|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
18-361 |
1.33e-171 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 482.03 E-value: 1.33e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 18 KNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDWLnGKKSVFPVGIAPTAFQKMATLDGELSTV 97
Cdd:pfam01070 3 KRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLL-GQRLSLPFGIAPVGMQGLAHPDGELALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 98 RGAAASNSIMICSSWSTTSVEDIgkeAKIVGATIWFQLYVYKDRAITESLIHRAEAAGVEALVLTVDTPVLGRRLKDTYN 177
Cdd:pfam01070 82 RAAAAAGIPFVLSTVSSTSLEEV---AAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 178 KFSLPKHLKFANFESNTQAEMPKGHVGESG----FMQYVSSQIDPSLDWNTLKWIRTKTNLPVIVKGVMRGDDALLALEA 253
Cdd:pfam01070 159 GFTLPPRLTPRNLLDLALHPRWALGVLRRGgaggAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 254 GVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLWGLATSGSAGVS 333
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVA 318
|
330 340
....*....|....*....|....*...
gi 193208036 334 AVLGLLQSEFYHALQLSGFRSIKELQND 361
Cdd:pfam01070 319 HALEILRDELERTMALLGCKSIADLTPS 346
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
4-361 |
8.78e-150 |
|
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: 426.86 E-value: 8.78e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 4 PALLTLDDYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDWLnGKKSVFPVGIAPTA 83
Cdd:COG1304 2 SRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLL-GKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 84 FQKMATLDGELSTVRGAAASNSIMICSSWSTTSVEDIgkeAKIVGATIWFQLYVYKDRAITESLIHRAEAAGVEALVLTV 163
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEV---AAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 164 DTPVLGRRLKDTYNKFSLPKHLKFANFESntQAEMPKGHVGESGFMQYVSSQIDPSLDWNTLKWIRTKTNLPVIVKGVMR 243
Cdd:COG1304 158 DTPVLGRRERDLREGFSQPPRLTPRNLLE--AATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 244 GDDALLALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLWG 323
Cdd:COG1304 236 PEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYG 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 193208036 324 LATSGSAGVSAVLGLLQSEFYHALQLSGFRSIKELQND 361
Cdd:COG1304 316 LAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRA 353
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
10-358 |
6.61e-149 |
|
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: 422.24 E-value: 6.61e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 10 DDYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDWLnGKKSVFPVGIAPTAFQKMAT 89
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLL-GQKLAMPFGIAPTGLQGLAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 90 LDGELSTVRGAAASNSIMICSSWSTTSVEDIGKEAkivGATIWFQLYVYKDRAITESLIHRAEAAGVEALVLTVDTPVLG 169
Cdd:cd02809 80 PDGELATARAAAAAGIPFTLSTVSTTSLEEVAAAA---PGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 170 RRLkdtynkfslpkhlkfanfesntqaempkghvgesgfmqyvssqidpslDWNTLKWIRTKTNLPVIVKGVMRGDDALL 249
Cdd:cd02809 157 RRL------------------------------------------------TWDDLAWLRSQWKGPLILKGILTPEDALR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 250 ALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLWGLATSGS 329
Cdd:cd02809 189 AVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGE 268
|
330 340
....*....|....*....|....*....
gi 193208036 330 AGVSAVLGLLQSEFYHALQLSGFRSIKEL 358
Cdd:cd02809 269 AGVAHVLEILRDELERAMALLGCASLADL 297
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
11-361 |
5.64e-114 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 336.32 E-value: 5.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 11 DYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDWLnGKKSVFPVGIAPTAFQKMATL 90
Cdd:PLN02493 8 EYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVL-GFKISMPIMVAPTAMQKMAHP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 91 DGELSTVRGAAASNSIMICSSWSTTSVEDIGKeakiVGATI-WFQLYVYKDRAITESLIHRAEAAGVEALVLTVDTPVLG 169
Cdd:PLN02493 87 DGEYATARAASAAGTIMTLSSWATSSVEEVAS----TGPGIrFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 170 RRLKDTYNKFSLPKHLKFANFESNTQAEMPKGHvgESGFMQYVSSQIDPSLDWNTLKWIRTKTNLPVIVKGVMRGDDALL 249
Cdd:PLN02493 163 RRESDIKNRFTLPPNLTLKNFEGLDLGKMDEAN--DSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 250 ALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLWGLATSGS 329
Cdd:PLN02493 241 AIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGE 320
|
330 340 350
....*....|....*....|....*....|..
