SitesBLAST
Comparing WP_086510176.1 NCBI__GCF_002151265.1:WP_086510176.1 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)
8i01A Crystal structure of escherichia coli glyoxylate carboligase (see paper)
77% identity, 99% coverage: 1:585/591 of query aligns to 2:586/594 of 8i01A
- binding flavin-adenine dinucleotide: R155 (= R154), G212 (= G211), G213 (= G212), G214 (= G213), N217 (= N216), T238 (= T237), L239 (= L238), M240 (= M239), V256 (= V255), G257 (= G256), Q259 (= Q258), T260 (= T259), G279 (= G278), N280 (= N279), R281 (= R280), A283 (= A282), R285 (= R284), H286 (= H285), D303 (= D302), I304 (= I303), Q308 (= Q307), D322 (= D321), A323 (= A322), G417 (= G416)
- binding magnesium ion: D447 (= D446), F452 (= F451), E455 (= E454), N474 (= N473), Y476 (= Y475)
- binding thiamine diphosphate: G395 (= G394), L396 (= L395), S397 (= S396), L422 (= L421), G446 (= G445), D447 (= D446), F448 (≠ Y447), D449 (= D448), N474 (= N473), Y476 (= Y475), L477 (= L476), G478 (= G477), L479 (= L478), I480 (= I479)
- binding 2,3-dimethoxy-5-methyl-1,4-benzoquinone: Q354 (= Q353), C492 (= C491), Q494 (= Q493)
Sites not aligning to the query:
8beoB Crystal structure of e. Coli glyoxylate carboligase mutant i393a with map
77% identity, 99% coverage: 2:585/591 of query aligns to 1:584/592 of 8beoB
- binding methyl hydrogen (s)-acetylphosphonate: C490 (= C491), Q492 (= Q493)
- binding flavin-adenine dinucleotide: R153 (= R154), P154 (= P155), G210 (= G211), G211 (= G212), G212 (= G213), N215 (= N216), T236 (= T237), L237 (= L238), M238 (= M239), V254 (= V255), G255 (= G256), Q257 (= Q258), T258 (= T259), G277 (= G278), N278 (= N279), R279 (= R280), A281 (= A282), R283 (= R284), H284 (= H285), D301 (= D302), I302 (= I303), Q306 (= Q307), D320 (= D321), A321 (= A322), G415 (= G416)
- binding magnesium ion: D445 (= D446), F450 (= F451), L451 (≠ M452), E453 (= E454), N472 (= N473), Y474 (= Y475)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1s)-1-hydroxy-1-[(r)-hydroxy(methoxy)phosphoryl]ethyl}-5-(2-{[(s)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: R283 (= R284), G393 (= G394), L394 (= L395), S395 (= S396), L420 (= L421), G444 (= G445), D445 (= D446), F446 (≠ Y447), D447 (= D448), N472 (= N473), Y474 (= Y475), L475 (= L476), G476 (= G477), L477 (= L478), I478 (= I479)
- binding 2,3-dimethoxy-5-methyl-1,4-benzoquinone: Q352 (= Q353), R356 (= R357)
Sites not aligning to the query:
8beoA Crystal structure of e. Coli glyoxylate carboligase mutant i393a with map
77% identity, 99% coverage: 2:585/591 of query aligns to 1:584/592 of 8beoA
- binding flavin-adenine dinucleotide: R153 (= R154), P154 (= P155), G210 (= G211), G211 (= G212), G212 (= G213), N215 (= N216), T236 (= T237), L237 (= L238), M238 (= M239), V254 (= V255), G255 (= G256), Q257 (= Q258), T258 (= T259), G277 (= G278), N278 (= N279), R279 (= R280), A281 (= A282), R283 (= R284), H284 (= H285), D301 (= D302), I302 (= I303), Q306 (= Q307), D320 (= D321), A321 (= A322), I397 (= I398), G415 (= G416)
- binding magnesium ion: R384 (= R385), V405 (= V406), F406 (≠ Y407), H410 (= H411), D445 (= D446), F450 (= F451), L451 (≠ M452), E453 (= E454), N472 (= N473), Y474 (= Y475)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1s)-1-hydroxy-1-[(r)-hydroxy(methoxy)phosphoryl]ethyl}-5-(2-{[(s)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: R283 (= R284), G393 (= G394), L394 (= L395), S395 (= S396), L420 (= L421), G444 (= G445), D445 (= D446), F446 (≠ Y447), D447 (= D448), N472 (= N473), Y474 (= Y475), L475 (= L476), G476 (= G477), L477 (= L478), I478 (= I479)
