|
Name |
Accession |
Description |
Interval |
E-value |
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
21-261 |
3.31e-113 |
|
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: 327.48 E-value: 3.31e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 101 GEMSTARA-----------------PE-------GLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR-- 154
Cdd:cd02809 82 GELATARAaaaagipftlstvsttsLEevaaaapGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRLtw 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 155 HDIRnQLRRnltLTDLQ-----------------------------------SPKKIDALTEVVAAVKGKIEVYLDGGVR 199
Cdd:cd02809 162 DDLA-WLRS---QWKGPlilkgiltpedalravdagadgivvsnhggrqldgAPATIDALPEIVAAVGGRIEVLLDGGIR 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370453364 200 TGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINR 261
Cdd:cd02809 238 RGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
26-265 |
1.87e-104 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 307.15 E-value: 1.87e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 26 AREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMST 105
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 106 ARA------------------------PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN-- 159
Cdd:pfam01070 81 ARAaaaagipfvlstvsstsleevaaaAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNgf 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 160 ---------------------------------------QLRRNLTLTDLQ----------------------------- 171
Cdd:pfam01070 161 tlpprltprnlldlalhprwalgvlrrggaggaaafvgsQFDPALTWDDLAwlrerwkgplvvkgilspedakraveagv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 172 ---------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEV 236
Cdd:pfam01070 241 dgivvsnhggrqldgAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHA 320
|
330 340
....*....|....*....|....*....
gi 1370453364 237 LNILTNEFHTSMALTGCRSVAEINRNLVQ 265
Cdd:pfam01070 321 LEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
17-264 |
6.31e-94 |
|
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: 280.48 E-value: 6.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:COG1304 5 LSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 97 VWPDGEMSTARA------------------------PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGN 152
Cdd:COG1304 85 AHPDGELALARAaaaagipmglstqsttsleevaaaAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 153 RRHDIRN-----------------------------------QLRRNLTLTDL-----QSPKK----------------- 175
Cdd:COG1304 165 RERDLREgfsqpprltprnlleaathprwalglaslaawldtNFDPSLTWDDIawlreRWPGPlivkgvlspedarravd 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 176 ----------------------IDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGV 233
Cdd:COG1304 245 agvdgidvsnhggrqldggpptIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGV 324
|
330 340 350
....*....|....*....|....*....|.
gi 1370453364 234 KEVLNILTNEFHTSMALTGCRSVAEINRNLV 264
Cdd:COG1304 325 ARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
17-268 |
4.14e-73 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 227.80 E-value: 4.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 97 VWPDGEMSTARAP------------------------EGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGN 152
Cdd:PLN02535 86 AHPEGEIATARAAaacntimvlsfmasctveevasscNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 153 RRHDIRNQL----RRNL-------------------------------------TLTDLQ-------------------- 171
Cdd:PLN02535 166 READIKNKMispqLKNFegllstevvsdkgsgleafasetfdaslswkdiewlrSITNLPilikgvltredaikavevgv 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 172 ---------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEV 236
Cdd:PLN02535 246 agiivsnhgarqldySPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRKV 325
|
330 340 350
....*....|....*....|....*....|..
gi 1370453364 237 LNILTNEFHTSMALTGCRSVAEINRNLVQFSR 268
Cdd:PLN02535 326 IEMLKDELEITMALSGCPSVKDITRSHVRTER 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 ... |
21-261 |
3.31e-113 |
|
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: 327.48 E-value: 3.31e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 101 GEMSTARA-----------------PE-------GLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR-- 154
Cdd:cd02809 82 GELATARAaaaagipftlstvsttsLEevaaaapGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRLtw 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 155 HDIRnQLRRnltLTDLQ-----------------------------------SPKKIDALTEVVAAVKGKIEVYLDGGVR 199
Cdd:cd02809 162 DDLA-WLRS---QWKGPlilkgiltpedalravdagadgivvsnhggrqldgAPATIDALPEIVAAVGGRIEVLLDGGIR 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370453364 200 TGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINR 261
Cdd:cd02809 238 RGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
26-265 |
1.87e-104 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 307.15 E-value: 1.87e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 26 AREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMST 105
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 106 ARA------------------------PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN-- 159
Cdd:pfam01070 81 ARAaaaagipfvlstvsstsleevaaaAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNgf 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 160 ---------------------------------------QLRRNLTLTDLQ----------------------------- 171
Cdd:pfam01070 161 tlpprltprnlldlalhprwalgvlrrggaggaaafvgsQFDPALTWDDLAwlrerwkgplvvkgilspedakraveagv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 172 ---------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEV 236
Cdd:pfam01070 241 dgivvsnhggrqldgAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHA 320
|
330 340
....*....|....*....|....*....
