SitesBLAST
Comparing H281DRAFT_00580 FitnessBrowser__Burk376:H281DRAFT_00580 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
71% identity, 98% coverage: 4:429/435 of query aligns to 3:423/423 of 6lrtA
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
69% identity, 97% coverage: 8:429/435 of query aligns to 9:426/426 of 6xppA
- active site: Y88 (= Y87), D107 (= D106), D152 (= D155), E154 (= E157), H179 (= H182), E181 (= E184), C190 (= C193), H192 (= H195), R227 (= R230), E284 (= E287), Q307 (= Q310), S314 (= S317), S316 (= S319)
- binding 2-methylidenebutanedioic acid: W92 (= W91), C190 (= C193), H192 (= H195), R227 (= R230), N312 (= N315), S314 (= S317), S316 (= S319), T346 (= T349)
- binding magnesium ion: A275 (= A278), A278 (= A281), Q307 (= Q310)
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
69% identity, 97% coverage: 8:429/435 of query aligns to 10:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y87), S91 (= S89), W93 (= W91), D153 (= D155), R228 (= R230), T347 (= T349)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C193), G192 (= G194), H193 (= H195), R228 (= R230), S315 (= S317), S317 (= S319), T347 (= T349)
- binding magnesium ion: A276 (= A278), A279 (= A281), Q308 (= Q310)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
69% identity, 97% coverage: 8:429/435 of query aligns to 10:427/427 of 6wsiA
- active site: Y89 (= Y87), D108 (= D106), D153 (= D155), E155 (= E157), H180 (= H182), E182 (= E184), C191 (= C193), H193 (= H195), R228 (= R230), E285 (= E287), Q308 (= Q310), S315 (= S317), S317 (= S319)
- binding magnesium ion: A276 (= A278), A279 (= A281), Q308 (= Q310)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C193), G192 (= G194), H193 (= H195), R228 (= R230), E285 (= E287), N313 (= N315), S315 (= S317), S317 (= S319), T347 (= T349)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
69% identity, 97% coverage: 8:429/435 of query aligns to 10:427/427 of 6vb9A
- active site: Y89 (= Y87), D108 (= D106), D153 (= D155), E155 (= E157), H180 (= H182), E182 (= E184), C191 (= C193), H193 (= H195), R228 (= R230), E285 (= E287), Q308 (= Q310), S315 (= S317), S317 (= S319)
- binding magnesium ion: A276 (= A278), A279 (= A281), Q308 (= Q310)
- binding oxalic acid: Y89 (= Y87), S91 (= S89), G92 (= G90), W93 (= W91), D153 (= D155), C191 (= C193), R228 (= R230), W283 (= W285), T347 (= T349)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
69% identity, 97% coverage: 8:429/435 of query aligns to 10:427/427 of 5dqlA
- active site: Y89 (= Y87), D108 (= D106), D153 (= D155), E155 (= E157), H180 (= H182), E182 (= E184), C191 (= C193), H193 (= H195), R228 (= R230), E285 (= E287), Q308 (= Q310), S315 (= S317), S317 (= S319)
- binding magnesium ion: A276 (= A278), A279 (= A281), Q308 (= Q310)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W91), D108 (= D106), C191 (= C193), H193 (= H195), S315 (= S317), S317 (= S319), T347 (= T349), L348 (= L350)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
69% identity, 97% coverage: 8:429/435 of query aligns to 11:428/428 of 6c4aA
- active site: Y90 (= Y87), D109 (= D106), D154 (= D155), E156 (= E157), H181 (= H182), E183 (= E184), C192 (= C193), H194 (= H195), R229 (= R230), E286 (= E287), Q309 (= Q310), S316 (= S317), S318 (= S319)
- binding 3-nitropropanoic acid: Y357 (= Y358), S358 (= S359), R380 (≠ A381)
- binding magnesium ion: A277 (= A278), A280 (= A281), Q309 (= Q310)
- binding pyruvic acid: Y90 (= Y87), S92 (= S89), G93 (= G90), W94 (= W91), D154 (= D155), C192 (= C193), R229 (= R230), W284 (= W285), T348 (= T349)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
69% identity, 97% coverage: 8:429/435 of query aligns to 10:427/428 of P9WKK7
- SGW 91:93 (= SGW 89:91) binding
- D153 (= D155) binding
- C191 (= C193) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 194:195) binding
- R228 (= R230) binding
- NCSPS 313:317 (= NCSPS 315:319) binding
- K334 (≠ R336) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T349) binding
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
69% identity, 99% coverage: 1:429/435 of query aligns to 1:434/434 of P0A9G6
- M1 (= M1) modified: Initiator methionine, Removed
- SGW 91:93 (= SGW 89:91) binding
- D157 (= D155) binding
- C195 (= C193) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A217) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R230) binding
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