gi 193208036 330 AGVSAVLGLLQSEFYHALQLSGFRSIKELQND 361
Cdd:PLN02493 321 AGVRKVLQMLRDEFELTMALSGCRSLKEISRN 352
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
10-358 |
3.57e-110 |
|
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: 325.71 E-value: 3.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 10 DDYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDWLnGKKSVFPVGIAPTAFQKMAT 89
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTIL-GHKVSLPFFISPAALAKLAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 90 LDGELSTVRGAAASNSIMICSSWSTTSVEDIgKEAKIVGATIWFQLYVYKDRAITESLIHRAEAAGVEALVLTVDTPVLG 169
Cdd:cd02922 80 PDGELNLARAAGKHGILQMISTNASCSLEEI-VDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 170 RRLKDTYnkfslpkhLKFANFESNTQAEMPKGHVGeSGFMQYVSSQIDPSLDWNTLKWIRTKTNLPVIVKGVMRGDDALL 249
Cdd:cd02922 159 KRERDER--------LKAEEAVSDGPAGKKTKAKG-GGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 250 ALEAGVDGIIVSNHGGRQMDCTVATIESLPEV---LRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLWGLAT 326
Cdd:cd02922 230 AAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIrkhCPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSA 309
|
330 340 350
....*....|....*....|....*....|..
gi 193208036 327 SGSAGVSAVLGLLQSEFYHALQLSGFRSIKEL 358
Cdd:cd02922 310 YGEEGVEKAIQILKDEIETTMRLLGVTSLDQL 341
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
9-358 |
4.28e-108 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 321.01 E-value: 4.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 9 LDDYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDWLNGKKSVfPVGIAPTAFQKMA 88
Cdd:PLN02535 8 VNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISA-PIMIAPTAMHKLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 89 TLDGELSTVRGAAASNSIMICSSWSTTSVEDIgkeAKIVGATIWFQLYVYKDRAITESLIHRAEAAGVEALVLTVDTPVL 168
Cdd:PLN02535 87 HPEGEIATARAAAACNTIMVLSFMASCTVEEV---ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 169 GRRLKDTYNKFSLPKhLKfaNFES--NTQAEMPKGhvgeSGFMQYVSSQIDPSLDWNTLKWIRTKTNLPVIVKGVMRGDD 246
Cdd:PLN02535 164 GRREADIKNKMISPQ-LK--NFEGllSTEVVSDKG----SGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLTRED 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 247 ALLALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLWGLAT 326
Cdd:PLN02535 237 AIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAA 316
|
330 340 350
....*....|....*....|....*....|..
gi 193208036 327 SGSAGVSAVLGLLQSEFYHALQLSGFRSIKEL 358
Cdd:PLN02535 317 KGEDGVRKVIEMLKDELEITMALSGCPSVKDI 348
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
2-365 |
1.32e-102 |
|
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: 307.67 E-value: 1.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 2 TPPALLTLDDYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDwLNGKKSVFPVGIAP 81
Cdd:cd03332 14 RPDLPVDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVE-LFGRTLAAPLLLAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 82 TAFQKMATLDGELSTVRGAAASNSIMICSSWSTTSVEDIGKEAKIVGAtiWFQLYVYKDRAITESLIHRAEAAGVEALVL 161
Cdd:cd03332 93 IGVQELFHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPR--WFQLYWPKDDDLTESLLRRAEKAGYRVLVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 162 TVDTPVLG---RRLKDTYNKFSlpKHLKFANFESNTQ-----AEMPKGHVGESGFMQ-----YVSSQIDPSLDWNTLKWI 228
Cdd:cd03332 171 TLDTWSLGwrpRDLDLGYLPFL--RGIGIANYFSDPVfrkklAEPVGEDPEAPPPMEaavarFVSVFSGPSLTWEDLAFL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 229 RTKTNLPVIVKGVMRGDDALLALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVA 308
Cdd:cd03332 249 REWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALA 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 193208036 309 LGARGVFVGRPVLWGLATSGSAGVSAVLGLLQSEFYHALQLSGFRSIKELqnDKHAI 365
Cdd:cd03332 329 LGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAEL--TRDAL 383
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
51-361 |
2.83e-100 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 301.26 E-value: 2.83e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 51 RPRCLRSVENIDTSIDWLnGKKSVFPVGIAPTAFQKMATLDGELSTVRGAAASNSIMICSSWSTTSVEDIGKeakiVGAT 130
