SitesBLAST
Comparing GFF3292 FitnessBrowser__Marino:GFF3292 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)
6g1oA Structure of pseudomonas aeruginosa isocitrate lyase, icl (see paper)
81% identity, 91% coverage: 3:485/530 of query aligns to 4:486/486 of 6g1oA
- active site: D184 (= D182), Q211 (= Q209), C222 (= C220), H224 (= H222), R260 (= R258), S382 (= S381), S384 (= S383)
- binding calcium ion: D184 (= D182), D186 (= D184)
- binding glyoxylic acid: D117 (= D115), D186 (= D184), E213 (= E211), S217 (= S215)
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
28% identity, 79% coverage: 96:513/530 of query aligns to 99:486/486 of 5e9gD
- active site: Y100 (= Y97), D119 (= D115), D173 (= D182), D175 (= D184), H200 (≠ Q209), E202 (= E211), C211 (= C220), H213 (= H222), R248 (= R258), E363 (= E351), Q386 (≠ A374), S393 (= S381), S395 (= S383)
- binding glyoxylic acid: Y100 (= Y97), S102 (= S99), G103 (= G100), W104 (= W101), D173 (= D182), H200 (≠ Q209), R248 (= R258), T424 (= T450)
- binding glycerol: C211 (= C220), G212 (= G221), H213 (= H222), R248 (= R258)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
28% identity, 77% coverage: 96:505/530 of query aligns to 80:398/425 of 7rbxC
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
26% identity, 96% coverage: 7:513/530 of query aligns to 1:406/423 of 6lrtA
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 77% coverage: 96:505/530 of query aligns to 88:409/434 of P0A9G6
- SGW 91:93 (= SGW 99:101) binding
- D157 (= D182) binding
- C195 (= C220) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A244) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R258) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
27% identity, 85% coverage: 62:513/530 of query aligns to 57:400/417 of 7cmyC
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
28% identity, 78% coverage: 96:506/530 of query aligns to 99:494/499 of 5e9gC
- active site: Y100 (= Y97), D119 (= D115), D173 (= D182), D175 (= D184), H200 (≠ Q209), E202 (= E211), C211 (= C220), H213 (= H222), R248 (= R258), E377 (= E351), Q400 (≠ A374), S407 (= S381), S409 (= S383)
- binding glyoxylic acid: Y100 (= Y97), S102 (= S99), W104 (= W101), R248 (= R258)
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
27% identity, 77% coverage: 96:505/530 of query aligns to 87:408/416 of 1igwC
- active site: Y88 (= Y97), D107 (= D115), D156 (= D182), E158 (≠ D184), H183 (≠ Q209), E185 (= E211), C194 (= C220), R231 (= R258), E288 (= E351), K311 (≠ A374), S318 (= S381), S320 (= S383)
- binding pyruvic acid: S90 (= S99), G91 (= G100), W92 (= W101), D156 (= D182), R231 (= R258), T350 (= T450)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
28% identity, 82% coverage: 96:529/530 of query aligns to 98:543/544 of 7ebeA
- active site: Y99 (= Y97), D118 (= D115), D172 (= D182), D174 (= D184), H199 (≠ Q209), E201 (= E211), C210 (= C220), H212 (= H222), R247 (= R258), E402 (= E351), Q425 (≠ A374), S432 (= S381), S434 (= S383)
- binding magnesium ion: G102 (= G100), W103 (= W101), D172 (= D182)
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
26% identity, 79% coverage: 96:513/530 of query aligns to 99:525/525 of 5e9gB
- active site: Y100 (= Y97), D119 (= D115), D173 (= D182), D175 (= D184), H200 (≠ Q209), E202 (= E211), C211 (= C220), H213 (= H222), R248 (= R258), E401 (= E351), Q424 (≠ A374), S431 (= S381), S433 (= S383)
- binding glyoxylic acid: Y100 (= Y97), S102 (= S99), G103 (= G100), W104 (= W101), D173 (= D182), T463 (= T450)
- binding glycerol: C211 (= C220), G212 (= G221), H213 (= H222), R248 (= R258), E401 (= E351), N429 (= N379), T463 (= T450)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
25% identity, 95% coverage: 5:505/530 of query aligns to 9:404/428 of 6c4aA
- active site: Y90 (= Y97), D109 (= D115), D154 (= D182), E156 (≠ D184), H181 (≠ Q209), E183 (= E211), C192 (= C220), H194 (= H222), R229 (= R258), E286 (= E351), Q309 (≠ A374), S316 (= S381), S318 (= S383)
- binding 3-nitropropanoic acid: Y357 (≠ L459), S358 (= S460), R380 (≠ K484)
- binding magnesium ion: A277 (≠ Q342), A280 (= A345), Q309 (≠ A374)
- binding pyruvic acid: Y90 (= Y97), S92 (= S99), G93 (= G100), W94 (= W101), D154 (= D182), C192 (= C220), R229 (= R258), W284 (= W349), T348 (= T450)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
25% identity, 95% coverage: 5:505/530 of query aligns to 8:403/428 of P9WKK7
- SGW 91:93 (= SGW 99:101) binding
- D153 (= D182) binding
- C191 (= C220) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 221:222) binding
- R228 (= R258) binding
- NCSPS 313:317 (≠ NNSPS 379:383) binding
- K334 (≠ R436) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T450) binding
