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Conserved domains on  [gi|495778142|ref|WP_008502721|]
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MULTISPECIES: quinone-dependent L-lactate dehydrogenase [Enterobacter]

Protein Classification

FMN-dependent L-lactate dehydrogenase LldD( domain architecture ID 11485264)

FMN-dependent L-lactate dehydrogenase LldD catalyzes the conversion of L-lactate to pyruvate, and is coupled to the respiratory chain

EC:  1.1.-.-
Gene Symbol:  lldD
Gene Ontology:  GO:0010181|GO:0004457|GO:0019516
PubMed:  22574176

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
lldD PRK11197
L-lactate dehydrogenase; Provisional
1-379 0e+00

L-lactate dehydrogenase; Provisional


:

Pssm-ID: 183033  Cd Length: 381  Bit Score: 829.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   1 MIISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGL 80
Cdd:PRK11197   1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  81 CGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:PRK11197  81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 161 PGARYRDAHSGMSGPNAALRRYWQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLANNFDPSISWKDLEWI 240
Cdd:PRK11197 161 PGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIA 320
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495778142 321 LGADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQEL 379
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGN 379
 
Name Accession Description Interval E-value
lldD PRK11197
L-lactate dehydrogenase; Provisional
1-379 0e+00

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 829.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   1 MIISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGL 80
Cdd:PRK11197   1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  81 CGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:PRK11197  81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 161 PGARYRDAHSGMSGPNAALRRYWQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLANNFDPSISWKDLEWI 240
Cdd:PRK11197 161 PGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIA 320
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495778142 321 LGADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQEL 379
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGN 379
L_lactate_LldD NF033901
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ...
1-377 0e+00

FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. It occurs in E. coli, Salmonella, and as one of two L-lactate dehydrogenases in Pseudomonas aeruginosa. It is unrelated to the NAD-dependent enzyme.


Pssm-ID: 411463  Cd Length: 377  Bit Score: 825.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   1 MIISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGL 80
Cdd:NF033901   1 MIISASTDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  81 CGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:NF033901  81 TGMYARRGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 161 PGARYRDAHSGMSGPNAALRRYWQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLANNFDPSISWKDLEWI 240
Cdd:NF033901 161 PGARYRDAHSGMSGPNAALRRMLQAVTHPQWAWDVGLLGRPHDLGNISAYRGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIA 320
Cdd:NF033901 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495778142 321 LGADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQ 377
Cdd:NF033901 321 LGADSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLVQ 377
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
3-377 1.32e-167

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: 473.08  E-value: 1.32e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   3 ISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCG 82
Cdd:COG1304    4 ILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  83 MYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPG 162
Cdd:COG1304   84 LAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 163 ARYRDAHSGMSGP-NAALRRYWQAVTHPQWAWdvglngrphdlgnisaylgkptGLEDYIGWLANNFDPSISWKDLEWIR 241
Cdd:COG1304  164 RRERDLREGFSQPpRLTPRNLLEAATHPRWAL----------------------GLASLAAWLDTNFDPSLTWDDIAWLR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 242 EFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIAL 321
Cdd:COG1304  222 ERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALAL 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495778142 322 GADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQ 377
Cdd:COG1304  302 GADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
FMN_dh pfam01070
FMN-dependent dehydrogenase;
13-376 1.34e-152

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 434.65  E-value: 1.34e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   13 AQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYARRGEVQA 92
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   93 AAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGM 172
Cdd:pfam01070  81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  173 S-GPNAALRRYWQAVTHPQWAWDVGLNGRPHDLGnisaylgkptgledyiGWLANNFDPSISWKDLEWIREFWDGPMVIK 251
Cdd:pfam01070 161 TlPPRLTPRNLLDLALHPRWALGVLRRGGAGGAA----------------AFVGSQFDPALTWDDLAWLRERWKGPLVVK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  252 GILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADSVLLGRA 331
Cdd:pfam01070 225 GILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRP 304
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 495778142  332 YLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLV 376
Cdd:pfam01070 305 FLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
7-372 4.16e-145

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: 413.77  E-value: 4.16e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   7 SDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYAR 86
Cdd:cd02809    1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  87 RGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARyr 166
Cdd:cd02809   81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 167 dahsgmsgpnaalrrywqavthpqwawdvglngrphdlgnisaylgkptgledyigwlannfdpsISWKDLEWIREFWDG 246
Cdd:cd02809  159 -----------------------------------------------------------------LTWDDLAWLRSQWKG 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADSV 326
Cdd:cd02809  174 PLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAV 253
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 495778142 327 LLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISR 372
Cdd:cd02809  254 LIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
 
