SitesBLAST
Comparing WP_058931237.1 NCBI__GCF_001484605.1:WP_058931237.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q7X2D3 D-amino-acid oxidase; DAAO; DAMOX; DAO; GpDAAO-1; GpDAAO-2; EC 1.4.3.3 from Glutamicibacter protophormiae (Brevibacterium protophormiae) (see paper)
40% identity, 90% coverage: 8:315/341 of query aligns to 7:316/326 of Q7X2D3
- K256 (≠ S255) mutation to T: Improves catalytic efficiency.
Q99489 D-aspartate oxidase; DASOX; DASPO; DDO; EC 1.4.3.1 from Homo sapiens (Human) (see 3 papers)
35% identity, 94% coverage: 5:325/341 of query aligns to 2:334/341 of Q99489
- D36 (≠ A37) binding FAD
- K37 (≠ H38) binding FAD
- T43 (≠ V44) binding FAD
- S44 (= S45) binding FAD
- M50 (≠ I51) binding FAD
- F136 (≠ C129) to L: in a breast cancer sample; somatic mutation
- CEC 141:143 (≠ ATM 134:136) mutation to YEG: Slightly decreases activity.
- R216 (≠ I208) to Q: decreases activity; decreases FAD binding; dbSNP:rs147072212
- G307 (= G298) binding FAD
- S308 (≠ G299) to N: decreases activity; decreases FAD binding; dbSNP:rs140566457
- I311 (≠ V302) binding FAD
- S312 (≠ T303) binding FAD
6rkfA Structure of human daspo (see paper)
35% identity, 94% coverage: 5:325/341 of query aligns to 2:334/335 of 6rkfA
- active site: M50 (≠ I51), S308 (≠ G299), S312 (≠ T303)
- binding flavin-adenine dinucleotide: G10 (= G13), A11 (= A14), G12 (= G15), V13 (= V16), V14 (≠ I17), S35 (≠ A36), D36 (≠ A37), K37 (≠ H38), T42 (= T43), T43 (≠ V44), S44 (= S45), A47 (= A48), A48 (= A49), M50 (≠ I51), S183 (≠ T175), G184 (= G176), G276 (= G271), R278 (= R273), G307 (= G298), S308 (≠ G299), G309 (≠ S300), I311 (≠ V302), S312 (≠ T303)
Q922Z0 D-aspartate oxidase; DASOX; DASPO; DDO; EC 1.4.3.1 from Mus musculus (Mouse) (see 4 papers)
35% identity, 96% coverage: 5:331/341 of query aligns to 2:337/341 of Q922Z0
- R216 (≠ I208) mutation R->A,E,M: Abolishes catalytic activity.; mutation to L: Decreases catalytic activity. Alters substrate specificity; when associated with Y-237.
- R237 (≠ A232) mutation to A: Resistance to thiolactomycin.; mutation R->E,A,Y: Decreases catalytic activity.; mutation to Y: Alters substrate specificity; when associated with L-216.
- S308 (≠ G299) mutation S->G,A: Increases catalytic activity and FAD binding.; mutation to Y: Decreases catalytic activity and FAD binding.