Cdd:PLN02979 47 RPRILIDVSKIDMTTTVL-GFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVAS----TGPG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 131 I-WFQLYVYKDRAITESLIHRAEAAGVEALVLTVDTPVLGRRLKDTYNKFSLPKHLKFANFESNTQAEMPKGHvgESGFM 209
Cdd:PLN02979 122 IrFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEAN--DSGLA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 210 QYVSSQIDPSLDWNTLKWIRTKTNLPVIVKGVMRGDDALLALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRI 289
Cdd:PLN02979 200 SYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRI 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193208036 290 PVWMDGGVRNGRDILKAVALGARGVFVGRPVLWGLATSGSAGVSAVLGLLQSEFYHALQLSGFRSIKELQND 361
Cdd:PLN02979 280 PVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRN 351
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
6-359 |
7.39e-98 |
|
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: 294.73 E-value: 7.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 6 LLTLDDYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDWLnGKKSVFPVGIAPTAFQ 85
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELL-GIKLKTPIIMAPIAAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 86 KMATLDGELSTVRGAAASNSIMICSSWSTTSVEDIGKEAKivGATIWFQLYVYKDRAITESLIHRAEAAGVEALVLTVDT 165
Cdd:cd04737 84 GLAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASN--GGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 166 PVLGRRLKDTYNKFSLPKHLKFANFESNTQAEmpkghvGESGFMQYVSSQIDPSLDwnTLKWIRTKTNLPVIVKGVMRGD 245
Cdd:cd04737 162 TVGGNREADIRNKFQFPFGMPNLNHFSEGTGK------GKGISEIYAAAKQKLSPA--DIEFIAKISGLPVIVKGIQSPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 246 DALLALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLWGLA 325
Cdd:cd04737 234 DADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLA 313
|
330 340 350
....*....|....*....|....*....|....
gi 193208036 326 TSGSAGVSAVLGLLQSEFYHALQLSGFRSIKELQ 359
Cdd:cd04737 314 LGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVK 347
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
11-361 |
9.29e-84 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 259.57 E-value: 9.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 11 DYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDwLNGKKSVFPVGIAPTAFQKMATL 90
Cdd:PRK11197 8 DYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETT-LFGEKLSMPVALAPVGLTGMYAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 91 DGELSTVRgAAASNSIMICssWSTTSVEDIGKEAKIVGATIWFQLYVYKDRAITESLIHRAEAAGVEALVLTVDTPVLGR 170
Cdd:PRK11197 87 RGEVQAAR-AADAKGIPFT--LSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 171 RLKDTYNKFSLPkhlkFANFESNTQAEMPKG---HVGESG--------------------FMQYVSSQIDPSLDWNTLKW 227
Cdd:PRK11197 164 RYRDAHSGMSGP----NAAMRRYLQAVTHPQwawDVGLNGrphdlgnisaylgkptgledYIGWLGNNFDPSISWKDLEW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 228 IRTKTNLPVIVKGVMRGDDALLALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAV 307
Cdd:PRK11197 240 IRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMI 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 193208036 308 ALGARGVFVGRPVLWGLATSGSAGVSAVLGLLQSEFYHALQLSGFRSIKELQND 361
Cdd:PRK11197 320 ALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRD 373
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
10-358 |
8.69e-82 |
|
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: 253.99 E-value: 8.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 10 DDYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDwLNGKKSVFPVGIAPTAFQKMAT 89
Cdd:cd04736 1 EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISAS-LFGKVWSAPLVIAPTGLNGAFW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 90 LDGELSTVRGAAASNSIMICSSWSTTSVEDIGKEAkivGATIWFQLYVYKdRAITESLIHRAEAAGVEALVLTVDTPVLG 169
Cdd:cd04736 80 PNGDLALARAAAKAGIPFVLSTASNMSIEDVARQA---DGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 170 RRLKDTYNKFSLPKH------------------------LKFANFES--NTQAEMpkghvgESGFMqyvSSQIDPSLDWN 223