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
25% identity, 95% coverage: 5:505/530 of query aligns to 8:403/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y97), S91 (= S99), W93 (= W101), D153 (= D182), R228 (= R258), T347 (= T450)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C220), G192 (= G221), H193 (= H222), R228 (= R258), S315 (= S381), S317 (= S383), T347 (= T450)
- binding magnesium ion: A276 (≠ Q342), A279 (= A345), Q308 (≠ A374)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
25% identity, 95% coverage: 5:505/530 of query aligns to 8:403/427 of 6wsiA
- active site: Y89 (= Y97), D108 (= D115), D153 (= D182), E155 (≠ D184), H180 (≠ Q209), E182 (= E211), C191 (= C220), H193 (= H222), R228 (= R258), E285 (= E351), Q308 (≠ A374), S315 (= S381), S317 (= S383)
- binding magnesium ion: A276 (≠ Q342), A279 (= A345), Q308 (≠ A374)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C220), G192 (= G221), H193 (= H222), R228 (= R258), E285 (= E351), N313 (= N379), S315 (= S381), S317 (= S383), T347 (= T450)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
25% identity, 95% coverage: 5:505/530 of query aligns to 8:403/427 of 6vb9A
- active site: Y89 (= Y97), D108 (= D115), D153 (= D182), E155 (≠ D184), H180 (≠ Q209), E182 (= E211), C191 (= C220), H193 (= H222), R228 (= R258), E285 (= E351), Q308 (≠ A374), S315 (= S381), S317 (= S383)
- binding magnesium ion: A276 (≠ Q342), A279 (= A345), Q308 (≠ A374)
- binding oxalic acid: Y89 (= Y97), S91 (= S99), G92 (= G100), W93 (= W101), D153 (= D182), C191 (= C220), R228 (= R258), W283 (= W349), T347 (= T450)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
25% identity, 95% coverage: 5:505/530 of query aligns to 8:403/427 of 5dqlA
- active site: Y89 (= Y97), D108 (= D115), D153 (= D182), E155 (≠ D184), H180 (≠ Q209), E182 (= E211), C191 (= C220), H193 (= H222), R228 (= R258), E285 (= E351), Q308 (≠ A374), S315 (= S381), S317 (= S383)
- binding magnesium ion: A276 (≠ Q342), A279 (= A345), Q308 (≠ A374)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W101), D108 (= D115), C191 (= C220), H193 (= H222), S315 (= S381), S317 (= S383), T347 (= T450), L348 (= L451)
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
25% identity, 95% coverage: 5:505/530 of query aligns to 7:402/426 of 6xppA
- active site: Y88 (= Y97), D107 (= D115), D152 (= D182), E154 (≠ D184), H179 (≠ Q209), E181 (= E211), C190 (= C220), H192 (= H222), R227 (= R258), E284 (= E351), Q307 (≠ A374), S314 (= S381), S316 (= S383)
- binding 2-methylidenebutanedioic acid: W92 (= W101), C190 (= C220), H192 (= H222), R227 (= R258), N312 (= N379), S314 (= S381), S316 (= S383), T346 (= T450)
- binding magnesium ion: A275 (≠ Q342), A278 (= A345), Q307 (≠ A374)
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)
26% identity, 82% coverage: 96:529/530 of query aligns to 103:550/557 of P28240
- K216 (≠ Q219) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (≠ Q223) mutation to L: Reduces activity by 45%; when associated with R-216.
Sites not aligning to the query:
- 53 T→A: Abolishes short-term enzyme inactivation by glucose addition.
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
25% identity, 95% coverage: 5:505/530 of query aligns to 8:403/427 of 1f8iA
- active site: Y89 (= Y97), D108 (= D115), D153 (= D182), E155 (≠ D184), H180 (≠ Q209), E182 (= E211), S191 (≠ C220), H193 (= H222), R228 (= R258), E285 (= E351), Q308 (≠ A374), S315 (= S381), S317 (= S383)
- binding glyoxylic acid: Y89 (= Y97), S91 (= S99), W93 (= W101), D153 (= D182), T347 (= T450)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
28% identity, 78% coverage: 96:506/530 of query aligns to 98:447/453 of 5e9fD
- active site: Y99 (= Y97), D118 (= D115), D172 (= D182), D174 (= D184), H199 (≠ Q209), E201 (= E211), R240 (= R258), E330 (= E351), Q353 (≠ A374), S360 (= S381), S362 (= S383)
- binding magnesium ion: D118 (= D115), D172 (= D182)
Query Sequence
>GFF3292 FitnessBrowser__Marino:GFF3292
MPYAQDVDQIASLLKQHPTWNAINPKHAARMRAQNKFKTGLDIAKYTAKIMREDMANYDK
DTSQYTQSLGCWHGFIGQQKMLSIKKHFGTTKRRYLYLSGWMVAALRSEFGPLPDQSMHE
KTAVSGLIEELYTFLRQADAWELNHLFRALEEAENAGDNAKAEELIKQIDNHETHVVPII
ADIDAGFGNAEATYLLAKQMIEAGACCIQIENQVSDEKQCGHQDGKVTVPHADFLSKINA
VRLAFLELGVDDGVIVARTDSLGAGLTQKIAVTNEPGDLGDQYNSFIDGEVIEKAEDINN
GDVVIKQNGQLVRPKRLASGLFQFKPGTGEDRVVLDCITSLQNGADLLWIETEKPHVGQI
AAMVNRIKEVVPDAKLVYNNSPSFNWTLNFRQQVFDAWKEEGKDVSAYDRAKLMSEEYDN
TELGQLADEWCRNFQRDGSREAGIFHHLITLPTYHTAALSTDNLAKGYFGDEGMLAYVAG
VQRKEIRQGIATVKHQDMAGSNIGDDHKEFFAGEAALKAGGKDNTMNQFG
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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