gi 1370453364 237 LNILTNEFHTSMALTGCRSVAEINRNLVQ 265
Cdd:pfam01070 321 LEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
17-264 |
6.31e-94 |
|
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: 280.48 E-value: 6.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:COG1304 5 LSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 97 VWPDGEMSTARA------------------------PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGN 152
Cdd:COG1304 85 AHPDGELALARAaaaagipmglstqsttsleevaaaAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 153 RRHDIRN-----------------------------------QLRRNLTLTDL-----QSPKK----------------- 175
Cdd:COG1304 165 RERDLREgfsqpprltprnlleaathprwalglaslaawldtNFDPSLTWDDIawlreRWPGPlivkgvlspedarravd 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 176 ----------------------IDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGV 233
Cdd:COG1304 245 agvdgidvsnhggrqldggpptIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGV 324
|
330 340 350
....*....|....*....|....*....|.
gi 1370453364 234 KEVLNILTNEFHTSMALTGCRSVAEINRNLV 264
Cdd:COG1304 325 ARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
17-268 |
4.14e-73 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 227.80 E-value: 4.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 97 VWPDGEMSTARAP------------------------EGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGN 152
Cdd:PLN02535 86 AHPEGEIATARAAaacntimvlsfmasctveevasscNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 153 RRHDIRNQL----RRNL-------------------------------------TLTDLQ-------------------- 171
Cdd:PLN02535 166 READIKNKMispqLKNFegllstevvsdkgsgleafasetfdaslswkdiewlrSITNLPilikgvltredaikavevgv 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 172 ---------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEV 236
Cdd:PLN02535 246 agiivsnhgarqldySPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRKV 325
|
330 340 350
....*....|....*....|....*....|..
gi 1370453364 237 LNILTNEFHTSMALTGCRSVAEINRNLVQFSR 268
Cdd:PLN02535 326 IEMLKDELEITMALSGCPSVKDITRSHVRTER 357
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
21-260 |
3.73e-71 |
|
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: 222.09 E-value: 3.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 101 GE--------------------------MSTARAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR 154
Cdd:cd02922 82 GElnlaraagkhgilqmistnascsleeIVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 155 HDIRNQLRR----------------------------NLTLTDLQ----------------------------------- 171
Cdd:cd02922 162 RDERLKAEEavsdgpagkktkakgggagramsgfidpTLTWDDIKwlrkhtklpivlkgvqtvedavlaaeygvdgivls 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 172 ---------SPKKIDALTEVV---AAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNI 239
Cdd:cd02922 242 nhggrqldtAPAPIEVLLEIRkhcPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQI 321
|
330 340
....*....|....*....|.
gi 1370453364 240 LTNEFHTSMALTGCRSVAEIN 260
Cdd:cd02922 322 LKDEIETTMRLLGVTSLDQLG 342
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
14-262 |
5.55e-67 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 212.28 E-value: 5.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 14 MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGF 93
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 94 HCLVWPDGEMSTARAPE------------------------GLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPV 149
Cdd:PLN02493 81 QKMAHPDGEYATARAASaagtimtlsswatssveevastgpGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 150 CGNRRHDIRN-----------------------------------QLRRNLTLTDLQ----------------------- 171
Cdd:PLN02493 161 LGRRESDIKNrftlppnltlknfegldlgkmdeandsglasyvagQIDRTLSWKDVQwlqtitklpilvkgvltgedari 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 172 ---------------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGE 230
Cdd:PLN02493 241 aiqagaagiivsnhgarqldyVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGE 320
|
330 340 350
....*....|....*....|....*....|..
