SitesBLAST
Comparing GFF1219 FitnessBrowser__Phaeo:GFF1219 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 20 (the maximum) hits to proteins with known functional sites (download)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
30% identity, 96% coverage: 16:546/554 of query aligns to 3:533/555 of 4rjiC
- binding magnesium ion: D438 (= D451), D465 (= D478), T467 (≠ S480)
- binding thiamine diphosphate: P24 (= P37), E48 (= E61), P74 (= P87), S387 (≠ A400), H388 (= H401), Q411 (≠ C424), G437 (= G450), D438 (= D451), G439 (≠ A452), G440 (= G453), T467 (≠ S480), Y468 (≠ L481), D469 (≠ A482), M470 (≠ L483), V471 (≠ I484)
Sites not aligning to the query:
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
30% identity, 96% coverage: 16:546/554 of query aligns to 2:532/552 of 4rjkF
- binding magnesium ion: D437 (= D451), D464 (= D478), T466 (≠ S480)
- binding pyruvic acid: A25 (≠ G39), K26 (≠ E40)
- binding thiamine diphosphate: P23 (= P37), E47 (= E61), P73 (= P87), G385 (= G399), S386 (≠ A400), H387 (= H401), Q410 (≠ C424), L412 (≠ M426), G436 (= G450), D437 (= D451), G438 (≠ A452), G439 (= G453), T466 (≠ S480), Y467 (≠ L481), D468 (≠ A482), M469 (≠ L483), V470 (≠ I484)
Sites not aligning to the query:
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
30% identity, 96% coverage: 16:546/554 of query aligns to 2:532/553 of 4rjkG
- binding magnesium ion: D437 (= D451), D464 (= D478), T466 (≠ S480)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-(1-carboxy-1-hydroxyethyl)-5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: E47 (= E61), Q110 (= Q124)
- binding thiamine diphosphate: I384 (≠ S398), G385 (= G399), S386 (≠ A400), H387 (= H401), Q410 (≠ C424), L412 (≠ M426), G436 (= G450), D437 (= D451), G438 (≠ A452), G439 (= G453), T466 (≠ S480), Y467 (≠ L481), D468 (≠ A482), M469 (≠ L483), V470 (≠ I484)
Sites not aligning to the query:
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
30% identity, 95% coverage: 18:546/554 of query aligns to 8:533/545 of 1ozfA
- active site: I26 (≠ M36), G28 (= G38), A29 (≠ G39), K30 (≠ E40), I31 (≠ V41), E51 (= E61), T74 (= T84), H113 (= H123), Q114 (= Q124), S115 (≠ V125), Q163 (≠ I172), L253 (= L263), E280 (≠ R292), M385 (≠ S398), Q411 (≠ C424), M413 (= M426), D438 (= D451), D465 (= D478), G467 (≠ S480), Y468 (≠ L481), M470 (≠ L483), V471 (≠ I484), Q474 (≠ K487)
- binding magnesium ion: D438 (= D451), D465 (= D478), G467 (≠ S480)
- binding phosphate ion: G249 (= G260), R250 (vs. gap), Q257 (≠ P265), R343 (≠ G356), R394 (≠ Q407), L396 (≠ W409), Y397 (≠ H410)
- binding thiamine diphosphate: G386 (= G399), S387 (≠ A400), F388 (≠ H401), Q411 (≠ C424), M413 (= M426), G437 (= G450), D438 (= D451), G439 (≠ A452), D465 (= D478), G467 (≠ S480), Y468 (≠ L481), N469 (≠ A482), M470 (≠ L483), V471 (≠ I484)
Sites not aligning to the query:
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
30% identity, 95% coverage: 18:546/554 of query aligns to 8:534/548 of 5d6rB
