SitesBLAST
Comparing WP_078430601.1 NCBI__GCF_002019605.1:WP_078430601.1 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)
7cmyC Isocitrate lyase from bacillus cereus atcc 14579 in complex with magnessium ion, glyoxylate, and succinate
81% identity, 98% coverage: 8:427/430 of query aligns to 3:417/417 of 7cmyC
6lrtA Crystal structure of isocitrate lyase (caur_3889) from chloroflexus aurantiacus in complex with isocitrate and manganese ion
77% identity, 97% coverage: 11:427/430 of query aligns to 8:423/423 of 6lrtA
P0A9G6 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Escherichia coli (strain K12) (see 3 papers)
69% identity, 98% coverage: 8:427/430 of query aligns to 6:434/434 of P0A9G6
- SGW 91:93 (= SGW 91:93) binding substrate
- D157 (= D152) binding Mg(2+)
- C195 (= C190) active site, Proton acceptor; mutation to A: Large decrease in activity.; mutation to S: Large decrease in activity.
- A219 (= A214) mutation to C: Isocitrate lyase activity is reduced compared to the wild-type.
- R232 (= R227) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7rb1A Isocitrate lyase-1 from mycobacterium tuberculosis covalently modified by 5-descarboxy-5-nitro-d-isocitric acid (see paper)
68% identity, 99% coverage: 1:427/430 of query aligns to 1:427/427 of 7rb1A
- binding dihydroxyacetic acid: Y89 (= Y89), S91 (= S91), W93 (= W93), D153 (= D152), R228 (= R227), T347 (= T346)
- binding (3E)-3-(hydroxyimino)propanoic acid: C191 (= C190), G192 (= G191), H193 (= H192), R228 (= R227), S315 (= S314), S317 (= S316), T347 (= T346)
- binding magnesium ion: A276 (= A275), A279 (= A278), Q308 (≠ K307)
6wsiA Intact cis-2,3-epoxysuccinic acid bound to isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
68% identity, 99% coverage: 1:427/430 of query aligns to 1:427/427 of 6wsiA
- active site: Y89 (= Y89), D108 (= D108), D153 (= D152), E155 (= E154), H180 (= H179), E182 (= E181), C191 (= C190), H193 (= H192), R228 (= R227), E285 (= E284), Q308 (≠ K307), S315 (= S314), S317 (= S316)
- binding magnesium ion: A276 (= A275), A279 (= A278), Q308 (≠ K307)
- binding (2R,3S)-oxirane-2,3-dicarboxylic acid: C191 (= C190), G192 (= G191), H193 (= H192), R228 (= R227), E285 (= E284), N313 (= N312), S315 (= S314), S317 (= S316), T347 (= T346)
6vb9A Covalent adduct of cis-2,3-epoxysuccinic acid with isocitrate lyase-1 from mycobacterium tuberculosis (see paper)
68% identity, 99% coverage: 1:427/430 of query aligns to 1:427/427 of 6vb9A
- active site: Y89 (= Y89), D108 (= D108), D153 (= D152), E155 (= E154), H180 (= H179), E182 (= E181), C191 (= C190), H193 (= H192), R228 (= R227), E285 (= E284), Q308 (≠ K307), S315 (= S314), S317 (= S316)
- binding magnesium ion: A276 (= A275), A279 (= A278), Q308 (≠ K307)
- binding oxalic acid: Y89 (= Y89), S91 (= S91), G92 (= G92), W93 (= W93), D153 (= D152), C191 (= C190), R228 (= R227), W283 (= W282), T347 (= T346)
5dqlA Crystal structure of 2-vinyl glyoxylate modified isocitrate lyase from mycobacterium tuberculosis (see paper)
68% identity, 99% coverage: 1:427/430 of query aligns to 1:427/427 of 5dqlA
- active site: Y89 (= Y89), D108 (= D108), D153 (= D152), E155 (= E154), H180 (= H179), E182 (= E181), C191 (= C190), H193 (= H192), R228 (= R227), E285 (= E284), Q308 (≠ K307), S315 (= S314), S317 (= S316)
- binding magnesium ion: A276 (= A275), A279 (= A278), Q308 (≠ K307)
- binding 4-hydroxy-2-oxobutanoic acid: W93 (= W93), D108 (= D108), C191 (= C190), H193 (= H192), S315 (= S314), S317 (= S316), T347 (= T346), L348 (= L347)
P9WKK7 Isocitrate lyase; ICL; Isocitrase; Isocitratase; EC 4.1.3.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
68% identity, 100% coverage: 1:428/430 of query aligns to 1:428/428 of P9WKK7
- SGW 91:93 (= SGW 91:93) binding substrate
- D153 (= D152) binding Mg(2+)
- C191 (= C190) mutation to S: Adopts a conformation almost identical to the wild-type.
