|
Name |
Accession |
Description |
Interval |
E-value |
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
1-380 |
0e+00 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 840.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 1 MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGL 80
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 81 CGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 161 PGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
Cdd:PRK11197 161 PGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIA 320
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 321 LGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLVQGLG 380
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGNA 380
|
|
| 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: 829.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 1 MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGL 80
Cdd:NF033901 1 MIISASTDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 81 CGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:NF033901 81 TGMYARRGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 161 PGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
Cdd:NF033901 161 PGARYRDAHSGMSGPNAALRRMLQAVTHPQWAWDVGLLGRPHDLGNISAYRGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIA 320
Cdd:NF033901 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131476 321 LGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLVQ 377
Cdd:NF033901 321 LGADSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLVQ 377
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
3-377 |
2.03e-172 |
|
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: 485.41 E-value: 2.03e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 3 ISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCG 82
Cdd:COG1304 4 ILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 83 MYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPG 162
Cdd:COG1304 84 LAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 163 ARYRDAHSGMSGP-NAAMRRYLQAVTHPQWAWdvglngrphdlgnisaylgkptGLEDYIGWLGNNFDPSISWKDLEWIR 241
Cdd:COG1304 164 RRERDLREGFSQPpRLTPRNLLEAATHPRWAL----------------------GLASLAAWLDTNFDPSLTWDDIAWLR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 242 DFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIAL 321
Cdd:COG1304 222 ERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALAL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131476 322 GADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLVQ 377
Cdd:COG1304 302 GADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
13-376 |
5.18e-159 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 450.83 E-value: 5.18e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 13 AQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARRGEVQA 92
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 93 AKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGM 172
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 173 S-GPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGnisaylgkptgledyiGWLGNNFDPSISWKDLEWIRDFWDGPMVIK 251
Cdd:pfam01070 161 TlPPRLTPRNLLDLALHPRWALGVLRRGGAGGAA----------------AFVGSQFDPALTWDDLAWLRERWKGPLVVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 252 GILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRA 331
Cdd:pfam01070 225 GILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRP 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16131476 332 FLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLV 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 |
3.83e-151 |
|
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.
Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 429.17 E-value: 3.83e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 7 SDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYAR 86
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 87 RGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARyr 166
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 167 dahsgmsgpnaamrrylqavthpqwawdvglngrphdlgnisaylgkptgledyigwlgnnfdpsISWKDLEWIRDFWDG 246
Cdd:cd02809 159 -----------------------------------------------------------------LTWDDLAWLRSQWKG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTV 326
Cdd:cd02809 174 PLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAV 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 16131476 327 LLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQ 372
Cdd:cd02809 254 LIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
8-371 |
7.82e-99 |
|
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: 298.28 E-value: 7.82e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 8 DYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARR 87
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 88 GEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRdRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRD 167
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRERD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 168 AHSGMSGP-NAAMRRYLQAVTHPQWAWDVGLNGRPHdLGNISAylGKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDG 246
Cdd:cd04736 161 LRNGFAIPfRYTPRVLLDGILHPRWLLRFLRNGMPQ-LANFAS--DDAIDVEVQAALMSRQMDASFNWQDLRWLRDLWPH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDiaILADSGIRNGLDVVRMIALGADTV 326
Cdd:cd04736 238 KLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYKP--VLIDSGIRRGSDIVKALALGANAV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16131476 327 LLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEIT 371
Cdd:cd04736 316 LLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLT 360
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
7-375 |
6.09e-98 |
|
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: 296.89 E-value: 6.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 7 SDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYAR 86
Cdd:cd03332 22 ERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 87 RGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKR-PMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARY 165
