SitesBLAST
Comparing WP_029767480.1 NCBI__GCF_000527155.1:WP_029767480.1 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)
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
75% identity, 98% coverage: 10:433/434 of query aligns to 8:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y95), S91 (= S97), W93 (= W99), D153 (= D159), R228 (= R234), T347 (= T353)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C197), G192 (= G198), H193 (= H199), R228 (= R234), S315 (= S321), S317 (= S323), T347 (= T353)
- binding magnesium ion: A276 (= A282), A279 (= A285), Q308 (= Q314)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
75% identity, 98% coverage: 10:433/434 of query aligns to 8:427/427 of 6wsiA
- active site: Y89 (= Y95), D108 (= D114), D153 (= D159), E155 (= E161), H180 (= H186), E182 (= E188), C191 (= C197), H193 (= H199), R228 (= R234), E285 (= E291), Q308 (= Q314), S315 (= S321), S317 (= S323)
- binding magnesium ion: A276 (= A282), A279 (= A285), Q308 (= Q314)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C197), G192 (= G198), H193 (= H199), R228 (= R234), E285 (= E291), N313 (= N319), S315 (= S321), S317 (= S323), T347 (= T353)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
75% identity, 98% coverage: 10:433/434 of query aligns to 8:427/427 of 6vb9A
- active site: Y89 (= Y95), D108 (= D114), D153 (= D159), E155 (= E161), H180 (= H186), E182 (= E188), C191 (= C197), H193 (= H199), R228 (= R234), E285 (= E291), Q308 (= Q314), S315 (= S321), S317 (= S323)
- binding magnesium ion: A276 (= A282), A279 (= A285), Q308 (= Q314)
- binding oxalic acid: Y89 (= Y95), S91 (= S97), G92 (= G98), W93 (= W99), D153 (= D159), C191 (= C197), R228 (= R234), W283 (= W289), T347 (= T353)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
75% identity, 98% coverage: 10:433/434 of query aligns to 8:427/427 of 5dqlA
- active site: Y89 (= Y95), D108 (= D114), D153 (= D159), E155 (= E161), H180 (= H186), E182 (= E188), C191 (= C197), H193 (= H199), R228 (= R234), E285 (= E291), Q308 (= Q314), S315 (= S321), S317 (= S323)
- binding magnesium ion: A276 (= A282), A279 (= A285), Q308 (= Q314)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W99), D108 (= D114), C191 (= C197), H193 (= H199), S315 (= S321), S317 (= S323), T347 (= T353), L348 (= L354)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
75% identity, 98% coverage: 10:433/434 of query aligns to 9:428/428 of 6c4aA
- active site: Y90 (= Y95), D109 (= D114), D154 (= D159), E156 (= E161), H181 (= H186), E183 (= E188), C192 (= C197), H194 (= H199), R229 (= R234), E286 (= E291), Q309 (= Q314), S316 (= S321), S318 (= S323)
- binding 3-nitropropanoic acid: Y357 (= Y362), S358 (= S363), R380 (= R385)
- binding magnesium ion: A277 (= A282), A280 (= A285), Q309 (= Q314)
- binding pyruvic acid: Y90 (= Y95), S92 (= S97), G93 (= G98), W94 (= W99), D154 (= D159), C192 (= C197), R229 (= R234), W284 (= W289), T348 (= T353)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
75% identity, 98% coverage: 10:433/434 of query aligns to 8:427/428 of P9WKK7
- SGW 91:93 (= SGW 97:99) binding substrate
- D153 (= D159) binding Mg(2+)
- C191 (= C197) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 198:199) binding substrate
- R228 (= R234) binding substrate
- NCSPS 313:317 (= NCSPS 319:323) binding substrate
- K334 (= K340) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T353) binding substrate
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
75% identity, 98% coverage: 10:433/434 of query aligns to 7:426/426 of 6xppA
- active site: Y88 (= Y95), D107 (= D114), D152 (= D159), E154 (= E161), H179 (= H186), E181 (= E188), C190 (= C197), H192 (= H199), R227 (= R234), E284 (= E291), Q307 (= Q314), S314 (= S321), S316 (= S323)
- binding 2-methylidenebutanedioic acid: W92 (= W99), C190 (= C197), H192 (= H199), R227 (= R234), N312 (= N319), S314 (= S321), S316 (= S323), T346 (= T353)
- binding magnesium ion: A275 (= A282), A278 (= A285), Q307 (= Q314)
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
74% identity, 98% coverage: 10:433/434 of query aligns to 8:427/427 of 1f8iA
- active site: Y89 (= Y95), D108 (= D114), D153 (= D159), E155 (= E161), H180 (= H186), E182 (= E188), S191 (≠ C197), H193 (= H199), R228 (= R234), E285 (= E291), Q308 (= Q314), S315 (= S321), S317 (= S323)
- binding glyoxylic acid: Y89 (= Y95), S91 (= S97), W93 (= W99), D153 (= D159), T347 (= T353)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
