|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
13-349 |
1.38e-173 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 486.27 E-value: 1.38e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 13 AQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAFHSIAWPDGEKST 92
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 93 ARAAQEANICYVISSYASYSLEDIVAAApEGFRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDTPVLGNRRRDKRNQ 172
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 173 LNLEANILLKDL-----------RALKEEKPTQSVPV--SFPKASFCWNDLSLLQSITRLPIILKGILTKEDAELAMKHN 239
Cdd:pfam01070 160 FTLPPRLTPRNLldlalhprwalGVLRRGGAGGAAAFvgSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 240 VQGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLACKGEDGVKE 319
Cdd:pfam01070 240 VDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAH 319
|
330 340 350
....*....|....*....|....*....|
gi 14091775 320 VLDILTAELHRCMTLSGCQSVAEISPDLIQ 349
Cdd:pfam01070 320 ALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
7-345 |
2.55e-168 |
|
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: 470.78 E-value: 2.55e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 7 ADFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAFHSIAWP 86
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 87 DGEKSTARAAQEANICYVISSYASYSLEDIVAAAPeGFRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDTPVLGNRr 166
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 167 rdkrnqlnleanillkdlralkeekptqsvpvsfpkasFCWNDLSLLQSITRLPIILKGILTKEDAELAMKHNVQGIVVS 246
Cdd:cd02809 159 --------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 247 NHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLACKGEDGVKEVLDILTA 326
Cdd:cd02809 201 NHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRD 280
|
330
....*....|....*....
gi 14091775 327 ELHRCMTLSGCQSVAEISP 345
Cdd:cd02809 281 ELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
1-348 |
5.18e-154 |
|
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: 436.87 E-value: 5.18e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 1 MP-LVCLADFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTA 79
Cdd:COG1304 1 MSrILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 80 FHSIAWPDGEKSTARAAQEANICYVISSYASYSLEDiVAAAPEGFRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDT 159
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEE-VAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 160 PVLGNRRRDKRNQLNL--------EANILLKDLRALKEEKPTQSVPVSFpKASFCWNDLSLLQSITRLPIILKGILTKED 231
Cdd:COG1304 160 PVLGRRERDLREGFSQpprltprnLLEAATHPRWALGLASLAAWLDTNF-DPSLTWDDIAWLRERWPGPLIVKGVLSPED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 232 AELAMKHNVQGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLAC 311
Cdd:COG1304 239 ARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAA 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 14091775 312 KGEDGVKEVLDILTAELHRCMTLSGCQSVAEISPDLI 348
Cdd:COG1304 319 GGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
8-345 |
6.09e-132 |
|
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: 380.40 E-value: 6.09e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 8 DFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAFHSIAWPD 87
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 88 GEKSTARAAQEANICYVISSYASYSLEDIVAAAPEG-FRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDTPVLGNRR 166
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDqPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 167 RDKRNQLNLEANILLKDLRALKEEKPTQSVPVSFPKASFCWNDLSLLQSITRLPIILKGILTKEDAELAMKHNVQGIVVS 246
Cdd:cd02922 162 RDERLKAEEAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 247 NHGGRQLDEVSASIDALREVV---AAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLACKGEDGVKEVLDI 323
Cdd:cd02922 242 NHGGRQLDTAPAPIEVLLEIRkhcPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQI 321
|
330 340
....*....|....*....|..
gi 14091775 324 LTAELHRCMTLSGCQSVAEISP 345
Cdd:cd02922 322 LKDEIETTMRLLGVTSLDQLGP 343
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
4-348 |
7.13e-122 |
|
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: 356.21 E-value: 7.13e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 4 VCLADFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAFHSI 83
Cdd:cd03332 19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 84 AWPDGEKSTARAAQEANICYVISSYASYSLEDIVAAAPEGFRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDTPVLG 163
Cdd:cd03332 99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 164 NRRRDKRN----QLNLE--ANIL-----LKDLRALKEEKPTQSVPVS---------FPKASFCWNDLSLLQSITRLPIIL 223
Cdd:cd03332 179 WRPRDLDLgylpFLRGIgiANYFsdpvfRKKLAEPVGEDPEAPPPMEaavarfvsvFSGPSLTWEDLAFLREWTDLPIVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 224 KGILTKEDAELAMKHNVQGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGR 303
Cdd:cd03332 259 KGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGR 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 14091775 304 PILWGLACKGEDGVKEVLDILTAELHRCMTLSGCQSVAEISPDLI 348
Cdd:cd03332 339 PYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
4-344 |
4.48e-114 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 335.65 E-value: 4.48e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 4 VCLADFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAFHSI 83
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 84 AWPDGEKSTARAAQEANICYVISSYASYSLEDiVAAAPEGFRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDTPVLG 163
Cdd:PLN02535 86 AHPEGEIATARAAAACNTIMVLSFMASCTVEE-VASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 164 NRRRDKRNQLNLEAnilLKDLRALKeekPTQSVPV------SFPK----ASFCWNDLSLLQSITRLPIILKGILTKEDAE 233
Cdd:PLN02535 165 RREADIKNKMISPQ---LKNFEGLL---STEVVSDkgsgleAFASetfdASLSWKDIEWLRSITNLPILIKGVLTREDAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 234 LAMKHNVQGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLACKG 313
Cdd:PLN02535 239 KAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKG 318
|
330 340 350
....*....|....*....|....*....|.