- binding 2,3-dimethoxy-5-methyl-1,4-benzoquinone: E248 (≠ P249), Q352 (= Q353)
Sites not aligning to the query:
8i07D Crystal structure of escherichia coli glyoxylate carboligase double mutant in complex with glycolaldehyde (see paper)
77% identity, 99% coverage: 1:585/591 of query aligns to 2:586/594 of 8i07D
- binding 2-oxidanylethanal: R285 (= R284), I480 (= I479)
- binding flavin-adenine dinucleotide: R155 (= R154), P156 (= P155), G212 (= G211), G213 (= G212), G214 (= G213), N217 (= N216), T238 (= T237), L239 (= L238), M240 (= M239), V256 (= V255), G257 (= G256), Q259 (= Q258), T260 (= T259), G279 (= G278), N280 (= N279), R281 (= R280), R285 (= R284), H286 (= H285), D303 (= D302), I304 (= I303), Q308 (= Q307), D322 (= D321), A323 (= A322), I399 (= I398), G417 (= G416)
- binding magnesium ion: D447 (= D446), F452 (= F451), L453 (≠ M452), E455 (= E454), N474 (= N473), Y476 (= Y475)
- binding thiamine diphosphate: V52 (= V51), T76 (= T75), G395 (= G394), L396 (= L395), S397 (= S396), L422 (= L421), G446 (= G445), D447 (= D446), F448 (≠ Y447), D449 (= D448), N474 (= N473), Y476 (= Y475), L477 (= L476), G478 (= G477), L479 (= L478), I480 (= I479)
- binding ubiquinone-1: Q354 (= Q353), R358 (= R357), C492 (= C491), Q494 (= Q493)
Sites not aligning to the query:
8i07A Crystal structure of escherichia coli glyoxylate carboligase double mutant in complex with glycolaldehyde (see paper)
77% identity, 99% coverage: 1:585/591 of query aligns to 2:586/594 of 8i07A
- binding flavin-adenine dinucleotide: R155 (= R154), P156 (= P155), G212 (= G211), G213 (= G212), G214 (= G213), N217 (= N216), T238 (= T237), L239 (= L238), M240 (= M239), V256 (= V255), G257 (= G256), Q259 (= Q258), T260 (= T259), G279 (= G278), N280 (= N279), R281 (= R280), R285 (= R284), H286 (= H285), D303 (= D302), I304 (= I303), Q308 (= Q307), D322 (= D321), A323 (= A322), I394 (= I393), I399 (= I398), G417 (= G416)
- binding magnesium ion: D447 (= D446), F452 (= F451), L453 (≠ M452), E455 (= E454), N474 (= N473), Y476 (= Y475)
- binding thiamine diphosphate: I394 (= I393), G395 (= G394), L396 (= L395), S397 (= S396), L422 (= L421), G446 (= G445), D447 (= D446), F448 (≠ Y447), D449 (= D448), N474 (= N473), Y476 (= Y475), L477 (= L476), G478 (= G477), L479 (= L478), I480 (= I479)
- binding ubiquinone-1: Q354 (= Q353), C492 (= C491), Q494 (= Q493)
Sites not aligning to the query:
P09342 Acetolactate synthase 1, chloroplastic; ALS I; Acetohydroxy-acid synthase I; Acetolactate synthase I; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see 2 papers)
34% identity, 92% coverage: 6:551/591 of query aligns to 96:638/667 of P09342
- C161 (= C72) modified: Disulfide link with 307
- P194 (= P105) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ I214) modified: Disulfide link with 161
P09114 Acetolactate synthase 2, chloroplastic; ALS II; Acetohydroxy-acid synthase II; Acetolactate synthase II; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see paper)
34% identity, 92% coverage: 6:551/591 of query aligns to 93:635/664 of P09114
- P191 (= P105) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (≠ A482) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
P17597 Acetolactate synthase, chloroplastic; AtALS; Acetohydroxy-acid synthase; Protein CHLORSULFURON RESISTANT 1; EC 2.2.1.6 from Arabidopsis thaliana (Mouse-ear cress) (see 8 papers)
33% identity, 93% coverage: 6:554/591 of query aligns to 99:640/670 of P17597