-287 |
5.73e-77 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 238.86 E-value: 5.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 14 MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGF 93
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 94 HCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTP 173
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 174 VCGNRRHDIRN-----------------------------------QLRRNLTLTDLQ---------------------- 196
Cdd:PLN02493 160 RLGRRESDIKNrftlppnltlknfegldlgkmdeandsglasyvagQIDRTLSWKDVQwlqtitklpilvkgvltgedar 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 197 ----------------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKG 254
Cdd:PLN02493 240 iaiqagaagiivsnhgarqldyVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEG 319
|
330 340 350
....*....|....*....|....*....|...
gi 1796958726 255 EHGVKEVLNILTNEFHTSMALTGCRSVAEINRN 287
Cdd:PLN02493 320 EAGVRKVLQMLRDEFELTMALSGCRSLKEISRN 352
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
16-286 |
1.28e-70 |
|
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: 221.93 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 16 LVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHC 95
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 96 LVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVC 175
Cdd:cd04737 85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 176 GNRRHDIRN-----------------------------QLRRNLTLTDLQ------------------------------ 196
Cdd:cd04737 165 GNREADIRNkfqfpfgmpnlnhfsegtgkgkgiseiyaAAKQKLSPADIEfiakisglpvivkgiqspedadvainagad 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 197 --------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVL 262
Cdd:cd04737 245 giwvsnhggrqldgGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVL 324
|
330 340
....*....|....*....|....
gi 1796958726 263 NILTNEFHTSMALTGCRSVAEINR 286
Cdd:cd04737 325 EHLNKELKIVMQLAGTRTIEDVKR 348
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
21-286 |
1.97e-63 |
|
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: 203.91 E-value: 1.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAApEGLRWFQLYV-HPDLQlnKQLIQRVESLGFKALVITLDTPVCGNRR 179
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQA-DGDLWFQLYVvHRELA--ELLVKRALAAGYTTLVLTTDVAVNGYRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 180 HDIRNQ--------------------------------------------------LRRNL------------------- 190
Cdd:cd04736 159 RDLRNGfaipfrytprvlldgilhprwllrflrngmpqlanfasddaidvevqaalMSRQMdasfnwqdlrwlrdlwphk 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 191 -------------------------------TLTDLQSPkkIDALTEVVAAVkgKIEVYLDGGVRTGNDVLKALALGAKC 239
Cdd:cd04736 239 llvkgivtaedakrcielgadgvilsnhggrQLDDAIAP--IEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1796958726 240 IFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINR 286
Cdd:cd04736 315 VLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
60-287 |
8.39e-63 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 202.26 E-value: 8.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 60 LRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRW 139
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 140 FQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN----------------------------------- 184
Cdd:PLN02979 125 FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNrftlppnltlknfegldlgkmdeandsglasyvag 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 185 QLRRNLTLTDLQ--------------------------------------------SPKKIDALTEVVAAVKGKIEVYLD 220
Cdd:PLN02979 205 QIDRTLSWKDVQwlqtitklpilvkgvltgedariaiqagaagiivsnhgarqldyVPATISALEEVVKATQGRIPVFLD 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796958726 221 GGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRN 287
Cdd:PLN02979 285 GGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRN 351
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
14-294 |
5.42e-55 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 182.53 E-value: 5.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 14 MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGF 93
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 94 HCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTP 173
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEE-VAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 174 VCGNRRHDIRN-------QLRRNL-------------------TL----TDLQSPKKID--------------------- 202
Cdd:PRK11197 160 VPGARYRDAHSgmsgpnaAMRRYLqavthpqwawdvglngrphDLgnisAYLGKPTGLEdyigwlgnnfdpsiswkdlew 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 203 -------------------------------------------------ALTEVVAAVKGKIEVYLDGGVRTGNDVLKAL 233