Cdd:cd03332 102 DAELATARAAAELGVPYILSTASSSSIEDVAAAAGDaPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 166 RDAHSGmSGPNAAMRRYLQAVTHPQW--AWDVGLNGRPHDLGNISAYLgkptgledyIGWLGNNFDPSISWKDLEWIRDF 243
Cdd:cd03332 182 RDLDLG-YLPFLRGIGIANYFSDPVFrkKLAEPVGEDPEAPPPMEAAV---------ARFVSVFSGPSLTWEDLAFLREW 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 244 WDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGA 323
Cdd:cd03332 252 TDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGA 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 16131476 324 DTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSL 375
Cdd:cd03332 332 KAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
7-370 |
1.30e-86 |
|
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: 266.39 E-value: 1.30e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 7 SDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYAR 86
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 87 RGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIK--RPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGAR 164
Cdd:cd02922 81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPpdQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 165 YRDAHSGMSGPNAAMRRYLQAVTHPQWAwdvglnGRPhdlgnISAYLgkptgledyigwlgnnfDPSISWKDLEWIRDFW 244
Cdd:cd02922 161 ERDERLKAEEAVSDGPAGKKTKAKGGGA------GRA-----MSGFI-----------------DPTLTWDDIKWLRKHT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 245 DGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAI---ADAVKGDIAILADSGIRNGLDVVRMIAL 321
Cdd:cd02922 213 KLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIrkhCPEVFDKIEVYVDGGVRRGTDVLKALCL 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16131476 322 GADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEI 370
Cdd:cd02922 293 GAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQL 341
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
8-375 |
1.66e-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: 256.21 E-value: 1.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 8 DYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARR 87
Cdd:cd04737 10 DLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 88 GEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKR-PMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGarYR 166
Cdd:cd04737 90 GEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGgPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGG--NR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 167 DAHSGMSGPnaamrrylqavthpqwawdvglngRPHDLGNISAYLgKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDG 246
Cdd:cd04737 168 EADIRNKFQ------------------------FPFGMPNLNHFS-EGTGKGKGISEIYAAAKQKLSPADIEFIAKISGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 247 PMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTV 326
Cdd:cd04737 223 PVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAV 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16131476 327 LLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSL 375
Cdd:cd04737 303 AVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRTFL 351
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
8-372 |
8.08e-75 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 237.04 E-value: 8.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 8 DYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARR 87
Cdd:PLN02535 10 EFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLAHPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 88 GEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRD 167
Cdd:PLN02535 90 GEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGRREAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 168 AHSGMSGPNaamRRYLQAVTHPQWAWDVGlngrphdlgnisaylgkpTGLEDYIGwlgNNFDPSISWKDLEWIRDFWDGP 247
Cdd:PLN02535 170 IKNKMISPQ---LKNFEGLLSTEVVSDKG------------------SGLEAFAS---ETFDASLSWKDIEWLRSITNLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 248 MVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVL 327
Cdd:PLN02535 226 ILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16131476 328 LGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQ 372
Cdd:PLN02535 306 VGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITR 350
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
1-376 |
2.05e-71 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 228.08 E-value: 2.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 1 MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGL 80
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 81 CGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPT 160
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 161 PGARYRDAHSGMS-GPNAAMRRYlqavthpqwawdVGLngrphDLGNISAylGKPTGLEDYIGwlgNNFDPSISWKDLEW 239
Cdd:PLN02493 161 LGRRESDIKNRFTlPPNLTLKNF------------EGL-----DLGKMDE--ANDSGLASYVA---GQIDRTLSWKDVQW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 240 IRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMI 319
Cdd:PLN02493 219 LQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKAL 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131476 320 ALGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLV 376
Cdd:PLN02493 299 ALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHIT 355
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
47-386 |
5.87e-60 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 198.41 E-value: 5.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 47 LRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWF 126
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 127 QLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMS-GPNAAMRRYlqavthpqwawdVGLngrphDLG 205
Cdd:PLN02979 126 QLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTlPPNLTLKNF------------EGL-----DLG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 206 NISAylGKPTGLEDYIGwlgNNFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLS 285
Cdd:PLN02979 189 KMDE--ANDSGLASYVA---GQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 286 SARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAK 365
Cdd:PLN02979 264 TISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCR 343
|
330 340
....*....|....*....|.
