SitesBLAST
Comparing CCNA_01841 FitnessBrowser__Caulo:CCNA_01841 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6g1oA Structure of pseudomonas aeruginosa isocitrate lyase, icl (see paper)
60% identity, 85% coverage: 34:492/539 of query aligns to 32:486/486 of 6g1oA
- active site: D184 (= D186), Q211 (= Q213), C222 (= C224), H224 (= H226), R260 (= R262), S382 (= S386), S384 (= S388)
- binding calcium ion: D184 (= D186), D186 (= D188)
- binding glyoxylic acid: D117 (= D119), D186 (= D188), E213 (= E215), S217 (= S219)
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
28% identity, 91% coverage: 30:520/539 of query aligns to 28:400/417 of 7cmyC
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
30% identity, 80% coverage: 87:518/539 of query aligns to 76:408/426 of 6xppA
- active site: Y88 (= Y101), D107 (= D119), D152 (= D186), E154 (≠ D188), H179 (≠ Q213), E181 (= E215), C190 (= C224), H192 (= H226), R227 (= R262), E284 (= E356), Q307 (≠ A379), S314 (= S386), S316 (= S388)
- binding 2-methylidenebutanedioic acid: W92 (= W105), C190 (= C224), H192 (= H226), R227 (= R262), N312 (= N384), S314 (= S386), S316 (= S388), T346 (= T457)
- binding magnesium ion: A275 (≠ G349), A278 (= A350), Q307 (≠ A379)
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
30% identity, 80% coverage: 87:518/539 of query aligns to 77:409/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y101), S91 (= S103), W93 (= W105), D153 (= D186), R228 (= R262), T347 (= T457)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C224), G192 (= G225), H193 (= H226), R228 (= R262), S315 (= S386), S317 (= S388), T347 (= T457)
- binding magnesium ion: A276 (≠ G349), A279 (= A350), Q308 (≠ A379)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
30% identity, 80% coverage: 87:518/539 of query aligns to 77:409/427 of 6wsiA
- active site: Y89 (= Y101), D108 (= D119), D153 (= D186), E155 (≠ D188), H180 (≠ Q213), E182 (= E215), C191 (= C224), H193 (= H226), R228 (= R262), E285 (= E356), Q308 (≠ A379), S315 (= S386), S317 (= S388)
- binding magnesium ion: A276 (≠ G349), A279 (= A350), Q308 (≠ A379)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C224), G192 (= G225), H193 (= H226), R228 (= R262), E285 (= E356), N313 (= N384), S315 (= S386), S317 (= S388), T347 (= T457)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
30% identity, 80% coverage: 87:518/539 of query aligns to 77:409/427 of 6vb9A
- active site: Y89 (= Y101), D108 (= D119), D153 (= D186), E155 (≠ D188), H180 (≠ Q213), E182 (= E215), C191 (= C224), H193 (= H226), R228 (= R262), E285 (= E356), Q308 (≠ A379), S315 (= S386), S317 (= S388)
- binding magnesium ion: A276 (≠ G349), A279 (= A350), Q308 (≠ A379)
- binding oxalic acid: Y89 (= Y101), S91 (= S103), G92 (= G104), W93 (= W105), D153 (= D186), C191 (= C224), R228 (= R262), W283 (= W354), T347 (= T457)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
30% identity, 80% coverage: 87:518/539 of query aligns to 77:409/427 of 5dqlA
- active site: Y89 (= Y101), D108 (= D119), D153 (= D186), E155 (≠ D188), H180 (≠ Q213), E182 (= E215), C191 (= C224), H193 (= H226), R228 (= R262), E285 (= E356), Q308 (≠ A379), S315 (= S386), S317 (= S388)
- binding magnesium ion: A276 (≠ G349), A279 (= A350), Q308 (≠ A379)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W105), D108 (= D119), C191 (= C224), H193 (= H226), S315 (= S386), S317 (= S388), T347 (= T457), L348 (= L458)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
30% identity, 80% coverage: 87:518/539 of query aligns to 78:410/428 of 6c4aA
- active site: Y90 (= Y101), D109 (= D119), D154 (= D186), E156 (≠ D188), H181 (≠ Q213), E183 (= E215), C192 (= C224), H194 (= H226), R229 (= R262), E286 (= E356), Q309 (≠ A379), S316 (= S386), S318 (= S388)
- binding 3-nitropropanoic acid: Y357 (≠ K466), S358 (= S467), R380 (= R490)
- binding magnesium ion: A277 (≠ G349), A280 (= A350), Q309 (≠ A379)
- binding pyruvic acid: Y90 (= Y101), S92 (= S103), G93 (= G104), W94 (= W105), D154 (= D186), C192 (= C224), R229 (= R262), W284 (= W354), T348 (= T457)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
30% identity, 80% coverage: 87:518/539 of query aligns to 77:409/428 of P9WKK7
- SGW 91:93 (= SGW 103:105) binding
- D153 (= D186) binding
- C191 (= C224) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 225:226) binding
- R228 (= R262) binding
- NCSPS 313:317 (≠ NNSPS 384:388) binding
- K334 (≠ V443) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T457) binding
