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Comparing RR42_RS25845 FitnessBrowser__Cup4G11:RR42_RS25845 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, 92% coverage: 1:482/526 of query aligns to 1:486/486 of 6g1oA
- active site: D184 (= D180), Q211 (= Q207), C222 (= C218), H224 (= H220), R260 (= R256), S382 (= S378), S384 (= S380)
- binding calcium ion: D184 (= D180), D186 (= D182)
- binding glyoxylic acid: D117 (= D117), D186 (= D182), E213 (= E209), S217 (= S213)
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: 98:526/526 of query aligns to 103:550/557 of P28240
- K216 (≠ Q217) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (≠ Q221) 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.
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 77% coverage: 98:502/526 of query aligns to 88:409/434 of P0A9G6
- SGW 91:93 (= SGW 101:103) binding
- D157 (= D180) binding
- C195 (= C218) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A242) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R256) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
26% identity, 93% coverage: 21:510/526 of query aligns to 13:406/423 of 6lrtA
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
28% identity, 77% coverage: 98:502/526 of query aligns to 87:408/416 of 1igwC
- active site: Y88 (= Y99), D107 (= D117), D156 (= D180), E158 (≠ D182), H183 (≠ Q207), E185 (= E209), C194 (= C218), R231 (= R256), E288 (= E348), K311 (≠ A371), S318 (= S378), S320 (= S380)
- binding pyruvic acid: S90 (= S101), G91 (= G102), W92 (= W103), D156 (= D180), R231 (= R256), T350 (= T447)
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
29% identity, 79% coverage: 98:510/526 of query aligns to 99:486/486 of 5e9gD
- active site: Y100 (= Y99), D119 (= D117), D173 (= D180), D175 (= D182), H200 (≠ Q207), E202 (= E209), C211 (= C218), H213 (= H220), R248 (= R256), E363 (= E348), Q386 (≠ A371), S393 (= S378), S395 (= S380)
- binding glyoxylic acid: Y100 (= Y99), S102 (= S101), G103 (= G102), W104 (= W103), D173 (= D180), H200 (≠ Q207), R248 (= R256), T424 (= T447)
- binding glycerol: C211 (= C218), G212 (= G219), H213 (= H220), R248 (= R256)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
27% identity, 82% coverage: 98:526/526 of query aligns to 98:543/544 of 7ebeA
- active site: Y99 (= Y99), D118 (= D117), D172 (= D180), D174 (= D182), H199 (≠ Q207), E201 (= E209), C210 (= C218), H212 (= H220), R247 (= R256), E402 (= E348), Q425 (≠ A371), S432 (= S378), S434 (= S380)
- binding magnesium ion: G102 (= G102), W103 (= W103), D172 (= D180)
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
25% identity, 95% coverage: 22:522/526 of query aligns to 18:412/417 of 7cmyC
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
28% identity, 77% coverage: 98:503/526 of query aligns to 99:494/499 of 5e9gC
- active site: Y100 (= Y99), D119 (= D117), D173 (= D180), D175 (= D182), H200 (≠ Q207), E202 (= E209), C211 (= C218), H213 (= H220), R248 (= R256), E377 (= E348), Q400 (≠ A371), S407 (= S378), S409 (= S380)
- binding glyoxylic acid: Y100 (= Y99), S102 (= S101), W104 (= W103), R248 (= R256)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
30% identity, 55% coverage: 98:387/526 of query aligns to 80:319/425 of 7rbxC
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
27% identity, 79% coverage: 98:510/526 of query aligns to 99:525/525 of 5e9gB
- active site: Y100 (= Y99), D119 (= D117), D173 (= D180), D175 (= D182), H200 (≠ Q207), E202 (= E209), C211 (= C218), H213 (= H220), R248 (= R256), E401 (= E348), Q424 (≠ A371), S431 (= S378), S433 (= S380)
- binding glyoxylic acid: Y100 (= Y99), S102 (= S101), G103 (= G102), W104 (= W103), D173 (= D180), T463 (= T447)
- binding glycerol: C211 (= C218), G212 (= G219), H213 (= H220), R248 (= R256), E401 (= E348), N429 (= N376), T463 (= T447)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
29% identity, 77% coverage: 98:503/526 of query aligns to 98:447/453 of 5e9fD
- active site: Y99 (= Y99), D118 (= D117), D172 (= D180), D174 (= D182), H199 (≠ Q207), E201 (= E209), R240 (= R256), E330 (= E348), Q353 (≠ A371), S360 (= S378), S362 (= S380)
- binding magnesium ion: D118 (= D117), D172 (= D180)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
28% identity, 77% coverage: 96:502/526 of query aligns to 87:404/428 of 6c4aA
- active site: Y90 (= Y99), D109 (= D117), D154 (= D180), E156 (≠ D182), H181 (≠ Q207), E183 (= E209), C192 (= C218), H194 (= H220), R229 (= R256), E286 (= E348), Q309 (≠ A371), S316 (= S378), S318 (= S380)
