SitesBLAST
Comparing WP_049326229.1 NCBI__GCF_000013785.1:WP_049326229.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 hits to proteins with known functional sites (download)
5i39A High resolution structure of l-amino acid deaminase from proteus vulgaris with the deletion of the specific insertion sequence (see paper)
23% identity, 82% coverage: 43:405/444 of query aligns to 23:370/383 of 5i39A
- active site: F66 (≠ N86), Q69 (= Q89), A70 (≠ L90), Q248 (≠ L284), P267 (≠ D303)
- binding flavin-adenine dinucleotide: V30 (= V50), G31 (= G51), G33 (= G53), I34 (≠ F54), L35 (≠ S55), V53 (≠ L73), E54 (= E74), K55 (≠ A75), Q62 (≠ A82), S63 (= S83), F66 (≠ N86), Y67 (≠ G87), Q69 (= Q89), A196 (≠ K224), A197 (≠ V225), G226 (≠ C252), G227 (≠ N253), W229 (≠ Y255), Q248 (≠ L284), Q250 (≠ R286), G321 (= G355), M323 (≠ I357), T348 (≠ S383), G349 (= G384), W350 (≠ H385), G351 (= G386), M352 (≠ L387), T353 (≠ N388)
1y56B Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
23% identity, 82% coverage: 43:406/444 of query aligns to 3:356/374 of 1y56B
- active site: F44 (≠ G84), G47 (= G87), T48 (≠ G88), H224 (≠ S272), P239 (≠ T293), G305 (= G355), M338 (≠ N388)
- binding flavin-adenine dinucleotide: G11 (= G51), G13 (= G53), I14 (≠ F54), V15 (≠ S55), I33 (≠ L73), E34 (= E74), K35 (≠ A75), S42 (≠ A82), T43 (≠ S83), R45 (= R85), C46 (≠ N86), G47 (= G87), G49 (≠ Q89), E170 (≠ K224), V171 (= V225), T200 (≠ C252), N201 (= N253), W203 (≠ Y255), G305 (= G355), Y306 (≠ M356), Y307 (≠ I357), G334 (= G384), H335 (= H385), G336 (= G386), F337 (≠ L387), M338 (≠ N388)
- binding flavin mononucleotide: F44 (≠ G84), R45 (= R85), I260 (≠ D310), R301 (≠ Y351), W303 (= W353)
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
25% identity, 69% coverage: 12:316/444 of query aligns to 10:303/857 of Q63342
- CV 52:53 (≠ FS 54:55) binding FAD
- EK 73:74 (≠ EA 74:75) binding FAD
- 80:88 (vs. 81:102, 9% identical) binding FAD
- H84 (≠ R85) modified: Tele-8alpha-FAD histidine
- V212 (= V225) binding FAD
- W244 (≠ Y255) 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
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
22% identity, 55% coverage: 160:405/444 of query aligns to 104:350/369 of O31616
- V174 (= V225) binding FAD
- H244 (≠ N292) 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 (≠ I357) binding substrate
- 327:333 (vs. 382:388, 14% identical) binding FAD
- R329 (≠ G384) binding substrate
Sites not aligning to the query:
- 14:15 binding FAD
- 34:35 binding FAD
- 42:43 binding FAD
- 47:49 binding FAD
- 51 G→R: 130-fold decrease in catalytic efficiency on glycine and 28-fold increase in that on glyphosate.; G→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.
- 54 A→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.
