SitesBLAST
Comparing BPHYT_RS12285 FitnessBrowser__BFirm:BPHYT_RS12285 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, 99% coverage: 1:428/434 of query aligns to 1:423/423 of 6lrtA
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
70% identity, 97% coverage: 8:428/434 of query aligns to 11:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y86), S91 (= S88), W93 (= W90), 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 (= A280), Q308 (= Q309)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
70% identity, 97% coverage: 8:428/434 of query aligns to 11:427/427 of 6wsiA
- active site: Y89 (= Y86), D108 (= D105), 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 (= A280), 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)
70% identity, 97% coverage: 8:428/434 of query aligns to 11:427/427 of 6vb9A
- active site: Y89 (= Y86), D108 (= D105), 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 (= A280), Q308 (= Q309)
- binding oxalic acid: Y89 (= Y86), S91 (= S88), G92 (= G89), W93 (= W90), 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)
70% identity, 97% coverage: 8:428/434 of query aligns to 11:427/427 of 5dqlA
- active site: Y89 (= Y86), D108 (= D105), 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 (= A280), Q308 (= Q309)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W90), D108 (= D105), C191 (= C192), H193 (= H194), S315 (= S316), S317 (= S318), T347 (= T348), L348 (= L349)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
70% identity, 97% coverage: 8:428/434 of query aligns to 12:428/428 of 6c4aA
- active site: Y90 (= Y86), D109 (= D105), 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 (≠ A380)
- binding magnesium ion: A277 (= A277), A280 (= A280), Q309 (= Q309)
- binding pyruvic acid: Y90 (= Y86), S92 (= S88), G93 (= G89), W94 (= W90), 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)
70% identity, 97% coverage: 8:428/434 of query aligns to 11:427/428 of P9WKK7
- SGW 91:93 (= SGW 88:90) 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
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
70% identity, 97% coverage: 8:428/434 of query aligns to 10:426/426 of 6xppA
- active site: Y88 (= Y86), D107 (= D105), 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 (= W90), C190 (= C192), H192 (= H194), R227 (= R229), N312 (= N314), S314 (= S316), S316 (= S318), T346 (= T348)
- binding magnesium ion: A275 (= A277), A278 (= A280), Q307 (= Q309)
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
69% identity, 98% coverage: 3:428/434 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: 8:428/434 of query aligns to 11:427/427 of 1f8iA
- active site: Y89 (= Y86), D108 (= D105), 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 (= Y86), S91 (= S88), W93 (= W90), D153 (= D154), T347 (= T348)
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
69% identity, 98% coverage: 2:428/434 of query aligns to 3:434/434 of P0A9G6
- SGW 91:93 (= SGW 88:90) 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)
69% identity, 94% coverage: 2:411/434 of query aligns to 2:415/416 of 1igwC
- active site: Y88 (= Y86), D107 (= D105), D156 (= D154), E158 (= E156), H183 (= H181), E185 (= E183), C194 (= C192), R231 (= R229), E288 (= E286), K311 (≠ Q309), S318 (= S316), S320 (= S318)
- binding pyruvic acid: S90 (= S88), G91 (= G89), W92 (= W90), D156 (= D154), R231 (= R229), T350 (= T348)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
68% identity, 94% coverage: 19:428/434 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: 2:411/434 of query aligns to 2:395/396 of 1igwA
- active site: Y88 (= Y86), D107 (= D105), D156 (= D154), E158 (= E156), H183 (= H181), E185 (= E183), C194 (= C192), R227 (= R229), E284 (= E286), K307 (≠ Q309)
- binding pyruvic acid: S90 (= S88), W92 (= W90), D156 (= D154), R227 (= R229), T330 (= T348)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 92% coverage: 12:410/434 of query aligns to 23:452/453 of 5e9fD
- active site: Y99 (= Y86), D118 (= D105), D172 (= D154), D174 (≠ E156), H199 (= H181), E201 (= E183), R240 (= R229), E330 (= E286), Q353 (= Q309), S360 (= S316), S362 (= S318)
- binding magnesium ion: D118 (= D105), D172 (= D154)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
39% identity, 57% coverage: 4:252/434 of query aligns to 16:270/544 of 7ebeA
- active site: Y99 (= Y86), D118 (= D105), D172 (= D154), D174 (≠ E156), H199 (= H181), E201 (= E183), C210 (= C192), H212 (= H194), R247 (= R229)
- binding magnesium ion: G102 (= G89), W103 (= W90), D172 (= D154)
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, 63% coverage: 12:285/434 of query aligns to 27:311/557 of P28240
- T53 (≠ S38) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K191) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (= M195) mutation to L: Reduces activity by 45%; when associated with R-216.
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 67% coverage: 12:302/434 of query aligns to 24:300/486 of 5e9gD
- active site: Y100 (= Y86), D119 (= D105), D173 (= D154), D175 (≠ E156), H200 (= H181), E202 (= E183), C211 (= C192), H213 (= H194), R248 (= R229)
- binding glyoxylic acid: Y100 (= Y86), S102 (= S88), G103 (= G89), W104 (= W90), 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)
40% identity, 56% coverage: 12:252/434 of query aligns to 24:271/499 of 5e9gC
- active site: Y100 (= Y86), D119 (= D105), D173 (= D154), D175 (≠ E156), H200 (= H181), E202 (= E183), C211 (= C192), H213 (= H194), R248 (= R229)
- binding glyoxylic acid: Y100 (= Y86), S102 (= S88), W104 (= W90), R248 (= R229)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 56% coverage: 12:252/434 of query aligns to 24:271/525 of 5e9gB
- active site: Y100 (= Y86), D119 (= D105), D173 (= D154), D175 (≠ E156), H200 (= H181), E202 (= E183), C211 (= C192), H213 (= H194), R248 (= R229)
- binding glyoxylic acid: Y100 (= Y86), S102 (= S88), G103 (= G89), W104 (= W90), D173 (= D154)
- binding glycerol: C211 (= C192), G212 (= G193), H213 (= H194), R248 (= R229)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS12285 FitnessBrowser__BFirm:BPHYT_RS12285
MSRQEQVKQLQQQWETDPRWKGVKRTYTAEDVIRLRGSVQVEHTLAKRGAEKLWESVNNE
PFVNSLGALTGNQAMQQVKAGLKAIYLSGWQVAGDANVAGEMYPDQSLYPANSVPLVVKR
INNTLTRADQIQWSEGKNPGDEGYVDYFQPIVADAEAGFGGVLNAFELMKAMIEAGAAGV
HFEDQLASVKKCGHMGGKVLVPTRENIAKLTAARLAADVSGTPTVLLARTDAEAADLITS
DIDENDKPFLTGERTVEGFYRTKPGLEQAISRGLAYAPYADMIWCETGKPDLEFAKKFAD
AIHKEYPDQLLSYNCSPSFNWKKNLDDATIAKFQRELGAMGYKFQFITLAGFHALNYSMF
NLAHGYARNQMTAFVEMQQAEFAAAEKGFTAVKHQREVGTGYFDAVTQTVEREASTTALH
GSTEDEQFFDKKVA
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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