SitesBLAST
Comparing GFF1136 FitnessBrowser__Phaeo:GFF1136 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 8 hits to proteins with known functional sites (download)
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
26% identity, 79% coverage: 52:395/436 of query aligns to 18:349/369 of S5FMM4
- G51 (= G85) mutation to S: Shows 4.3- and 107-fold increase of affinity to glyphosate and glycine, respectively. Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with R-54, R-81, C-202, V-332 and V-342.
- A54 (≠ Q88) mutation to R: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-81, C-202, V-332 and V-342.
- K81 (= K115) mutation to R: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, C-202, V-332 and V-342.
- S202 (≠ C246) mutation to C: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, V-332 and V-342.
- I332 (≠ V378) mutation to V: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, C-202 and V-342.
- M342 (= M388) mutation to V: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, C-202 and V-332.
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
24% identity, 77% coverage: 56:389/436 of query aligns to 22:343/364 of 1ng3A
- active site: A47 (≠ G81), G48 (= G82), M49 (≠ Q83)
- binding acetylamino-acetic acid: Y246 (= Y297), R302 (≠ L350), R329 (≠ G375)
- binding flavin-adenine dinucleotide: F33 (≠ L67), E34 (= E68), S35 (≠ A69), R41 (≠ G75), T42 (≠ A76), T43 (≠ S77), A46 (≠ N80), A47 (≠ G81), G48 (= G82), M49 (≠ Q83), V174 (= V219), S202 (≠ C246), G203 (≠ N247), W205 (≠ Y249), F209 (≠ L253), G300 (= G348), R302 (≠ L350), H327 (≠ Y373), R329 (≠ G375), N330 (≠ H376), G331 (= G377), I332 (≠ V378)
- binding phosphate ion: R89 (≠ D128), R254 (= R305)
Sites not aligning to the query:
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
24% identity, 77% coverage: 56:389/436 of query aligns to 22:343/369 of O31616
- ES 34:35 (≠ EA 68:69) binding FAD
- TT 42:43 (≠ AS 76:77) binding FAD
- AGM 47:49 (≠ GGQ 81:83) binding FAD
- G51 (= G85) mutation to R: 130-fold decrease in catalytic efficiency on glycine and 28-fold increase in that on glyphosate.; mutation to S: 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with R-54 and A-244.
- A54 (≠ Q88) mutation to R: 20-fold decrease in catalytic efficiency on glycine and 34-fold increase in that on glyphosate. 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with S-51 and A-244.
- V174 (= V219) binding FAD
- H244 (≠ N296) mutation to A: 2-fold decrease in catalytic efficiency on glycine and similar catalytic efficiency on glyphosate. 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with S-51 and R-54.
- R302 (≠ L350) binding substrate
- 327:333 (vs. 373:379, 14% identical) binding FAD
- R329 (≠ G375) binding substrate
Sites not aligning to the query:
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
24% identity, 77% coverage: 56:389/436 of query aligns to 22:343/364 of 3if9A
- active site: A47 (≠ G81), G48 (= G82), M49 (≠ Q83)
- binding flavin-adenine dinucleotide: E34 (= E68), S35 (≠ A69), T42 (≠ A76), T43 (≠ S77), A46 (≠ N80), A47 (≠ G81), G48 (= G82), M49 (≠ Q83), P173 (≠ E218), V174 (= V219), S202 (≠ C246), G203 (≠ N247), W205 (≠ Y249), F209 (≠ L253), G300 (= G348), R302 (≠ L350), H327 (≠ Y373), F328 (≠ S374), R329 (≠ G375), N330 (≠ H376), G331 (= G377), I332 (≠ V378)
- binding glycolic acid: Y246 (= Y297), R302 (≠ L350), R329 (≠ G375)
