SitesBLAST
Comparing WP_012383064.1 NCBI__GCF_000019845.1:WP_012383064.1 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)
78% identity, 91% coverage: 2:485/530 of query aligns to 3:486/486 of 6g1oA
- active site: D184 (= D183), Q211 (= Q210), C222 (= C221), H224 (= H223), R260 (= R259), S382 (= S381), S384 (= S383)
- binding calcium ion: D184 (= D183), D186 (= D185)
- binding glyoxylic acid: D117 (= D116), D186 (= D185), E213 (= E212), S217 (= S216)
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 88% coverage: 21:486/530 of query aligns to 20:387/434 of P0A9G6
- SGW 91:93 (= SGW 100:102) binding substrate
- D157 (= D183) binding Mg(2+)
- C195 (= C221) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A245) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R259) binding substrate
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)
28% identity, 88% coverage: 21:486/530 of query aligns to 19:386/416 of 1igwC
- active site: Y88 (= Y98), D107 (= D116), D156 (= D183), E158 (≠ D185), H183 (≠ Q210), E185 (= E212), C194 (= C221), R231 (= R259), E288 (= E351), K311 (≠ A374), S318 (= S381), S320 (= S383)
- binding pyruvic acid: S90 (= S100), G91 (= G101), W92 (= W102), D156 (= D183), R231 (= R259), T350 (= T450)
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
29% identity, 69% coverage: 21:386/530 of query aligns to 18:314/417 of 7cmyC
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
25% identity, 94% coverage: 14:513/530 of query aligns to 7:406/423 of 6lrtA
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
29% identity, 72% coverage: 8:390/530 of query aligns to 1:319/425 of 7rbxC
Sites not aligning to the query:
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
27% identity, 83% coverage: 74:513/530 of query aligns to 81:486/486 of 5e9gD
- active site: Y100 (= Y98), D119 (= D116), D173 (= D183), D175 (= D185), H200 (≠ Q210), E202 (= E212), C211 (= C221), H213 (= H223), R248 (= R259), E363 (= E351), Q386 (≠ A374), S393 (= S381), S395 (= S383)
- binding glyoxylic acid: Y100 (= Y98), S102 (= S100), G103 (= G101), W104 (= W102), D173 (= D183), H200 (≠ Q210), R248 (= R259), T424 (= T450)
- binding glycerol: C211 (= C221), G212 (= G222), H213 (= H223), R248 (= R259)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
25% identity, 81% coverage: 97:525/530 of query aligns to 98:531/544 of 7ebeA
- active site: Y99 (= Y98), D118 (= D116), D172 (= D183), D174 (= D185), H199 (≠ Q210), E201 (= E212), C210 (= C221), H212 (= H223), R247 (= R259), E402 (= E351), Q425 (≠ A374), S432 (= S381), S434 (= S383)
- binding magnesium ion: G102 (= G101), W103 (= W102), D172 (= D183)
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
27% identity, 82% coverage: 74:506/530 of query aligns to 81:494/499 of 5e9gC
- active site: Y100 (= Y98), D119 (= D116), D173 (= D183), D175 (= D185), H200 (≠ Q210), E202 (= E212), C211 (= C221), H213 (= H223), R248 (= R259), E377 (= E351), Q400 (≠ A374), S407 (= S381), S409 (= S383)
- binding glyoxylic acid: Y100 (= Y98), S102 (= S100), W104 (= W102), R248 (= R259)
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
29% identity, 55% coverage: 95:386/530 of query aligns to 85:319/426 of 6xppA
- active site: Y88 (= Y98), D107 (= D116), D152 (= D183), E154 (≠ D185), H179 (≠ Q210), E181 (= E212), C190 (= C221), H192 (= H223), R227 (= R259), E284 (= E351), Q307 (≠ A374), S314 (= S381), S316 (= S383)
- binding 2-methylidenebutanedioic acid: W92 (= W102), C190 (= C221), H192 (= H223), R227 (= R259), N312 (= N379), S314 (= S381), S316 (= S383)
- binding magnesium ion: A275 (≠ Q342), A278 (= A345), Q307 (≠ A374)
Sites not aligning to the query:
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
29% identity, 55% coverage: 95:386/530 of query aligns to 87:321/428 of 6c4aA
- active site: Y90 (= Y98), D109 (= D116), D154 (= D183), E156 (≠ D185), H181 (≠ Q210), E183 (= E212), C192 (= C221), H194 (= H223), R229 (= R259), E286 (= E351), Q309 (≠ A374), S316 (= S381), S318 (= S383)
- binding magnesium ion: A277 (≠ Q342), A280 (= A345), Q309 (≠ A374)
- binding pyruvic acid: Y90 (= Y98), S92 (= S100), G93 (= G101), W94 (= W102), D154 (= D183), C192 (= C221), R229 (= R259), W284 (= W349)
Sites not aligning to the query:
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 55% coverage: 95:386/530 of query aligns to 86:320/428 of P9WKK7
- SGW 91:93 (= SGW 100:102) binding substrate
- D153 (= D183) binding Mg(2+)
- C191 (= C221) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 222:223) binding substrate
- R228 (= R259) binding substrate
