SitesBLAST
Comparing WP_085636469.1 NCBI__GCF_002115805.1:WP_085636469.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 6 hits to proteins with known functional sites (download)
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
27% identity, 66% coverage: 26:311/434 of query aligns to 38:314/866 of Q9UI17
- CV 59:60 (≠ YT 46:47) binding FAD
- EK 80:81 (≠ DA 66:67) binding FAD
- 87:95 (vs. 73:81, 22% identical) binding FAD
- H91 (≠ R77) modified: Tele-8alpha-FAD histidine
- H109 (≠ G98) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (= V217) binding FAD
- S279 (≠ G273) to P: in dbSNP:rs532964
Sites not aligning to the query:
- 397:402 binding FAD
- 530 A → G: in dbSNP:rs1805073
- 646 S → P: in dbSNP:rs1805074
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
27% identity, 66% coverage: 27:311/434 of query aligns to 33:307/857 of Q63342
- CV 52:53 (≠ YT 46:47) binding FAD
- EK 73:74 (≠ DA 66:67) binding FAD
- 80:88 (vs. 73:81, 22% identical) binding FAD
- H84 (≠ R77) modified: Tele-8alpha-FAD histidine
- V212 (= V217) binding FAD
- W244 (vs. gap) 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
7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
24% identity, 83% coverage: 36:396/434 of query aligns to 1:350/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (= I42), G8 (= G43), G10 (= G45), V11 (≠ Y46), I12 (≠ T47), V30 (≠ L65), E31 (≠ D66), K32 (≠ A67), E38 (≠ G73), A39 (= A74), S40 (= S75), A43 (≠ N78), G45 (= G80), L46 (≠ Q81), V171 (= V217), G200 (= G244), G201 (≠ N245), W203 (≠ Y247), G298 (= G346), R300 (≠ L348), P301 (≠ A349), Y326 (≠ S372), R327 (≠ G373), N328 (≠ H374), G329 (= G375), I330 (≠ V376)
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)
26% identity, 88% coverage: 16:399/434 of query aligns to 12:392/824 of Q8GAI3
- W66 (≠ G76) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- H67 (≠ R77) mutation to A: Contains a non-covalently bound FAD. Exhibits about 10% of the wild-type enzyme activity.
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
23% identity, 81% coverage: 50:402/434 of query aligns to 18:361/369 of S5FMM4
- G51 (= G83) 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 (≠ Q86) 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 (≠ V120) 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 (≠ G244) 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 (≠ V376) 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 (≠ L386) 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.
5i39A High resolution structure of l-amino acid deaminase from proteus vulgaris with the deletion of the specific insertion sequence (see paper)
22% identity, 75% coverage: 36:362/434 of query aligns to 24:337/383 of 5i39A
- active site: F66 (≠ N78), Q69 (= Q81), A70 (≠ L82), Q248 (≠ E274), P267 (≠ V293)
- binding flavin-adenine dinucleotide: V30 (≠ I42), G31 (= G43), G33 (= G45), I34 (≠ Y46), L35 (≠ T47), V53 (≠ L65), E54 (≠ D66), K55 (≠ A67), Q62 (≠ A74), S63 (= S75), F66 (≠ N78), Y67 (≠ G79), Q69 (= Q81), A196 (≠ H216), A197 (≠ V217), G226 (= G244), G227 (≠ N245), W229 (≠ I256), Q248 (≠ E274), Q250 (≠ R276), G321 (= G346), M323 (≠ L348)
Sites not aligning to the query:
Query Sequence
>WP_085636469.1 NCBI__GCF_002115805.1:WP_085636469.1
MNLLFSNDARGSYPDSWYAATATPLPPFAPLQGETRADVCIIGAGYTGLSAALHLAEMGA
DVVLLDAHRVGFGASGRNGGQLGSGQRQDQITLEKLVGSDAARALWDLGEDSKTLVRDLV
ARHGLDCYLRDGVAWAASRPADADDLHQYAEHLQTRYGYDRIEALDRDAFHALCPSPDYI
GGTLDMGAGHLHPLRLALGLADAAAKAGARIHERSHVHDIRHGSKITVRTDAGHVIADQV
ILAGNGYLGGLDRQVIARVMPINNYIVATEPLGEDRMKVLTRDVAVADSRFVVNYFRLSH
DGRLLFGGGETYGYRFPADIPALVRKRMAVIYPHLRDVRIDYAWGGTLAITIRRMPYLAR
VRPNMLSASGYSGHGVGTAIQAGKLLAEATRGTSDGFETYNAIPHTPFPGGGMFRTPLLT
LAMTWFAMRDRLGI
Or try a new SitesBLAST search
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