|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
16-362 |
0e+00 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 510.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 16 RSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATV 95
Cdd:pfam01070 2 RKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 96 RACQTMGTGMMLSSWATSSIEEVAEAGpEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRIDDVRNRF 175
Cdd:pfam01070 82 RAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 176 KLPPQLRMKNFEtnDLAFSPKGNF-----GDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVKH 250
Cdd:pfam01070 161 TLPPRLTPRNLL--DLALHPRWALgvlrrGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 251 GVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGVQ 330
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVA 318
|
330 340 350
....*....|....*....|....*....|..
gi 13124296 331 DVLEILKEEFRLAMALSGCQNVKVIDKTLVRK 362
Cdd:pfam01070 319 HALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
9-357 |
2.35e-169 |
|
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: 474.24 E-value: 2.35e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRi 168
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 169 ddvrnrfklppqlrmknfetndlafspkgnfgdnsglaeyvaqaidpsLSWDDITWLRRLTSLPIVVKGILRGDDAKEAV 248
Cdd:cd02809 159 ------------------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 249 KHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKG 328
Cdd:cd02809 191 DAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAG 270
|
330 340
....*....|....*....|....*....
gi 13124296 329 VQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd02809 271 VAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
2-361 |
1.38e-164 |
|
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: 464.22 E-value: 1.38e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 2 LPRLVCISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATA 81
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 82 MQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDT 161
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAP-APLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 162 PYLGNRIDDVRNRFKLPPQLRMKNFEtnDLAFSPKGNFGdNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRG 241
Cdd:COG1304 160 PVLGRRERDLREGFSQPPRLTPRNLL--EAATHPRWALG-LASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 242 DDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGL 321
Cdd:COG1304 237 EDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 13124296 322 AFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:COG1304 317 AAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
8-357 |
4.76e-140 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 402.57 E-value: 4.76e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 8 ISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAH 87
Cdd:PLN02493 6 VTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 88 VDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNR 167
Cdd:PLN02493 86 PDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 168 IDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEA 247
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 248 VKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEK 327
Cdd:PLN02493 242 IQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEA 321
|
330 340 350
....*....|....*....|....*....|
gi 13124296 328 GVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02493 322 GVRKVLQMLRDEFELTMALSGCRSLKEISR 351
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
1-361 |
2.60e-138 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 398.05 E-value: 2.60e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 1 MLPRLVCISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGAT 80
Cdd:PLN02535 1 MADEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 81 AMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAeAGPEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVD 160
Cdd:PLN02535 81 AMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVA-SSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 161 TPYLGNRIDDVRNRFKLPpqlRMKNFETndlAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILR 240
Cdd:PLN02535 160 VPRLGRREADIKNKMISP---QLKNFEG---LLSTEVVSDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 241 GDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWG 320
Cdd:PLN02535 234 REDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYG 313
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 13124296 321 LAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:PLN02535 314 LAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVR 354
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
9-353 |
1.49e-130 |
|
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: 377.32 E-value: 1.49e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPE-ALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNR 167
Cdd:cd02922 81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPPdQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 168 IDDVRNRFKlppqlrmknfETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEA 247
Cdd:cd02922 161 ERDERLKAE----------EAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 248 VKHGVDGILVSNHGARQLDGVPATIDVLPEIVE---AVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQ 324
Cdd:cd02922 231 AEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAY 310
|
330 340
....*....|....*....|....*....
gi 13124296 325 GEKGVQDVLEILKEEFRLAMALSGCQNVK 353
Cdd:cd02922 311 GEEGVEKAIQILKDEIETTMRLLGVTSLD 339
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
9-360 |
2.64e-128 |
|
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: 373.16 E-value: 2.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd03332 22 ERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRI 168
Cdd:cd03332 102 DAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 169 DDVRNRFKlpPQLRMKNFE--TNDLAF------SPKGNFGDNSGLAEYVAQAI----DPSLSWDDITWLRRLTSLPIVVK 236
Cdd:cd03332 182 RDLDLGYL--PFLRGIGIAnyFSDPVFrkklaePVGEDPEAPPPMEAAVARFVsvfsGPSLTWEDLAFLREWTDLPIVLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 237 GILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRP 316
Cdd:cd03332 260 GILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRP 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 13124296 317 IIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV 360
Cdd:cd03332 340 YAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
51-357 |
1.69e-126 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 368.28 E-value: 1.69e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 51 PRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQ 130
Cdd:PLN02979 48 PRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 131 LYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRIDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVA 210
Cdd:PLN02979 127 LYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 211 QAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFL 290
Cdd:PLN02979 204 GQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFL 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124296 291 DGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02979 284 DGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR 350
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
10-358 |
2.89e-118 |
|
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: 346.74 E-value: 2.89e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 10 DYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVD 89
Cdd:cd04737 10 DLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 90 GELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRID 169
Cdd:cd04737 90 GEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGGNREA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 170 DVRNRFKLPpqLRMKNFEtNDLAFSPKGnfgdnSGLAEYVAQAiDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVK 249
Cdd:cd04737 170 DIRNKFQFP--FGMPNLN-HFSEGTGKG-----KGISEIYAAA-KQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 250 HGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGV 329
Cdd:cd04737 241 AGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGV 320
|
330 340
....*....|....*....|....*....
