SitesBLAST
Comparing WP_043461725.1 NCBI__GCF_000430725.1:WP_043461725.1 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)
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
73% identity, 99% coverage: 5:437/438 of query aligns to 3:434/434 of P0A9G6
- SGW 91:93 (= SGW 94:96) binding substrate
- D157 (= D160) binding Mg(2+)
- C195 (= C198) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A222) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R235) 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)
72% identity, 95% coverage: 5:420/438 of query aligns to 2:416/416 of 1igwC
- active site: Y88 (= Y92), D107 (= D111), D156 (= D160), E158 (= E162), H183 (= H187), E185 (= E189), C194 (= C198), R231 (= R235), E288 (= E292), K311 (= K315), S318 (= S322), S320 (= S324)
- binding pyruvic acid: S90 (= S94), G91 (= G95), W92 (= W96), D156 (= D160), R231 (= R235), T350 (= T354)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
68% identity, 95% coverage: 5:420/438 of query aligns to 2:396/396 of 1igwA
- active site: Y88 (= Y92), D107 (= D111), D156 (= D160), E158 (= E162), H183 (= H187), E185 (= E189), C194 (= C198), R227 (= R235), E284 (= E292), K307 (= K315)
- binding pyruvic acid: S90 (= S94), W92 (= W96), D156 (= D160), R227 (= R235), T330 (= T354)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
61% identity, 99% coverage: 4:437/438 of query aligns to 1:423/423 of 6lrtA
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
60% identity, 99% coverage: 6:437/438 of query aligns to 1:417/417 of 7cmyC
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
57% identity, 100% coverage: 1:438/438 of query aligns to 1:428/428 of P9WKK7
- SGW 91:93 (= SGW 94:96) binding substrate
- D153 (= D160) binding Mg(2+)
- C191 (= C198) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 199:200) binding substrate
- R228 (= R235) binding substrate
- NCSPS 313:317 (= NCSPS 320:324) binding substrate
- K334 (≠ E341) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T354) binding substrate
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
57% identity, 100% coverage: 1:437/438 of query aligns to 1:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y92), S91 (= S94), W93 (= W96), D153 (= D160), R228 (= R235), T347 (= T354)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C198), G192 (= G199), H193 (= H200), R228 (= R235), S315 (= S322), S317 (= S324), T347 (= T354)
- binding magnesium ion: A276 (= A283), A279 (= A286), Q308 (≠ K315)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
57% identity, 100% coverage: 1:437/438 of query aligns to 1:427/427 of 6wsiA
- active site: Y89 (= Y92), D108 (= D111), D153 (= D160), E155 (= E162), H180 (= H187), E182 (= E189), C191 (= C198), H193 (= H200), R228 (= R235), E285 (= E292), Q308 (≠ K315), S315 (= S322), S317 (= S324)
- binding magnesium ion: A276 (= A283), A279 (= A286), Q308 (≠ K315)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C198), G192 (= G199), H193 (= H200), R228 (= R235), E285 (= E292), N313 (= N320), S315 (= S322), S317 (= S324), T347 (= T354)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
57% identity, 100% coverage: 1:437/438 of query aligns to 1:427/427 of 6vb9A
- active site: Y89 (= Y92), D108 (= D111), D153 (= D160), E155 (= E162), H180 (= H187), E182 (= E189), C191 (= C198), H193 (= H200), R228 (= R235), E285 (= E292), Q308 (≠ K315), S315 (= S322), S317 (= S324)
- binding magnesium ion: A276 (= A283), A279 (= A286), Q308 (≠ K315)
- binding oxalic acid: Y89 (= Y92), S91 (= S94), G92 (= G95), W93 (= W96), D153 (= D160), C191 (= C198), R228 (= R235), W283 (= W290), T347 (= T354)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
57% identity, 100% coverage: 1:437/438 of query aligns to 1:427/427 of 5dqlA
- active site: Y89 (= Y92), D108 (= D111), D153 (= D160), E155 (= E162), H180 (= H187), E182 (= E189), C191 (= C198), H193 (= H200), R228 (= R235), E285 (= E292), Q308 (≠ K315), S315 (= S322), S317 (= S324)
- binding magnesium ion: A276 (= A283), A279 (= A286), Q308 (≠ K315)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W96), D108 (= D111), C191 (= C198), H193 (= H200), S315 (= S322), S317 (= S324), T347 (= T354), L348 (= L355)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
57% identity, 100% coverage: 1:437/438 of query aligns to 2:428/428 of 6c4aA
- active site: Y90 (= Y92), D109 (= D111), D154 (= D160), E156 (= E162), H181 (= H187), E183 (= E189), C192 (= C198), H194 (= H200), R229 (= R235), E286 (= E292), Q309 (≠ K315), S316 (= S322), S318 (= S324)
