SitesBLAST
Comparing Dsui_0011 FitnessBrowser__PS:Dsui_0011 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)
72% identity, 100% coverage: 1:435/436 of query aligns to 1:434/434 of P0A9G6
- M1 (= M1) modified: Initiator methionine, Removed
- SGW 91:93 (= SGW 92:94) binding
- D157 (= D158) binding
- C195 (= C196) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A220) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R233) binding
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
72% identity, 95% coverage: 3:418/436 of query aligns to 2:416/416 of 1igwC
- active site: Y88 (= Y90), D107 (= D109), D156 (= D158), E158 (= E160), H183 (= H185), E185 (= E187), C194 (= C196), R231 (= R233), E288 (= E290), K311 (= K313), S318 (= S320), S320 (= S322)
- binding pyruvic acid: S90 (= S92), G91 (= G93), W92 (= W94), D156 (= D158), R231 (= R233), T350 (= T352)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
68% identity, 95% coverage: 3:418/436 of query aligns to 2:396/396 of 1igwA
- active site: Y88 (= Y90), D107 (= D109), D156 (= D158), E158 (= E160), H183 (= H185), E185 (= E187), C194 (= C196), R227 (= R233), E284 (= E290), K307 (= K313)
- binding pyruvic acid: S90 (= S92), W92 (= W94), D156 (= D158), R227 (= R233), T330 (= T352)
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
60% identity, 99% coverage: 4:435/436 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
61% identity, 99% coverage: 4:435/436 of query aligns to 3:423/423 of 6lrtA
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
58% identity, 98% coverage: 11:436/436 of query aligns to 13:428/428 of P9WKK7
- SGW 91:93 (= SGW 92:94) binding
- D153 (= D158) binding
- C191 (= C196) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 197:198) binding
- R228 (= R233) binding
- NCSPS 313:317 (= NCSPS 318:322) binding
- K334 (≠ E339) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T352) binding
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
58% identity, 97% coverage: 11:435/436 of query aligns to 12:426/426 of 6xppA
- active site: Y88 (= Y90), D107 (= D109), D152 (= D158), E154 (= E160), H179 (= H185), E181 (= E187), C190 (= C196), H192 (= H198), R227 (= R233), E284 (= E290), Q307 (≠ K313), S314 (= S320), S316 (= S322)
- binding 2-methylidenebutanedioic acid: W92 (= W94), C190 (= C196), H192 (= H198), R227 (= R233), N312 (= N318), S314 (= S320), S316 (= S322), T346 (= T352)
- binding magnesium ion: A275 (= A281), A278 (= A284), Q307 (≠ K313)
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
58% identity, 97% coverage: 11:435/436 of query aligns to 13:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y90), S91 (= S92), W93 (= W94), D153 (= D158), R228 (= R233), T347 (= T352)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C196), G192 (= G197), H193 (= H198), R228 (= R233), S315 (= S320), S317 (= S322), T347 (= T352)
- binding magnesium ion: A276 (= A281), A279 (= A284), Q308 (≠ K313)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
58% identity, 97% coverage: 11:435/436 of query aligns to 13:427/427 of 6wsiA
- active site: Y89 (= Y90), D108 (= D109), D153 (= D158), E155 (= E160), H180 (= H185), E182 (= E187), C191 (= C196), H193 (= H198), R228 (= R233), E285 (= E290), Q308 (≠ K313), S315 (= S320), S317 (= S322)
- binding magnesium ion: A276 (= A281), A279 (= A284), Q308 (≠ K313)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C196), G192 (= G197), H193 (= H198), R228 (= R233), E285 (= E290), N313 (= N318), S315 (= S320), S317 (= S322), T347 (= T352)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
58% identity, 97% coverage: 11:435/436 of query aligns to 13:427/427 of 6vb9A
- active site: Y89 (= Y90), D108 (= D109), D153 (= D158), E155 (= E160), H180 (= H185), E182 (= E187), C191 (= C196), H193 (= H198), R228 (= R233), E285 (= E290), Q308 (≠ K313), S315 (= S320), S317 (= S322)
- binding magnesium ion: A276 (= A281), A279 (= A284), Q308 (≠ K313)
- binding oxalic acid: Y89 (= Y90), S91 (= S92), G92 (= G93), W93 (= W94), D153 (= D158), C191 (= C196), R228 (= R233), W283 (= W288), T347 (= T352)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
58% identity, 97% coverage: 11:435/436 of query aligns to 13:427/427 of 5dqlA
- active site: Y89 (= Y90), D108 (= D109), D153 (= D158), E155 (= E160), H180 (= H185), E182 (= E187), C191 (= C196), H193 (= H198), R228 (= R233), E285 (= E290), Q308 (≠ K313), S315 (= S320), S317 (= S322)