4qfdA Co-crystal structure of compound 2 (3-(7-hydroxy-2-oxo-4-phenyl-2h- chromen-6-yl)propanoic acid) and fad bound to human daao at 2.85a (see paper)
32% identity, 91% coverage: 8:319/341 of query aligns to 2:319/322 of 4qfdA
- active site: L46 (≠ I51), G299 (= G299), T303 (= T303)
- binding 3-(7-hydroxy-2-oxo-4-phenyl-2H-chromen-6-yl)propanoic acid: Q48 (≠ A53), Y50 (= Y55), L51 (≠ H56), T206 (≠ D210), Y214 (vs. gap), S216 (≠ P216), Y218 (= Y218), R273 (= R273)
- binding flavin-adenine dinucleotide: G7 (= G13), A8 (= A14), G9 (= G15), I11 (= I17), A31 (= A36), D32 (≠ A37), R33 (≠ H38), T39 (≠ V44), T40 (≠ S45), A43 (= A48), G45 (≠ A50), L46 (≠ I51), V154 (= V159), T172 (= T175), W175 (≠ N178), G271 (= G271), R273 (= R273), G298 (= G298), G299 (= G299), Y300 (≠ S300), G301 (= G301), L302 (≠ V302), T303 (= T303)
4qfcA Co-crystal structure of compound 3 (4-hydroxy-6-[2-(7-hydroxy-2-oxo-4- phenyl-2h-chromen-6-yl)ethyl]pyridazin-3(2h)-one) and fad bound to human daao at 2.4a (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:326/330 of 4qfcA
- active site: L51 (≠ I51), G306 (= G299), T310 (= T303)
- binding 4-hydroxy-6-[2-(7-hydroxy-2-oxo-4-phenyl-2H-chromen-6-yl)ethyl]pyridazin-3(2H)-one: Q53 (≠ A53), Y55 (= Y55), L215 (≠ D209), Y220 (≠ A214), Y224 (= Y218), I226 (= I220), R279 (= R273), G306 (= G299)
- binding flavin-adenine dinucleotide: G7 (= G13), A8 (= A14), G9 (= G15), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), K163 (≠ S158), V164 (= V159), T182 (= T175), R279 (= R273), G305 (= G298), G306 (= G299), Y307 (≠ S300), G308 (= G301), L309 (≠ V302), T310 (= T303)
P14920 D-amino-acid oxidase; DAAO; DAMOX; DAO; EC 1.4.3.3 from Homo sapiens (Human) (see 23 papers)
30% identity, 94% coverage: 8:329/341 of query aligns to 2:343/347 of P14920
- A8 (= A14) binding FAD
- G9 (= G15) binding FAD
- V10 (= V16) binding FAD
- I11 (= I17) binding FAD
- D31 (= D31) mutation to H: Increases affinity for the FAD cofactor and D-serine. Decreases the cellular ratio of D-serine to L-serine.
- D37 (≠ A37) binding FAD
- R38 (≠ H38) binding FAD; to H: found in a patient with ALS; impairs FAD binding; 20-fold decreased affinity for D-serine; 300-fold decreased affinity for D-alanine; 3-fold decreased affinity for D-proline; dbSNP:rs368093324
- T43 (= T43) binding FAD
- T44 (≠ V44) binding FAD
- T45 (≠ S45) binding FAD
- G50 (≠ A50) binding FAD
- L51 (≠ I51) binding FAD
- Q53 (≠ A53) binding D-dopa
- R120 (≠ E117) mutation R->E,L: Increases activity and FAD-binding. Decreases protein localization to peroxisomes with protein mislocalized to the nucleus and cytosol.
- E121 (= E118) to K: found in a patient with ALS; abolishes activity; impairs FAD binding; over 900-fold decreased affinity for D-alanine; over 200-fold decreased affinity for D-serine; leads to the formation of protein aggregates; increases the occurrence of cell death
- V164 (= V159) binding FAD
- G183 (= G176) mutation to R: Abolishes activity. Impairs the ability to bind the FAD cofactor. Impairs targeting to peroxisomes and results in abnormal peroxisomal morphology. Leads to the formation of ubiquitinated protein aggregates and the induction of apoptosis.
- R199 (= R192) to Q: found in a patient with ALS; impairs FAD binding; over 200-fold decreased affinity for D-serine; 1800-fold decreased affinity for D-alanine; dbSNP:rs200850756; to W: found in a patient with ALS; decreased function in D-serine catabolic process; 3- to 4-fold decrease in Vmax with D-serine, D-alanine and D-proline as substrates; impairs FAD binding; decreased affinity for D-serine, D-alanine and D-proline; leads to tetramerization of the holoenzyme; leads to the formation of ubiquitinated protein aggregates; promotes induction of apoptosis; causes cell death in motor neurons in a manner at least partially dependent on the N-methyl-D-aspartic acid receptor; dbSNP:rs139166976
- Q201 (= Q194) to R: found in a patient with ALS; impairs FAD binding; decreased affinity for D-serine, D-alanine and D-proline; leads to tetramerization of the holoenzyme
- W209 (≠ P203) to R: found in a patient with ALS; no effect on activity; decreases the cellular ratio of D-serine to L-serine.; dbSNP:rs111347906
- P219 (= P213) mutation to L: Increases catalytic efficiency and inhibition by benzoate.
- Y224 (vs. gap) mutation to F: Decreases activity.
- R279 (= R269) mutation to A: Increases affinity for the FAD cofactor and D-serine. Decreases the cellular ratio of D-serine to L-serine.