Cdd:PRK11197 240 irdfwdgpmvikgildpedardavrfgadgivvsnhggrqldgvlssarALPAIADAVKGDITILADSGIRNGLDVVRMI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1796958726 234 ALGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRN-LVQFSRL 294
Cdd:PRK11197 320 ALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDsLVQGNAA 381
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
55-283 |
2.11e-13 |
|
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: 69.45 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 55 FKRIRLRPRYLR--DVSEVDTRTTIQGEEISAPICI-APTGFHclvwPDGE---MSTARAAQAAGIcyitsTFASCS--- 125
Cdd:cd02811 22 FDDVRLVHNALPelDLDDIDLSTEFLGKRLSAPLLIsAMTGGS----EKAKeinRNLAEAAEELGI-----AMGVGSqra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 126 -LED-----------------IVIA-------APEGLRWFQ----------LYVHpdlqLN--KQLIQ---------RVE 159
Cdd:cd02811 93 aLEDpelaesftvvreappngPLIAnlgavqlNGYGVEEARravemieadaLAIH----LNplQEAVQpegdrdfrgWLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 160 SLgfKALVITLDTPV------CGNRRHDI---------------------------RNQLRRNLTLTDLQS---PKKiDA 203
Cdd:cd02811 169 RI--EELVKALSVPVivkevgFGISRETAkrladagvkaidvagaggtswarvenyRAKDSDQRLAEYFADwgiPTA-AS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 204 LTEVVAAVKgKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILwGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAE 283
Cdd:cd02811 246 LLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVIETIEQIIEELRTAMFLTGAKNLAE 323
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
95-244 |
1.56e-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: 47.97 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 95 CLVWPDGEMS---TARAAQAAGICYITSTFASCSLEDI---------VIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLG 162
Cdd:cd04722 5 LLAGGPSGDPvelAKAAAEAGADAIIVGTRSSDPEEAEtddkevlkeVAAETDLPLGVQLAINDAAAAVDIAAAAARAAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958726 163 FKALVITLDtpvCGNRRHDIRNQLRR--------------NLTLTDLQSPKKIDALTEVV-------------------- 208
Cdd:cd04722 85 ADGVEIHGA---VGYLAREDLELIRElreavpdvkvvvklSPTGELAAAAAEEAGVDEVGlgngggggggrdavpiadll 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1796958726 209 -AAVKGKIEVYL--DGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:cd04722 162 lILAKRGSKVPViaGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
201-252 |
2.77e-05 |
|
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: 45.22 E-value: 2.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1796958726 201 IDALTEVV-----AAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAC 252
Cdd:cd02808 267 ELGLARAHqalvkNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGC 323
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
203-253 |
3.43e-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: 44.63 E-value: 3.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1796958726 203 ALTEVVAAVK-----GKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACK 253
Cdd:pfam01645 257 ALAEAHQTLKenglrDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCI 312
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
203-245 |
2.00e-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: 42.12 E-value: 2.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1796958726 203 ALTEVVAAVKG-KIEVYLDGGVRTGNDVLKALALGAKCIFLGRP 245
Cdd:cd00381 185 AVADVAAAARDyGVPVIADGGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
220-244 |
6.14e-04 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 41.11 E-value: 6.14e-04
10 20
....*....|....*....|....*
gi 1796958726 220 DGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:PTZ00314 350 DGGIKNSGDICKALALGADCVMLGS 374
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
203-244 |
3.49e-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: 3.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1796958726 203 ALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:COG0516 186 AAMDTVTEARMAIAIAADGGIGYIHDNAKALAAGADAVMLGS 227
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
203-244 |
3.74e-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: 38.52 E-value: 3.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1796958726 203 ALTEVVAAVKG-KIEVYLDGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:pfam00478 311 AIYDVAEAAKKyGVPVIADGGIKYSGDIVKALAAGADAVMLGS 353
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
202-237 |
4.24e-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: 38.69 E-value: 4.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1796958726 202 DALTEVVAA-----VKGKIEVYLDGGVRTGNDVLKALALGA 237
Cdd:COG0069 423 LGLAEVHQTlvgngLRDRIRLIADGKLKTGRDVAIAAALGA 463
|
|
| |