Name Accession Description Interval E-value
lldD PRK11197
L-lactate dehydrogenase; Provisional
1-379 0e+00

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 829.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   1 MIISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGL 80
Cdd:PRK11197   1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  81 CGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:PRK11197  81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 161 PGARYRDAHSGMSGPNAALRRYWQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLANNFDPSISWKDLEWI 240
Cdd:PRK11197 161 PGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIA 320
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495778142 321 LGADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQEL 379
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGN 379
L_lactate_LldD NF033901
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ...
1-377 0e+00

FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. It occurs in E. coli, Salmonella, and as one of two L-lactate dehydrogenases in Pseudomonas aeruginosa. It is unrelated to the NAD-dependent enzyme.


Pssm-ID: 411463  Cd Length: 377  Bit Score: 825.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   1 MIISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGL 80
Cdd:NF033901   1 MIISASTDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  81 CGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:NF033901  81 TGMYARRGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 161 PGARYRDAHSGMSGPNAALRRYWQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLANNFDPSISWKDLEWI 240
Cdd:NF033901 161 PGARYRDAHSGMSGPNAALRRMLQAVTHPQWAWDVGLLGRPHDLGNISAYRGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIA 320
Cdd:NF033901 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495778142 321 LGADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQ 377
Cdd:NF033901 321 LGADSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLVQ 377
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
3-377 1.32e-167

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: 473.08  E-value: 1.32e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   3 ISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCG 82
Cdd:COG1304    4 ILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  83 MYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPG 162
Cdd:COG1304   84 LAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 163 ARYRDAHSGMSGP-NAALRRYWQAVTHPQWAWdvglngrphdlgnisaylgkptGLEDYIGWLANNFDPSISWKDLEWIR 241
Cdd:COG1304  164 RRERDLREGFSQPpRLTPRNLLEAATHPRWAL----------------------GLASLAAWLDTNFDPSLTWDDIAWLR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 242 EFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIAL 321
Cdd:COG1304  222 ERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALAL 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495778142 322 GADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQ 377
Cdd:COG1304  302 GADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
FMN_dh pfam01070
FMN-dependent dehydrogenase;
13-376 1.34e-152

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 434.65  E-value: 1.34e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   13 AQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYARRGEVQA 92
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   93 AAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGM 172
Cdd:pfam01070  81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  173 S-GPNAALRRYWQAVTHPQWAWDVGLNGRPHDLGnisaylgkptgledyiGWLANNFDPSISWKDLEWIREFWDGPMVIK 251
Cdd:pfam01070 161 TlPPRLTPRNLLDLALHPRWALGVLRRGGAGGAA----------------AFVGSQFDPALTWDDLAWLRERWKGPLVVK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  252 GILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADSVLLGRA 331
Cdd:pfam01070 225 GILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRP 304
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 495778142  332 YLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLV 376
Cdd:pfam01070 305 FLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
7-372 4.16e-145

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: 413.77  E-value: 4.16e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   7 SDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYAR 86
Cdd:cd02809    1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  87 RGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARyr 166
Cdd:cd02809   81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 167 dahsgmsgpnaalrrywqavthpqwawdvglngrphdlgnisaylgkptgledyigwlannfdpsISWKDLEWIREFWDG 246
Cdd:cd02809  159 -----------------------------------------------------------------LTWDDLAWLRSQWKG 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADSV 326
Cdd:cd02809  174 PLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAV 253
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 495778142 327 LLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISR 372
Cdd:cd02809  254 LIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
7-375 4.15e-96

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: 292.26  E-value: 4.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   7 SDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYAR 86
Cdd:cd03332   22 ERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  87 RGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKR-PMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARY 165
Cdd:cd03332  102 DAELATARAAAELGVPYILSTASSSSIEDVAAAAGDaPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRP 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 166 RDAHSG----MSGPNAAlrrywQAVTHPQW--AWDVGLNGRPHDLGNISAYLgkptgledyIGWLANNFDPSISWKDLEW 239
Cdd:cd03332  182 RDLDLGylpfLRGIGIA-----NYFSDPVFrkKLAEPVGEDPEAPPPMEAAV---------ARFVSVFSGPSLTWEDLAF 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 240 IREFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMI 319
Cdd:cd03332  248 LREWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKAL 327
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495778142 320 ALGADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSL 375
Cdd:cd03332  328 ALGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
8-372 8.11e-94