- active site: I26 (≠ M36), G28 (= G38), A29 (≠ G39), K30 (≠ E40), I31 (≠ V41), E51 (= E61), T74 (= T84), H113 (= H123), Q114 (= Q124), S115 (≠ V125), Q163 (≠ I172), L254 (= L263), E281 (≠ R292), M386 (≠ S398), Q412 (≠ C424), M414 (= M426), D439 (= D451), D466 (= D478), G468 (≠ S480), Y469 (≠ L481), M471 (≠ L483), V472 (≠ I484), Q475 (≠ K487)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(Z)-2-fluoro-1-hydroxy-2-phosphonoethenyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: M386 (≠ S398), G387 (= G399), S388 (≠ A400), Q412 (≠ C424), M414 (= M426), D439 (= D451), G440 (≠ A452), G468 (≠ S480), Y469 (≠ L481), N470 (≠ A482), M471 (≠ L483)
- binding magnesium ion: R63 (≠ H73), Q212 (≠ A222), D439 (= D451), D466 (= D478), G468 (≠ S480)
Sites not aligning to the query:
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
30% identity, 95% coverage: 18:546/554 of query aligns to 20:540/557 of 5dx6B
- active site: I38 (≠ M36), G40 (= G38), A41 (≠ G39), K42 (≠ E40), I43 (≠ V41), E63 (= E61), T86 (= T84), H125 (= H123), Q126 (= Q124), S127 (≠ V125), Q175 (≠ I172), L268 (= L263), E295 (≠ R292), M392 (≠ S398), Q418 (≠ C424), M420 (= M426), D445 (= D451), D472 (= D478), G474 (≠ S480), Y475 (≠ L481), M477 (≠ L483), V478 (≠ I484), Q481 (≠ K487)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G260), R265 (vs. gap), Q272 (≠ P265), A400 (≠ S406), R401 (≠ Q407), Y404 (≠ H410)
- binding magnesium ion: S135 (≠ A133), T138 (= T136), D445 (= D451), D472 (= D478), G474 (≠ S480)
- binding thiamine diphosphate: G393 (= G399), S394 (≠ A400), F395 (≠ H401), Q418 (≠ C424), M420 (= M426), G444 (= G450), D445 (= D451), G446 (≠ A452), D472 (= D478), G474 (≠ S480), Y475 (≠ L481), N476 (≠ A482), M477 (≠ L483), V478 (≠ I484)
Sites not aligning to the query:
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
30% identity, 95% coverage: 18:546/554 of query aligns to 9:537/549 of 1ozgA
- active site: I27 (≠ M36), G29 (= G38), A30 (≠ G39), K31 (≠ E40), I32 (≠ V41), E52 (= E61), T75 (= T84), H114 (= H123), Q115 (= Q124), S116 (≠ V125), Q164 (≠ I172), L257 (= L263), E284 (≠ R292), M389 (≠ S398), Q415 (≠ C424), M417 (= M426), D442 (= D451), D469 (= D478), G471 (≠ S480), Y472 (≠ L481), M474 (≠ L483), V475 (≠ I484), Q478 (≠ K487)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ S398), G390 (= G399), S391 (≠ A400), F392 (≠ H401), Q415 (≠ C424), M417 (= M426), G441 (= G450), D442 (= D451), G443 (≠ A452), D469 (= D478), G471 (≠ S480), Y472 (≠ L481), N473 (≠ A482), M474 (≠ L483), V475 (≠ I484)
- binding magnesium ion: D442 (= D451), D469 (= D478), G471 (≠ S480)
- binding phosphate ion: G253 (= G260), R254 (vs. gap), Q261 (≠ P265), R347 (≠ G356), R398 (≠ Q407), Y401 (≠ H410)
Sites not aligning to the query:
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
30% identity, 95% coverage: 18:546/554 of query aligns to 9:529/541 of 5dx6A