gi 14091775 314 EDGVKEVLDILTAELHRCMTLSGCQSVAEIS 344
Cdd:PLN02535 319 EDGVRKVIEMLKDELEITMALSGCPSVKDIT 349
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
3-344 |
4.36e-107 |
|
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: 317.46 E-value: 4.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 3 LVCLADFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAFHS 82
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 83 IAWPDGEKSTARAAQEANICYVISSYASYSLEDIVAAAPEGFRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDTPVL 162
Cdd:cd04737 85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 163 GNRRRDKRN--QLNLEANILLKDLRALKEEKPTQSVPVSFpKASFCWNDLSLLQSITRLPIILKGILTKEDAELAMKHNV 240
Cdd:cd04737 165 GNREADIRNkfQFPFGMPNLNHFSEGTGKGKGISEIYAAA-KQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAINAGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 241 QGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLACKGEDGVKEV 320
Cdd:cd04737 244 DGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASV 323
|
330 340
....*....|....*....|....
gi 14091775 321 LDILTAELHRCMTLSGCQSVAEIS 344
Cdd:cd04737 324 LEHLNKELKIVMQLAGTRTIEDVK 347
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
1-348 |
9.00e-105 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 312.05 E-value: 9.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 1 MPLVCLADFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAF 80
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 81 HSIAWPDGEKSTARAAQEANICYVISSYASYSLEDIVAAAPeGFRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDTP 160
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 161 VLGNRRRDKRNQLNLEANILLKDLRAL---KEEKPTQSVPVSFPKA----SFCWNDLSLLQSITRLPIILKGILTKEDAE 233
Cdd:PLN02493 160 RLGRRESDIKNRFTLPPNLTLKNFEGLdlgKMDEANDSGLASYVAGqidrTLSWKDVQWLQTITKLPILVKGVLTGEDAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 234 LAMKHNVQGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLACKG 313
Cdd:PLN02493 240 IAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEG 319
|
330 340 350
....*....|....*....|....*....|....*
gi 14091775 314 EDGVKEVLDILTAELHRCMTLSGCQSVAEISPDLI 348
Cdd:PLN02493 320 EAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 354
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
47-348 |
9.91e-94 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 283.92 E-value: 9.91e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 47 LRPRYLRDMSKVDTRTTIQGQEISAPICISPTAFHSIAWPDGEKSTARAAQEANICYVISSYASYSLEDIVAAAPeGFRW 126
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 127 FQLYMKSDWDFNKQMVQRAEALGFKALVITIDTPVLGNRRRDKRNQLNLEANILLKDLRAL---KEEKPTQSVPVSFPKA 203
Cdd:PLN02979 125 FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLdlgKMDEANDSGLASYVAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 204 ----SFCWNDLSLLQSITRLPIILKGILTKEDAELAMKHNVQGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMD 279
Cdd:PLN02979 205 qidrTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLD 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14091775 280 GGVRTGTDVLKALALGARCIFLGRPILWGLACKGEDGVKEVLDILTAELHRCMTLSGCQSVAEISPDLI 348
Cdd:PLN02979 285 GGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 353
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
7-345 |
1.71e-89 |
|
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: 272.86 E-value: 1.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 7 ADFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAFHSIAWP 86
Cdd:cd04736 1 EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 87 DGEKSTARAAQEANICYVISSYASYSLEDiVAAAPEGFRWFQLYMKSDwDFNKQMVQRAEALGFKALVITIDTPVLGNRR 166
Cdd:cd04736 81 NGDLALARAAAKAGIPFVLSTASNMSIED-VARQADGDLWFQLYVVHR-ELAELLVKRALAAGYTTLVLTTDVAVNGYRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 167 RDKRNQLNLEANI--------------LLKDLR----ALKEEKPTQSVPVSFP--------KASFCWNDLSLLQSITRLP 220
Cdd:cd04736 159 RDLRNGFAIPFRYtprvlldgilhprwLLRFLRngmpQLANFASDDAIDVEVQaalmsrqmDASFNWQDLRWLRDLWPHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 221 IILKGILTKEDAELAMKHNVQGIVVSNHGGRQLDEVSASIDALREVVAAVKgkIEVYMDGGVRTGTDVLKALALGARCIF 300
