SitesBLAST
Comparing HSERO_RS10565 FitnessBrowser__HerbieS:HSERO_RS10565 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)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
72% identity, 97% coverage: 4:425/434 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
69% identity, 97% coverage: 4:425/434 of query aligns to 1:417/417 of 7cmyC
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
69% identity, 98% coverage: 1:425/434 of query aligns to 1:434/434 of P0A9G6
- M1 (= M1) modified: Initiator methionine, Removed
- SGW 91:93 (= SGW 89:91) binding
- D157 (= D150) binding
- C195 (= C188) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A212) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R225) binding
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
69% identity, 93% coverage: 3:407/434 of query aligns to 2:415/416 of 1igwC
- active site: Y88 (= Y87), D107 (= D106), D156 (= D150), E158 (= E152), H183 (= H177), E185 (= E179), C194 (= C188), R231 (= R225), E288 (= E282), K311 (= K305), S318 (= S312), S320 (= S314)
- binding pyruvic acid: S90 (= S89), G91 (= G90), W92 (= W91), D156 (= D150), R231 (= R225), T350 (= T344)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
70% identity, 94% coverage: 20:425/434 of query aligns to 14:423/425 of 7rbxC
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
66% identity, 96% coverage: 9:425/434 of query aligns to 12:428/428 of 6c4aA
- active site: Y90 (= Y87), D109 (= D106), D154 (= D150), E156 (= E152), H181 (= H177), E183 (= E179), C192 (= C188), H194 (= H190), R229 (= R225), E286 (= E282), Q309 (≠ K305), S316 (= S312), S318 (= S314)
- binding 3-nitropropanoic acid: Y357 (= Y353), S358 (= S354), R380 (≠ A376)
- binding magnesium ion: A277 (= A273), A280 (= A276), Q309 (≠ K305)
- binding pyruvic acid: Y90 (= Y87), S92 (= S89), G93 (= G90), W94 (= W91), D154 (= D150), C192 (= C188), R229 (= R225), W284 (= W280), T348 (= T344)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
66% identity, 96% coverage: 9:425/434 of query aligns to 11:427/428 of P9WKK7
- SGW 91:93 (= SGW 89:91) binding
- D153 (= D150) binding
- C191 (= C188) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 189:190) binding
- R228 (= R225) binding
- NCSPS 313:317 (= NCSPS 310:314) binding
- K334 (≠ R331) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T344) binding
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
66% identity, 96% coverage: 9:425/434 of query aligns to 11:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y87), S91 (= S89), W93 (= W91), D153 (= D150), R228 (= R225), T347 (= T344)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C188), G192 (= G189), H193 (= H190), R228 (= R225), S315 (= S312), S317 (= S314), T347 (= T344)
- binding magnesium ion: A276 (= A273), A279 (= A276), Q308 (≠ K305)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
66% identity, 96% coverage: 9:425/434 of query aligns to 11:427/427 of 6wsiA
- active site: Y89 (= Y87), D108 (= D106), D153 (= D150), E155 (= E152), H180 (= H177), E182 (= E179), C191 (= C188), H193 (= H190), R228 (= R225), E285 (= E282), Q308 (≠ K305), S315 (= S312), S317 (= S314)
- binding magnesium ion: A276 (= A273), A279 (= A276), Q308 (≠ K305)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C188), G192 (= G189), H193 (= H190), R228 (= R225), E285 (= E282), N313 (= N310), S315 (= S312), S317 (= S314), T347 (= T344)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
66% identity, 96% coverage: 9:425/434 of query aligns to 11:427/427 of 6vb9A
- active site: Y89 (= Y87), D108 (= D106), D153 (= D150), E155 (= E152), H180 (= H177), E182 (= E179), C191 (= C188), H193 (= H190), R228 (= R225), E285 (= E282), Q308 (≠ K305), S315 (= S312), S317 (= S314)
- binding magnesium ion: A276 (= A273), A279 (= A276), Q308 (≠ K305)
- binding oxalic acid: Y89 (= Y87), S91 (= S89), G92 (= G90), W93 (= W91), D153 (= D150), C191 (= C188), R228 (= R225), W283 (= W280), T347 (= T344)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
66% identity, 96% coverage: 9:425/434 of query aligns to 11:427/427 of 5dqlA
- active site: Y89 (= Y87), D108 (= D106), D153 (= D150), E155 (= E152), H180 (= H177), E182 (= E179), C191 (= C188), H193 (= H190), R228 (= R225), E285 (= E282), Q308 (≠ K305), S315 (= S312), S317 (= S314)