gi 1370453364 231 HGVKEVLNILTNEFHTSMALTGCRSVAEINRN 262
Cdd:PLN02493 321 AGVRKVLQMLRDEFELTMALSGCRSLKEISRN 352
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
17-264 |
5.85e-62 |
|
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: 199.82 E-value: 5.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:cd03332 19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 97 VWPDGEMSTARA-------------------------PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 151
Cdd:cd03332 99 FHPDAELATARAaaelgvpyilstassssiedvaaaaGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 152 NRRHDIRN---------------------------------------------------------QLRRNLTLTDL---- 170
Cdd:cd03332 179 WRPRDLDLgylpflrgigianyfsdpvfrkklaepvgedpeapppmeaavarfvsvfsgpsltweDLAFLREWTDLpivl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 171 ---QSPK----------------------------KIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 219
Cdd:cd03332 259 kgiLHPDdarraveagvdgvvvsnhggrqvdgsiaALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGR 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1370453364 220 PILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLV 264
Cdd:cd03332 339 PYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
16-261 |
1.49e-58 |
|
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: 189.96 E-value: 1.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 16 LVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHC 95
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 96 LVWPDGEMSTARA-------------------------PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVC 150
Cdd:cd04737 85 LAHATGEVATARGmaevgslfsistysntsleeiakasNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 151 GNRRHDIRN-----------------------------QLRRNLTLTDLQ------------------------------ 171
Cdd:cd04737 165 GNREADIRNkfqfpfgmpnlnhfsegtgkgkgiseiyaAAKQKLSPADIEfiakisglpvivkgiqspedadvainagad 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 172 --------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVL 237
Cdd:cd04737 245 giwvsnhggrqldgGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVL 324
|
330 340
....*....|....*....|....
gi 1370453364 238 NILTNEFHTSMALTGCRSVAEINR 261
Cdd:cd04737 325 EHLNKELKIVMQLAGTRTIEDVKR 348
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
21-261 |
4.77e-53 |
|
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: 176.18 E-value: 4.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 101 GEMSTARAP------------------------EGLRWFQLYV-HPDLQlnKQLIQRVESLGFKALVITLDTPVCGNRRH 155
Cdd:cd04736 82 GDLALARAAakagipfvlstasnmsiedvarqaDGDLWFQLYVvHRELA--ELLVKRALAAGYTTLVLTTDVAVNGYRER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 156 DIRNQ--------------------------------------------------LRRNL-------------------- 165
Cdd:cd04736 160 DLRNGfaipfrytprvlldgilhprwllrflrngmpqlanfasddaidvevqaalMSRQMdasfnwqdlrwlrdlwphkl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 166 ------------------------------TLTDLQSPkkIDALTEVVAAVkgKIEVYLDGGVRTGNDVLKALALGAKCI 215
Cdd:cd04736 240 lvkgivtaedakrcielgadgvilsnhggrQLDDAIAP--IEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANAV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1370453364 216 FLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINR 261
Cdd:cd04736 316 LLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
60-262 |
5.06e-53 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 176.07 E-value: 5.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 60 LRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAPE------------------------GLRWF 115
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASaagtimtlsswatssveevastgpGIRFF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 116 QLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN-----------------------------------Q 160
Cdd:PLN02979 126 QLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNrftlppnltlknfegldlgkmdeandsglasyvagQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 161 LRRNLTLTDLQ--------------------------------------------SPKKIDALTEVVAAVKGKIEVYLDG 196
Cdd:PLN02979 206 IDRTLSWKDVQwlqtitklpilvkgvltgedariaiqagaagiivsnhgarqldyVPATISALEEVVKATQGRIPVFLDG 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453364 197 GVRTGNDVLKALALGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRN 262
Cdd:PLN02979 286 GVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRN 351
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
14-269 |