Cdd:cd04736 239 LLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATY--KPVLIDSGIRRGSDIVKALALGANAVL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 14091775 301 LGRPILWGLACKGEDGVKEVLDILTAELHRCMTLSGCQSVAEISP 345
Cdd:cd04736 317 LGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
1-348 |
6.84e-82 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 254.18 E-value: 6.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 1 MPLVCLADFKAHAQKQLSKTSWDFIEGEADDGITYSENIAAFKRIRLRPRYLRDMSKVDTRTTIQGQEISAPICISPTAF 80
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 81 HSIAWPDGEKSTARAAQEANICYVISSYASYSLEDiVAAAPEGFRWFQLYMKSDWDFNKQMVQRAEALGFKALVITIDTP 160
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEE-VAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 161 VLGNRRRDKRNQLNLEANILLKDLRALKeeKPTQSVPVSF--------------PKA----------------SFCWNDL 210
Cdd:PRK11197 160 VPGARYRDAHSGMSGPNAAMRRYLQAVT--HPQWAWDVGLngrphdlgnisaylGKPtgledyigwlgnnfdpSISWKDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 211 SLLQSITRLPIILKGILTKEDAELAMKHNVQGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLK 290
Cdd:PRK11197 238 EWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 14091775 291 ALALGARCIFLGRPILWGLACKGEDGVKEVLDILTAELHRCMTLSGCQSVAEISPDLI 348
Cdd:PRK11197 318 MIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
42-342 |
1.75e-15 |
|
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: 76.38 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 42 FKRIRLRPRYLR--DMSKVDTRTTIQGQEISAPICISP-TAFHsiawPDGEK---STARAAQEANICYVISSYaSYSLED 115
Cdd:cd02811 22 FDDVRLVHNALPelDLDDIDLSTEFLGKRLSAPLLISAmTGGS----EKAKEinrNLAEAAEELGIAMGVGSQ-RAALED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 116 --------IV-AAAPEGFRW-----FQLYmksdwDFNKQMVQRA-EALGFKALVITIDTP-----VLGNRrrDKRNqlnl 175
Cdd:cd02811 97 pelaesftVVrEAPPNGPLIanlgaVQLN-----GYGVEEARRAvEMIEADALAIHLNPLqeavqPEGDR--DFRG---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 176 eaniLLKDLRALKEEkptqsVPVsfpkasfcwndlsllqsitrlPIILK----GIlTKEDAELAMKHNVQGIVVSNHGG- 250
Cdd:cd02811 166 ----WLERIEELVKA-----LSV---------------------PVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGt 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 251 --------RQLDEVSASID-----------ALREVVAAVKgKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILwGLAC 311
Cdd:cd02811 215 swarvenyRAKDSDQRLAEyfadwgiptaaSLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAAL 292
|
330 340 350
....*....|....*....|....*....|.
gi 14091775 312 KGEDGVKEVLDILTAELHRCMTLSGCQSVAE 342
Cdd:cd02811 293 EGEEAVIETIEQIIEELRTAMFLTGAKNLAE 323
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
211-311 |
4.27e-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: 51.39 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 211 SLLQSITRL-------PIILKGILTKEDAELAM---KHNVQGIVVSNHGG-------RQLDEVS-ASIDALREVV----- 267
Cdd:cd02808 200 DLAQLIEDLreatggkPIGVKLVAGHGEGDIAAgvaAAGADFITIDGAEGgtgaaplTFIDHVGlPTELGLARAHqalvk 279
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 14091775 268 AAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLAC 311
Cdd:cd02808 280 NGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGC 323
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
73-303 |
8.75e-07 |
|
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: 49.12 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 73 ICISPTAFHSIAWPDgekSTARAAQEANICYVISSYAS----------YSLEDIVAAAPEGFRWFQLYMKSDWDFNKQMV 142
Cdd:cd04722 1 VILALLAGGPSGDPV---ELAKAAAEAGADAIIVGTRSsdpeeaetddKEVLKEVAAETDLPLGVQLAINDAAAAVDIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 143 QRAEALGFKALVITIDTPVLgnrrrdkrnqlnleANILLKDLRALKEEKPTQsvpvsfpkasfcwndlsllqsitrlPII 222
Cdd:cd04722 78 AAARAAGADGVEIHGAVGYL--------------AREDLELIRELREAVPDV-------------------------KVV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 223 LKGILTKEDAELAMK-HNVQGIVVSNHGGRQLDEVSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFL 301
Cdd:cd04722 119 VKLSPTGELAAAAAEeAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIV 198
|
..
