SitesBLAST
Comparing 200655 FitnessBrowser__MR1:200655 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)
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
79% identity, 98% coverage: 8:440/440 of query aligns to 3:434/434 of P0A9G6
- SGW 91:93 (= SGW 97:99) binding substrate
- D157 (= D163) binding Mg(2+)
- C195 (= C201) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A225) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R238) binding substrate
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)
79% identity, 95% coverage: 8:423/440 of query aligns to 2:416/416 of 1igwC
- active site: Y88 (= Y95), D107 (= D114), D156 (= D163), E158 (= E165), H183 (= H190), E185 (= E192), C194 (= C201), R231 (= R238), E288 (= E295), K311 (≠ Q318), S318 (= S325), S320 (= S327)
- binding pyruvic acid: S90 (= S97), G91 (= G98), W92 (= W99), D156 (= D163), R231 (= R238), T350 (= T357)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
75% identity, 95% coverage: 8:423/440 of query aligns to 2:396/396 of 1igwA
- active site: Y88 (= Y95), D107 (= D114), D156 (= D163), E158 (= E165), H183 (= H190), E185 (= E192), C194 (= C201), R227 (= R238), E284 (= E295), K307 (≠ Q318)
- binding pyruvic acid: S90 (= S97), W92 (= W99), D156 (= D163), R227 (= R238), T330 (= T357)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
68% identity, 98% coverage: 9:440/440 of query aligns to 3:423/423 of 6lrtA
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
64% identity, 98% coverage: 9:440/440 of query aligns to 1:417/417 of 7cmyC
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
62% identity, 97% coverage: 14:440/440 of query aligns to 11:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y95), S91 (= S97), W93 (= W99), D153 (= D163), R228 (= R238), T347 (= T357)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C201), G192 (= G202), H193 (= H203), R228 (= R238), S315 (= S325), S317 (= S327), T347 (= T357)
- binding magnesium ion: A276 (= A286), A279 (= A289), Q308 (= Q318)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
62% identity, 97% coverage: 14:440/440 of query aligns to 11:427/427 of 6wsiA
- active site: Y89 (= Y95), D108 (= D114), D153 (= D163), E155 (= E165), H180 (= H190), E182 (= E192), C191 (= C201), H193 (= H203), R228 (= R238), E285 (= E295), Q308 (= Q318), S315 (= S325), S317 (= S327)
- binding magnesium ion: A276 (= A286), A279 (= A289), Q308 (= Q318)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C201), G192 (= G202), H193 (= H203), R228 (= R238), E285 (= E295), N313 (= N323), S315 (= S325), S317 (= S327), T347 (= T357)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
62% identity, 97% coverage: 14:440/440 of query aligns to 11:427/427 of 6vb9A
- active site: Y89 (= Y95), D108 (= D114), D153 (= D163), E155 (= E165), H180 (= H190), E182 (= E192), C191 (= C201), H193 (= H203), R228 (= R238), E285 (= E295), Q308 (= Q318), S315 (= S325), S317 (= S327)
- binding magnesium ion: A276 (= A286), A279 (= A289), Q308 (= Q318)
- binding oxalic acid: Y89 (= Y95), S91 (= S97), G92 (= G98), W93 (= W99), D153 (= D163), C191 (= C201), R228 (= R238), W283 (= W293), T347 (= T357)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
62% identity, 97% coverage: 14:440/440 of query aligns to 11:427/427 of 5dqlA
- active site: Y89 (= Y95), D108 (= D114), D153 (= D163), E155 (= E165), H180 (= H190), E182 (= E192), C191 (= C201), H193 (= H203), R228 (= R238), E285 (= E295), Q308 (= Q318), S315 (= S325), S317 (= S327)
- binding magnesium ion: A276 (= A286), A279 (= A289), Q308 (= Q318)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W99), D108 (= D114), C191 (= C201), H193 (= H203), S315 (= S325), S317 (= S327), T347 (= T357), L348 (= L358)
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
62% identity, 97% coverage: 14:440/440 of query aligns to 10:426/426 of 6xppA
- active site: Y88 (= Y95), D107 (= D114), D152 (= D163), E154 (= E165), H179 (= H190), E181 (= E192), C190 (= C201), H192 (= H203), R227 (= R238), E284 (= E295), Q307 (= Q318), S314 (= S325), S316 (= S327)
- binding 2-methylidenebutanedioic acid: W92 (= W99), C190 (= C201), H192 (= H203), R227 (= R238), N312 (= N323), S314 (= S325), S316 (= S327), T346 (= T357)
- binding magnesium ion: A275 (= A286), A278 (= A289), Q307 (= Q318)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
62% identity, 97% coverage: 14:440/440 of query aligns to 12:428/428 of 6c4aA
