SitesBLAST
Comparing WP_089299936.1 NCBI__GCF_900188115.1:WP_089299936.1 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)
74% identity, 99% coverage: 7:428/428 of query aligns to 6:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y91), S91 (= S93), W93 (= W95), D153 (= D154), R228 (= R229), T347 (= T348)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C192), G192 (= G193), H193 (= H194), R228 (= R229), S315 (= S316), S317 (= S318), T347 (= T348)
- binding magnesium ion: A276 (= A277), A279 (≠ S280), Q308 (= Q309)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
74% identity, 99% coverage: 7:428/428 of query aligns to 6:427/427 of 6wsiA
- active site: Y89 (= Y91), D108 (= D110), D153 (= D154), E155 (= E156), H180 (= H181), E182 (= E183), C191 (= C192), H193 (= H194), R228 (= R229), E285 (= E286), Q308 (= Q309), S315 (= S316), S317 (= S318)
- binding magnesium ion: A276 (= A277), A279 (≠ S280), Q308 (= Q309)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C192), G192 (= G193), H193 (= H194), R228 (= R229), E285 (= E286), N313 (= N314), S315 (= S316), S317 (= S318), T347 (= T348)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
74% identity, 99% coverage: 7:428/428 of query aligns to 6:427/427 of 6vb9A
- active site: Y89 (= Y91), D108 (= D110), D153 (= D154), E155 (= E156), H180 (= H181), E182 (= E183), C191 (= C192), H193 (= H194), R228 (= R229), E285 (= E286), Q308 (= Q309), S315 (= S316), S317 (= S318)
- binding magnesium ion: A276 (= A277), A279 (≠ S280), Q308 (= Q309)
- binding oxalic acid: Y89 (= Y91), S91 (= S93), G92 (= G94), W93 (= W95), D153 (= D154), C191 (= C192), R228 (= R229), W283 (= W284), T347 (= T348)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
74% identity, 99% coverage: 7:428/428 of query aligns to 6:427/427 of 5dqlA
- active site: Y89 (= Y91), D108 (= D110), D153 (= D154), E155 (= E156), H180 (= H181), E182 (= E183), C191 (= C192), H193 (= H194), R228 (= R229), E285 (= E286), Q308 (= Q309), S315 (= S316), S317 (= S318)
- binding magnesium ion: A276 (= A277), A279 (≠ S280), Q308 (= Q309)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W95), D108 (= D110), C191 (= C192), H193 (= H194), S315 (= S316), S317 (= S318), T347 (= T348), L348 (= L349)
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
74% identity, 99% coverage: 7:428/428 of query aligns to 5:426/426 of 6xppA
- active site: Y88 (= Y91), D107 (= D110), D152 (= D154), E154 (= E156), H179 (= H181), E181 (= E183), C190 (= C192), H192 (= H194), R227 (= R229), E284 (= E286), Q307 (= Q309), S314 (= S316), S316 (= S318)
- binding 2-methylidenebutanedioic acid: W92 (= W95), C190 (= C192), H192 (= H194), R227 (= R229), N312 (= N314), S314 (= S316), S316 (= S318), T346 (= T348)
- binding magnesium ion: A275 (= A277), A278 (≠ S280), Q307 (= Q309)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
74% identity, 99% coverage: 7:428/428 of query aligns to 7:428/428 of 6c4aA
- active site: Y90 (= Y91), D109 (= D110), D154 (= D154), E156 (= E156), H181 (= H181), E183 (= E183), C192 (= C192), H194 (= H194), R229 (= R229), E286 (= E286), Q309 (= Q309), S316 (= S316), S318 (= S318)
- binding 3-nitropropanoic acid: Y357 (= Y357), S358 (= S358), R380 (= R380)
- binding magnesium ion: A277 (= A277), A280 (≠ S280), Q309 (= Q309)
- binding pyruvic acid: Y90 (= Y91), S92 (= S93), G93 (= G94), W94 (= W95), D154 (= D154), C192 (= C192), R229 (= R229), W284 (= W284), T348 (= T348)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
74% identity, 99% coverage: 7:428/428 of query aligns to 6:427/428 of P9WKK7
- SGW 91:93 (= SGW 93:95) binding
- D153 (= D154) binding
- C191 (= C192) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 193:194) binding
- R228 (= R229) binding
- NCSPS 313:317 (= NCSPS 314:318) binding
- K334 (≠ R335) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T348) binding
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
74% identity, 99% coverage: 7:428/428 of query aligns to 6:427/427 of 1f8iA
- active site: Y89 (= Y91), D108 (= D110), D153 (= D154), E155 (= E156), H180 (= H181), E182 (= E183), S191 (≠ C192), H193 (= H194), R228 (= R229), E285 (= E286), Q308 (= Q309), S315 (= S316), S317 (= S318)
- binding glyoxylic acid: Y89 (= Y91), S91 (= S93), W93 (= W95), D153 (= D154), T347 (= T348)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
