SitesBLAST
Comparing WP_066920215.1 NCBI__GCF_001579945.1:WP_066920215.1 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)
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
72% identity, 98% coverage: 7:424/428 of query aligns to 8:423/423 of 6lrtA
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
70% identity, 98% coverage: 7:424/428 of query aligns to 6:417/417 of 7cmyC
7rbxC Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from brucella melitensis biovar abortus 2308 bound to itaconic acid (see paper)
70% identity, 95% coverage: 18:424/428 of query aligns to 14:423/425 of 7rbxC
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
67% identity, 98% coverage: 7:424/428 of query aligns to 9:434/434 of P0A9G6
- SGW 91:93 (= SGW 87:89) binding substrate
- D157 (= D148) binding Mg(2+)
- C195 (= C186) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A210) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R223) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
67% identity, 99% coverage: 2:424/428 of query aligns to 5:426/426 of 6xppA
- active site: Y88 (= Y85), D107 (= D104), D152 (= D148), E154 (= E150), H179 (= H175), E181 (= E177), C190 (= C186), H192 (= H188), R227 (= R223), E284 (= E281), Q307 (≠ K304), S314 (= S311), S316 (= S313)
- binding 2-methylidenebutanedioic acid: W92 (= W89), C190 (= C186), H192 (= H188), R227 (= R223), N312 (= N309), S314 (= S311), S316 (= S313), T346 (= T343)
- binding magnesium ion: A275 (= A272), A278 (≠ C275), Q307 (≠ K304)
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
67% identity, 99% coverage: 2:424/428 of query aligns to 6:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y85), S91 (= S87), W93 (= W89), D153 (= D148), R228 (= R223), T347 (= T343)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C186), G192 (= G187), H193 (= H188), R228 (= R223), S315 (= S311), S317 (= S313), T347 (= T343)
- binding magnesium ion: A276 (= A272), A279 (≠ C275), Q308 (≠ K304)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
67% identity, 99% coverage: 2:424/428 of query aligns to 6:427/427 of 6wsiA
- active site: Y89 (= Y85), D108 (= D104), D153 (= D148), E155 (= E150), H180 (= H175), E182 (= E177), C191 (= C186), H193 (= H188), R228 (= R223), E285 (= E281), Q308 (≠ K304), S315 (= S311), S317 (= S313)
- binding magnesium ion: A276 (= A272), A279 (≠ C275), Q308 (≠ K304)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C186), G192 (= G187), H193 (= H188), R228 (= R223), 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)
67% identity, 99% coverage: 2:424/428 of query aligns to 6:427/427 of 6vb9A
- active site: Y89 (= Y85), D108 (= D104), D153 (= D148), E155 (= E150), H180 (= H175), E182 (= E177), C191 (= C186), H193 (= H188), R228 (= R223), E285 (= E281), Q308 (≠ K304), S315 (= S311), S317 (= S313)
- binding magnesium ion: A276 (= A272), A279 (≠ C275), Q308 (≠ K304)
- binding oxalic acid: Y89 (= Y85), S91 (= S87), G92 (= G88), W93 (= W89), D153 (= D148), C191 (= C186), R228 (= R223), W283 (= W279), T347 (= T343)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
67% identity, 99% coverage: 2:424/428 of query aligns to 6:427/427 of 5dqlA
- active site: Y89 (= Y85), D108 (= D104), D153 (= D148), E155 (= E150), H180 (= H175), E182 (= E177), C191 (= C186), H193 (= H188), R228 (= R223), E285 (= E281), Q308 (≠ K304), S315 (= S311), S317 (= S313)
- binding magnesium ion: A276 (= A272), A279 (≠ C275), Q308 (≠ K304)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W89), D108 (= D104), C191 (= C186), H193 (= H188), S315 (= S311), S317 (= S313), T347 (= T343), L348 (= L344)
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
67% identity, 99% coverage: 2:424/428 of query aligns to 7:428/428 of 6c4aA
- active site: Y90 (= Y85), D109 (= D104), D154 (= D148), E156 (= E150), H181 (= H175), E183 (= E177), C192 (= C186), H194 (= H188), R229 (= R223), E286 (= E281), Q309 (≠ K304), S316 (= S311), S318 (= S313)
- binding 3-nitropropanoic acid: Y357 (≠ H352), S358 (= S353), R380 (≠ L375)
- binding magnesium ion: A277 (= A272), A280 (≠ C275), Q309 (≠ K304)
- binding pyruvic acid: Y90 (= Y85), S92 (= S87), G93 (= G88), W94 (= W89), D154 (= D148), C192 (= C186), R229 (= R223), 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)
67% identity, 99% coverage: 2:424/428 of query aligns to 6:427/428 of P9WKK7
- SGW 91:93 (= SGW 87:89) binding substrate
- D153 (= D148) binding Mg(2+)