- GH 192:193 (= GH 191:192) binding substrate
- R228 (= R227) binding substrate
- NCSPS 313:317 (= NCSPS 312:316) binding substrate
- K334 (≠ Q333) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T347 (= T346) binding substrate
6c4aA Crystal structure of 3-nitropropionate modified isocitrate lyase from mycobacterium tuberculosis with pyruvate (see paper)
68% identity, 99% coverage: 1:427/430 of query aligns to 2:428/428 of 6c4aA
- active site: Y90 (= Y89), D109 (= D108), D154 (= D152), E156 (= E154), H181 (= H179), E183 (= E181), C192 (= C190), H194 (= H192), R229 (= R227), E286 (= E284), Q309 (≠ K307), S316 (= S314), S318 (= S316)
- binding 3-nitropropanoic acid: Y357 (= Y355), S358 (= S356), R380 (≠ A378)
- binding magnesium ion: A277 (= A275), A280 (= A278), Q309 (≠ K307)
- binding pyruvic acid: Y90 (= Y89), S92 (= S91), G93 (= G92), W94 (= W93), D154 (= D152), C192 (= C190), R229 (= R227), W284 (= W282), T348 (= T346)
6xppA Crystal structure of itaconate modified mycobaterium tuberculosis isocitrate lyase (see paper)
69% identity, 99% coverage: 4:427/430 of query aligns to 3:426/426 of 6xppA
- active site: Y88 (= Y89), D107 (= D108), D152 (= D152), E154 (= E154), H179 (= H179), E181 (= E181), C190 (= C190), H192 (= H192), R227 (= R227), E284 (= E284), Q307 (≠ K307), S314 (= S314), S316 (= S316)
- binding 2-methylidenebutanedioic acid: W92 (= W93), C190 (= C190), H192 (= H192), R227 (= R227), N312 (= N312), S314 (= S314), S316 (= S316), T346 (= T346)
- binding magnesium ion: A275 (= A275), A278 (= A278), Q307 (≠ K307)
1f8iA Crystal structure of isocitrate lyase:nitropropionate:glyoxylate complex from mycobacterium tuberculosis (see paper)
68% identity, 99% coverage: 4:427/430 of query aligns to 4:427/427 of 1f8iA
- active site: Y89 (= Y89), D108 (= D108), D153 (= D152), E155 (= E154), H180 (= H179), E182 (= E181), S191 (≠ C190), H193 (= H192), R228 (= R227), E285 (= E284), Q308 (≠ K307), S315 (= S314), S317 (= S316)
- binding glyoxylic acid: Y89 (= Y89), S91 (= S91), W93 (= W93), D153 (= D152), T347 (= T346)
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: 22:428/430 of query aligns to 14:424/425 of 7rbxC
1igwC Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
69% identity, 94% coverage: 8:410/430 of query aligns to 5:416/416 of 1igwC
- active site: Y88 (= Y89), D107 (= D108), D156 (= D152), E158 (= E154), H183 (= H179), E185 (= E181), C194 (= C190), R231 (= R227), E288 (= E284), K311 (= K307), S318 (= S314), S320 (= S316)
- binding pyruvic acid: S90 (= S91), G91 (= G92), W92 (= W93), D156 (= D152), R231 (= R227), T350 (= T346)
1igwA Crystal structure of the isocitrate lyase from the a219c mutant of escherichia coli (see paper)
65% identity, 94% coverage: 8:410/430 of query aligns to 5:396/396 of 1igwA
- active site: Y88 (= Y89), D107 (= D108), D156 (= D152), E158 (= E154), H183 (= H179), E185 (= E181), C194 (= C190), R227 (= R227), E284 (= E284), K307 (= K307)
- binding pyruvic acid: S90 (= S91), W92 (= W93), D156 (= D152), R227 (= R227), T330 (= T346)