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: 285.57  E-value: 8.11e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   8 DYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYARR 87
Cdd:cd04736    2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  88 GEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRdRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRD 167
Cdd:cd04736   82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRERD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 168 AHSGMSGP-NAALRRYWQAVTHPQWAWDVGLNGRPHdLGNISAylGKPTGLEDYIGWLANNFDPSISWKDLEWIREFWDG 246
Cdd:cd04736  161 LRNGFAIPfRYTPRVLLDGILHPRWLLRFLRNGMPQ-LANFAS--DDAIDVEVQAALMSRQMDASFNWQDLRWLRDLWPH 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDiaILADSGIRNGLDVVRMIALGADSV 326
Cdd:cd04736  238 KLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYKP--VLIDSGIRRGSDIVKALALGANAV 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 495778142 327 LLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISR 372
Cdd:cd04736  316 LLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
8-375 6.89e-82

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: 254.67  E-value: 6.89e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   8 DYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYARR 87
Cdd:cd04737   10 DLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHAT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  88 GEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKR-PMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGarYR 166
Cdd:cd04737   90 GEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGgPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGG--NR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 167 DAHSGMSGPnaalrrywqavthpqwawdvglngRPHDLGNISAYLgKPTGLEDYIGWLANNFDPSISWKDLEWIREFWDG 246
Cdd:cd04737  168 EADIRNKFQ------------------------FPFGMPNLNHFS-EGTGKGKGISEIYAAAKQKLSPADIEFIAKISGL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADSV 326
Cdd:cd04737  223 PVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAV 302
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 495778142 327 LLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSL 375
Cdd:cd04737  303 AVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRTFL 351
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
7-370 1.51e-78

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: 245.58  E-value: 1.51e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   7 SDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYAR 86
Cdd:cd02922    1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  87 RGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIK--RPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGAR 164
Cdd:cd02922   81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPpdQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 165 YRDAHSGMSGPNAALRRYWQAVTHPQWAwdvglnGRPhdlgnISAYLgkptgledyigwlannfDPSISWKDLEWIREFW 244
Cdd:cd02922  161 ERDERLKAEEAVSDGPAGKKTKAKGGGA------GRA-----MSGFI-----------------DPTLTWDDIKWLRKHT 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 245 DGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAI---ADAVKGDIAILADSGIRNGLDVVRMIAL 321
Cdd:cd02922  213 KLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIrkhCPEVFDKIEVYVDGGVRRGTDVLKALCL 292
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 495778142 322 GADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEI 370
Cdd:cd02922  293 GAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQL 341
PLN02535 PLN02535
glycolate oxidase
8-386 9.92e-72

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 228.95  E-value: 9.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   8 DYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYARR 87
Cdd:PLN02535  10 EFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLAHPE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  88 GEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRD 167
Cdd:PLN02535  90 GEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGRREAD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 168 AHSGMSGPNaalRRYWQAVTHPQWAWDVGlngrphdlgnisaylgkpTGLEDYIgwlANNFDPSISWKDLEWIREFWDGP 247
Cdd:PLN02535 170 IKNKMISPQ---LKNFEGLLSTEVVSDKG------------------SGLEAFA---SETFDASLSWKDIEWLRSITNLP 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 248 MVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADSVL 327
Cdd:PLN02535 226 ILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVL 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495778142 328 LGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQELSKLPAAL 386
Cdd:PLN02535 306 VGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVRTERERLQSML 364
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
1-378 1.18e-68

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 221.14  E-value: 1.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142   1 MIISAASDYRAAAQRILPPFLFHYIDGGAYAEYTLRRNVEDLSEVALRQRVLKNMSDLSLETKLFNETLSMPVALAPVGL 80
Cdd:PLN02493   1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  81 CGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:PLN02493  81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 161 PGARYRDAHSGMS-GPNAALRRYwqavthpqwawdVGLngrphDLGNISAylGKPTGLEDYIgwlANNFDPSISWKDLEW 239
Cdd:PLN02493 161 LGRRESDIKNRFTlPPNLTLKNF------------EGL-----DLGKMDE--ANDSGLASYV---AGQIDRTLSWKDVQW 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 240 IREFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMI 319
Cdd:PLN02493 219 LQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKAL 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495778142 320 ALGADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKTISEISRDSLVQE 378
Cdd:PLN02493 299 ALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHITTE 357
PLN02979 PLN02979
glycolate oxidase
47-378 8.55e-58