- binding 3-nitropropanoic acid: Y357 (= Y363), S358 (≠ N364), R380 (≠ P388)
- binding magnesium ion: A277 (= A283), A280 (= A286), Q309 (≠ K315)
- binding pyruvic acid: Y90 (= Y92), S92 (= S94), G93 (= G95), W94 (= W96), D154 (= D160), C192 (= C198), R229 (= R235), W284 (= W290), T348 (= T354)
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
58% identity, 97% coverage: 13:437/438 of query aligns to 12:426/426 of 6xppA
- active site: Y88 (= Y92), D107 (= D111), D152 (= D160), E154 (= E162), H179 (= H187), E181 (= E189), C190 (= C198), H192 (= H200), R227 (= R235), E284 (= E292), Q307 (≠ K315), S314 (= S322), S316 (= S324)
- binding 2-methylidenebutanedioic acid: W92 (= W96), C190 (= C198), H192 (= H200), R227 (= R235), N312 (= N320), S314 (= S322), S316 (= S324), T346 (= T354)
- binding magnesium ion: A275 (= A283), A278 (= A286), Q307 (≠ K315)
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
58% identity, 97% coverage: 13:437/438 of query aligns to 13:427/427 of 1f8iA
- active site: Y89 (= Y92), D108 (= D111), D153 (= D160), E155 (= E162), H180 (= H187), E182 (= E189), S191 (≠ C198), H193 (= H200), R228 (= R235), E285 (= E292), Q308 (≠ K315), S315 (= S322), S317 (= S324)
- binding glyoxylic acid: Y89 (= Y92), S91 (= S94), W93 (= W96), D153 (= D160), T347 (= T354)
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
58% identity, 95% coverage: 22:437/438 of query aligns to 14:423/425 of 7rbxC
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 92% coverage: 15:418/438 of query aligns to 23:452/453 of 5e9fD
- active site: Y99 (= Y92), D118 (= D111), D172 (= D160), D174 (≠ E162), H199 (= H187), E201 (= E189), R240 (= R235), E330 (= E292), Q353 (≠ K315), S360 (= S322), S362 (= S324)
- binding magnesium ion: D118 (= D111), D172 (= D160)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
38% identity, 59% coverage: 7:264/438 of query aligns to 16:276/544 of 7ebeA
- active site: Y99 (= Y92), D118 (= D111), D172 (= D160), D174 (≠ E162), H199 (= H187), E201 (= E189), C210 (= C198), H212 (= H200), R247 (= R235)
- binding magnesium ion: G102 (= G95), W103 (= W96), D172 (= D160)
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, 64% coverage: 11:291/438 of query aligns to 24:311/557 of P28240
- T53 (≠ S41) mutation to A: Abolishes short-term enzyme inactivation by glucose addition.
- K216 (= K197) mutation to R: Reduces activity by 45%; when associated with L-220.
- M220 (= M201) mutation to L: Reduces activity by 45%; when associated with R-216.
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 56% coverage: 15:258/438 of query aligns to 24:271/525 of 5e9gB
- active site: Y100 (= Y92), D119 (= D111), D173 (= D160), D175 (≠ E162), H200 (= H187), E202 (= E189), C211 (= C198), H213 (= H200), R248 (= R235)
- binding glyoxylic acid: Y100 (= Y92), S102 (= S94), G103 (= G95), W104 (= W96), D173 (= D160)
- binding glycerol: C211 (= C198), G212 (= G199), H213 (= H200), R248 (= R235)
Sites not aligning to the query:
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 56% coverage: 15:258/438 of query aligns to 24:271/499 of 5e9gC
- active site: Y100 (= Y92), D119 (= D111), D173 (= D160), D175 (≠ E162), H200 (= H187), E202 (= E189), C211 (= C198), H213 (= H200), R248 (= R235)
- binding glyoxylic acid: Y100 (= Y92), S102 (= S94), W104 (= W96), R248 (= R235)
Sites not aligning to the query:
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 56% coverage: 15:258/438 of query aligns to 24:271/486 of 5e9gD
- active site: Y100 (= Y92), D119 (= D111), D173 (= D160), D175 (≠ E162), H200 (= H187), E202 (= E189), C211 (= C198), H213 (= H200), R248 (= R235)
- binding glyoxylic acid: Y100 (= Y92), S102 (= S94), G103 (= G95), W104 (= W96), D173 (= D160), H200 (= H187), R248 (= R235)
- binding glycerol: C211 (= C198), G212 (= G199), H213 (= H200), R248 (= R235)
Sites not aligning to the query:
Query Sequence
>WP_043461725.1 NCBI__GCF_000430725.1:WP_043461725.1
MSQLTREQQIAALEKDWAENPRWKLVKRGYSAADVVRLRGSLQPEYTLAQRGAEKLWEKV
NGGAKKGYVNAFGAITAGQAMQQAKAGLEAVYLSGWQVAADGNTSETMYPDQSLYAYDSV
PTMVRRINNTFKRADEIQWSRGINPGDEGFVDYFLPIVADAEAGFGGVLNAFELMKNMIA
AGAAGVHFEDQLAAVKKCGHMGGKVLVPTREAVEKLIAARFAADVMGVPTIVLARTDAEA
ANLLTSDCDDNDKPFVTGERTQEGFYRVKNGLEQAISRGVAYAPYADLVWCETGVPDIGF
AREFAQAVHAACPGKLLSYNCSPSFNWRKNLDDKQIAAFQEELSALGYKYQFITLAGIHI
NWYNTFQFAHAYARGEGMKHYVNMVQEPEFQAREQGYTFVSHQQEVGAGYFDDVTTVIQG
GSSSVKALTGSTEEEQFH
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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