- active site: I27 (≠ M36), G29 (= G38), A30 (≠ G39), K31 (≠ E40), I32 (≠ V41), E52 (= E61), T75 (= T84), Q159 (≠ I172), L249 (= L263), E276 (≠ R292), M381 (≠ S398), Q407 (≠ C424), M409 (= M426), D434 (= D451), D461 (= D478), G463 (≠ S480), Y464 (≠ L481), M466 (≠ L483), V467 (≠ I484), Q470 (≠ K487)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(1R)-2-fluoro-1-hydroxyethyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: M381 (≠ S398), G382 (= G399), S383 (≠ A400), F384 (≠ H401), Q407 (≠ C424), M409 (= M426), G433 (= G450), D434 (= D451), G435 (≠ A452), D461 (= D478), G463 (≠ S480), Y464 (≠ L481), N465 (≠ A482)
- binding magnesium ion: S119 (≠ A133), T122 (= T136), D434 (= D451), D461 (= D478), G463 (≠ S480)
Sites not aligning to the query:
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
29% identity, 95% coverage: 18:546/554 of query aligns to 9:526/538 of 5wdgA
- active site: I27 (≠ M36), G29 (= G38), A30 (≠ G39), K31 (≠ E40), I32 (≠ V41), E52 (= E61), T75 (= T84), Q157 (≠ I172), L246 (= L263), E273 (≠ R292), M378 (≠ S398), Q404 (≠ C424), M406 (= M426), D431 (= D451), D458 (= D478), G460 (≠ S480), Y461 (≠ L481), M463 (≠ L483), V464 (≠ I484), Q467 (≠ K487)
- binding (2S,3S)-2,3-dihydroxy-3-[(7S,8R,9aS)-8-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2,7-dimethyl-5,7,8,10-tetrahydro-9aH-pyrimido[4,5-d][1,3]thiazolo[3,2-a]pyrimidin-9a-yl]-2-methylbutanoic acid: M378 (≠ S398), S380 (≠ A400), F381 (≠ H401), Q404 (≠ C424), M406 (= M426), G430 (= G450), D431 (= D451), G432 (≠ A452), G433 (= G453), D458 (= D478), G460 (≠ S480), Y461 (≠ L481), N462 (≠ A482), M463 (≠ L483), V464 (≠ I484)
- binding magnesium ion: R64 (≠ H73), S117 (≠ A133), T120 (= T136), Q204 (≠ A222), D431 (= D451), D458 (= D478), G460 (≠ S480)
- binding pyruvic acid: G94 (≠ R103), R147 (= R162)
Sites not aligning to the query:
- active site: 527
- binding (2S,3S)-2,3-dihydroxy-3-[(7S,8R,9aS)-8-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2,7-dimethyl-5,7,8,10-tetrahydro-9aH-pyrimido[4,5-d][1,3]thiazolo[3,2-a]pyrimidin-9a-yl]-2-methylbutanoic acid: 527
6lpiB Crystal structure of ahas holo-enzyme (see paper)
30% identity, 85% coverage: 18:488/554 of query aligns to 9:465/539 of 6lpiB
- active site: I27 (≠ M36), G29 (= G38), G30 (= G39), S31 (≠ E40), I32 (≠ V41), E53 (= E61), C76 (≠ T84), F115 (≠ H123), Q116 (= Q124), E117 (≠ V125), K165 (≠ I172), M256 (≠ L263), A283 (≠ P293), V375 (≠ S398), G401 (≠ C424), M403 (= M426), D428 (= D451), N455 (≠ D478), A457 (≠ S480), L458 (= L481), L460 (= L483), V461 (≠ I484), Q464 (≠ K487)
- binding flavin-adenine dinucleotide: R155 (= R162), G212 (= G217), G213 (≠ L218), G214 (≠ D219), T236 (≠ S243), L237 (≠ Y244), M238 (≠ K245), L254 (≠ A261), M256 (≠ L263), H257 (≠ S264), G276 (= G285), A277 (≠ Y286), R278 (≠ D287), D280 (≠ E290), R282 (= R292), A283 (≠ P293), D300 (≠ C310), I301 (≠ A311), D319 (≠ T337), V320 (= V338), M380 (≠ I403), G398 (≠ S421)
- binding magnesium ion: D428 (= D451), N455 (≠ D478)