gi 13124296 330 QDVLEILKEEFRLAMALSGCQNVKVIDKT 358
Cdd:cd04737 321 ASVLEHLNKELKIVMQLAGTRTIEDVKRT 349
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
10-357 |
4.24e-92 |
|
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: 280.18 E-value: 4.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 10 DYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVD 89
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 90 GELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYIYKdREISRQIVKRAEKQGYKAIFVTVDTPYLGNRID 169
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDL-WFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 170 DVRNRFKLP--------------PQLRMKNFETNDLAfspKGNFG--DNSGLAEYVA---QAIDPSLSWDDITWLRRLTS 230
Cdd:cd04736 160 DLRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPQ---LANFAsdDAIDVEVQAAlmsRQMDASFNWQDLRWLRDLWP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 231 LPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVegKVEVFLDGGVRKGTDVLKALALGAKA 310
Cdd:cd04736 237 HKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 13124296 311 VFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd04736 315 VLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
7-366 |
2.93e-89 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 273.44 E-value: 2.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 7 CISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPIC---VGATAMq 83
Cdd:PRK11197 5 AASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVAlapVGLTGM- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 84 cMAHvDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPY 163
Cdd:PRK11197 84 -YAR-RGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPM-WFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 164 LGNRIDDVRNRFKLPP-------QLRMKNFETNDLAFSPK----GN----FGDNSGLAEYVAQA---IDPSLSWDDITWL 225
Cdd:PRK11197 161 PGARYRDAHSGMSGPNaamrrylQAVTHPQWAWDVGLNGRphdlGNisayLGKPTGLEDYIGWLgnnFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 226 RRLTSLPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALA 305
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124296 306 LGAKAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLA 366
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGNAA 381
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
56-353 |
2.11e-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: 82.16 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 56 NVADIDLSTSVLGQRVSMPICVGAtamqcM-------AHVDGELAtvRACQTMGTGMMLSS----------WATSSIeeV 118
Cdd:cd02811 36 DLDDIDLSTEFLGKRLSAPLLISA-----MtggsekaKEINRNLA--EAAEELGIAMGVGSqraaledpelAESFTV--V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 119 AEAGPEALRWMQLYIYKDREISRQIVKRA-EKQGYKAIFVTVdtpylgnriddvrNrfklPPQlrmknfEtndlAFSPKG 197
Cdd:cd02811 107 REAPPNGPLIANLGAVQLNGYGVEEARRAvEMIEADALAIHL-------------N----PLQ------E----AVQPEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 198 --NFgdnSGLAEYVAQaidpslswdditwLRRLTSLPIVVK----GILRgDDAKEAVKHGVDGILVSNHG---------A 262
Cdd:cd02811 160 drDF---RGWLERIEE-------------LVKALSVPVIVKevgfGISR-ETAKRLADAGVKAIDVAGAGgtswarvenY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 263 RQLD------------GVPaTIDVLPEIVEAVEgKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIwGLAFQGEKGVQ 330
Cdd:cd02811 223 RAKDsdqrlaeyfadwGIP-TAASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVI 299
|
330 340
....*....|....*....|...
gi 13124296 331 DVLEILKEEFRLAMALSGCQNVK 353
Cdd:cd02811 300 ETIEQIIEELRTAMFLTGAKNLA 322
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
204-315 |
1.52e-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: 57.21 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 204 GLAEYVAQAIDPSLSWDDITWLR-RLTSLPIVVKGILRG-DDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEA 281
Cdd:cd04722 87 GVEIHGAVGYLAREDLELIRELReAVPDVKVVVKLSPTGeLAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAK 166
|
90 100 110
....*....|....*....|....*....|....