Cdd:cd04736 156 YRERDLRNGFAIPFRytprvlldgilhprwllrflrngmPQLANFASddAIDVEV------QAALM---SRQMDASFNWQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 224 TLKWIRTKTNLPVIVKGVMRGDDALLALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAvdNRIPVWMDGGVRNGRDI 303
Cdd:cd04736 227 DLRWLRDLWPHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAA--TYKPVLIDSGIRRGSDI 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 193208036 304 LKAVALGARGVFVGRPVLWGLATSGSAGVSAVLGLLQSEFYHALQLSGFRSIKEL 358
Cdd:cd04736 305 VKALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASL 359
|
|
| L_lactate_LldD |
NF033901 |
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ... |
11-361 |
9.74e-73 |
|
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: 230.86 E-value: 9.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 11 DYRKFSEKNLVKLARDYYESGAEQEESLRRNISAFNNLLIRPRCLRSVENIDTSIDwLNGKKSVFPVGIAPTAFQKMATL 90
Cdd:NF033901 8 DYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETK-LFGETLAMPVALAPVGLTGMYAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 91 DGELSTVRGAAASNsimICSSWSTTSVEDIGKEAKIVGATIWFQLYVYKDRAITESLIHRAEAAGVEALVLTVDTPVLGR 170
Cdd:NF033901 87 RGEVQAARAAAAKG---IPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPTPGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 171 RLKDTYNKFSLPKHLKFANFESNTQAE-------MPKGH------------VGESGFMQYVSSQIDPSLDWNTLKWIRTK 231
Cdd:NF033901 164 RYRDAHSGMSGPNAALRRMLQAVTHPQwawdvglLGRPHdlgnisayrgkpTGLEDYIGWLGNNFDPSISWKDLEWIREF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 232 TNLPVIVKGVMRGDDALLALEAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGA 311
Cdd:NF033901 244 WDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIALGA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 193208036 312 RGVFVGRPVLWGLATSGSAGVSAVLGLLQSEFYHALQLSGFRSIKELQND 361
Cdd:NF033901 324 DSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRD 373
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
225-360 |
5.28e-17 |
|
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: 81.01 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 225 LKWIRTKTNLPVIVKGV---MRGDDALLALEAGVDGIIVSNHGG-----------RQMDCTVA---------TIESLPEV 281
Cdd:cd02811 170 IEELVKALSVPVIVKEVgfgISRETAKRLADAGVKAIDVAGAGGtswarvenyraKDSDQRLAeyfadwgipTAASLLEV 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193208036 282 lRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLwGLATSGSAGVSAVLGLLQSEFYHALQLSGFRSIKELQN 360
Cdd:cd02811 250 -RSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVIETIEQIIEELRTAMFLTGAKNLAELKQ 326
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
245-317 |
1.94e-12 |
|
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: 66.35 E-value: 1.94e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193208036 245 DDALLALEAGVDGIIVSNH--GGRQMDCTVATIESLPEVLRAVDnrIPVWMDGGVRNGRDILKAVALGARGVFVG 317
Cdd:cd04730 113 EEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
247-317 |
5.66e-12 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 65.90 E-value: 5.66e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193208036 247 ALLALEAGVDGIIVSNH--GGRQMDCTVATIESLPEVLRAVDnrIPVWMDGGVRNGRDILKAVALGARGVFVG 317
Cdd:COG2070 117 ARKAEKAGADAVVAEGAeaGGHRGADEVSTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMG 187
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
223-319 |
1.71e-11 |
|
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: 64.46 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 223 NTLKWIRTK-TNLPVIVKGVMRGDDALLALEAGVDGIIVSNHGGR------QMDCTVATIESLPEVLRAVDNR-IPVWMD 294
Cdd:cd00381 124 EMIKFIKKKyPNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSicttriVTGVGVPQATAVADVAAAARDYgVPVIAD 203
|
90 100
....*....|....*....|....*
gi 193208036 295 GGVRNGRDILKAVALGARGVFVGRP 319
Cdd:cd00381 204 GGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
218-318 |
2.50e-11 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 62.22 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 218 PSLDWNTLKWIRTKT-NLPVIVKGVMRGDDALLAL-EAGVDGIIVSNHGGRQMDCTVATIESLPEVLRAVDNRIPVWMDG 295
Cdd:cd04722 98 AREDLELIRELREAVpDVKVVVKLSPTGELAAAAAeEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGG 177
|
90 100
....*....|....*....|...