- binding thiamine diphosphate: E53 (= E61), C76 (≠ T84), P79 (= P87), G376 (= G399), Q377 (≠ A400), H378 (= H401), G401 (≠ C424), M403 (= M426), G427 (= G450), D428 (= D451), G429 (≠ A452), S430 (≠ G453), M433 (= M456), N455 (≠ D478), A457 (≠ S480), L458 (= L481), G459 (≠ A482), L460 (= L483), V461 (≠ I484)
8beoB Crystal structure of e. Coli glyoxylate carboligase mutant i393a with map
27% identity, 87% coverage: 15:494/554 of query aligns to 3:486/592 of 8beoB
- binding flavin-adenine dinucleotide: R153 (= R162), P154 (≠ N163), G210 (= G217), G211 (≠ L218), G212 (≠ D219), N215 (≠ A222), T236 (≠ S243), L237 (≠ Y244), M238 (≠ K245), V254 (≠ A261), G255 (= G262), Q257 (≠ S264), T258 (≠ L266), G277 (= G285), N278 (≠ Y286), R279 (≠ D287), A281 (≠ I289), R283 (≠ M291), H284 (≠ R292), D301 (= D308), I302 (= I309), Q306 (≠ N314), D320 (≠ G328), A321 (≠ L329), G415 (≠ S421)
- binding magnesium ion: D445 (= D451), F450 (≠ M456), L451 (≠ V457), E453 (≠ G459), N472 (≠ D478), Y474 (≠ S480)
- 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 (≠ M291), G393 (= G399), L394 (≠ A400), S395 (≠ H401), L420 (≠ M426), G444 (= G450), D445 (= D451), F446 (≠ A452), D447 (≠ G453), N472 (≠ D478), Y474 (≠ S480), L475 (= L481), G476 (≠ A482), L477 (= L483), I478 (= I484)
- binding 2,3-dimethoxy-5-methyl-1,4-benzoquinone: Q352 (≠ P358), R356 (= R362)
Sites not aligning to the query:
8beoA Crystal structure of e. Coli glyoxylate carboligase mutant i393a with map
27% identity, 87% coverage: 15:494/554 of query aligns to 3:486/592 of 8beoA
- binding flavin-adenine dinucleotide: R153 (= R162), P154 (≠ N163), G210 (= G217), G211 (≠ L218), G212 (≠ D219), N215 (≠ A222), T236 (≠ S243), L237 (≠ Y244), M238 (≠ K245), V254 (≠ A261), G255 (= G262), Q257 (≠ S264), T258 (≠ L266), G277 (= G285), N278 (≠ Y286), R279 (≠ D287), A281 (≠ I289), R283 (≠ M291), H284 (≠ R292), D301 (= D308), I302 (= I309), Q306 (≠ N314), D320 (≠ G328), A321 (≠ L329), I397 (= I403), G415 (≠ S421)
- binding magnesium ion: R384 (≠ A390), V405 (≠ C411), F406 (≠ Y412), H410 (≠ A416), D445 (= D451), F450 (≠ M456), L451 (≠ V457), E453 (≠ G459), N472 (≠ D478), Y474 (≠ S480)
- 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 (≠ M291), G393 (= G399), L394 (≠ A400), S395 (≠ H401), L420 (≠ M426), G444 (= G450), D445 (= D451), F446 (≠ A452), D447 (≠ G453), N472 (≠ D478), Y474 (≠ S480), L475 (= L481), G476 (≠ A482), L477 (= L483), I478 (= I484)
- binding 2,3-dimethoxy-5-methyl-1,4-benzoquinone: E248 (≠ P255), Q352 (≠ P358)
Sites not aligning to the query:
8i01A Crystal structure of escherichia coli glyoxylate carboligase
27% identity, 87% coverage: 15:494/554 of query aligns to 5:490/594 of 8i01A
- binding flavin-adenine dinucleotide: R155 (= R162), G212 (= G217), G213 (≠ L218), G214 (≠ D219), N217 (≠ A222), T238 (≠ S243), L239 (≠ Y244), M240 (≠ K245), V256 (≠ A261), G257 (= G262), Q259 (≠ S264), T260 (≠ L266), G279 (= G285), N280 (≠ Y286), R281 (≠ D287), A283 (≠ I289), R285 (≠ M291), H286 (≠ R292), D303 (= D308), I304 (= I309), Q308 (≠ N314), D322 (≠ G328), A323 (≠ L329), G417 (≠ S421)