- R283 (= R273) binding D-dopa; binding D-serine; binding FAD
- G312 (= G298) binding FAD
- G313 (= G299) binding D-dopa; binding FAD
- G315 (= G301) binding FAD
- L316 (≠ V302) binding FAD
- T317 (= T303) binding FAD
- G331 (≠ D317) to V: leads to the formation of ubiquitinated protein aggregates; impairs targeting to peroxisomes; results in abnormal peroxisomal morphology; decreases cell viability; dbSNP:rs4262766
Sites not aligning to the query:
- 1:16 Required for protein stability
5zjaA Human d-amino acid oxidase complexed with 5-chlorothiophene-2- carboxylic acid (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 5zjaA
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding 5-chloro thiophene-2-carboxylic acid: Y224 (vs. gap), Y228 (= Y218), R283 (= R273)
- binding flavin-adenine dinucleotide: I6 (= I12), G7 (= G13), A8 (= A14), G9 (= G15), V10 (= V16), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), L51 (≠ I51), K163 (≠ S158), V164 (= V159), T182 (= T175), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
5zj9A Human d-amino acid oxidase complexed with 5-chlorothiophene-3- carboxylic acid (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 5zj9A
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding 5-chloro thiophene-3-carboxylic acid: Q53 (≠ A53), Y224 (vs. gap), Y228 (= Y218), R283 (= R273)
- binding flavin-adenine dinucleotide: G7 (= G13), A8 (= A14), G9 (= G15), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), L51 (≠ I51), V164 (= V159), T182 (= T175), G281 (= G271), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
3znpA In vitro and in vivo inhibition of human d-amino acid oxidase: regulation of d-serine concentration in the brain (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 3znpA
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding flavin-adenine dinucleotide: I6 (= I12), G7 (= G13), G9 (= G15), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), V164 (= V159), C181 (≠ A174), T182 (= T175), W185 (≠ N178), G281 (= G271), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
- binding 3-hydroxy-2h-chromen-2-one: L51 (≠ I51), Y224 (vs. gap), Y228 (= Y218), R283 (= R273), G313 (= G299)
3znoA In vitro and in vivo inhibition of human d-amino acid oxidase: regulation of d-serine concentration in the brain (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 3znoA
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding flavin-adenine dinucleotide: I6 (= I12), G7 (= G13), A8 (= A14), G9 (= G15), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T43 (= T43), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), K163 (≠ S158), V164 (= V159), C181 (≠ A174), T182 (= T175), W185 (≠ N178), R283 (= R273), H311 (= H297), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
- binding 4-(4-chlorophenethyl)-1H-pyrrole-2-carboxylic acid: L56 (≠ H56), L215 (≠ D209), I223 (vs. gap), Y224 (vs. gap), Y228 (= Y218), I230 (= I220), R283 (= R273), G313 (= G299)
3znnA In vitro and in vivo inhibition of human d-amino acid oxidase: regulation of d-serine concentration in the brain (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 3znnA
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding 4h-thieno[3,2-b]pyrole-5-carboxylic acid: L51 (≠ I51), Y224 (vs. gap), Y228 (= Y218), R283 (= R273), G313 (= G299)
- binding flavin-adenine dinucleotide: G7 (= G13), A8 (= A14), G9 (= G15), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), K163 (≠ S158), V164 (= V159), T182 (= T175), W185 (≠ N178), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
3w4kA Crystal structure of human daao in complex with coumpound 13 (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 3w4kA
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding 3-hydroxy-6-(2-phenylethyl)pyridazin-4(1H)-one: L215 (≠ D209), Y224 (vs. gap), Y228 (= Y218), R283 (= R273), G313 (= G299)
- binding flavin-adenine dinucleotide: G7 (= G13), A8 (= A14), G9 (= G15), V10 (= V16), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), V164 (= V159), T182 (= T175), G183 (= G176), W185 (≠ N178), P284 (= P274), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
3w4jA Crystal structure of human daao in complex with coumpound 12 (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 3w4jA