gi 16131476 366 SISEITQDSLVQGLGKELPAA 386
Cdd:PLN02979 344 SLKEISRNHITTEWDTPRPSA 364
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
219-372 |
1.11e-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: 86.01 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 219 DYIGWLGNnfdpsiswkdLEWIRDFWDGPMVIK----GIlDPEDARDAVRFGADGIVVSNHGG---------RQLDGV-- 283
Cdd:cd02811 162 DFRGWLER----------IEELVKALSVPVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSDqr 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 284 ---------LSSARALPAIADAVKgDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYAlATAGQAGVANLLNLIEKE 354
Cdd:cd02811 231 laeyfadwgIPTAASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEE 308
|
170
....*....|....*...
gi 16131476 355 MKVAMTLTGAKSISEITQ 372
Cdd:cd02811 309 LRTAMFLTGAKNLAELKQ 326
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
234-330 |
2.68e-08 |
|
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: 53.74 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 234 WKDLEWIRDFW-DGPMVIKGILDPEDAR-DAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRN 311
Cdd:cd04722 102 LELIRELREAVpDVKVVVKLSPTGELAAaAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIND 181
|
90
....*....|....*....
gi 16131476 312 GLDVVRMIALGADTVLLGR 330
Cdd:cd04722 182 PEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
297-378 |
3.88e-08 |
|
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: 54.85 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 297 VKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYAL-----------------AT------------AGQAGVANL 347
Cdd:cd02808 282 LRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALgciqarkchtntcpvgvATqdpelrrrldveGKAERVANY 361
|
90 100 110
....*....|....*....|....*....|.
gi 16131476 348 LNLIEKEMKVAMTLTGAKSISEITQDSLVQG 378
Cdd:cd02808 362 LKSLAEELRELAAALGKRSLELLGRSDLLAL 392
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
237-333 |
6.60e-08 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 52.87 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 237 LEWIRDFwdGPMVIKGILDPEDARDAVRFGADGIVVSN-----HGGRQLDGVLSSaraLPAIADAVkgDIAILADSGIRN 311
Cdd:cd04730 95 VERLKAA--GIKVIPTVTSVEEARKAEAAGADALVAQGaeaggHRGTFDIGTFAL---VPEVRDAV--DIPVIAAGGIAD 167
|
90 100
....*....|....*....|..
gi 16131476 312 GLDVVRMIALGADTVLLGRAFL 333
Cdd:cd04730 168 GRGIAAALALGADGVQMGTRFL 189
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
237-332 |
1.02e-06 |
|
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: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 237 LEWIRD-FWDGPMVIKGILDPEDARDAVRFGADGIVV-----SNHGGRQLDGV-LSSARALPAIADAVKG-DIAILADSG 308
Cdd:cd00381 126 IKFIKKkYPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgVPQATAVADVAAAARDyGVPVIADGG 205
|
90 100
....*....|....*....|....
gi 16131476 309 IRNGLDVVRMIALGADTVLLGRAF 332
Cdd:cd00381 206 IRTSGDIVKALAAGADAVMLGSLL 229
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
237-333 |
1.48e-06 |
|
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: 49.27 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 237 LEWIRDFWDGPMVIK--GILDPED----ARDAVRFGADGIVVSNH-------------GGRQLDGVLSSARALPA----- 292
Cdd:cd02810 154 LKAVKAAVDIPLLVKlsPYFDLEDivelAKAAERAGADGLTAINTisgrvvdlktvgpGPKRGTGGLSGAPIRPLalrwv 233
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 16131476 293 --IADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFL 333
Cdd:cd02810 234 arLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALM 276
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
237-332 |
2.13e-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: 49.69 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 237 LEWIRDFWDGPMVIKG-ILDPEDARDAVRFGADGI-------------VVSNHGGRQLDGVLSSARAlpaiadAVKGDIA 302
Cdd:pfam00478 252 VKWIKKKYPDVQVIAGnVATAEGAKALIEAGADAVkvgigpgsicttrVVAGVGVPQLTAIYDVAEA------AKKYGVP 325
|
90 100 110
....*....|....*....|....*....|
gi 16131476 303 ILADSGIRNGLDVVRMIALGADTVLLGRAF 332
Cdd:pfam00478 326 VIADGGIKYSGDIVKALAAGADAVMLGSLL 355
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
255-333 |
1.06e-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: 46.64 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 255 DPEDARDAVRFGADGIVVSN-----HGGRQLdgvLSSARALPAIADAVkgDIAILADSGIRNGLDVVRMIALGADTVLLG 329
Cdd:COG2070 113 SVREARKAEKAGADAVVAEGaeaggHRGADE---VSTFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 187
|
....