72% identity, 97% coverage: 14:428/428 of query aligns to 9:423/423 of 6lrtA
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
68% identity, 97% coverage: 14:428/428 of query aligns to 7:417/417 of 7cmyC
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
69% identity, 95% coverage: 24:428/428 of query aligns to 14:423/425 of 7rbxC
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
65% identity, 99% coverage: 6:428/428 of query aligns to 2:434/434 of P0A9G6
- SGW 91:93 (= SGW 93:95) binding
- D157 (= D154) binding
- C195 (= C192) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A216) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R229) 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)
64% identity, 95% coverage: 6:411/428 of query aligns to 1:415/416 of 1igwC
- active site: Y88 (= Y91), D107 (= D110), D156 (= D154), E158 (= E156), H183 (= H181), E185 (= E183), C194 (= C192), R231 (= R229), E288 (= E286), K311 (≠ Q309), S318 (= S316), S320 (= S318)
- binding pyruvic acid: S90 (= S93), G91 (= G94), W92 (= W95), D156 (= D154), R231 (= R229), T350 (= T348)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
61% identity, 95% coverage: 6:411/428 of query aligns to 1:395/396 of 1igwA
- active site: Y88 (= Y91), D107 (= D110), D156 (= D154), E158 (= E156), H183 (= H181), E185 (= E183), C194 (= C192), R227 (= R229), E284 (= E286), K307 (≠ Q309)
- binding pyruvic acid: S90 (= S93), W92 (= W95), D156 (= D154), R227 (= R229), T330 (= T348)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
35% identity, 92% coverage: 19:411/428 of query aligns to 25:453/453 of 5e9fD
- active site: Y99 (= Y91), D118 (= D110), D172 (= D154), D174 (≠ E156), H199 (= H181), E201 (= E183), R240 (= R229), E330 (= E286), Q353 (= Q309), S360 (= S316), S362 (= S318)
- binding magnesium ion: D118 (= D110), D172 (= D154)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
38% identity, 56% coverage: 19:257/428 of query aligns to 25:275/544 of 7ebeA
- active site: Y99 (= Y91), D118 (= D110), D172 (= D154), D174 (≠ E156), H199 (= H181), E201 (= E183), C210 (= C192), H212 (= H194), R247 (= R229)
- binding magnesium ion: G102 (= G94), W103 (= W95), D172 (= D154)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
38% identity, 55% coverage: 19:252/428 of query aligns to 26:271/525 of 5e9gB
- active site: Y100 (= Y91), D119 (= D110), D173 (= D154), D175 (≠ E156), H200 (= H181), E202 (= E183), C211 (= C192), H213 (= H194), R248 (= R229)
- binding glyoxylic acid: Y100 (= Y91), S102 (= S93), G103 (= G94), W104 (= W95), D173 (= D154)
- binding glycerol: C211 (= C192), G212 (= G193), H213 (= H194), R248 (= R229)
Sites not aligning to the query:
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
35% identity, 67% coverage: 19:304/428 of query aligns to 26:302/486 of 5e9gD
- active site: Y100 (= Y91), D119 (= D110), D173 (= D154), D175 (≠ E156), H200 (= H181), E202 (= E183), C211 (= C192), H213 (= H194), R248 (= R229)
- binding glyoxylic acid: Y100 (= Y91), S102 (= S93), G103 (= G94), W104 (= W95), D173 (= D154), H200 (= H181), R248 (= R229)
- binding glycerol: C211 (= C192), G212 (= G193), H213 (= H194), R248 (= R229)
Sites not aligning to the query:
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
38% identity, 55% coverage: 19:252/428 of query aligns to 26:271/499 of 5e9gC
- active site: Y100 (= Y91), D119 (= D110), D173 (= D154), D175 (≠ E156), H200 (= H181), E202 (= E183), C211 (= C192), H213 (= H194), R248 (= R229)
- binding glyoxylic acid: Y100 (= Y91), S102 (= S93), W104 (= W95), R248 (= R229)
Sites not aligning to the query:
5e9hA Structural insights of isocitrate lyases from fusarium graminearum (see paper)
37% identity, 58% coverage: 10:256/428 of query aligns to 11:269/518 of 5e9hA
Sites not aligning to the query:
Query Sequence
>WP_089299936.1 NCBI__GCF_900188115.1:WP_089299936.1
MTEKSKTPEQAAAELAADWENNPRWKGITRPYSAADVVKLRGSVVEENTYARRGAEKLWD
LLNNEDYIHALGALTGNQAVQQVRAGLQAIYLSGWQVAGDANLAGQTYPDQSLYPANSVP
AVVRRINNALARADQITWAEGDTSIDWFAPIVADAEAGFGGPLNAFELMKGMISAGAAGV
HWEDQLASEKKCGHLGGKVLVPTKQHERTLNAARLAADIAGVPSLIIARTDAQAATLLTS
DIDERDQKHVTGERTSEGFYRVQNGLQPCIDRGLAYAPYSDLLWMETSEPDLDVARRFAE
AIKDKYPDQMLAYNCSPSFNWRKNLDDSTIAKFQRELAHMGYKFQFITLAGFHALNYSMF
DLAKGYATEDMTAYVDLQEREFAAEERGYTATKHQREVGTGWFDQVSTVLNPESSTTALT
GSTEEAQF
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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