- binding magnesium ion: A276 (= A273), A279 (= A276), Q308 (≠ K305)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W91), D108 (= D106), C191 (= C188), H193 (= H190), S315 (= S312), S317 (= S314), T347 (= T344), L348 (= L345)
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
66% identity, 96% coverage: 9:425/434 of query aligns to 10:426/426 of 6xppA
- active site: Y88 (= Y87), D107 (= D106), D152 (= D150), E154 (= E152), H179 (= H177), E181 (= E179), C190 (= C188), H192 (= H190), R227 (= R225), E284 (= E282), Q307 (≠ K305), S314 (= S312), S316 (= S314)
- binding 2-methylidenebutanedioic acid: W92 (= W91), C190 (= C188), H192 (= H190), R227 (= R225), N312 (= N310), S314 (= S312), S316 (= S314), T346 (= T344)
- binding magnesium ion: A275 (= A273), A278 (= A276), Q307 (≠ K305)
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
66% identity, 96% coverage: 9:425/434 of query aligns to 11:427/427 of 1f8iA
- active site: Y89 (= Y87), D108 (= D106), D153 (= D150), E155 (= E152), H180 (= H177), E182 (= E179), S191 (≠ C188), H193 (= H190), R228 (= R225), E285 (= E282), Q308 (≠ K305), S315 (= S312), S317 (= S314)
- binding glyoxylic acid: Y89 (= Y87), S91 (= S89), W93 (= W91), D153 (= D150), T347 (= T344)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
65% identity, 93% coverage: 3:407/434 of query aligns to 2:395/396 of 1igwA
- active site: Y88 (= Y87), D107 (= D106), D156 (= D150), E158 (= E152), H183 (= H177), E185 (= E179), C194 (= C188), R227 (= R225), E284 (= E282), K307 (= K305)
- binding pyruvic acid: S90 (= S89), W92 (= W91), D156 (= D150), R227 (= R225), T330 (= T344)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
35% identity, 91% coverage: 13:406/434 of query aligns to 23:452/453 of 5e9fD
- active site: Y99 (= Y87), D118 (= D106), D172 (= D150), D174 (≠ E152), H199 (= H177), E201 (= E179), R240 (= R225), E330 (= E282), Q353 (≠ K305), S360 (= S312), S362 (= S314)
- binding magnesium ion: D118 (= D106), D172 (= D150)
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
34% identity, 91% coverage: 13:406/434 of query aligns to 24:484/486 of 5e9gD
- active site: Y100 (= Y87), D119 (= D106), D173 (= D150), D175 (≠ E152), H200 (= H177), E202 (= E179), C211 (= C188), H213 (= H190), R248 (vs. gap), E363 (= E282), Q386 (≠ K305), S393 (= S312), S395 (= S314)
- binding glyoxylic acid: Y100 (= Y87), S102 (= S89), G103 (= G90), W104 (= W91), D173 (= D150), H200 (= H177), R248 (vs. gap), T424 (= T344)
- binding glycerol: C211 (= C188), G212 (= G189), H213 (= H190), R248 (vs. gap)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
39% identity, 56% coverage: 5:248/434 of query aligns to 16:270/544 of 7ebeA
- active site: Y99 (= Y87), D118 (= D106), D172 (= D150), D174 (≠ E152), H199 (= H177), E201 (= E179), C210 (= C188), H212 (= H190), R247 (= R225)
- binding magnesium ion: G102 (= G90), W103 (= W91), D172 (= D150)
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)
37% identity, 65% coverage: 15:298/434 of query aligns to 29:323/557 of P28240
- T53 (≠ S39) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K187) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (= M191) mutation to L: Reduces activity by 45%; when associated with R-216.
5e9hA Structural insights of isocitrate lyases from fusarium graminearum (see paper)
38% identity, 56% coverage: 5:248/434 of query aligns to 11:265/518 of 5e9hA
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
38% identity, 54% coverage: 13:248/434 of query aligns to 24:271/525 of 5e9gB
- active site: Y100 (= Y87), D119 (= D106), D173 (= D150), D175 (≠ E152), H200 (= H177), E202 (= E179), C211 (= C188), H213 (= H190), R248 (= R225)
- binding glyoxylic acid: Y100 (= Y87), S102 (= S89), G103 (= G90), W104 (= W91), D173 (= D150)
- binding glycerol: C211 (= C188), G212 (= G189), H213 (= H190), R248 (= R225)
Sites not aligning to the query:
Query Sequence
>HSERO_RS10565 FitnessBrowser__HerbieS:HSERO_RS10565
MSTREQQIQALERDWAENPRWKGIKRNYSAADVVRLRGSLQIEHTIAKRGADKLWNLVNN
EPFVNALGALTGNQAMQQVKAGLKAIYLSGWQVAGDANLAGEMYPDQSLYPANSVPMVVK
RINNTFARADQIQWSEGKDDIDFFAPIVADAEAGFGGVLNAFELMKSMIEAGAAGVHFED
QLASVKKCGHMGGKVLVPTREAVEKLNAARLAADVMGTKTLVIARTDAEAADLLTSDVDA
NDKPFLSGERTVEGFFKTHPGIDQAISRGLAYAEYADMVWCETGKPDLAFAKTFAEAIHA
KFPGKLLAYNCSPSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHALNYSMFNLAH
GYARNQMSAFVELQEAEFAAATKGFTAVKHQREVGTGYFDAVTQAIQQGQSSTTALHGST
EDEQFFDDKAKKAA
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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