SitesBLAST
Comparing RR42_RS12200 FitnessBrowser__Cup4G11:RR42_RS12200 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)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
72% identity, 99% coverage: 1:424/430 of query aligns to 1:423/423 of 6lrtA
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
72% identity, 97% coverage: 7:424/430 of query aligns to 9:426/426 of 6xppA
- active site: Y88 (= Y86), D107 (= D105), D152 (= D149), E154 (= E151), H179 (= H176), E181 (= E178), C190 (= C187), H192 (= H189), R227 (= R224), E284 (= E281), Q307 (≠ K304), S314 (= S311), S316 (= S313)
- binding 2-methylidenebutanedioic acid: W92 (= W90), C190 (= C187), H192 (= H189), R227 (= R224), N312 (= N309), S314 (= S311), S316 (= S313), T346 (= T343)
- binding magnesium ion: A275 (= A272), A278 (= A275), Q307 (≠ K304)
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
70% identity, 97% coverage: 10:424/430 of query aligns to 8:417/417 of 7cmyC
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
72% identity, 97% coverage: 7:424/430 of query aligns to 10:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y86), S91 (= S88), W93 (= W90), D153 (= D149), R228 (= R224), T347 (= T343)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C187), G192 (= G188), H193 (= H189), R228 (= R224), S315 (= S311), S317 (= S313), T347 (= T343)
- binding magnesium ion: A276 (= A272), A279 (= A275), Q308 (≠ K304)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
72% identity, 97% coverage: 7:424/430 of query aligns to 10:427/427 of 6wsiA
- active site: Y89 (= Y86), D108 (= D105), D153 (= D149), E155 (= E151), H180 (= H176), E182 (= E178), C191 (= C187), H193 (= H189), R228 (= R224), E285 (= E281), Q308 (≠ K304), S315 (= S311), S317 (= S313)
- binding magnesium ion: A276 (= A272), A279 (= A275), Q308 (≠ K304)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C187), G192 (= G188), H193 (= H189), R228 (= R224), E285 (= E281), N313 (= N309), S315 (= S311), S317 (= S313), T347 (= T343)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
72% identity, 97% coverage: 7:424/430 of query aligns to 10:427/427 of 6vb9A
- active site: Y89 (= Y86), D108 (= D105), D153 (= D149), E155 (= E151), H180 (= H176), E182 (= E178), C191 (= C187), H193 (= H189), R228 (= R224), E285 (= E281), Q308 (≠ K304), S315 (= S311), S317 (= S313)
- binding magnesium ion: A276 (= A272), A279 (= A275), Q308 (≠ K304)
- binding oxalic acid: Y89 (= Y86), S91 (= S88), G92 (= G89), W93 (= W90), D153 (= D149), C191 (= C187), R228 (= R224), W283 (= W279), T347 (= T343)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
72% identity, 97% coverage: 7:424/430 of query aligns to 10:427/427 of 5dqlA
- active site: Y89 (= Y86), D108 (= D105), D153 (= D149), E155 (= E151), H180 (= H176), E182 (= E178), C191 (= C187), H193 (= H189), R228 (= R224), E285 (= E281), Q308 (≠ K304), S315 (= S311), S317 (= S313)
- binding magnesium ion: A276 (= A272), A279 (= A275), Q308 (≠ K304)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W90), D108 (= D105), C191 (= C187), H193 (= H189), S315 (= S311), S317 (= S313), T347 (= T343), L348 (= L344)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
72% identity, 97% coverage: 7:424/430 of query aligns to 11:428/428 of 6c4aA
- active site: Y90 (= Y86), D109 (= D105), D154 (= D149), E156 (= E151), H181 (= H176), E183 (= E178), C192 (= C187), H194 (= H189), R229 (= R224), E286 (= E281), Q309 (≠ K304), S316 (= S311), S318 (= S313)
- binding 3-nitropropanoic acid: Y357 (= Y352), S358 (= S353), R380 (≠ N375)
- binding magnesium ion: A277 (= A272), A280 (= A275), Q309 (≠ K304)
- binding pyruvic acid: Y90 (= Y86), S92 (= S88), G93 (= G89), W94 (= W90), D154 (= D149), C192 (= C187), R229 (= R224), W284 (= W279), T348 (= T343)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
72% identity, 97% coverage: 7:424/430 of query aligns to 10:427/428 of P9WKK7
- SGW 91:93 (= SGW 88:90) binding
- D153 (= D149) binding
- C191 (= C187) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 188:189) binding
- R228 (= R224) binding
- NCSPS 313:317 (= NCSPS 309:313) binding
- K334 (= K330) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T343) binding
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
72% identity, 97% coverage: 7:424/430 of query aligns to 10:427/427 of 1f8iA