gi 193208036 296 GVRNGRDILKAVALGARGVFVGR 318
Cdd:cd04722 178 GINDPEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
235-318 |
1.66e-10 |
|
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: 61.79 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 235 PVIVK---GVMRGDDALLALEAGVDGIIVSNHGG-------RQMDCT-VATIESLPEVLRAVD-----NRIPVWMDGGVR 298
Cdd:cd02808 216 PIGVKlvaGHGEGDIAAGVAAAGADFITIDGAEGgtgaaplTFIDHVgLPTELGLARAHQALVknglrDRVSLIASGGLR 295
|
90 100
....*....|....*....|
gi 193208036 299 NGRDILKAVALGARGVFVGR 318
Cdd:cd02808 296 TGADVAKALALGADAVGIGT 315
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
213-318 |
5.21e-08 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 54.59 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 213 SSQIDPSLDWNTLKWIRTKT-NLPVIVKGVMRGDDALLALEAGVDGIIVSNHGGR------QMDCTVATIESLPEVLR-A 284
Cdd:PTZ00314 261 SSQGNSIYQIDMIKKLKSNYpHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSicitqeVCAVGRPQASAVYHVARyA 340
|
90 100 110
....*....|....*....|....*....|....
gi 193208036 285 VDNRIPVWMDGGVRNGRDILKAVALGARGVFVGR 318
Cdd:PTZ00314 341 RERGVPCIADGGIKNSGDICKALALGADCVMLGS 374
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
223-318 |
1.75e-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: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 223 NTLKWIRTK-TNLPVIVKGVMRGDDALLALEAGVDGI-------------IVSNHGGRQ----MDCTvatieslpEVLRA 284
Cdd:pfam00478 250 DTVKWIKKKyPDVQVIAGNVATAEGAKALIEAGADAVkvgigpgsicttrVVAGVGVPQltaiYDVA--------EAAKK 321
|
90 100 110
....*....|....*....|....*....|....
gi 193208036 285 VDnrIPVWMDGGVRNGRDILKAVALGARGVFVGR 318
Cdd:pfam00478 322 YG--VPVIADGGIKYSGDIVKALAAGADAVMLGS 353
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
235-321 |
1.91e-06 |
|
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: 49.25 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 235 PVIVK---GVMRGDDALLALEAGVDGIIVSNHGGRqmdcTVA------------TIESLPEV---LRAVD--NRIPVWMD 294
Cdd:pfam01645 204 PISVKlvsGHGVGTIAAGVAKAGADIILIDGYDGG----TGAspktsikhaglpWELALAEAhqtLKENGlrDRVSLIAD 279
|
90 100
....*....|....*....|....*..
gi 193208036 295 GGVRNGRDILKAVALGARGVFVGRPVL 321
Cdd:pfam01645 280 GGLRTGADVAKAAALGADAVYIGTAAL 306
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
245-361 |
4.82e-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: 44.81 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 245 DDALLALEAGVDGIIV--SNHGGRQMDCTVATIES---LPEVLRAVDnrIPVWMDGGVRNGRDILKAVALGARGVFVGRP 319
Cdd:pfam03060 147 KEARIAEARGADALIVqgPEAGGHQGTPEYGDKGLfrlVPQVPDAVD--IPVIAAGGIWDRRGVAAALALGASGVQMGTR 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 193208036 320 VLwgLATSGSAGVSAVLGLLQSEFYHALQLSGF--RSIKELQND 361
Cdd:pfam03060 225 FL--LTKESGAHDAHKQKITEAGEDDTLVTSPFsgRPARALANG 266
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
246-323 |
1.93e-04 |
|
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA); Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). HBPHA catalyzes HBP to salicyaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. CBPHA is homologous to HBPHA and catalyzes the cleavage of CBP to 2-carboxylbenzaldehyde and pyruvate during the degradation of phenanthrene. They are member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188639 Cd Length: 309 Bit Score: 42.82 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 246 DALLAleAGVDGIIVSNHGGrqmDCTVATIESLPE----VLRAVDNRIPVWMDGGVRNGRD----ILKAVALGARGVFVG 317
Cdd:cd00952 36 ERLIA--AGVDGILTMGTFG---ECATLTWEEKQAfvatVVETVAGRVPVFVGATTLNTRDtiarTRALLDLGADGTMLG 110
|
....*.