- binding magnesium ion: D447 (= D451), F452 (≠ M456), E455 (≠ G459), N474 (≠ D478), Y476 (≠ S480)
- binding thiamine diphosphate: G395 (= G399), L396 (≠ A400), S397 (≠ H401), L422 (≠ M426), G446 (= G450), D447 (= D451), F448 (≠ A452), D449 (≠ G453), N474 (≠ D478), Y476 (≠ S480), L477 (= L481), G478 (≠ A482), L479 (= L483), I480 (= I484)
- binding 2,3-dimethoxy-5-methyl-1,4-benzoquinone: Q354 (≠ P358)
Sites not aligning to the query:
P0DUV9 2-hydroxyacyl-CoA lyase; AcHACL; HACL; 2-hydroxyisobutyryl-CoA lyase; EC 4.1.-.- from Actinomycetospora chiangmaiensis (strain DSM 45062 / JCM 15998 / CCTCC AA 205017 / NBRC 104400 / YIM 0006) (see paper)
27% identity, 95% coverage: 5:532/554 of query aligns to 9:541/590 of P0DUV9
- G43 (= G39) binding
- Q255 (≠ Y244) binding
- RS 273:274 (≠ GL 262:263) binding
- R362 (≠ Q357) binding
- GD--L 410:412 (≠ GAHRI 399:403) binding
- R417 (≠ M408) binding
- G433 (≠ C424) binding
- D460 (= D451) binding
- GA 461:462 (≠ AG 452:453) binding
- N487 (≠ D478) binding
- NRAWNI 487:492 (≠ DASLAL 478:483) binding
- A489 (≠ S480) binding
- E493 (≠ I484) mutation to A: 10-fold decrease of 2-HIB-CoA cleavage rate, 6-fold increase in KM.; mutation to K: No cleavage of 2-HIB-CoA.; mutation to Q: 50-fold decrease of 2-HIB-CoA cleavage rate, 1.5-fold increase in KM.
Sites not aligning to the query:
- 561:564 binding
- 566:590 C-terminal lid
8i07D Crystal structure of escherichia coli glyoxylate carboligase double mutant in complex with glycolaldehyde
27% identity, 87% coverage: 15:494/554 of query aligns to 5:488/594 of 8i07D
- binding 2-oxidanylethanal: R285 (≠ M291), I480 (= I484)
- binding flavin-adenine dinucleotide: R155 (= R162), P156 (≠ N163), G212 (= G217), G213 (≠ L218), G214 (≠ D219), N217 (≠ A222), T238 (≠ S243), L239 (≠ Y244), M240 (≠ K245), V256 (≠ A261), G257 (= G262), Q259 (≠ S264), T260 (≠ L266), G279 (= G285), N280 (≠ Y286), R281 (≠ D287), R285 (≠ M291), H286 (≠ R292), D303 (= D308), I304 (= I309), Q308 (≠ N314), D322 (≠ G328), A323 (≠ L329), I399 (= I403), G417 (≠ S421)
- binding magnesium ion: D447 (= D451), F452 (≠ M456), L453 (≠ V457), E455 (≠ G459), N474 (≠ D478), Y476 (≠ S480)
- binding thiamine diphosphate: V52 (≠ E61), T76 (= T84), G395 (= G399), L396 (≠ A400), S397 (≠ H401), L422 (≠ M426), G446 (= G450), D447 (= D451), F448 (≠ A452), D449 (≠ G453), N474 (≠ D478), Y476 (≠ S480), L477 (= L481), G478 (≠ A482), L479 (= L483), I480 (= I484)
- binding ubiquinone-1: Q354 (≠ P358), R358 (= R362)
Sites not aligning to the query:
8i07A Crystal structure of escherichia coli glyoxylate carboligase double mutant in complex with glycolaldehyde
27% identity, 87% coverage: 15:494/554 of query aligns to 5:488/594 of 8i07A