- binding 3-nitropropanoic acid: Y357 (≠ L456), S358 (= S457), R380 (≠ K481)
- binding magnesium ion: A277 (≠ Q339), A280 (= A342), Q309 (≠ A371)
- binding pyruvic acid: Y90 (= Y99), S92 (= S101), G93 (= G102), W94 (= W103), D154 (= D180), C192 (= C218), R229 (= R256), W284 (= W346), T348 (= T447)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
28% identity, 77% coverage: 96:502/526 of query aligns to 86:403/428 of P9WKK7
- SGW 91:93 (= SGW 101:103) binding
- D153 (= D180) binding
- C191 (= C218) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 219:220) binding
- R228 (= R256) binding
- NCSPS 313:317 (≠ NNSPS 376:380) binding
- K334 (≠ T418) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T447) binding
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
28% identity, 77% coverage: 96:502/526 of query aligns to 86:403/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y99), S91 (= S101), W93 (= W103), D153 (= D180), R228 (= R256), T347 (= T447)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C218), G192 (= G219), H193 (= H220), R228 (= R256), S315 (= S378), S317 (= S380), T347 (= T447)
- binding magnesium ion: A276 (≠ Q339), A279 (= A342), Q308 (≠ A371)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
28% identity, 77% coverage: 96:502/526 of query aligns to 86:403/427 of 6wsiA
- active site: Y89 (= Y99), D108 (= D117), D153 (= D180), E155 (≠ D182), H180 (≠ Q207), E182 (= E209), C191 (= C218), H193 (= H220), R228 (= R256), E285 (= E348), Q308 (≠ A371), S315 (= S378), S317 (= S380)
- binding magnesium ion: A276 (≠ Q339), A279 (= A342), Q308 (≠ A371)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C218), G192 (= G219), H193 (= H220), R228 (= R256), E285 (= E348), N313 (= N376), S315 (= S378), S317 (= S380), T347 (= T447)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
28% identity, 77% coverage: 96:502/526 of query aligns to 86:403/427 of 6vb9A
- active site: Y89 (= Y99), D108 (= D117), D153 (= D180), E155 (≠ D182), H180 (≠ Q207), E182 (= E209), C191 (= C218), H193 (= H220), R228 (= R256), E285 (= E348), Q308 (≠ A371), S315 (= S378), S317 (= S380)
- binding magnesium ion: A276 (≠ Q339), A279 (= A342), Q308 (≠ A371)
- binding oxalic acid: Y89 (= Y99), S91 (= S101), G92 (= G102), W93 (= W103), D153 (= D180), C191 (= C218), R228 (= R256), W283 (= W346), T347 (= T447)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
28% identity, 77% coverage: 96:502/526 of query aligns to 86:403/427 of 5dqlA
- active site: Y89 (= Y99), D108 (= D117), D153 (= D180), E155 (≠ D182), H180 (≠ Q207), E182 (= E209), C191 (= C218), H193 (= H220), R228 (= R256), E285 (= E348), Q308 (≠ A371), S315 (= S378), S317 (= S380)
- binding magnesium ion: A276 (≠ Q339), A279 (= A342), Q308 (≠ A371)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W103), D108 (= D117), C191 (= C218), H193 (= H220), S315 (= S378), S317 (= S380), T347 (= T447), L348 (= L448)
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
28% identity, 77% coverage: 96:502/526 of query aligns to 85:402/426 of 6xppA
- active site: Y88 (= Y99), D107 (= D117), D152 (= D180), E154 (≠ D182), H179 (≠ Q207), E181 (= E209), C190 (= C218), H192 (= H220), R227 (= R256), E284 (= E348), Q307 (≠ A371), S314 (= S378), S316 (= S380)
- binding 2-methylidenebutanedioic acid: W92 (= W103), C190 (= C218), H192 (= H220), R227 (= R256), N312 (= N376), S314 (= S378), S316 (= S380), T346 (= T447)
- binding magnesium ion: A275 (≠ Q339), A278 (= A342), Q307 (≠ A371)
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
27% identity, 77% coverage: 96:498/526 of query aligns to 86:399/427 of 1f8iA
- active site: Y89 (= Y99), D108 (= D117), D153 (= D180), E155 (≠ D182), H180 (≠ Q207), E182 (= E209), S191 (≠ C218), H193 (= H220), R228 (= R256), E285 (= E348), Q308 (≠ A371), S315 (= S378), S317 (= S380)
- binding glyoxylic acid: Y89 (= Y99), S91 (= S101), W93 (= W103), D153 (= D180), T347 (= T447)
Query Sequence
>RR42_RS25845 FitnessBrowser__Cup4G11:RR42_RS25845
MAQYQDDIKAVAGLKENHGSAWNAINPEYAARMRAQNKFKTGLDIAKYTAKIMRADMAAY
DADSSKYTQSLGCWHGFIGQQKMISIKKHFNSTERRYLYLSGWMVAALRSEFGPLPDQSM
HEKTSVSALIRELYTFLRQADARELGGLFRELDAAQGPAKAAIQEKIDNHVTHVVPIIAD
IDAGFGNAEATYLLAKQFIEAGACCIQIENQVSDEKQCGHQDGKVTVPHEDFLAKIRAIR
YAFLELGVDDGVIVARTDSLGAGLTKQIAVTNTTGDLGDQYNSFLDCEELSADELGNGDV
IIKRDGKLLRPKRLPSNLFQFRAGTGEARCVLDCVTALQNGADLLWIETEKPHIAQIGGM
VSEIRKVIPNAKLVYNNSPSFNWTLNFRQQVYDAMKAAGKDVSAYERTQLMNVEYDQTEL
AKLADEKIRTFQADSSREAGIFHHLITLPTYHTAALSTDNLAKEYFGDQGMLGYVAGVQR
KEIRQGIACVKHQNMSGSDIGDDHKEYFSGEAALKAAGKDNTMNQF
Or try a new SitesBLAST search
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