- binding magnesium ion: A276 (= A281), A279 (= A284), Q308 (≠ K313)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W94), D108 (= D109), C191 (= C196), H193 (= H198), S315 (= S320), S317 (= S322), T347 (= T352), L348 (= L353)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
58% identity, 97% coverage: 11:435/436 of query aligns to 14:428/428 of 6c4aA
- active site: Y90 (= Y90), D109 (= D109), D154 (= D158), E156 (= E160), H181 (= H185), E183 (= E187), C192 (= C196), H194 (= H198), R229 (= R233), E286 (= E290), Q309 (≠ K313), S316 (= S320), S318 (= S322)
- binding 3-nitropropanoic acid: Y357 (= Y361), S358 (≠ N362), R380 (≠ P386)
- binding magnesium ion: A277 (= A281), A280 (= A284), Q309 (≠ K313)
- binding pyruvic acid: Y90 (= Y90), S92 (= S92), G93 (= G93), W94 (= W94), D154 (= D158), C192 (= C196), R229 (= R233), W284 (= W288), T348 (= T352)
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
58% identity, 97% coverage: 11:435/436 of query aligns to 13:427/427 of 1f8iA
- active site: Y89 (= Y90), D108 (= D109), D153 (= D158), E155 (= E160), H180 (= H185), E182 (= E187), S191 (≠ C196), H193 (= H198), R228 (= R233), E285 (= E290), Q308 (≠ K313), S315 (= S320), S317 (= S322)
- binding glyoxylic acid: Y89 (= Y90), S91 (= S92), W93 (= W94), D153 (= D158), T347 (= T352)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
58% identity, 95% coverage: 20:435/436 of query aligns to 14:423/425 of 7rbxC
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 93% coverage: 13:416/436 of query aligns to 23:452/453 of 5e9fD
- active site: Y99 (= Y90), D118 (= D109), D172 (= D158), D174 (≠ E160), H199 (= H185), E201 (= E187), R240 (= R233), E330 (= E290), Q353 (≠ K313), S360 (= S320), S362 (= S322)
- binding magnesium ion: D118 (= D109), D172 (= D158)
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
36% identity, 93% coverage: 13:418/436 of query aligns to 24:486/486 of 5e9gD
- active site: Y100 (= Y90), D119 (= D109), D173 (= D158), D175 (≠ E160), H200 (= H185), E202 (= E187), C211 (= C196), H213 (= H198), R248 (vs. gap), E363 (= E290), Q386 (≠ K313), S393 (= S320), S395 (= S322)
- binding glyoxylic acid: Y100 (= Y90), S102 (= S92), G103 (= G93), W104 (= W94), D173 (= D158), H200 (= H185), R248 (vs. gap), T424 (= T352)
- binding glycerol: C211 (= C196), G212 (= G197), H213 (= H198), R248 (vs. gap)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
38% identity, 59% coverage: 5:262/436 of query aligns to 16:276/544 of 7ebeA
- active site: Y99 (= Y90), D118 (= D109), D172 (= D158), D174 (≠ E160), H199 (= H185), E201 (= E187), C210 (= C196), H212 (= H198), R247 (= R233)
- binding magnesium ion: G102 (= G93), W103 (= W94), D172 (= D158)
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)
38% identity, 64% coverage: 9:289/436 of query aligns to 24:311/557 of P28240
- T53 (≠ S39) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K195) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (= M199) mutation to L: Reduces activity by 45%; when associated with R-216.
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 56% coverage: 13:256/436 of query aligns to 24:271/499 of 5e9gC
- active site: Y100 (= Y90), D119 (= D109), D173 (= D158), D175 (≠ E160), H200 (= H185), E202 (= E187), C211 (= C196), H213 (= H198), R248 (= R233)
- binding glyoxylic acid: Y100 (= Y90), S102 (= S92), W104 (= W94), R248 (= R233)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 56% coverage: 13:256/436 of query aligns to 24:271/525 of 5e9gB
- active site: Y100 (= Y90), D119 (= D109), D173 (= D158), D175 (≠ E160), H200 (= H185), E202 (= E187), C211 (= C196), H213 (= H198), R248 (= R233)
- binding glyoxylic acid: Y100 (= Y90), S102 (= S92), G103 (= G93), W104 (= W94), D173 (= D158)
- binding glycerol: C211 (= C196), G212 (= G197), H213 (= H198), R248 (= R233)
Sites not aligning to the query:
Query Sequence
>Dsui_0011 FitnessBrowser__PS:Dsui_0011
MSTREQQIAALEKDWAENPRWKGVKRGYSAADVVRLRGSLQPEYTFAQRGAKVLWEKVNG
GAKKGYVNAFGAITAGQAMQQAKAGLEAVYLSGWQVAADGNTSETMYPDQSLYAYDSVPT
MVRRINNTFKRADEIQWSRGINPGDKEFIDYFLPIVADAEAGFGGVLNAFELMKNMIAAG
AAGVHFEDQLAAAKKCGHMGGKVLVPTREAVEKLISARFAADVMGVPTLILARTDAEAAN
LITSDYDANDKPFLTGERTQEGFFRVKNGLEQSISRGVAYAPYADLVWCETGVPDIGFAR
EFAQAVHAACPGKLLSYNCSPSFNWKKNLNDSQIASFQEELSALGYKYQFITLAGIHVNW
YNTFKFAKAYAGGEGMKHYVEMVQEPEFAAREDGYTFVSHQQEVGTGYFDDVTTVIQGGS
SSVKALTGSTEEEQFH
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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