gi 14091775 302 GR 303
Cdd:cd04722 199 GS 200
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
262-304 |
2.07e-04 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 42.50 E-value: 2.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 14091775 262 ALREVVAAVKG-KIEVYMDGGVRTGTDVLKALALGARCIFLGRP 304
Cdd:cd00381 185 AVADVAAAARDyGVPVIADGGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
262-312 |
2.40e-04 |
|
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: 42.70 E-value: 2.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 14091775 262 ALREVVAAVK-----GKIEVYMDGGVRTGTDVLKALALGARCIFLGRPILWGLACK 312
Cdd:pfam01645 257 ALAEAHQTLKenglrDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCI 312
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
142-342 |
3.76e-04 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 42.03 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 142 VQRAEALGFKA--LVITIDTP-VLGNRRRDKRNQLNleanILLKDLRALKEEKPTQSVPvsfpkasfcwndlsllqsitR 218
Cdd:PLN02826 207 VQGVRALSQYAdyLVINVSSPnTPGLRKLQGRKQLK----DLLKKVLAARDEMQWGEEG--------------------P 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 219 LPIILK--GILTKED----AELAMKHNVQGIVVSNHGGRQLDEVSA------------------SIDALREVVAAVKGKI 274
Cdd:PLN02826 263 PPLLVKiaPDLSKEDlediAAVALALGIDGLIISNTTISRPDSVLGhphadeagglsgkplfdlSTEVLREMYRLTRGKI 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14091775 275 EVYMDGGVRTGTDVLKALALGARCIFLgrpiLWGLACKGedgvKEVLDILTAELHRCMTLSGCQSVAE 342
Cdd:PLN02826 343 PLVGCGGVSSGEDAYKKIRAGASLVQL----YTAFAYEG----PALIPRIKAELAACLERDGFKSIQE 402
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
256-302 |
9.22e-04 |
|
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: 9.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 14091775 256 VSASIDALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLG 302
Cdd:cd00945 155 GGATVEDVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
279-303 |
1.50e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 40.34 E-value: 1.50e-03
10 20
....*....|....*....|....*
gi 14091775 279 DGGVRTGTDVLKALALGARCIFLGR 303
Cdd:PTZ00314 350 DGGIKNSGDICKALALGADCVMLGS 374
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
228-296 |
1.84e-03 |
|
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: 39.39 E-value: 1.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14091775 228 TKEDAELAMKHNVQGIVVSNH--GGRQLDEVSASIDALREVVAAVKgkIEVYMDGGVRTGTDVLKALALGA 296
Cdd:cd04730 111 SVEEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGA 179
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
262-303 |
4.21e-03 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 38.65 E-value: 4.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 14091775 262 ALREVVAAVKGKIEVYMDGGVRTGTDVLKALALGARCIFLGR 303
Cdd:COG0516 186 AAMDTVTEARMAIAIAADGGIGYIHDNAKALAAGADAVMLGS 227
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
261-296 |
7.23e-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: 7.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 14091775 261 DALREVVAA-----VKGKIEVYMDGGVRTGTDVLKALALGA 296
Cdd:COG0069 423 LGLAEVHQTlvgngLRDRIRLIADGKLKTGRDVAIAAALGA 463
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
220-296 |
8.45e-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: 37.48 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14091775 220 PIILKgI---LTKED----AELAMKHNVQGIVVSN--------HGGRQLDE---VS------ASIDALREVVAAVKGKIE 275
Cdd:cd04738 204 PLLVK-IapdLSDEElediADVALEHGVDGIIATNttisrpglLRSPLANEtggLSgaplkeRSTEVLRELYKLTGGKIP 282
|
90 100
....*....|....*....|.
gi 14091775 276 VYMDGGVRTGTDVLKALALGA 296
Cdd:cd04738 283 IIGVGGISSGEDAYEKIRAGA 303
|
|
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
271-296 |
9.82e-03 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 37.93 E-value: 9.82e-03
10 20
....*....|....*....|....*.
gi 14091775 271 KGKIEVYMDGGVRTGTDVLKALALGA 296
Cdd:PRK11750 1065 RHKIRLQVDGGLKTGLDVIKAAILGA 1090
|
|
| |
