SitesBLAST
Comparing 5208774 FitnessBrowser__PV4:5208774 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)
81% identity, 96% coverage: 18:450/450 of query aligns to 3:434/434 of P0A9G6
- SGW 91:93 (= SGW 107:109) binding
- D157 (= D173) binding
- C195 (= C211) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A235) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R248) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
80% identity, 92% coverage: 18:433/450 of query aligns to 2:416/416 of 1igwC
- active site: Y88 (= Y105), D107 (= D124), D156 (= D173), E158 (= E175), H183 (= H200), E185 (= E202), C194 (= C211), R231 (= R248), E288 (= E305), K311 (≠ Q328), S318 (= S335), S320 (= S337)
- binding pyruvic acid: S90 (= S107), G91 (= G108), W92 (= W109), D156 (= D173), R231 (= R248), T350 (= T367)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
76% identity, 92% coverage: 18:433/450 of query aligns to 2:396/396 of 1igwA
- active site: Y88 (= Y105), D107 (= D124), D156 (= D173), E158 (= E175), H183 (= H200), E185 (= E202), C194 (= C211), R227 (= R248), E284 (= E305), K307 (≠ Q328)
- binding pyruvic acid: S90 (= S107), W92 (= W109), D156 (= D173), R227 (= R248), T330 (= T367)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
68% identity, 96% coverage: 17:450/450 of query aligns to 1:423/423 of 6lrtA
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
66% identity, 96% coverage: 19:450/450 of query aligns to 1:417/417 of 7cmyC
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
65% identity, 94% coverage: 26:450/450 of query aligns to 12:426/426 of 6xppA
- active site: Y88 (= Y105), D107 (= D124), D152 (= D173), E154 (= E175), H179 (= H200), E181 (= E202), C190 (= C211), H192 (= H213), R227 (= R248), E284 (= E305), Q307 (= Q328), S314 (= S335), S316 (= S337)
- binding 2-methylidenebutanedioic acid: W92 (= W109), C190 (= C211), H192 (= H213), R227 (= R248), N312 (= N333), S314 (= S335), S316 (= S337), T346 (= T367)
- binding magnesium ion: A275 (= A296), A278 (= A299), Q307 (= Q328)
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
65% identity, 94% coverage: 26:450/450 of query aligns to 13:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y105), S91 (= S107), W93 (= W109), D153 (= D173), R228 (= R248), T347 (= T367)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C211), G192 (= G212), H193 (= H213), R228 (= R248), S315 (= S335), S317 (= S337), T347 (= T367)
- binding magnesium ion: A276 (= A296), A279 (= A299), Q308 (= Q328)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
65% identity, 94% coverage: 26:450/450 of query aligns to 13:427/427 of 6wsiA
- active site: Y89 (= Y105), D108 (= D124), D153 (= D173), E155 (= E175), H180 (= H200), E182 (= E202), C191 (= C211), H193 (= H213), R228 (= R248), E285 (= E305), Q308 (= Q328), S315 (= S335), S317 (= S337)
- binding magnesium ion: A276 (= A296), A279 (= A299), Q308 (= Q328)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C211), G192 (= G212), H193 (= H213), R228 (= R248), E285 (= E305), N313 (= N333), S315 (= S335), S317 (= S337), T347 (= T367)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
65% identity, 94% coverage: 26:450/450 of query aligns to 13:427/427 of 6vb9A
- active site: Y89 (= Y105), D108 (= D124), D153 (= D173), E155 (= E175), H180 (= H200), E182 (= E202), C191 (= C211), H193 (= H213), R228 (= R248), E285 (= E305), Q308 (= Q328), S315 (= S335), S317 (= S337)
- binding magnesium ion: A276 (= A296), A279 (= A299), Q308 (= Q328)
- binding oxalic acid: Y89 (= Y105), S91 (= S107), G92 (= G108), W93 (= W109), D153 (= D173), C191 (= C211), R228 (= R248), W283 (= W303), T347 (= T367)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
65% identity, 94% coverage: 26:450/450 of query aligns to 13:427/427 of 5dqlA
- active site: Y89 (= Y105), D108 (= D124), D153 (= D173), E155 (= E175), H180 (= H200), E182 (= E202), C191 (= C211), H193 (= H213), R228 (= R248), E285 (= E305), Q308 (= Q328), S315 (= S335), S317 (= S337)
- binding magnesium ion: A276 (= A296), A279 (= A299), Q308 (= Q328)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W109), D108 (= D124), C191 (= C211), H193 (= H213), S315 (= S335), S317 (= S337), T347 (= T367), L348 (= L368)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