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
22% identity, 55% coverage: 160:405/444 of query aligns to 104:350/364 of 1ng3A
- binding acetylamino-acetic acid: Y246 (≠ A294), R302 (≠ I357), R329 (≠ G384)
- binding flavin-adenine dinucleotide: V174 (= V225), S202 (≠ C252), G203 (≠ N253), W205 (≠ Y255), F209 (vs. gap), G300 (= G355), R302 (≠ I357), H327 (≠ Y382), R329 (≠ G384), N330 (≠ H385), G331 (= G386), I332 (≠ L387)
- binding phosphate ion: R254 (= R312)
Sites not aligning to the query:
- active site: 47, 48, 49
- binding flavin-adenine dinucleotide: 11, 13, 15, 33, 34, 35, 41, 42, 43, 46, 47, 48, 49
- binding phosphate ion: 89
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
22% identity, 55% coverage: 160:405/444 of query aligns to 104:350/364 of 3if9A
- binding flavin-adenine dinucleotide: P173 (≠ K224), V174 (= V225), S202 (≠ C252), G203 (≠ N253), W205 (≠ Y255), F209 (vs. gap), G300 (= G355), R302 (≠ I357), H327 (≠ Y382), F328 (≠ S383), R329 (≠ G384), N330 (≠ H385), G331 (= G386), I332 (≠ L387)
- binding glycolic acid: Y246 (≠ A294), R302 (≠ I357), R329 (≠ G384)
Sites not aligning to the query:
- active site: 47, 48, 49
- binding flavin-adenine dinucleotide: 11, 13, 15, 34, 35, 42, 43, 46, 47, 48, 49
5hxwA L-amino acid deaminase from proteus vulgaris (see paper)
25% identity, 48% coverage: 43:255/444 of query aligns to 15:221/433 of 5hxwA
- active site: F58 (≠ N86), Q61 (= Q89), A62 (≠ L90)
- binding flavin-adenine dinucleotide: V22 (= V50), G23 (= G51), G25 (= G53), I26 (≠ F54), L27 (≠ S55), E46 (= E74), K47 (≠ A75), E53 (≠ G81), Q54 (≠ A82), S55 (= S83), R57 (= R85), F58 (≠ N86), Y59 (≠ G87), G60 (= G88), Q61 (= Q89), A188 (≠ K224), A189 (≠ V225), G218 (≠ C252), G219 (≠ N253), W221 (≠ Y255)
Sites not aligning to the query:
- active site: 240, 284, 288
- binding cetyl-trimethyl-ammonium: 291, 294, 310, 311, 317, 318, 320, 373, 379, 399, 400
- binding flavin-adenine dinucleotide: 240, 242, 331, 371, 373, 398, 399, 400, 401, 402, 403
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
25% identity, 62% coverage: 40:316/444 of query aligns to 45:310/866 of Q9UI17
- CV 59:60 (≠ FS 54:55) binding FAD
- EK 80:81 (≠ EA 74:75) binding FAD
- 87:95 (vs. 81:102, 9% identical) binding FAD
- H91 (≠ R85) modified: Tele-8alpha-FAD histidine
- H109 (≠ G117) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (= V225) binding FAD
- S279 (≠ P281) 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
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
22% identity, 46% coverage: 198:401/444 of query aligns to 147:346/369 of S5FMM4
- S202 (≠ C252) 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 (≠ L387) 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 (≠ L397) 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.
Sites not aligning to the query:
- 51 G→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.
- 54 A→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.
- 81 K→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.
Query Sequence
>WP_049326229.1 NCBI__GCF_000013785.1:WP_049326229.1
MQTFHDTSVNHRASASNTSDHAPSYYAASVNRELSFEPLQGEQRADVCIVGGGFSGLNTA
IELAERGLSVILLEAHCIGWGASGRNGGQLIRGVGHDVEQFTNILGEEGVDELKRMGFEA
VEIVRQRIERYAIDCDLTWGYCDLATKPRHLKGFDEDYSDLLRLGYPHPLQRVSRPNLAT
VIGSQRYLGGLLDMGSGHLHPLNLALGEAAAAQSLGVRLFEHSKVERIEYGQQVKVHTAN
GVVQAETLVLACNAYLNGLQPKLAGKVLPAGSYIIATERLPEPLCRELLPQNTAVCDQRV
ALDYFRLSADGRLLFGGACHYSGRDPKDIAAYMQPKMLEVFPQLIGIGIDYQWGGMIGIG
ANRLPQIGRLPEQPNVFYAQAYSGHGLNATHLAGRLLAEAITAQQSHGFDLFAKVPHPTF
PGGRLLRSPLLAMGMLWYRLKDRF
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