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 192.63  E-value: 8.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  47 LRQRVLKNMSDLSLETKLFNETLSMPVALAPVGLCGMYARRGEVQAAAAADAKGIPFTLSTVSVCPIEEVAPTIKRPMWF 126
Cdd:PLN02979  46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFF 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 127 QLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMS-GPNAALRRYwqavthpqwawdVGLngrphDLG 205
Cdd:PLN02979 126 QLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTlPPNLTLKNF------------EGL-----DLG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 206 NISAylGKPTGLEDYIgwlANNFDPSISWKDLEWIREFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLS 285
Cdd:PLN02979 189 KMDE--ANDSGLASYV---AGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPA 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 286 SARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADSVLLGRAYLYALATAGQAGVANLLNLIEKEMKVAMTLTGAK 365
Cdd:PLN02979 264 TISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCR 343
                        330
                 ....*....|...
gi 495778142 366 TISEISRDSLVQE 378
Cdd:PLN02979 344 SLKEISRNHITTE 356
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
219-369 4.94e-18

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: 84.09  E-value: 4.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 219 DYIGWLANnfdpsiswkdLEWIREFWDGPMVIK----GIlDPEDARDAVRFGADGIVVSNHGG---------RQLDGV-- 283
Cdd:cd02811  162 DFRGWLER----------IEELVKALSVPVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSDqr 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 284 ---------LSSARALPAIADAVKgDIAILADSGIRNGLDVVRMIALGADSVLLGRAYLYAlATAGQAGVANLLNLIEKE 354
Cdd:cd02811  231 laeyfadwgIPTAASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEE 308
                        170
                 ....*....|....*
gi 495778142 355 MKVAMTLTGAKTISE 369
Cdd:cd02811  309 LRTAMFLTGAKNLAE 323
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
234-330 4.66e-09

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: 55.67  E-value: 4.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 234 WKDLEWIREFW-DGPMVIKGILDPEDAR-DAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRN 311
Cdd:cd04722  102 LELIRELREAVpDVKVVVKLSPTGELAAaAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIND 181
                         90
                 ....*....|....*....
gi 495778142 312 GLDVVRMIALGADSVLLGR 330
Cdd:cd04722  182 PEDAAEALALGADGVIVGS 200
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
297-377 8.49e-09

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: 56.78  E-value: 8.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 297 VKGDIAILADSGIRNGLDVVRMIALGADSVLLGRAYLYAL-----------------AT------------AGQAGVANL 347
Cdd:cd02808  282 LRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALgciqarkchtntcpvgvATqdpelrrrldveGKAERVANY 361
                         90       100       110
                 ....*....|....*....|....*....|
gi 495778142 348 LNLIEKEMKVAMTLTGAKTISEISRDSLVQ 377
Cdd:cd02808  362 LKSLAEELRELAAALGKRSLELLGRSDLLA 391
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
237-333 2.15e-07

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: 51.33  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 237 LEWIREFwdGPMVIKGILDPEDARDAVRFGADGIVVSN-----HGGRQLDGVLSSaraLPAIADAVkgDIAILADSGIRN 311
Cdd:cd04730   95 VERLKAA--GIKVIPTVTSVEEARKAEAAGADALVAQGaeaggHRGTFDIGTFAL---VPEVRDAV--DIPVIAAGGIAD 167
                         90       100
                 ....*....|....*....|..
gi 495778142 312 GLDVVRMIALGADSVLLGRAYL 333
Cdd:cd04730  168 GRGIAAALALGADGVQMGTRFL 189
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
237-331 3.70e-07

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 51.20  E-value: 3.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 237 LEWIREFWDGPMVIK--GILDPED----ARDAVRFGADGIVVSNH-------------GGRQLDGVLSSARALPA----- 292
Cdd:cd02810  154 LKAVKAAVDIPLLVKlsPYFDLEDivelAKAAERAGADGLTAINTisgrvvdlktvgpGPKRGTGGLSGAPIRPLalrwv 233
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 495778142 293 --IADAVKGDIAILADSGIRNGLDVVRMIALGADSVLLGRA 331
Cdd:cd02810  234 arLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATA 274
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
237-330 9.66e-07