- active site: Y90 (= Y95), D109 (= D114), D154 (= D163), E156 (= E165), H181 (= H190), E183 (= E192), C192 (= C201), H194 (= H203), R229 (= R238), E286 (= E295), Q309 (= Q318), S316 (= S325), S318 (= S327)
- binding 3-nitropropanoic acid: Y357 (= Y366), S358 (≠ N367), R380 (≠ V391)
- binding magnesium ion: A277 (= A286), A280 (= A289), Q309 (= Q318)
- binding pyruvic acid: Y90 (= Y95), S92 (= S97), G93 (= G98), W94 (= W99), D154 (= D163), C192 (= C201), R229 (= R238), W284 (= W293), T348 (= T357)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
62% identity, 97% coverage: 14:440/440 of query aligns to 11:427/428 of P9WKK7
- SGW 91:93 (= SGW 97:99) binding substrate
- D153 (= D163) binding Mg(2+)
- C191 (= C201) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 202:203) binding substrate
- R228 (= R238) binding substrate
- NCSPS 313:317 (= NCSPS 323:327) binding substrate
- K334 (≠ Q344) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T357) binding substrate
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
62% identity, 97% coverage: 14:440/440 of query aligns to 11:427/427 of 1f8iA
- active site: Y89 (= Y95), D108 (= D114), D153 (= D163), E155 (= E165), H180 (= H190), E182 (= E192), S191 (≠ C201), H193 (= H203), R228 (= R238), E285 (= E295), Q308 (= Q318), S315 (= S325), S317 (= S327)
- binding glyoxylic acid: Y89 (= Y95), S91 (= S97), W93 (= W99), D153 (= D163), T347 (= T357)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
60% identity, 95% coverage: 25:440/440 of query aligns to 14:423/425 of 7rbxC
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 92% coverage: 18:421/440 of query aligns to 23:452/453 of 5e9fD
- active site: Y99 (= Y95), D118 (= D114), D172 (= D163), D174 (≠ E165), H199 (= H190), E201 (= E192), R240 (= R238), E330 (= E295), Q353 (= Q318), S360 (= S325), S362 (= S327)
- binding magnesium ion: D118 (= D114), D172 (= D163)
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
35% identity, 92% coverage: 18:423/440 of query aligns to 24:486/486 of 5e9gD
- active site: Y100 (= Y95), D119 (= D114), D173 (= D163), D175 (≠ E165), H200 (= H190), E202 (= E192), C211 (= C201), H213 (= H203), R248 (= R223), E363 (= E295), Q386 (= Q318), S393 (= S325), S395 (= S327)
- binding glyoxylic acid: Y100 (= Y95), S102 (= S97), G103 (= G98), W104 (= W99), D173 (= D163), H200 (= H190), R248 (= R223), T424 (= T357)
- binding glycerol: C211 (= C201), G212 (= G202), H213 (= H203), R248 (= R223)
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 55% coverage: 18:261/440 of query aligns to 24:271/525 of 5e9gB
- active site: Y100 (= Y95), D119 (= D114), D173 (= D163), D175 (≠ E165), H200 (= H190), E202 (= E192), C211 (= C201), H213 (= H203), R248 (= R238)
- binding glyoxylic acid: Y100 (= Y95), S102 (= S97), G103 (= G98), W104 (= W99), D173 (= D163)
- binding glycerol: C211 (= C201), G212 (= G202), H213 (= H203), R248 (= R238)
Sites not aligning to the query:
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 55% coverage: 18:261/440 of query aligns to 24:271/499 of 5e9gC
- active site: Y100 (= Y95), D119 (= D114), D173 (= D163), D175 (≠ E165), H200 (= H190), E202 (= E192), C211 (= C201), H213 (= H203), R248 (= R238)
- binding glyoxylic acid: Y100 (= Y95), S102 (= S97), W104 (= W99), R248 (= R238)
Sites not aligning to the query:
5e9hA Structural insights of isocitrate lyases from fusarium graminearum (see paper)
38% identity, 60% coverage: 10:272/440 of query aligns to 11:275/518 of 5e9hA
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)
35% identity, 67% coverage: 2:297/440 of query aligns to 8:314/557 of P28240
- T53 (≠ S44) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K200) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (= M204) mutation to L: Reduces activity by 45%; when associated with R-216.
Query Sequence
>200655 FitnessBrowser__MR1:200655
MTKATQTSRQAQIDAIKKDWAENPRWKNVRRPYTAEEVVALRGSIVPENTIAKRGAAKLW
DLVNGGSKKGYVNSLGALTGGQAVQQAKAGIEAIYLSGWQVAADANLAGTMYPDQSLYPA
NSVPAVVSRINNSFRRADQIQWSNGVNPEDENFVDYFLPIIADAEAGFGGVLNAFELMKS
MIDAGAAGVHFEDQLASVKKCGHMGGKVLVPTQEAVQKLVAARLAADVSGVETLVIARTD
ANAADLLTSDCDPYDRDFVTGERTNEGFYRVNAGLDQAISRGLAYAPYADLIWCETAKPD
LEEARRFAEAIHAQYPDQLLAYNCSPSFNWKKNLDDATIARFQQALSDMGYKYQFITLAG
IHNMWYNMFDLAYDYARGEGMKHYVEKVQEVEFAAAKKGYTFVAHQQEVGTGYFDQVTTV
IQGGHSSVTALTGSTEEEQF
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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