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
30% identity, 80% coverage: 87:518/539 of query aligns to 77:409/427 of 1f8iA
- active site: Y89 (= Y101), D108 (= D119), D153 (= D186), E155 (≠ D188), H180 (≠ Q213), E182 (= E215), S191 (≠ C224), H193 (= H226), R228 (= R262), E285 (= E356), Q308 (≠ A379), S315 (= S386), S317 (= S388)
- binding glyoxylic acid: Y89 (= Y101), S91 (= S103), W93 (= W105), D153 (= D186), T347 (= T457)
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 90% coverage: 35:520/539 of query aligns to 33:417/434 of P0A9G6
- SGW 91:93 (= SGW 103:105) binding
- D157 (= D186) binding
- C195 (= C224) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A248) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R262) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
28% identity, 84% coverage: 69:520/539 of query aligns to 57:406/425 of 7rbxC
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
29% identity, 90% coverage: 35:520/539 of query aligns to 32:416/416 of 1igwC
- active site: Y88 (= Y101), D107 (= D119), D156 (= D186), E158 (≠ D188), H183 (≠ Q213), E185 (= E215), C194 (= C224), R231 (= R262), E288 (= E356), K311 (≠ A379), S318 (= S386), S320 (= S388)
- binding pyruvic acid: S90 (= S103), G91 (= G104), W92 (= W105), D156 (= D186), R231 (= R262), T350 (= T457)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
27% identity, 84% coverage: 66:520/539 of query aligns to 58:406/423 of 6lrtA
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
27% identity, 85% coverage: 64:520/539 of query aligns to 75:486/486 of 5e9gD
- active site: Y100 (= Y101), D119 (= D119), D173 (= D186), D175 (= D188), H200 (≠ Q213), E202 (= E215), C211 (= C224), H213 (= H226), R248 (= R262), E363 (= E356), Q386 (≠ A379), S393 (= S386), S395 (= S388)
- binding glyoxylic acid: Y100 (= Y101), S102 (= S103), G103 (= G104), W104 (= W105), D173 (= D186), H200 (≠ Q213), R248 (= R262), T424 (= T457)
- binding glycerol: C211 (= C224), G212 (= G225), H213 (= H226), R248 (= R262)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
27% identity, 90% coverage: 35:520/539 of query aligns to 32:396/396 of 1igwA
- active site: Y88 (= Y101), D107 (= D119), D156 (= D186), E158 (≠ D188), H183 (≠ Q213), E185 (= E215), C194 (= C224), R227 (= R262), E284 (= E356), K307 (≠ A379)
- binding pyruvic acid: S90 (= S103), W92 (= W105), D156 (= D186), R227 (= R262), T330 (= T457)
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
27% identity, 84% coverage: 64:518/539 of query aligns to 75:499/499 of 5e9gC
- active site: Y100 (= Y101), D119 (= D119), D173 (= D186), D175 (= D188), H200 (≠ Q213), E202 (= E215), C211 (= C224), H213 (= H226), R248 (= R262), E377 (= E356), Q400 (≠ A379), S407 (= S386), S409 (= S388)
- binding glyoxylic acid: Y100 (= Y101), S102 (= S103), W104 (= W105), R248 (= R262)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
27% identity, 84% coverage: 64:518/539 of query aligns to 74:452/453 of 5e9fD
- active site: Y99 (= Y101), D118 (= D119), D172 (= D186), D174 (= D188), H199 (≠ Q213), E201 (= E215), R240 (= R262), E330 (= E356), Q353 (≠ A379), S360 (= S386), S362 (= S388)
- binding magnesium ion: D118 (= D119), D172 (= D186)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
30% identity, 35% coverage: 350:536/539 of query aligns to 396:543/544 of 7ebeA
Sites not aligning to the query:
- active site: 99, 118, 172, 174, 199, 201, 210, 212, 247
- binding magnesium ion: 102, 103, 172
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)
31% identity, 32% coverage: 100:270/539 of query aligns to 103:262/557 of P28240
- K216 (≠ Q223) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (≠ Q227) 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.
Query Sequence
>CCNA_01841 FitnessBrowser__Caulo:CCNA_01841
MTQRKTYAEHRDALLARYPQGVTPGGVDVDDIIQLKLQNTFNTHLDIARAMAPVMRADMA
EYDRDSSKFTQSLGCWSGFHAQQMIKAVKRLRGTTKGAYVYLSGWMVAGLRNRFGHLPDQ
SMHEKTSVVDLIEEIYVSLRQADEVAINDLFKALSAARKAGDQIAEQAAIKAIDNFETHV
VPIIADIDAGFGNEHATYLLAKEMIKAGACCLQIENQVSDAKQCGHQDGKVTVPREDFIE
KLRACRLAFEELGVDDGVIVARTDSLGAGLTQKIPVSQEPGDLASDYIKWLKTEPVTPEN
PLKDGELAIMKDGAFVKPVRMPNGLFAFQDGTGRQRVIEDCIANLTQGGADLLWIETDTP
NVDEIASMVAEVRRVVPNAKLTYNNSPSFNWTLNLRKQVRDQWIAEGKIHKDSYPDGNAL
MSAEYDKSDLGREADERLARFQVDIAARAGVFHNLITLPTFHLTAKSVDELSRGYFGEDR
MQAYVNTVQREEIRRGVSAVKHQHEVGSDLGDTFKEMVAGERALKAGGHANTMNQFAAE
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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