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: 50.21  E-value: 9.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 237 LEWIRE-FWDGPMVIKGILDPEDARDAVRFGADGIVV-----SNHGGRQLDGV-LSSARALPAIADAVKG-DIAILADSG 308
Cdd:cd00381  126 IKFIKKkYPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgVPQATAVADVAAAARDyGVPVIADGG 205
                         90       100
                 ....*....|....*....|..
gi 495778142 309 IRNGLDVVRMIALGADSVLLGR 330
Cdd:cd00381  206 IRTSGDIVKALAAGADAVMLGS 227
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
237-330 5.01e-06

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 48.15  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  237 LEWIREFWDGPMVIKG-ILDPEDARDAVRFGADGI-------------VVSNHGGRQLDGVLSSARAlpaiadAVKGDIA 302
Cdd:pfam00478 252 VKWIKKKYPDVQVIAGnVATAEGAKALIEAGADAVkvgigpgsicttrVVAGVGVPQLTAIYDVAEA------AKKYGVP 325
                          90       100
                  ....*....|....*....|....*...
gi 495778142  303 ILADSGIRNGLDVVRMIALGADSVLLGR 330
Cdd:pfam00478 326 VIADGGIKYSGDIVKALAAGADAVMLGS 353
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
248-374 1.44e-05

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 46.96  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 248 MVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALP---AIADAVK----GDIAILADSGIRNGLDVVRMIA 320
Cdd:PRK06843 197 LIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPqitAICDVYEvcknTNICIIADGGIRFSGDVVKAIA 276
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495778142 321 LGADSVLLGRAYLYALATAGQAGVANllnliEKEMKvamTLTGAKTISEISRDS 374
Cdd:PRK06843 277 AGADSVMIGNLFAGTKESPSEEIIYN-----GKKFK---SYVGMGSISAMKRGS 322
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
244-336 1.53e-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: 46.56  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  244 WDGPMVIK---GILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSAR--ALP---AIADAVKG--------DIAILADS 307
Cdd:pfam01645 201 PKAPISVKlvsGHGVGTIAAGVAKAGADIILIDGYDGGTGASPKTSIKhaGLPwelALAEAHQTlkenglrdRVSLIADG 280
                          90       100
                  ....*....|....*....|....*....
gi 495778142  308 GIRNGLDVVRMIALGADSVLLGRAYLYAL 336
Cdd:pfam01645 281 GLRTGADVAKAAALGADAVYIGTAALIAL 309
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
255-333 3.39e-05

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 45.10  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 255 DPEDARDAVRFGADGIVVSN-----HGGRQLdgvLSSARALPAIADAVkgDIAILADSGIRNGLDVVRMIALGADSVLLG 329
Cdd:COG2070  113 SVREARKAEKAGADAVVAEGaeaggHRGADE---VSTFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 187

                 ....
gi 495778142 330 RAYL 333
Cdd:COG2070  188 TRFL 191
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
246-333 1.99e-04

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 42.89  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142  246 GPMVIKGILDPEDARDAVRFGADGIVVSN-----HGGRQLDGVLSSARALPAIADAVkgDIAILADSGIRNGLDVVRMIA 320
Cdd:pfam03060 136 GVALIPTISSAKEARIAEARGADALIVQGpeaggHQGTPEYGDKGLFRLVPQVPDAV--DIPVIAAGGIWDRRGVAAALA 213
                          90
                  ....*....|...
gi 495778142  321 LGADSVLLGRAYL 333
Cdd:pfam03060 214 LGASGVQMGTRFL 226
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
297-336 5.58e-04

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: 42.16  E-value: 5.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 495778142 297 VKGDIAILADSGIRNGLDVVRMIALGADSVLLGRAYLYAL 336
Cdd:COG0069  437 LRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVAL 476
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
249-330 2.91e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 39.57  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778142 249 VIKG-ILDPEDARDAVRFGADGI-------------VVSNHGGRQLDGVLSSARAlpaiadAVKGDIAILADSGIRNGLD 314
Cdd:PTZ00314 285 IIAGnVVTADQAKNLIDAGADGLrigmgsgsicitqEVCAVGRPQASAVYHVARY------ARERGVPCIADGGIKNSGD 358
                         90
                 ....*....|....*.
gi 495778142 315 VVRMIALGADSVLLGR 330
Cdd:PTZ00314 359 ICKALALGADCVMLGS 374
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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