- active site: Y89 (= Y86), D108 (= D105), D153 (= D149), E155 (= E151), H180 (= H176), E182 (= E178), S191 (≠ C187), H193 (= H189), R228 (= R224), E285 (= E281), Q308 (≠ K304), S315 (= S311), S317 (= S313)
- binding glyoxylic acid: Y89 (= Y86), S91 (= S88), W93 (= W90), D153 (= D149), T347 (= T343)
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
69% identity, 98% coverage: 2:424/430 of query aligns to 3:434/434 of P0A9G6
- SGW 91:93 (= SGW 88:90) binding
- D157 (= D149) binding
- C195 (= C187) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A211) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R224) 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)
70% identity, 94% coverage: 19:424/430 of query aligns to 14:423/425 of 7rbxC
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
69% identity, 94% coverage: 2:407/430 of query aligns to 2:416/416 of 1igwC
- active site: Y88 (= Y86), D107 (= D105), D156 (= D149), E158 (= E151), H183 (= H176), E185 (= E178), C194 (= C187), R231 (= R224), E288 (= E281), K311 (= K304), S318 (= S311), S320 (= S313)
- binding pyruvic acid: S90 (= S88), G91 (= G89), W92 (= W90), D156 (= D149), R231 (= R224), T350 (= T343)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
65% identity, 94% coverage: 2:407/430 of query aligns to 2:396/396 of 1igwA
- active site: Y88 (= Y86), D107 (= D105), D156 (= D149), E158 (= E151), H183 (= H176), E185 (= E178), C194 (= C187), R227 (= R224), E284 (= E281), K307 (= K304)
- binding pyruvic acid: S90 (= S88), W92 (= W90), D156 (= D149), R227 (= R224), T330 (= T343)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
36% identity, 92% coverage: 12:405/430 of query aligns to 23:452/453 of 5e9fD
- active site: Y99 (= Y86), D118 (= D105), D172 (= D149), D174 (≠ E151), H199 (= H176), E201 (= E178), R240 (= R224), E330 (= E281), Q353 (≠ K304), S360 (= S311), S362 (= S313)
- binding magnesium ion: D118 (= D105), D172 (= D149)
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
40% identity, 56% coverage: 12:253/430 of query aligns to 23:276/544 of 7ebeA
- active site: Y99 (= Y86), D118 (= D105), D172 (= D149), D174 (≠ E151), H199 (= H176), E201 (= E178), C210 (= C187), H212 (= H189), R247 (= R224)
- binding magnesium ion: G102 (= G89), W103 (= W90), D172 (= D149)
Sites not aligning to the query:
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 55% coverage: 12:247/430 of query aligns to 24:271/486 of 5e9gD
- active site: Y100 (= Y86), D119 (= D105), D173 (= D149), D175 (≠ E151), H200 (= H176), E202 (= E178), C211 (= C187), H213 (= H189), R248 (= R224)
- binding glyoxylic acid: Y100 (= Y86), S102 (= S88), G103 (= G89), W104 (= W90), D173 (= D149), H200 (= H176), R248 (= R224)
- binding glycerol: C211 (= C187), G212 (= G188), H213 (= H189), R248 (= R224)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 55% coverage: 12:247/430 of query aligns to 24:271/525 of 5e9gB
- active site: Y100 (= Y86), D119 (= D105), D173 (= D149), D175 (≠ E151), H200 (= H176), E202 (= E178), C211 (= C187), H213 (= H189), R248 (= R224)
- binding glyoxylic acid: Y100 (= Y86), S102 (= S88), G103 (= G89), W104 (= W90), D173 (= D149)
- binding glycerol: C211 (= C187), G212 (= G188), H213 (= H189), R248 (= R224)
Sites not aligning to the query:
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
39% identity, 55% coverage: 12:247/430 of query aligns to 24:271/499 of 5e9gC
- active site: Y100 (= Y86), D119 (= D105), D173 (= D149), D175 (≠ E151), H200 (= H176), E202 (= E178), C211 (= C187), H213 (= H189), R248 (= R224)
- binding glyoxylic acid: Y100 (= Y86), S102 (= S88), W104 (= W90), R248 (= R224)
Sites not aligning to the query:
6edwB Crystal structure of mycobacterium tuberculosis icl2 in the apo form (see paper)
37% identity, 55% coverage: 11:247/430 of query aligns to 15:264/746 of 6edwB
Sites not aligning to the query:
Query Sequence
>RR42_RS12200 FitnessBrowser__Cup4G11:RR42_RS12200
MSRETEARNLQKEWDTNPRWKGVARHYTADDVVRLRGSVQIEHTLARRGAEKLWHLLNTE
PFVNTLGALTGNQAMQQVKAGLKAIYLSGWQVAGDANLAGEMYPDQSLYPANSVPQVVRR
INNTFQRADQIQWSEGKGDTDFFAPIVADAEAGFGGVLNAFELMKSMIDAGAAGVHFEDQ
LASVKKCGHMGGKVLVPTREAVAKLTAARLAADVSGVPTLVIARTDAEAADLLTSDVDER
DRPFCTGERTVEGFYRVKPGIEQSISRALAYAEVADLVWCETGKPDLEFAKKFAEAVHAK
FPGKMLAYNCSPSFNWKKNLDDATIAKFQKELGAMGYKFQFITLAGFHSLNYSMFNLAYG
YARNHMSAFVELQENEFTAAEKGFTAVKHQREVGTGYFDAVTQTIEGGQSSTTALKGSTE
DEQFFDKKVA
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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