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding 3-hydroxy-5-(2-phenylethyl)pyridin-2(1H)-one: Q53 (≠ A53), L215 (≠ D209), H217 (≠ S211), Y224 (vs. gap), Y228 (= Y218), R283 (= R273), G313 (= G299)
- binding flavin-adenine dinucleotide: G7 (= G13), A8 (= A14), G9 (= G15), V10 (= V16), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), V164 (= V159), T182 (= T175), W185 (≠ N178), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
3w4iA Crystal structure of human daao in complex with coumpound 8 (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 3w4iA
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding pyridine-2,3-diol: Y224 (vs. gap), Y228 (= Y218), R283 (= R273), G313 (= G299)
- binding flavin-adenine dinucleotide: G7 (= G13), A8 (= A14), G9 (= G15), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), V164 (= V159), T182 (= T175), W185 (≠ N178), G281 (= G271), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
3g3eA Crystal structure of human d-amino acid oxidase in complex with hydroxyquinolin-2(1h) (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 3g3eA
- active site: L51 (≠ I51), G313 (= G299), T317 (= T303)
- binding flavin-adenine dinucleotide: G7 (= G13), G9 (= G15), V10 (= V16), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), V164 (= V159), T182 (= T175), W185 (≠ N178), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
- binding 3-hydroxyquinolin-2(1H)-one: Y224 (vs. gap), Y228 (= Y218), R283 (= R273), G313 (= G299)
2e82A Crystal structure of human d-amino acid oxidase complexed with imino- dopa (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 2e82A
- active site: G313 (= G299), T317 (= T303)
- binding flavin-adenine dinucleotide: I6 (= I12), G7 (= G13), G9 (= G15), D37 (≠ A37), R38 (≠ H38), T43 (= T43), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), V164 (= V159), T182 (= T175), G183 (= G176), G281 (= G271), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
- binding (2e)-3-(3,4-dihydroxyphenyl)-2-iminopropanoic acid: H217 (≠ S211), Y224 (vs. gap), Y228 (= Y218), R283 (= R273), G313 (= G299)
2e4aA Crystal structure of human d-amino acid oxidase in complex with o- aminobenzoate (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 2e4aA
- active site: G313 (= G299), T317 (= T303)
- binding 2-aminobenzoic acid: Y224 (vs. gap), Y228 (= Y218), R283 (= R273)
- binding flavin-adenine dinucleotide: G7 (= G13), G9 (= G15), I11 (= I17), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), G50 (≠ A50), L51 (≠ I51), K163 (≠ S158), V164 (= V159), T182 (= T175), G183 (= G176), W185 (≠ N178), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
2e49A Crystal structure of human d-amino acid oxidase in complex with imino- serine (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 2e49A
- active site: G313 (= G299), T317 (= T303)
- binding flavin-adenine dinucleotide: G7 (= G13), G9 (= G15), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), V47 (= V47), A48 (= A48), G50 (≠ A50), L51 (≠ I51), K163 (≠ S158), V164 (= V159), T182 (= T175), G281 (= G271), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
- binding 3-hydroxy-2-iminopropanoic acid: Y224 (vs. gap), R283 (= R273), G313 (= G299)
2du8A Crystal structure of human d-amino acid oxidase (see paper)
31% identity, 91% coverage: 8:319/341 of query aligns to 2:333/340 of 2du8A
- active site: G313 (= G299), T317 (= T303)
- binding flavin-adenine dinucleotide: G7 (= G13), A8 (= A14), G9 (= G15), V10 (= V16), I11 (= I17), A36 (= A36), D37 (≠ A37), R38 (≠ H38), T44 (≠ V44), T45 (≠ S45), A48 (= A48), L51 (≠ I51), V164 (= V159), T182 (= T175), R283 (= R273), G312 (= G298), G313 (= G299), Y314 (≠ S300), G315 (= G301), L316 (≠ V302), T317 (= T303)
Query Sequence
>WP_058931237.1 NCBI__GCF_001484605.1:WP_058931237.1
MTPSDRPQVAVIGAGVIGLTTALVAARAGYDVTVTAAHRPEDTVSAVAAAIWAPYHAEPE
ALVGSWGAVTFKVLAGLAASSPESGVEMREGVVVVRAGSTPLKWPASVGGHRPAREEELP
RGTESGIVCTVPIATMSSYLPWLQRQCTDAGVSWEWRSVHTLADIPANDLVVLATGLNSL
GLHADDGLYPVRGQVARIGDARPTRWIIDDSNPAGPTYIIPRSDEVVCGGTAQVGENSLE
PDAATEHRILSTVRSLEPVLDGGVFLGSRVGLRPGRDSVRLGLTEDHGRPVIHSYGHGGS
GVTVSWGVAFSTLELIDRVTTAAETLHAPTATPPGRAQAGR
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