gi 193208036 318 RPvLWG 323
Cdd:cd00952 111 RP-MWL 115
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
221-318 |
8.65e-04 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 40.96 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 221 DWNTLKWIR-TKTNLPVIVKGVMRGDdALLAL-EAGVDGIIVSNHGGRQmdCT---VATIeSLP------EVLRAVDNRI 289
Cdd:COG0516 123 GGDAMKKIKlTFDDVLLIPGNSATVE-PARALvDAGADLTKVGIGPGSI--CTtrvVIGL-GIPqlsaamDTVTEARMAI 198
|
90 100
....*....|....*....|....*....
gi 193208036 290 PVWMDGGVRNGRDILKAVALGARGVFVGR 318
Cdd:COG0516 199 AIAADGGIGYIHDNAKALAAGADAVMLGS 227
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
247-317 |
1.05e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 40.00 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193208036 247 ALLALEAGVDGIIVSNHGGRQMdctvATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVG 317
Cdd:cd00945 135 ARIAAEAGADFIKTSTGFGGGG----ATVEDVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
213-317 |
1.17e-03 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 40.81 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 213 SSQIDPSLDWNTLKWI-RTKTNLPVIVKGVMRGDDALLALEAGVDGIIVSNHGGR----QMDCTV----ATieSLPEVLR 283
Cdd:PLN02274 268 SSQGDSIYQLEMIKYIkKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMGSGSicttQEVCAVgrgqAT--AVYKVAS 345
|
90 100 110
....*....|....*....|....*....|....*
gi 193208036 284 -AVDNRIPVWMDGGVRNGRDILKAVALGARGVFVG 317
Cdd:PLN02274 346 iAAQHGVPVIADGGISNSGHIVKALTLGASTVMMG 380
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
218-260 |
3.74e-03 |
|
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 37.91 E-value: 3.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 193208036 218 PSLDWNTLKWIRTKTNLPVIVKGVMRGDDALLALEAGVDGIIV 260
Cdd:pfam02581 134 PPLGLEGLKAIAEAVEIPVVAIGGITPENVPEVIEAGADGVAV 176
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
216-318 |
5.57e-03 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 38.52 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 216 IDPS---LDW--NTLKWIRTKTNLPVIVKG--VMRGDDALLALEAGVDGIIVSNHGG--------RQMDCTVATieSLPE 280
Cdd:PRK07107 260 IDSSegySEWqkRTLDWIREKYGDSVKVGAgnVVDREGFRYLAEAGADFVKVGIGGGsicitreqKGIGRGQAT--ALIE 337
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 193208036 281 VLRAVDNR-------IPVWMDGGVRNGRDILKAVALGARGVFVGR 318
Cdd:PRK07107 338 VAKARDEYfeetgvyIPICSDGGIVYDYHMTLALAMGADFIMLGR 382
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
276-311 |
8.62e-03 |
|
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439839 Cd Length: 728 Bit Score: 38.31 E-value: 8.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 193208036 276 ESLPEV---LRAVD--NRIPVWMDGGVRNGRDILKAVALGA 311
Cdd:COG0069 423 LGLAEVhqtLVGNGlrDRIRLIADGKLKTGRDVAIAAALGA 463
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
217-322 |
9.07e-03 |
|
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: 37.72 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208036 217 DPSLDWNTLKWIRTKTNLPVIVK-----GVMRGDDALLAL-EAGVDGIIVSNH-------------GGRQMDCTV----- 272
Cdd:cd02810 146 DPEAVANLLKAVKAAVDIPLLVKlspyfDLEDIVELAKAAeRAGADGLTAINTisgrvvdlktvgpGPKRGTGGLsgapi 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 193208036 273 --ATIESLPEVLRAVDNRIPVWMDGGVRNGRDILKAVALGARGVFVGRPVLW 322
Cdd:cd02810 226 rpLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMW 277
|
|
| |