gi 13124296 282 VEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:cd04722 167 RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
242-314 |
7.81e-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: 52.49 E-value: 7.81e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13124296 242 DDAKEAVKHGVDGILVSN-----HGARQLDGvpaTIDVLPEIVEAVegKVEVFLDGGVRKGTDVLKALALGAKAVFVG 314
Cdd:cd04730 113 EEARKAEAAGADALVAQGaeaggHRGTFDIG---TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
232-316 |
8.63e-08 |
|
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: 53.49 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 232 PIVVK---GILRGDDAKEAVKHGVDGILVSNH----GA-----RQLDGVPaTIDVLPEIVEAV--EG---KVEVFLDGGV 294
Cdd:pfam01645 204 PISVKlvsGHGVGTIAAGVAKAGADIILIDGYdggtGAspktsIKHAGLP-WELALAEAHQTLkeNGlrdRVSLIADGGL 282
|
90 100
....*....|....*....|..
gi 13124296 295 RKGTDVLKALALGAKAVFVGRP 316
Cdd:pfam01645 283 RTGADVAKAAALGADAVYIGTA 304
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
222-315 |
1.96e-07 |
|
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: 52.54 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 222 ITWLRRLT-SLPIVVK---GILRGDDAkEAVKHG-VDGILVSNH----GARQLD-----GVPaTIDVLPEIVEA-----V 282
Cdd:cd02808 205 IEDLREATgGKPIGVKlvaGHGEGDIA-AGVAAAgADFITIDGAeggtGAAPLTfidhvGLP-TELGLARAHQAlvkngL 282
|
90 100 110
....*....|....*....|....*....|...
gi 13124296 283 EGKVEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:cd02808 283 RDRVSLIASGGLRTGADVAKALALGADAVGIGT 315
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
244-314 |
4.87e-07 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 50.88 E-value: 4.87e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124296 244 AKEAVKHGVDGILVSNHGA---RQLDGVPaTIDVLPEIVEAVegKVEVFLDGGVRKGTDVLKALALGAKAVFVG 314
Cdd:COG2070 117 ARKAEKAGADAVVAEGAEAgghRGADEVS-TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 187
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
222-316 |
1.15e-04 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 43.66 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 222 ITWLRRL-TSLPIVVKGILRGDDAKEAVKHGVDGILV-----SNHGARQLDGV--P---ATIDVlpeiVEAVEG-KVEVF 289
Cdd:cd00381 126 IKFIKKKyPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgvPqatAVADV----AAAARDyGVPVI 201
|
90 100
....*....|....*....|....*..
gi 13124296 290 LDGGVRKGTDVLKALALGAKAVFVGRP 316
Cdd:cd00381 202 ADGGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
220-315 |
2.50e-04 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 43.03 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 220 DDITWLRRLT-SLPIVVKGILRGDDAKEAVKHGVDGI-------------LVSNHGARQLDGVpatIDVLPEiveAVEGK 285
Cdd:PTZ00314 271 DMIKKLKSNYpHVDIIAGNVVTADQAKNLIDAGADGLrigmgsgsicitqEVCAVGRPQASAV---YHVARY---ARERG 344
|
90 100 110
....*....|....*....|....*....|
gi 13124296 286 VEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:PTZ00314 345 VPCIADGGIKNSGDICKALALGADCVMLGS 374
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
233-314 |
7.58e-03 |
|
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: 37.88 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124296 233 IVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATID-----VLPEIVEAVEgkVEVFLDGGVRKGTDVLKALALG 307
Cdd:pfam03060 138 ALIPTISSAKEARIAEARGADALIVQGPEAGGHQGTPEYGDkglfrLVPQVPDAVD--IPVIAAGGIWDRRGVAAALALG 215
|
....*..
gi 13124296 308 AKAVFVG 314
Cdd:pfam03060 216 ASGVQMG 222
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
265-314 |
9.92e-03 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 37.07 E-value: 9.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 13124296 265 LDGVPATIDVLPEIVEAVEGKVEVflDGGVRKGTDVLKALALGAKAVFVG 314
Cdd:pfam00977 55 KEGRPVNLDVVEEIAEEVFIPVQV--GGGIRSLEDVERLLSAGADRVIIG 102
|
|
| |