gi 16131476 330 RAFL 333
Cdd:COG2070 188 TRFL 191
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
248-374 |
2.59e-05 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 46.19 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 248 MVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALP---AIADAVK----GDIAILADSGIRNGLDVVRMIA 320
Cdd:PRK06843 197 LIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPqitAICDVYEvcknTNICIIADGGIRFSGDVVKAIA 276
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 16131476 321 LGADTVLLGRAFLYALATAGQAGVANllnliEKEMKvamTLTGAKSISEITQDS 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 |
7.44e-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: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 244 WDGPMVIK---GILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSAR--ALP---AIADAVKG--------DIAILADS 307
Cdd:pfam01645 201 PKAPISVKlvsGHGVGTIAAGVAKAGADIILIDGYDGGTGASPKTSIKhaGLPwelALAEAHQTlkenglrdRVSLIADG 280
|
90 100
....*....|....*....|....*....
gi 16131476 308 GIRNGLDVVRMIALGADTVLLGRAFLYAL 336
Cdd:pfam01645 281 GLRTGADVAKAAALGADAVYIGTAALIAL 309
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
246-333 |
7.80e-05 |
|
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.
Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 44.43 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 246 GPMVIKGILDPEDARDAVRFGADGIVVSN-----HGGRQLDGVLSSARALPAIADAVkgDIAILADSGIRNGLDVVRMIA 320
Cdd:pfam03060 136 GVALIPTISSAKEARIAEARGADALIVQGpeaggHQGTPEYGDKGLFRLVPQVPDAV--DIPVIAAGGIWDRRGVAAALA 213
|
90
....*....|...
gi 16131476 321 LGADTVLLGRAFL 333
Cdd:pfam03060 214 LGASGVQMGTRFL 226
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
297-336 |
3.56e-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: 42.54 E-value: 3.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 16131476 297 VKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYAL 336
Cdd:COG0069 437 LRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVAL 476
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
257-332 |
1.30e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 40.72 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 257 EDARDAVRFGADGI-------------VVSNHGGRQLDGVLSSARAlpaiadAVKGDIAILADSGIRNGLDVVRMIALGA 323
Cdd:PTZ00314 294 DQAKNLIDAGADGLrigmgsgsicitqEVCAVGRPQASAVYHVARY------ARERGVPCIADGGIKNSGDICKALALGA 367
|
....*....
gi 16131476 324 DTVLLGRAF 332
Cdd:PTZ00314 368 DCVMLGSLL 376
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
254-334 |
3.07e-03 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. 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, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 39.40 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131476 254 LDPEDARD----AVRFGADGIVVSN-----HGGRQLD-----GVLS-------SARALPAIADAVKGDIAILADSGIRNG 312
Cdd:cd04738 213 LSDEELEDiadvALEHGVDGIIATNttisrPGLLRSPlanetGGLSgaplkerSTEVLRELYKLTGGKIPIIGVGGISSG 292
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90 100
....*....|....*....|..
gi 16131476 313 LDVVRMIALGADTVLLGRAFLY 334
Cdd:cd04738 293 EDAYEKIRAGASLVQLYTGLVY 314
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| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
293-335 |
5.52e-03 |
|
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.
Pssm-ID: 238203 Cd Length: 217 Bit Score: 37.83 E-value: 5.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 16131476 293 IADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYA 335
Cdd:cd00331 165 LAPLIPKDVILVSESGISTPEDVKRLAEAGADAVLIGESLMRA 207
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