- binding flavin-adenine dinucleotide: R155 (= R162), P156 (≠ N163), G212 (= G217), G213 (≠ L218), G214 (≠ D219), N217 (≠ A222), T238 (≠ S243), L239 (≠ Y244), M240 (≠ K245), V256 (≠ A261), G257 (= G262), Q259 (≠ S264), T260 (≠ L266), G279 (= G285), N280 (≠ Y286), R281 (≠ D287), R285 (≠ M291), H286 (≠ R292), D303 (= D308), I304 (= I309), Q308 (≠ N314), D322 (≠ G328), A323 (≠ L329), I394 (≠ S398), I399 (= I403), G417 (≠ S421)
- binding magnesium ion: D447 (= D451), F452 (≠ M456), L453 (≠ V457), E455 (≠ G459), N474 (≠ D478), Y476 (≠ S480)
- binding thiamine diphosphate: I394 (≠ S398), G395 (= G399), L396 (≠ A400), S397 (≠ H401), L422 (≠ M426), G446 (= G450), D447 (= D451), F448 (≠ A452), D449 (≠ G453), N474 (≠ D478), Y476 (≠ S480), L477 (= L481), G478 (≠ A482), L479 (= L483), I480 (= I484)
- binding ubiquinone-1: Q354 (≠ P358)
Sites not aligning to the query:
7pt4A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with a covalently bound reaction intermediate as well as products formyl-coa and acetone (see paper)
27% identity, 93% coverage: 18:532/554 of query aligns to 8:527/580 of 7pt4A
- binding s-{(9r,13s,15r)-17-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-9,13,15-trihydroxy-10,10-dimethyl-13,15-dioxido-4,8-dioxo-12,14,16-trioxa-3,7-diaza-13,15-diphosphaheptadec-1-yl} thioformate : Q241 (≠ Y244), G256 (= G259), S257 (≠ G260), R259 (≠ G262), S260 (≠ L263), Y278 (≠ L280), Q279 (≠ I281), Y352 (≠ A361), R403 (≠ M408), L404 (≠ W409)
- binding magnesium ion: D446 (= D451), N473 (≠ D478), A475 (≠ S480)
- binding thiamine diphosphate: G396 (= G399), D397 (≠ R402), L398 (≠ I403), G419 (≠ C424), L421 (≠ M426), G445 (= G450), D446 (= D451), G447 (≠ A452), A448 (≠ G453), N473 (≠ D478), A475 (≠ S480), W476 (≠ L481), N477 (≠ A482), I478 (≠ L483), E479 (≠ I484)
Sites not aligning to the query:
- binding s-{(9r,13s,15r)-17-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-9,13,15-trihydroxy-10,10-dimethyl-13,15-dioxido-4,8-dioxo-12,14,16-trioxa-3,7-diaza-13,15-diphosphaheptadec-1-yl} thioformate : 552
7pt1A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with substrate 2-hib-coa and inactive cofactor 3-deaza-thdp (see paper)
27% identity, 93% coverage: 18:532/554 of query aligns to 8:527/574 of 7pt1A
- binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} 2-hydroxy-2-methylpropanethioate: L113 (≠ H123), Q114 (= Q124), G256 (= G259), S257 (≠ G260), R259 (≠ G262), S260 (≠ L263), Q279 (≠ R292), Y352 (≠ A361), R403 (≠ M408), L404 (≠ W409), G419 (≠ C424)
- binding magnesium ion: D446 (= D451), N473 (≠ D478), A475 (≠ S480)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E61), T74 (= T84), P77 (= P87), G396 (= G399), D397 (≠ A400), L398 (≠ I403), G419 (≠ C424), L421 (≠ M426), G445 (= G450), D446 (= D451), G447 (≠ A452), A448 (≠ G453), N473 (≠ D478), A475 (≠ S480), W476 (≠ L481), N477 (≠ A482), I478 (≠ L483), E479 (≠ I484)
Sites not aligning to the query:
- binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} 2-hydroxy-2-methylpropanethioate: 547, 552
7pt4B Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with a covalently bound reaction intermediate as well as products formyl-coa and acetone (see paper)
27% identity, 93% coverage: 18:532/554 of query aligns to 8:527/584 of 7pt4B
- binding magnesium ion: D446 (= D451), N473 (≠ D478), A475 (≠ S480)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1r,11r,15s,17r)-19-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-1,11,15,17-tetrahydroxy-12,12-dimethyl-15,17-dioxido-6,10-dioxo-14,16,18-trioxa-2-thia-5,9-diaza-15,17-diphosphanonadec-1-yl}-5-(2-{[(r)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: S257 (≠ G260), R259 (≠ G262), S260 (≠ L263), Q279 (≠ R292), Y352 (≠ A361), G395 (≠ S398), G396 (= G399), D397 (≠ A400), L398 (≠ I403), L399 (= L404), R403 (≠ M408), L404 (≠ W409), G419 (≠ C424), L421 (≠ M426), G445 (= G450), D446 (= D451), G447 (≠ A452), A448 (≠ G453), N473 (≠ D478), A475 (≠ S480), W476 (≠ L481), N477 (≠ A482), I478 (≠ L483), E479 (≠ I484)
Sites not aligning to the query:
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1r,11r,15s,17r)-19-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-1,11,15,17-tetrahydroxy-12,12-dimethyl-15,17-dioxido-6,10-dioxo-14,16,18-trioxa-2-thia-5,9-diaza-15,17-diphosphanonadec-1-yl}-5-(2-{[(r)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: 547, 561
2ihuC Carboxyethylarginine synthase from streptomyces clavuligerus: putative reaction intermediate complex (see paper)
27% identity, 88% coverage: 52:537/554 of query aligns to 38:541/551 of 2ihuC
- active site: E47 (= E61), T70 (= T84), H110 (= H123), Q111 (= Q124), C112 (≠ V125), V160 (≠ I172), I265 (≠ P265), L292 (≠ M291), I400 (≠ S398), S426 (≠ C424), F428 (≠ M426), D453 (= D451), N480 (≠ D478), T482 (≠ S480), N483 (≠ L481), L485 (= L483), I486 (= I484), Y489 (≠ K487)
- binding magnesium ion: D453 (= D451), N480 (≠ D478), T482 (≠ S480)
- binding 5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2-[(1z)-1-hydroxy-3-(phosphonooxy)prop-1-en-1-yl]-3-{[(4z)-4-imino-2-methyl-4,5-dihydropyrimidin-5-yl]methyl}-4-methyl-1,3-thiazol-3-ium: G401 (= G399), F402 (≠ A400), F403 (≠ H401), F428 (≠ M426), G452 (= G450), D453 (= D451), G454 (≠ A452), T482 (≠ S480), N483 (≠ L481), G484 (≠ A482), L485 (= L483), I486 (= I484), Y489 (≠ K487)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: E47 (= E61), T70 (= T84), P73 (= P87)
Sites not aligning to the query:
Query Sequence
>GFF1219 FitnessBrowser__Phaeo:GFF1219
MTETNSAAAAATDPLRAADVLAQRLYAAGCRHAFGMPGGEVLTLVDALTKAGISFHLAKH
ENSAGFMGEGVYHSDGAPVILVATLGPGALNGVNVVANAHQDRVPMLVLTGCVDAAEAAT
YTHQVLDHQAVFAPITKATYRLNAEAAGVIADKALRIATQPRNGPVHIDVPISVADAPAG
PHRPYLAPARATQPQPADLAQARAWLAEADRPVAVVGLDAVAEDAGASLRAFLEHYQIPF
VTSYKAKGILPEDHPLCLGGAGLSPLADRHLLPLLREADLILALGYDPIEMRPGWRNAWD
CSRQRVIDICAEDNTHYMHTASLTVVAGLAPSLRALTVGAQLADDAPQGNAHWPDGQPEA
ARDALAAAFAADADWGPAAIIAECQATLPADTLATADSGAHRILLSQMWHCYEPRALIQS
SGLCTMGCAVPMAIGRKLAEPQRTVVSFSGDAGFLMVAGELSTAAELGVAPIFVVFVDAS
LALIDLKQRQRRLDNAGVDFGLHDFAAMGRAFGGNGVRVRDRASLRAALSEAQQAERFTV
IAAEFDREAYDGLI
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