65% identity, 94% coverage: 26:450/450 of query aligns to 14:428/428 of 6c4aA
- active site: Y90 (= Y105), D109 (= D124), D154 (= D173), E156 (= E175), H181 (= H200), E183 (= E202), C192 (= C211), H194 (= H213), R229 (= R248), E286 (= E305), Q309 (= Q328), S316 (= S335), S318 (= S337)
- binding 3-nitropropanoic acid: Y357 (= Y376), S358 (≠ N377), R380 (≠ V401)
- binding magnesium ion: A277 (= A296), A280 (= A299), Q309 (= Q328)
- binding pyruvic acid: Y90 (= Y105), S92 (= S107), G93 (= G108), W94 (= W109), D154 (= D173), C192 (= C211), R229 (= R248), W284 (= W303), T348 (= T367)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
65% identity, 94% coverage: 26:450/450 of query aligns to 13:427/428 of P9WKK7
- SGW 91:93 (= SGW 107:109) binding
- D153 (= D173) binding
- C191 (= C211) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 212:213) binding
- R228 (= R248) binding
- NCSPS 313:317 (= NCSPS 333:337) binding
- K334 (≠ Q354) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T367) binding
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
64% identity, 94% coverage: 26:450/450 of query aligns to 13:427/427 of 1f8iA
- active site: Y89 (= Y105), D108 (= D124), D153 (= D173), E155 (= E175), H180 (= H200), E182 (= E202), S191 (≠ C211), H193 (= H213), R228 (= R248), E285 (= E305), Q308 (= Q328), S315 (= S335), S317 (= S337)
- binding glyoxylic acid: Y89 (= Y105), S91 (= S107), W93 (= W109), D153 (= D173), T347 (= T367)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
60% identity, 92% coverage: 35:450/450 of query aligns to 14:423/425 of 7rbxC
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 91% coverage: 21:431/450 of query aligns to 17:452/453 of 5e9fD
- active site: Y99 (= Y105), D118 (= D124), D172 (= D173), D174 (≠ E175), H199 (= H200), E201 (= E202), R240 (= R248), E330 (= E305), Q353 (= Q328), S360 (= S335), S362 (= S337)
- binding magnesium ion: D118 (= D124), D172 (= D173)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
39% identity, 57% coverage: 20:276/450 of query aligns to 16:275/544 of 7ebeA
- active site: Y99 (= Y105), D118 (= D124), D172 (= D173), D174 (≠ E175), H199 (= H200), E201 (= E202), C210 (= C211), H212 (= H213), R247 (= R248)
- binding magnesium ion: G102 (= G108), W103 (= W109), D172 (= D173)
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, 62% coverage: 28:307/450 of query aligns to 27:314/557 of P28240
- T53 (≠ S54) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K210) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (= M214) mutation to L: Reduces activity by 45%; when associated with R-216.
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 56% coverage: 21:271/450 of query aligns to 18:271/486 of 5e9gD
- active site: Y100 (= Y105), D119 (= D124), D173 (= D173), D175 (≠ E175), H200 (= H200), E202 (= E202), C211 (= C211), H213 (= H213), R248 (= R248)
- binding glyoxylic acid: Y100 (= Y105), S102 (= S107), G103 (= G108), W104 (= W109), D173 (= D173), H200 (= H200), R248 (= R248)
- binding glycerol: C211 (= C211), G212 (= G212), H213 (= H213), R248 (= R248)
Sites not aligning to the query:
5e9hA Structural insights of isocitrate lyases from fusarium graminearum (see paper)
39% identity, 57% coverage: 20:275/450 of query aligns to 11:269/518 of 5e9hA
Sites not aligning to the query:
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 56% coverage: 21:271/450 of query aligns to 18:271/499 of 5e9gC
- active site: Y100 (= Y105), D119 (= D124), D173 (= D173), D175 (≠ E175), H200 (= H200), E202 (= E202), C211 (= C211), H213 (= H213), R248 (= R248)
- binding glyoxylic acid: Y100 (= Y105), S102 (= S107), W104 (= W109), R248 (= R248)
Sites not aligning to the query:
Query Sequence
>5208774 FitnessBrowser__PV4:5208774
MLTPEMEKIMTKATTQISRQQQIDAIKQDWAENPRWAGVRRPYSAEDVVALRGSIVPENT
LATRGAEKLWQLVNGGAKKGYVNSLGALTGGQAVQQAKAGIEAIYLSGWQVAADANLAGT
MYPDQSLYPANSVPAVVQRINNSFRRADQIQWSNEIDPQDERYTDYFLPIVADAEAGFGG
VLNAYELMKNMIDAGAAGVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVSARLAADVSG
VPTLVIARTDANAADLLTSDCDPYDRDFITGERTSEGFYRVNAGIDQAISRGLAYAPYAD
LIWCETAKPDLEEARRFAEAIHAQYPDQLLAYNCSPSFNWKKNLDDATIARFQQELSDMG
YKYQFITLAGIHNMWYNMFDLAYDYARGEGMKHYVEKVQEVEFAAAKKGYTFVAHQQEVG
TGYFDKVTNVIQGGESSVTALTGSTEEEQF
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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