SitesBLAST
Comparing WP_050463021.1 NCBI__GCF_001189915.1:WP_050463021.1 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, 100% coverage: 1:590/591 of query aligns to 2:591/594 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 (≠ R353), C492 (= C491), Q494 (= Q493), C589 (≠ S588)
8beoB Crystal structure of e. Coli glyoxylate carboligase mutant i393a with map
77% identity, 100% coverage: 2:590/591 of query aligns to 1:589/592 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 (≠ R353), R356 (= R357), C587 (≠ S588)
8beoA Crystal structure of e. Coli glyoxylate carboligase mutant i393a with map
77% identity, 100% coverage: 2:590/591 of query aligns to 1:589/592 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 (≠ R353), C587 (≠ S588)
8i07D Crystal structure of escherichia coli glyoxylate carboligase double mutant in complex with glycolaldehyde (see paper)
77% identity, 100% coverage: 1:590/591 of query aligns to 2:591/594 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 (≠ R353), R358 (= R357), C492 (= C491), Q494 (= Q493), C589 (≠ S588)
8i07A Crystal structure of escherichia coli glyoxylate carboligase double mutant in complex with glycolaldehyde (see paper)
77% identity, 100% coverage: 1:590/591 of query aligns to 2:591/594 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 (≠ R353), C492 (= C491), Q494 (= Q493), C589 (≠ S588)
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)
35% identity, 82% coverage: 5:486/591 of query aligns to 95:575/667 of P09342
- C161 (= C72) modified: Disulfide link with 307
- P194 (= P105) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ V214) modified: Disulfide link with 161
6lpiB Crystal structure of ahas holo-enzyme (see paper)
34% identity, 81% coverage: 11:486/591 of query aligns to 13:468/539 of 6lpiB
- active site: I27 (≠ V25), G29 (= G27), G30 (≠ A28), S31 (≠ A29), I32 (= I30), E53 (≠ V51), C76 (≠ T75), F115 (= F114), Q116 (= Q115), E117 (≠ A116), K165 (≠ F164), M256 (≠ L257), A283 (≠ H285), V375 (≠ I393), G401 (= G419), M403 (≠ L421), D428 (= D446), N455 (= N473), A457 (≠ Y475), L458 (= L476), L460 (= L478), V461 (≠ I479), Q464 (≠ A482)
- binding flavin-adenine dinucleotide: R155 (= R154), G212 (= G211), G213 (= G212), G214 (= G213), T236 (= T237), L237 (= L238), M238 (= M239), L254 (≠ V255), M256 (≠ L257), H257 (≠ Q258), G276 (= G278), A277 (≠ N279), R278 (= R280), D280 (≠ A282), R282 (= R284), A283 (≠ H285), D300 (= D302), I301 (= I303), D319 (= D321), V320 (≠ A322), M380 (≠ I398), G398 (= G416)
- binding magnesium ion: D428 (= D446), N455 (= N473)
- binding thiamine diphosphate: E53 (≠ V51), C76 (≠ T75), P79 (= P78), G376 (= G394), Q377 (≠ L395), H378 (≠ S396), G401 (= G419), M403 (≠ L421), G427 (= G445), D428 (= D446), G429 (≠ Y447), S430 (≠ D448), M433 (≠ F451), N455 (= N473), A457 (≠ Y475), L458 (= L476), G459 (= G477), L460 (= L478), V461 (≠ I479)
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)
35% identity, 82% coverage: 5:486/591 of query aligns to 92:572/664 of P09114