- C191 (= C186) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 187:188) binding substrate
- R228 (= R223) binding substrate
- NCSPS 313:317 (= NCSPS 309:313) binding substrate
- K334 (≠ R330) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T343) binding substrate
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
67% identity, 99% coverage: 2:424/428 of query aligns to 6:427/427 of 1f8iA
- active site: Y89 (= Y85), D108 (= D104), D153 (= D148), E155 (= E150), H180 (= H175), E182 (= E177), S191 (≠ C186), H193 (= H188), R228 (= R223), E285 (= E281), Q308 (≠ K304), S315 (= S311), S317 (= S313)
- binding glyoxylic acid: Y89 (= Y85), S91 (= S87), W93 (= W89), D153 (= D148), T347 (= T343)
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
67% identity, 93% coverage: 7:405/428 of query aligns to 8:414/416 of 1igwC
- active site: Y88 (= Y85), D107 (= D104), D156 (= D148), E158 (= E150), H183 (= H175), E185 (= E177), C194 (= C186), R231 (= R223), E288 (= E281), K311 (= K304), S318 (= S311), S320 (= S313)
- binding pyruvic acid: S90 (= S87), G91 (= G88), W92 (= W89), D156 (= D148), R231 (= R223), T350 (= T343)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
63% identity, 93% coverage: 7:405/428 of query aligns to 8:394/396 of 1igwA
- active site: Y88 (= Y85), D107 (= D104), D156 (= D148), E158 (= E150), H183 (= H175), E185 (= E177), C194 (= C186), R227 (= R223), E284 (= E281), K307 (= K304)
- binding pyruvic acid: S90 (= S87), W92 (= W89), D156 (= D148), R227 (= R223), T330 (= T343)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 93% coverage: 11:406/428 of query aligns to 23:453/453 of 5e9fD
- active site: Y99 (= Y85), D118 (= D104), D172 (= D148), D174 (≠ E150), H199 (= H175), E201 (= E177), R240 (= R223), E330 (= E281), Q353 (≠ K304), S360 (= S311), S362 (= S313)
- binding magnesium ion: D118 (= D104), D172 (= D148)
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 93% coverage: 11:406/428 of query aligns to 24:485/486 of 5e9gD
- active site: Y100 (= Y85), D119 (= D104), D173 (= D148), D175 (≠ E150), H200 (= H175), E202 (= E177), C211 (= C186), H213 (= H188), R248 (= R223), E363 (= E281), Q386 (≠ K304), S393 (= S311), S395 (= S313)
- binding glyoxylic acid: Y100 (= Y85), S102 (= S87), G103 (= G88), W104 (= W89), D173 (= D148), H200 (= H175), R248 (= R223), T424 (= T343)
- binding glycerol: C211 (= C186), G212 (= G187), H213 (= H188), R248 (= R223)
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
41% identity, 55% coverage: 11:244/428 of query aligns to 24:269/499 of 5e9gC
- active site: Y100 (= Y85), D119 (= D104), D173 (= D148), D175 (≠ E150), H200 (= H175), E202 (= E177), C211 (= C186), H213 (= H188), R248 (= R223)
- binding glyoxylic acid: Y100 (= Y85), S102 (= S87), W104 (= W89), R248 (= R223)
Sites not aligning to the query:
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
41% identity, 55% coverage: 11:244/428 of query aligns to 24:269/525 of 5e9gB
- active site: Y100 (= Y85), D119 (= D104), D173 (= D148), D175 (≠ E150), H200 (= H175), E202 (= E177), C211 (= C186), H213 (= H188), R248 (= R223)
- binding glyoxylic acid: Y100 (= Y85), S102 (= S87), G103 (= G88), W104 (= W89), D173 (= D148)
- binding glycerol: C211 (= C186), G212 (= G187), H213 (= H188), R248 (= R223)
Sites not aligning to the query:
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
40% identity, 55% coverage: 11:244/428 of query aligns to 23:268/544 of 7ebeA
- active site: Y99 (= Y85), D118 (= D104), D172 (= D148), D174 (≠ E150), H199 (= H175), E201 (= E177), C210 (= C186), H212 (= H188), R247 (= R223)
- binding magnesium ion: G102 (= G88), W103 (= W89), D172 (= D148)
Sites not aligning to the query:
5e9hA Structural insights of isocitrate lyases from fusarium graminearum (see paper)
40% identity, 55% coverage: 11:244/428 of query aligns to 18:263/518 of 5e9hA
Sites not aligning to the query:
Query Sequence
>WP_066920215.1 NCBI__GCF_001579945.1:WP_066920215.1
MTQLNAEQLRKEWQNNPRWQGVERPYQAEDVVRLRGSVHIEHSLARLGAEKLWKYVNEKP
FVNALGALTGNQAMQQVKAGLDAIYLSGWQVAGDANLAGEMYPDQSLYPANSVPSVIRRI
NNTLLRADQIHHAEGDRSIDWLKPIVADAEAGFGGVLNAFELMKGMIEAGAAGVHFEDQL
SSAKKCGHMGGKVLVPTSEAVSKLIAARLAADACGVPTVLVARTDAESANLLTTDVDERD
REFISSQERTSEGFFYVRAGLEQAIARGLAYAPYCDLIWCETATPDLREAKRFAEAIHQR
FPGKLLAYNCSPSFNWKKKLDDATIAKFQRELGAMGYKFQFITLAGFHALNHSMFELARG
YKATQMSAYVALQELEFASEKDGYTATKHQREVGAGYFDDVTQTVTAGRSSVTAMKGSTE
EAQFDQRG
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