69% identity, 98% coverage: 4:429/435 of query aligns to 1:417/417 of 7cmyC
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
69% identity, 97% coverage: 8:429/435 of query aligns to 10:427/427 of 1f8iA
- active site: Y89 (= Y87), D108 (= D106), D153 (= D155), E155 (= E157), H180 (= H182), E182 (= E184), S191 (≠ C193), H193 (= H195), R228 (= R230), E285 (= E287), Q308 (= Q310), S315 (= S317), S317 (= S319)
- binding glyoxylic acid: Y89 (= Y87), S91 (= S89), W93 (= W91), D153 (= D155), T347 (= T349)
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
69% identity, 94% coverage: 3:412/435 of query aligns to 2:415/416 of 1igwC
- active site: Y88 (= Y87), D107 (= D106), D156 (= D155), E158 (= E157), H183 (= H182), E185 (= E184), C194 (= C193), R231 (= R230), E288 (= E287), K311 (≠ Q310), S318 (= S317), S320 (= S319)
- binding pyruvic acid: S90 (= S89), G91 (= G90), W92 (= W91), D156 (= D155), R231 (= R230), T350 (= T349)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
67% identity, 94% coverage: 20:429/435 of query aligns to 14:423/425 of 7rbxC
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
65% identity, 94% coverage: 3:412/435 of query aligns to 2:395/396 of 1igwA
- active site: Y88 (= Y87), D107 (= D106), D156 (= D155), E158 (= E157), H183 (= H182), E185 (= E184), C194 (= C193), R227 (= R230), E284 (= E287), K307 (≠ Q310)
- binding pyruvic acid: S90 (= S89), W92 (= W91), D156 (= D155), R227 (= R230), T330 (= T349)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 92% coverage: 13:411/435 of query aligns to 23:452/453 of 5e9fD
- active site: Y99 (= Y87), D118 (= D106), D172 (= D155), D174 (≠ E157), H199 (= H182), E201 (= E184), R240 (= R230), E330 (= E287), Q353 (= Q310), S360 (= S317), S362 (= S319)
- binding magnesium ion: D118 (= D106), D172 (= D155)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
39% identity, 55% coverage: 13:253/435 of query aligns to 23:270/544 of 7ebeA
- active site: Y99 (= Y87), D118 (= D106), D172 (= D155), D174 (≠ E157), H199 (= H182), E201 (= E184), C210 (= C193), H212 (= H195), R247 (= R230)
- binding magnesium ion: G102 (= G90), W103 (= W91), D172 (= D155)
Sites not aligning to the query:
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
31% identity, 92% coverage: 13:411/435 of query aligns to 24:484/486 of 5e9gD
- active site: Y100 (= Y87), D119 (= D106), D173 (= D155), D175 (≠ E157), H200 (vs. gap), E202 (= E175), C211 (vs. gap), H213 (vs. gap), R248 (= R205), E363 (= E287), Q386 (= Q310), S393 (= S317), S395 (= S319)
- binding glyoxylic acid: Y100 (= Y87), S102 (= S89), G103 (= G90), W104 (= W91), D173 (= D155), H200 (vs. gap), R248 (= R205), T424 (= T349)
- binding glycerol: C211 (vs. gap), G212 (vs. gap), H213 (vs. gap), R248 (= R205)
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 55% coverage: 13:253/435 of query aligns to 24:271/499 of 5e9gC
- active site: Y100 (= Y87), D119 (= D106), D173 (= D155), D175 (≠ E157), H200 (= H182), E202 (= E184), C211 (= C193), H213 (= H195), R248 (= R230)
- binding glyoxylic acid: Y100 (= Y87), S102 (= S89), W104 (= W91), R248 (= R230)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 55% coverage: 13:253/435 of query aligns to 24:271/525 of 5e9gB
- active site: Y100 (= Y87), D119 (= D106), D173 (= D155), D175 (≠ E157), H200 (= H182), E202 (= E184), C211 (= C193), H213 (= H195), R248 (= R230)
- binding glyoxylic acid: Y100 (= Y87), S102 (= S89), G103 (= G90), W104 (= W91), D173 (= D155)
- binding glycerol: C211 (= C193), G212 (= G194), H213 (= H195), R248 (= R230)
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, 63% coverage: 13:286/435 of query aligns to 27:311/557 of P28240
- T53 (≠ S39) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K192) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (= M196) mutation to L: Reduces activity by 45%; when associated with R-216.
Query Sequence
>H281DRAFT_00580 FitnessBrowser__Burk376:H281DRAFT_00580
MTTREEQARQLQQQWETDPRWKGVKRSYTAEDVIRLRGSVQVEHTLAKRGAEKLWHSVNT
EPFVNSLGALTGNQAMQQVKAGLKAIYLSGWQVAGDANVAGEMYPDQSLYPANSVPLVVK
RINNTLTRADQIQWSEGKNPGDEGYIDYFAPIVADAEAGFGGVLNAFELMKAMIEAGAAG
VHFEDQLASVKKCGHMGGKVLVPTRENVAKLTAARLAADVSGVSTVLLARTDAEAADLIT
SDVDENDKPFLTGERTVEGFYRTKPGLEQAISRGLAYAPYADMIWCETGKPDLEFAKKFA
DAIHKEYPDQLLSYNCSPSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHALNYSM
FNLAHGYARNQMTAFVEMQQAEFAAAEKGFTAVKHQREVGTGYFDAVTQTVEREASTTAL
HGSTEDEQFFDKKVA
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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