5e9gD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 92% coverage: 15:410/430 of query aligns to 24:486/486 of 5e9gD
- active site: Y100 (= Y89), D119 (= D108), D173 (= D152), D175 (≠ E154), H200 (= H179), E202 (= E181), C211 (= C190), H213 (= H192), R248 (= R227), E363 (= E284), Q386 (≠ K307), S393 (= S314), S395 (= S316)
- binding glyoxylic acid: Y100 (= Y89), S102 (= S91), G103 (= G92), W104 (= W93), D173 (= D152), H200 (= H179), R248 (= R227), T424 (= T346)
- binding glycerol: C211 (= C190), G212 (= G191), H213 (= H192), R248 (= R227)
5e9fD Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
37% identity, 92% coverage: 15:409/430 of query aligns to 23:453/453 of 5e9fD
- active site: Y99 (= Y89), D118 (= D108), D172 (= D152), D174 (≠ E154), H199 (= H179), E201 (= E181), R240 (= R227), E330 (= E284), Q353 (≠ K307), S360 (= S314), S362 (= S316)
- binding magnesium ion: D118 (= D108), D172 (= D152)
5e9gB Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 56% coverage: 15:254/430 of query aligns to 24:275/525 of 5e9gB
- active site: Y100 (= Y89), D119 (= D108), D173 (= D152), D175 (≠ E154), H200 (= H179), E202 (= E181), C211 (= C190), H213 (= H192), R248 (= R227)
- binding glyoxylic acid: Y100 (= Y89), S102 (= S91), G103 (= G92), W104 (= W93), D173 (= D152)
- binding glycerol: C211 (= C190), G212 (= G191), H213 (= H192), R248 (= R227)
Sites not aligning to the query:
5e9gC Structural insights of isocitrate lyases from magnaporthe oryzae (see paper)
40% identity, 56% coverage: 15:254/430 of query aligns to 24:275/499 of 5e9gC
- active site: Y100 (= Y89), D119 (= D108), D173 (= D152), D175 (≠ E154), H200 (= H179), E202 (= E181), C211 (= C190), H213 (= H192), R248 (= R227)
- binding glyoxylic acid: Y100 (= Y89), S102 (= S91), W104 (= W93), R248 (= R227)
Sites not aligning to the query:
7ebeA Crystal structure of isocitrate lyase-1 from candida albicans (see paper)
37% identity, 59% coverage: 4:256/430 of query aligns to 6:276/544 of 7ebeA
- active site: Y99 (= Y89), D118 (= D108), D172 (= D152), D174 (≠ E154), H199 (= H179), E201 (= E181), C210 (= C190), H212 (= H192), R247 (= R227)
- binding magnesium ion: G102 (= G92), W103 (= W93), D172 (= D152)
Sites not aligning to the query:
5e9hA Structural insights of isocitrate lyases from fusarium graminearum (see paper)
38% identity, 57% coverage: 6:250/430 of query aligns to 10:265/518 of 5e9hA
Sites not aligning to the query:
Query Sequence
>WP_078430601.1 NCBI__GCF_002019605.1:WP_078430601.1
MAKVNIQEEAKKLQQQWDTDPRWMGIERPYSAEEVVKLRGSVQIDHTLARLGSEKLWKLV
NEEPYVNALGALTGGQAVQQVKAGLKAIYLSGWQVAADANLAGHMYPDQSLYPANSVPQV
VKRINNSLQRADQIQHMEGEGDVDYFAPIVADAEAGFGGQLNVFELMKGMIEAGASGVHF
EDQLASEKKCGHLGGKVLIPTQTAVRNLVSARLAADVSGVPTLVIARTDADAADLITSDI
DPVDAPFITGERTPEGFYRTNAGIDQAIARGLAYAPYADLIWCETSKPSLEEAKQFADAI
HAKFPGKMLAYNCSPSFNWEANLDKATIETYQQELGKMGYKFQFVTLAGFHALNYSMFEL
ARGYKTRGMGAYSELQQAEFAAEEHGYTATRHQREVGTGYFDQVSQTVSGGTSSTTALKG
STEEAQFQKN
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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