4.29e-44 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 153.26 E-value: 4.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 14 MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGF 93
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 94 HCLVWPDGEMSTARAPEGLR------------------------WFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPV 149
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGipftlstvsvcpieevapaikrpmWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 150 CGNRRHDIRN-------QLRRNL-------------------TL----TDLQSPKKID---------------------- 177
Cdd:PRK11197 161 PGARYRDAHSgmsgpnaAMRRYLqavthpqwawdvglngrphDLgnisAYLGKPTGLEdyigwlgnnfdpsiswkdlewi 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 178 ------------------------------------------------ALTEVVAAVKGKIEVYLDGGVRTGNDVLKALA 209
Cdd:PRK11197 241 rdfwdgpmvikgildpedardavrfgadgivvsnhggrqldgvlssarALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370453364 210 LGAKCIFLGRPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRN-LVQFSRL 269
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDsLVQGNAA 381
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
177-258 |
2.06e-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: 68.68 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 177 DALTEVVAAVKgKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILwGLACKGEHGVKEVLNILTNEFHTSMALTGCRSV 256
Cdd:cd02811 244 ASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVIETIEQIIEELRTAMFLTGAKNL 321
|
..
gi 1370453364 257 AE 258
Cdd:cd02811 322 AE 323
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
176-227 |
1.89e-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: 1.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370453364 176 IDALTEVV-----AAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAC 227
Cdd:cd02808 267 ELGLARAHqalvkNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGC 323
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
178-228 |
2.82e-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: 2.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453364 178 ALTEVVAAVK-----GKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACK 228
Cdd:pfam01645 257 ALAEAHQTLKenglrDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCI 312
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
106-219 |
5.13e-05 |
|
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: 42.96 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453364 106 ARAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDtpvCGNRRHDIRNQLRR--------------NLTLTDLQ 171
Cdd:cd04722 53 AAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGA---VGYLAREDLELIRElreavpdvkvvvklSPTGELAA 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370453364 172 SPKKIDALTEVV---------------------AAVKGKIEVYL--DGGVRTGNDVLKALALGAKCIFLGR 219
Cdd:cd04722 130 AAAEEAGVDEVGlgngggggggrdavpiadlllILAKRGSKVPViaGGGINDPEDAAEALALGADGVIVGS 200
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
178-220 |
1.36e-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: 42.50 E-value: 1.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1370453364 178 ALTEVVAAVKG-KIEVYLDGGVRTGNDVLKALALGAKCIFLGRP 220
Cdd:cd00381 185 AVADVAAAARDyGVPVIADGGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
195-219 |
5.10e-04 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 41.11 E-value: 5.10e-04
10 20
....*....|....*....|....*
gi 1370453364 195 DGGVRTGNDVLKALALGAKCIFLGR 219
Cdd:PTZ00314 350 DGGIKNSGDICKALALGADCVMLGS 374
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
178-219 |
2.74e-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: 2.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1370453364 178 ALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 219
Cdd:COG0516 186 AAMDTVTEARMAIAIAADGGIGYIHDNAKALAAGADAVMLGS 227
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
178-219 |
2.78e-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: 2.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1370453364 178 ALTEVVAAVKG-KIEVYLDGGVRTGNDVLKALALGAKCIFLGR 219
Cdd:pfam00478 311 AIYDVAEAAKKyGVPVIADGGIKYSGDIVKALAAGADAVMLGS 353
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
177-212 |
3.22e-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: 3.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1370453364 177 DALTEVVAA-----VKGKIEVYLDGGVRTGNDVLKALALGA 212
Cdd:COG0069 423 LGLAEVHQTlvgngLRDRIRLIADGKLKTGRDVAIAAALGA 463
|
|
| |