65% identity, 98% coverage: 7:433/434 of query aligns to 2:423/423 of 6lrtA
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
64% identity, 98% coverage: 8:433/434 of query aligns to 1:417/417 of 7cmyC
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
67% identity, 95% coverage: 24:434/434 of query aligns to 14:424/425 of 7rbxC
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
62% identity, 98% coverage: 8:433/434 of query aligns to 4:434/434 of P0A9G6
- SGW 91:93 (= SGW 97:99) binding substrate
- D157 (= D159) binding Mg(2+)
- C195 (= C197) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A221) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R234) 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)
62% identity, 94% coverage: 8:416/434 of query aligns to 3:415/416 of 1igwC
- active site: Y88 (= Y95), D107 (= D114), D156 (= D159), E158 (= E161), H183 (= H186), E185 (= E188), C194 (= C197), R231 (= R234), E288 (= E291), K311 (≠ Q314), S318 (= S321), S320 (= S323)
- binding pyruvic acid: S90 (= S97), G91 (= G98), W92 (= W99), D156 (= D159), R231 (= R234), T350 (= T353)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
59% identity, 94% coverage: 8:416/434 of query aligns to 3:395/396 of 1igwA
- active site: Y88 (= Y95), D107 (= D114), D156 (= D159), E158 (= E161), H183 (= H186), E185 (= E188), C194 (= C197), R227 (= R234), E284 (= E291), K307 (≠ Q314)
- binding pyruvic acid: S90 (= S97), W92 (= W99), D156 (= D159), R227 (= R234), T330 (= T353)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 92% coverage: 19:416/434 of query aligns to 25:453/453 of 5e9fD
- active site: Y99 (= Y95), D118 (= D114), D172 (= D159), D174 (≠ E161), H199 (= H186), E201 (= E188), R240 (= R234), E330 (= E291), Q353 (= Q314), S360 (= S321), S362 (= S323)
- binding magnesium ion: D118 (= D114), D172 (= D159)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
37% identity, 62% coverage: 19:288/434 of query aligns to 25:296/544 of 7ebeA
- active site: Y99 (= Y95), D118 (= D114), D172 (= D159), D174 (≠ E161), H199 (= H186), E201 (= E188), C210 (= C197), H212 (= H199), R247 (= R234)
- binding magnesium ion: G102 (= G98), W103 (= W99), D172 (= D159)
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, 55% coverage: 19:257/434 of query aligns to 29:277/557 of P28240
- T53 (≠ R43) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K196) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (≠ L200) mutation to L: Reduces activity by 45%; when associated with R-216.
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 55% coverage: 19:257/434 of query aligns to 26:271/499 of 5e9gC
- active site: Y100 (= Y95), D119 (= D114), D173 (= D159), D175 (≠ E161), H200 (= H186), E202 (= E188), C211 (= C197), H213 (= H199), R248 (= R234)
- binding glyoxylic acid: Y100 (= Y95), S102 (= S97), W104 (= W99), R248 (= R234)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 55% coverage: 19:257/434 of query aligns to 26:271/525 of 5e9gB
- active site: Y100 (= Y95), D119 (= D114), D173 (= D159), D175 (≠ E161), H200 (= H186), E202 (= E188), C211 (= C197), H213 (= H199), R248 (= R234)
- binding glyoxylic acid: Y100 (= Y95), S102 (= S97), G103 (= G98), W104 (= W99), D173 (= D159)
- binding glycerol: C211 (= C197), G212 (= G198), H213 (= H199), R248 (= R234)
Sites not aligning to the query:
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 55% coverage: 19:257/434 of query aligns to 26:271/486 of 5e9gD
- active site: Y100 (= Y95), D119 (= D114), D173 (= D159), D175 (≠ E161), H200 (= H186), E202 (= E188), C211 (= C197), H213 (= H199), R248 (= R234)
- binding glyoxylic acid: Y100 (= Y95), S102 (= S97), G103 (= G98), W104 (= W99), D173 (= D159), H200 (= H186), R248 (= R234)
- binding glycerol: C211 (= C197), G212 (= G198), H213 (= H199), R248 (= R234)
Sites not aligning to the query:
Query Sequence
>WP_029767480.1 NCBI__GCF_000527155.1:WP_029767480.1
MTDHRSDKVQTAEELSADWESNPRWANITRDYSAEDVIALRGRVQEEHTLARRGAEKLWR
QLTTEAETDGYTNALGALSGNQAVQQVKAGLRAIYLSGWQVAADANLSGHTYPDQSLYPA
NSVPAVVRRINNALMRADQIEFAEGEQSVEDWLVPIVADAEAGFGGPLNAYELMKGMIAS
GASAVHWEDQLASEKKCGHLGGKVLIPTSQHIRTLNAARLAADVEGVPSLLVARTDAEAA
TLMTSDIDERDRPFLTGDRTAEGYFQVRGGIEPCIARAKSYAPYADLLWMETGTPDLTVA
RAFAEEVKAEFPDQMLAYNCSPSFNWRRNLDDDTIAKFQKELAAMGYTFQFITLAGFHAL
NYSMFDLAHGYADGGMSAYVDLQEREFAAEERGYTATKHQREVGTGYFDRVSTILNPKGS
TLAMVNSTEAGQFE
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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