Sites not aligning to the query:
2gagB Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution (see paper)
25% identity, 82% coverage: 40:395/436 of query aligns to 21:373/403 of 2gagB
- active site: A61 (≠ G78), T64 (≠ G81), T65 (≠ G82)
- binding flavin-adenine dinucleotide: G26 (= G45), G28 (= G47), G29 (≠ Y48), H30 (≠ T49), E51 (= E68), K52 (≠ A69), G58 (= G75), N59 (≠ A76), M60 (≠ S77), R62 (= R79), N63 (= N80), T64 (≠ G81), I66 (≠ Q83), V195 (= V219), G224 (≠ C246), A225 (≠ N247), H227 (≠ Y249), L231 (= L253), L246 (= L274), G352 (≠ S374), T353 (≠ G375), G354 (≠ H376), G355 (= G377), F356 (≠ V378), K357 (≠ G379)
- binding flavin mononucleotide: A61 (≠ G78), R62 (= R79), H171 (≠ P195), V250 (≠ A278), E278 (≠ R305), R321 (≠ Y344), W323 (= W346)
- binding 2-furoic acid: T64 (≠ G81), I66 (≠ Q83), R68 (≠ G85), M263 (≠ D290), Y270 (= Y297), K357 (≠ G379)
- binding sulfite ion: K170 (≠ H194), K276 (≠ D303)
Sites not aligning to the query:
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
24% identity, 66% coverage: 28:313/436 of query aligns to 32:307/857 of Q63342
- CV 52:53 (≠ YT 48:49) binding FAD
- EK 73:74 (≠ EA 68:69) binding FAD
- 80:88 (vs. 75:83, 22% identical) binding FAD
- H84 (≠ R79) modified: Tele-8alpha-FAD histidine
- V212 (= V219) binding FAD
- W244 (≠ Y249) binding FAD
Sites not aligning to the query:
- 390:395 binding FAD
- 573:575 binding (6S)-5,6,7,8-tetrahydrofolate
- 669 binding (6S)-5,6,7,8-tetrahydrofolate
- 676:678 binding (6S)-5,6,7,8-tetrahydrofolate
- 737 binding (6S)-5,6,7,8-tetrahydrofolate
1y56B Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
19% identity, 77% coverage: 54:389/436 of query aligns to 20:348/374 of 1y56B
- active site: F44 (≠ G78), G47 (= G85), T48 (≠ S86), H224 (≠ N266), P239 (≠ V281), G305 (= G348), M338 (≠ G379)
- binding flavin-adenine dinucleotide: I33 (≠ L67), E34 (= E68), K35 (≠ A69), S42 (≠ A76), T43 (≠ S77), R45 (= R79), C46 (≠ L84), G47 (= G85), G49 (= G87), E170 (= E218), V171 (= V219), T200 (≠ C246), N201 (= N247), W203 (≠ Y249), G305 (= G348), Y306 (≠ T349), Y307 (≠ L350), G334 (= G375), H335 (= H376), G336 (= G377), F337 (≠ V378), M338 (≠ G379)
- binding flavin mononucleotide: F44 (≠ G78), R45 (= R79), I260 (≠ D303), R301 (≠ Y344), W303 (= W346)
Sites not aligning to the query:
Q8GAI3 4-methylaminobutanoate oxidase (formaldehyde-forming); MABO; Demethylating gamma-N-methylaminobutyrate oxidase; Gamma-N-methylaminobutyrate oxidase 1; EC 1.5.3.19 from Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans) (see paper)
24% identity, 90% coverage: 32:422/436 of query aligns to 21:412/824 of Q8GAI3
- W66 (≠ G78) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- H67 (≠ R79) mutation to A: Contains a non-covalently bound FAD. Exhibits about 10% of the wild-type enzyme activity.
Query Sequence
>GFF1136 FitnessBrowser__Phaeo:GFF1136
MALNLLYSNDRKGTYPNSWYAATATPLAPFAPLQGEARADVCIVGGGYTGLSAALHLAEA
GRSVILLEANRVGFGASGRNGGQLGSGQRMEQDGLESLMGEPDAAKLWHLAEDAKDLVKS
LIARHDIDCHLKPGIAHACFSKSDVSHEHRYVEHLQTRYGYGDITALDKAALQAICPSPA
YVGGSLDMGAGHLHPLAYALGLARAAAAAGVQICEGSEVLDIEDGAQIRLRTAEGQVTAD
HLILACNGYLGGLNRQVAARVMPINNFIAATEPLGADAAQVLARDVAVADSKFVVNYFRL
SHDGRLLFGGGESYGYRFPSDIAATVRKPMTEIFPHLRDVKIDYAWGGTLAITLKRMPYL
ARLGPNILSASGYSGHGVGTATHAGQLMALAVAGDGDGFDTMARVPAPAFPGGAAMRSPL
LALAMTWYALRDRLGI
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory