SitesBLAST
Comparing 18043 FitnessBrowser__Keio:18043 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)
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
100% identity, 100% coverage: 1:434/434 of query aligns to 1:434/434 of P0A9G6
- M1 (= M1) modified: Initiator methionine, Removed
- SGW 91:93 (= SGW 91:93) binding
- D157 (= D157) binding
- C195 (= C195) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A219) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R232) binding
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
100% identity, 96% coverage: 2:417/434 of query aligns to 1:416/416 of 1igwC
- active site: Y88 (= Y89), D107 (= D108), D156 (= D157), E158 (= E159), H183 (= H184), E185 (= E186), C194 (= C195), R231 (= R232), E288 (= E289), K311 (= K312), S318 (= S319), S320 (= S321)
- binding pyruvic acid: S90 (= S91), G91 (= G92), W92 (= W93), D156 (= D157), R231 (= R232), T350 (= T351)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
95% identity, 96% coverage: 2:417/434 of query aligns to 1:396/396 of 1igwA
- active site: Y88 (= Y89), D107 (= D108), D156 (= D157), E158 (= E159), H183 (= H184), E185 (= E186), C194 (= C195), R227 (= R232), E284 (= E289), K307 (= K312)
- binding pyruvic acid: S90 (= S91), W92 (= W93), D156 (= D157), R227 (= R232), T330 (= T351)
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
68% identity, 99% coverage: 4:434/434 of query aligns to 1:417/417 of 7cmyC
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
67% identity, 99% coverage: 4:434/434 of query aligns to 3:423/423 of 6lrtA
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
62% identity, 98% coverage: 9:434/434 of query aligns to 11:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y89), S91 (= S91), W93 (= W93), D153 (= D157), R228 (= R232), T347 (= T351)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C195), G192 (= G196), H193 (= H197), R228 (= R232), S315 (= S319), S317 (= S321), T347 (= T351)
- binding magnesium ion: A276 (= A280), A279 (= A283), Q308 (≠ K312)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
62% identity, 98% coverage: 9:434/434 of query aligns to 11:427/427 of 6wsiA
- active site: Y89 (= Y89), D108 (= D108), D153 (= D157), E155 (= E159), H180 (= H184), E182 (= E186), C191 (= C195), H193 (= H197), R228 (= R232), E285 (= E289), Q308 (≠ K312), S315 (= S319), S317 (= S321)
- binding magnesium ion: A276 (= A280), A279 (= A283), Q308 (≠ K312)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C195), G192 (= G196), H193 (= H197), R228 (= R232), E285 (= E289), N313 (= N317), S315 (= S319), S317 (= S321), T347 (= T351)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
62% identity, 98% coverage: 9:434/434 of query aligns to 11:427/427 of 6vb9A
- active site: Y89 (= Y89), D108 (= D108), D153 (= D157), E155 (= E159), H180 (= H184), E182 (= E186), C191 (= C195), H193 (= H197), R228 (= R232), E285 (= E289), Q308 (≠ K312), S315 (= S319), S317 (= S321)
- binding magnesium ion: A276 (= A280), A279 (= A283), Q308 (≠ K312)
- binding oxalic acid: Y89 (= Y89), S91 (= S91), G92 (= G92), W93 (= W93), D153 (= D157), C191 (= C195), R228 (= R232), W283 (= W287), T347 (= T351)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
62% identity, 98% coverage: 9:434/434 of query aligns to 11:427/427 of 5dqlA
- active site: Y89 (= Y89), D108 (= D108), D153 (= D157), E155 (= E159), H180 (= H184), E182 (= E186), C191 (= C195), H193 (= H197), R228 (= R232), E285 (= E289), Q308 (≠ K312), S315 (= S319), S317 (= S321)
- binding magnesium ion: A276 (= A280), A279 (= A283), Q308 (≠ K312)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W93), D108 (= D108), C191 (= C195), H193 (= H197), S315 (= S319), S317 (= S321), T347 (= T351), L348 (= L352)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
62% identity, 98% coverage: 9:434/434 of query aligns to 12:428/428 of 6c4aA
- active site: Y90 (= Y89), D109 (= D108), D154 (= D157), E156 (= E159), H181 (= H184), E183 (= E186), C192 (= C195), H194 (= H197), R229 (= R232), E286 (= E289), Q309 (≠ K312), S316 (= S319), S318 (= S321)
- binding 3-nitropropanoic acid: Y357 (≠ F360), S358 (≠ N361), R380 (≠ P385)
- binding magnesium ion: A277 (= A280), A280 (= A283), Q309 (≠ K312)
- binding pyruvic acid: Y90 (= Y89), S92 (= S91), G93 (= G92), W94 (= W93), D154 (= D157), C192 (= C195), R229 (= R232), W284 (= W287), T348 (= T351)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
62% identity, 98% coverage: 9:434/434 of query aligns to 11:427/428 of P9WKK7
- SGW 91:93 (= SGW 91:93) binding
- D153 (= D157) binding
- C191 (= C195) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 196:197) binding
- R228 (= R232) binding
- NCSPS 313:317 (= NCSPS 317:321) binding
- K334 (≠ Q338) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T351) binding
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
62% identity, 98% coverage: 9:434/434 of query aligns to 10:426/426 of 6xppA
- active site: Y88 (= Y89), D107 (= D108), D152 (= D157), E154 (= E159), H179 (= H184), E181 (= E186), C190 (= C195), H192 (= H197), R227 (= R232), E284 (= E289), Q307 (≠ K312), S314 (= S319), S316 (= S321)
- binding 2-methylidenebutanedioic acid: W92 (= W93), C190 (= C195), H192 (= H197), R227 (= R232), N312 (= N317), S314 (= S319), S316 (= S321), T346 (= T351)
- binding magnesium ion: A275 (= A280), A278 (= A283), Q307 (≠ K312)
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
62% identity, 98% coverage: 9:434/434 of query aligns to 11:427/427 of 1f8iA
- active site: Y89 (= Y89), D108 (= D108), D153 (= D157), E155 (= E159), H180 (= H184), E182 (= E186), S191 (≠ C195), H193 (= H197), R228 (= R232), E285 (= E289), Q308 (≠ K312), S315 (= S319), S317 (= S321)
- binding glyoxylic acid: Y89 (= Y89), S91 (= S91), W93 (= W93), D153 (= D157), T347 (= T351)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
62% identity, 96% coverage: 19:434/434 of query aligns to 14:423/425 of 7rbxC
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
36% identity, 94% coverage: 6:415/434 of query aligns to 17:452/453 of 5e9fD
- active site: Y99 (= Y89), D118 (= D108), D172 (= D157), D174 (≠ E159), H199 (= H184), E201 (= E186), R240 (= R232), E330 (= E289), Q353 (≠ K312), S360 (= S319), S362 (= S321)
- binding magnesium ion: D118 (= D108), D172 (= D157)
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
30% identity, 95% coverage: 6:417/434 of query aligns to 18:486/486 of 5e9gD
- active site: Y100 (= Y89), D119 (= D108), D173 (= D157), D175 (≠ E159), H200 (= H184), E202 (= E186), C211 (= C195), H213 (vs. gap), R248 (≠ A220), E363 (= E289), Q386 (≠ K312), S393 (= S319), S395 (= S321)
- binding glyoxylic acid: Y100 (= Y89), S102 (= S91), G103 (= G92), W104 (= W93), D173 (= D157), H200 (= H184), R248 (≠ A220), T424 (= T351)
- binding glycerol: C211 (= C195), G212 (= G196), H213 (vs. gap), R248 (≠ A220)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
40% identity, 59% coverage: 6:260/434 of query aligns to 17:275/544 of 7ebeA
- active site: Y99 (= Y89), D118 (= D108), D172 (= D157), D174 (≠ E159), H199 (= H184), E201 (= E186), C210 (= C195), H212 (= H197), R247 (= R232)
- binding magnesium ion: G102 (= G92), W103 (= W93), D172 (= D157)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 58% coverage: 6:255/434 of query aligns to 18:271/525 of 5e9gB
- active site: Y100 (= Y89), D119 (= D108), D173 (= D157), D175 (≠ E159), H200 (= H184), E202 (= E186), C211 (= C195), H213 (= H197), R248 (= R232)
- binding glyoxylic acid: Y100 (= Y89), S102 (= S91), G103 (= G92), W104 (= W93), D173 (= D157)
- binding glycerol: C211 (= C195), G212 (= G196), H213 (= H197), R248 (= R232)
Sites not aligning to the query:
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 58% coverage: 6:255/434 of query aligns to 18:271/499 of 5e9gC
- active site: Y100 (= Y89), D119 (= D108), D173 (= D157), D175 (≠ E159), H200 (= H184), E202 (= E186), C211 (= C195), H213 (= H197), R248 (= R232)
- binding glyoxylic acid: Y100 (= Y89), S102 (= S91), W104 (= W93), R248 (= R232)
Sites not aligning to the query:
P28240 Isocitrate lyase; ICL; Methylisocitrate lyase; MICA; Threo-D(S)-isocitrate glyoxylate-lyase; EC 4.1.3.1; EC 4.1.3.30 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
36% identity, 64% coverage: 10:288/434 of query aligns to 25:311/557 of P28240
- T53 (≠ S38) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K194) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (= M198) mutation to L: Reduces activity by 45%; when associated with R-216.
Query Sequence
>18043 FitnessBrowser__Keio:18043
MKTRTQQIEELQKEWTQPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAAKMWRLLHGE
SKKGYINSLGALTGGQALQQAKAGIEAVYLSGWQVAADANLAASMYPDQSLYPANSVPAV
VERINNTFRRADQIQWSAGIEPGDPRYVDYFLPIVADAEAGFGGVLNAFELMKAMIEAGA
AAVHFEDQLASVKKCGHMGGKVLVPTQEAIQKLVAARLAADVTGVPTLLVARTDADAADL
ITSDCDPYDSEFITGERTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELARR
FAQAIHAKYPGKLLAYNCSPSFNWQKNLDDKTIASFQQQLSDMGYKFQFITLAGIHSMWF
NMFDLANAYAQGEGMKHYVEKVQQPEFAAAKDGYTFVSHQQEVGTGYFDKVTTIIQGGTS
SVTALTGSTEESQF
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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