- NCSPS 313:317 (≠ NNSPS 379:383) binding substrate
Sites not aligning to the query:
- 334 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- 347 binding substrate
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
29% identity, 55% coverage: 95:386/530 of query aligns to 86:320/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y98), S91 (= S100), W93 (= W102), D153 (= D183), R228 (= R259)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C221), G192 (= G222), H193 (= H223), R228 (= R259), S315 (= S381), S317 (= S383)
- binding magnesium ion: A276 (≠ Q342), A279 (= A345), Q308 (≠ A374)
Sites not aligning to the query:
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
29% identity, 55% coverage: 95:386/530 of query aligns to 86:320/427 of 6wsiA
- active site: Y89 (= Y98), D108 (= D116), D153 (= D183), E155 (≠ D185), H180 (≠ Q210), E182 (= E212), C191 (= C221), H193 (= H223), R228 (= R259), 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 (= C221), G192 (= G222), H193 (= H223), R228 (= R259), E285 (= E351), N313 (= N379), S315 (= S381), S317 (= S383)
Sites not aligning to the query:
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
29% identity, 55% coverage: 95:386/530 of query aligns to 86:320/427 of 6vb9A
- active site: Y89 (= Y98), D108 (= D116), D153 (= D183), E155 (≠ D185), H180 (≠ Q210), E182 (= E212), C191 (= C221), H193 (= H223), R228 (= R259), E285 (= E351), Q308 (≠ A374), S315 (= S381), S317 (= S383)
- binding magnesium ion: A276 (≠ Q342), A279 (= A345), Q308 (≠ A374)
- binding oxalic acid: Y89 (= Y98), S91 (= S100), G92 (= G101), W93 (= W102), D153 (= D183), C191 (= C221), R228 (= R259), W283 (= W349)
Sites not aligning to the query:
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
29% identity, 55% coverage: 95:386/530 of query aligns to 86:320/427 of 5dqlA
- active site: Y89 (= Y98), D108 (= D116), D153 (= D183), E155 (≠ D185), H180 (≠ Q210), E182 (= E212), C191 (= C221), H193 (= H223), R228 (= R259), E285 (= E351), Q308 (≠ A374), S315 (= S381), S317 (= S383)
- binding magnesium ion: A276 (≠ Q342), A279 (= A345), Q308 (≠ A374)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W102), D108 (= D116), C191 (= C221), H193 (= H223), S315 (= S381), S317 (= S383)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
24% identity, 83% coverage: 74:513/530 of query aligns to 81:525/525 of 5e9gB
- active site: Y100 (= Y98), D119 (= D116), D173 (= D183), D175 (= D185), H200 (≠ Q210), E202 (= E212), C211 (= C221), H213 (= H223), R248 (= R259), E401 (= E351), Q424 (≠ A374), S431 (= S381), S433 (= S383)
- binding glyoxylic acid: Y100 (= Y98), S102 (= S100), G103 (= G101), W104 (= W102), D173 (= D183), T463 (= T450)
- binding glycerol: C211 (= C221), G212 (= G222), H213 (= H223), R248 (= R259), E401 (= E351), N429 (= N379), T463 (= T450)
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
29% identity, 55% coverage: 95:386/530 of query aligns to 86:320/427 of 1f8iA
- active site: Y89 (= Y98), D108 (= D116), D153 (= D183), E155 (≠ D185), H180 (≠ Q210), E182 (= E212), S191 (≠ C221), H193 (= H223), R228 (= R259), E285 (= E351), Q308 (≠ A374), S315 (= S381), S317 (= S383)
- binding glyoxylic acid: Y89 (= Y98), S91 (= S100), W93 (= W102), D153 (= D183)
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)
26% identity, 81% coverage: 97:525/530 of query aligns to 103:538/557 of P28240
- K216 (≠ Q220) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (≠ Q224) 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.
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
26% identity, 82% coverage: 74:506/530 of query aligns to 80:447/453 of 5e9fD
- active site: Y99 (= Y98), D118 (= D116), D172 (= D183), D174 (= D185), H199 (≠ Q210), E201 (= E212), R240 (= R259), E330 (= E351), Q353 (≠ A374), S360 (= S381), S362 (= S383)
- binding magnesium ion: D118 (= D116), D172 (= D183)
Query Sequence
>WP_012383064.1 NCBI__GCF_000019845.1:WP_012383064.1
MSYQDQITEVSQLIKSKNGTWDGINAEAVVRMRLQNRFKTGLDIAKYTAAIMRRDMAAYD
ADTTKYTQSLGCWHGFIGQQKVISIKKHFGTTERRYLYLSGWMVAALRSEFGPLPDQSMH
EKTSVPALIEELYTFLRQADARELNDIFRAIDAARKAGDSAKAKELLTQAENHQTHVIPI
IADIDAGFGNAEATYLLAKKMIEAGAGALQIENQVSDEKQCGHQDGKVTVPHEDFLAKVR
ACRYAFLELGVDDGIVVTRTDSLGAGLTKQIAVSHKPGDLGDQYNSFLDVEEVPAGGGAN
GDVIINRDGKLFRPKRLPSNLFQFRKGTGEDRCVLDSITSLQNGADLLWIETEKPHVEQI
AGMMDRIRAVIPNAKLVYNNSPSFNWTINFRQQVYDAWKEAGKDVSAYDRAGLMDVKYDG
SDLAAEADEKIRTFQADASKRAGIFHHLITLPTYHTAALSTDNLAKEYFGEQGMLGYVLN
VQRQEIRQKIACAKHQNMAGSDIGDDHKEYFAGEAALKAGGADNTMNQFG
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