SitesBLAST
Comparing Echvi_1545 FitnessBrowser__Cola:Echvi_1545 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)
4y2wA Crystal structure of a thermostable alanine racemase from thermoanaerobacter tengcongensis mb4 (see paper)
33% identity, 99% coverage: 5:384/384 of query aligns to 9:376/388 of 4y2wA
- active site: K40 (= K36), R138 (= R135), H168 (= H165), R224 (= R222), Y268 (= Y276), C315 (≠ T323), D317 (≠ N325)
- binding alanine: Y268 (= Y276), Y287 (= Y295), C315 (≠ T323), M316 (= M324)
- binding phosphate ion: N208 (≠ C206), A209 (≠ S207), I227 (= I225)
6q70A Crystal structure of the alanine racemase bsu17640 from bacillus subtilis in the presence of hepes (see paper)
32% identity, 97% coverage: 7:380/384 of query aligns to 10:376/386 of 6q70A
- active site: K39 (= K36), R139 (= R135), H169 (= H165), R225 (= R222), Y272 (= Y276), T319 (= T323), D321 (≠ N325)
- binding pyridoxal-5'-phosphate: V37 (= V34), K39 (= K36), Y43 (= Y40), L85 (≠ M83), R139 (= R135), H169 (= H165), T210 (≠ S207), R225 (= R222), G227 (= G224), I228 (= I225), Y364 (= Y368)
5irpA Crystal structure of the alanine racemase bsu17640 from bacillus subtilis (see paper)
32% identity, 97% coverage: 7:380/384 of query aligns to 10:376/386 of 5irpA
- active site: K39 (= K36), R139 (= R135), H169 (= H165), R225 (= R222), Y272 (= Y276), T319 (= T323), D321 (≠ N325)
- binding magnesium ion: L155 (≠ Y151), K156 (≠ E152), S158 (≠ G154), L161 (= L157)
- binding 2-amino-2-hydroxymethyl-propane-1,3-diol: D174 (≠ E170), P235 (= P232), Y364 (= Y368)
- binding (5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: Y43 (= Y40), L85 (≠ M83), R139 (= R135), H169 (= H165), N209 (≠ C206), T210 (≠ S207), R225 (= R222), G227 (= G224), I228 (= I225), Y364 (= Y368)
4lusB Alanine racemase [clostridium difficile 630] (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 9:358/374 of 4lusB
- active site: K37 (= K36), H160 (= H165), R213 (= R222), Y258 (= Y276), C304 (≠ T323), D306 (≠ N325)
- binding 3,3',3''-phosphanetriyltripropanoic acid: T77 (≠ N77), P79 (≠ D79), K98 (≠ R98), C124 (≠ K124)
I0J1I6 Broad specificity amino-acid racemase; Arginine racemase; Broad substrate specificity racemase; EC 5.1.1.10 from Pseudomonas taetrolens (see 2 papers)
32% identity, 96% coverage: 7:374/384 of query aligns to 45:394/409 of I0J1I6
- C70 (≠ S32) modified: Disulfide link with 96; mutation to A: The catalytic efficiency with arginine, lysine, and ornithine is very similar to that of wild-type, and that with both L-alanine and D-alanine increases approximately five times; when associated with A-96.
- C96 (≠ H58) modified: Disulfide link with 70; mutation to A: The catalytic efficiency with arginine, lysine, and ornithine is very similar to that of wild-type, and that with both L-alanine and D-alanine increases approximately five times; when associated with A-70.
Sites not aligning to the query:
4lutA Alanine racemase [clostridium difficile 630] complex with cycloserine (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 9:359/375 of 4lutA
- active site: K37 (= K36), H158 (= H165), R214 (= R222), Y259 (= Y276), C305 (≠ T323), D307 (≠ N325)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: K37 (= K36), Y41 (= Y40), L83 (≠ M83), H158 (= H165), S199 (= S207), R214 (= R222), G216 (= G224), I217 (= I225), Y259 (= Y276), Y278 (= Y295), M306 (= M324), Y347 (= Y368)
I6LNY0 Broad specificity amino-acid racemase; EC 5.1.1.10 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
31% identity, 98% coverage: 7:383/384 of query aligns to 46:408/409 of I6LNY0
- C71 (≠ S32) modified: Disulfide link with 97
- K75 (= K36) modified: N6-(pyridoxal phosphate)lysine
- C97 (≠ I56) modified: Disulfide link with 71
- R174 (= R135) mutation R->A,K: Loss of catalytic activity.
- N175 (≠ T136) mutation to L: Loss of catalytic activity.
- A393 (≠ Y368) mutation to Y: Reduces the catalytic activity towards L-Lys by 2-fold. Loss of racemase activity towards L-Arg.
4fs9A Complex structure of a broad specificity amino acid racemase (bar) within the reactive intermediate (see paper)
30% identity, 98% coverage: 7:383/384 of query aligns to 21:383/384 of 4fs9A
- active site: K50 (= K36), R149 (= R135), H180 (= H165), R236 (= R222), Y276 (= Y276), S323 (≠ T323), N325 (= N325)
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-lysine: K50 (= K36), Y54 (= Y40), V96 (≠ M83), H180 (= H165), S221 (= S207), R236 (= R222), G238 (= G224), G239 (≠ I225), Y276 (= Y276), M324 (= M324)
1ftxA Crystal structure of alanine racemase in complex with d-alanine phosphonate
29% identity, 97% coverage: 8:380/384 of query aligns to 10:365/380 of 1ftxA
- active site: K38 (= K36), R135 (= R135), H165 (= H165), R218 (= R222), Y264 (= Y276), C310 (≠ T323), D312 (≠ N325)
- binding (1s)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]ethylphosphonic acid: K38 (= K36), Y42 (= Y40), R135 (= R135), H165 (= H165), N202 (≠ C206), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), Y264 (= Y276), C310 (≠ T323), M311 (= M324), Y353 (= Y368)
1sftA Alanine racemase (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 10:365/382 of 1sftA
- active site: K38 (= K36), R135 (= R135), H165 (= H165), R218 (= R222), Y264 (= Y276), C310 (≠ T323), D312 (≠ N325)
- binding pyridoxal-5'-phosphate: K38 (= K36), Y42 (= Y40), L84 (≠ M83), R135 (= R135), H165 (= H165), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), Y353 (= Y368)
A0KLG5 Broad specificity amino-acid racemase; Broad spectrum racemase; EC 5.1.1.10 from Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) (see paper)
29% identity, 98% coverage: 7:382/384 of query aligns to 44:406/408 of A0KLG5
- K74 (= K36) modified: N6-(pyridoxal phosphate)lysine
1l6gA Alanine racemase bound with n-(5'-phosphopyridoxyl)-d-alanine (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 10:365/382 of 1l6gA
- active site: K38 (= K36), R135 (= R135), H165 (= H165), R218 (= R222), Y264 (= Y276), C310 (≠ T323), D312 (≠ N325)
- binding n-(5'-phosphopyridoxyl)-d-alanine: K38 (= K36), Y42 (= Y40), R135 (= R135), H165 (= H165), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), Y264 (= Y276), C310 (≠ T323), M311 (= M324), Y353 (= Y368)
1l6fA Alanine racemase bound with n-(5'-phosphopyridoxyl)-l-alanine (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 10:365/382 of 1l6fA
- active site: K38 (= K36), R135 (= R135), H165 (= H165), R218 (= R222), Y264 (= Y276), C310 (≠ T323), D312 (≠ N325)
- binding alanyl-pyridoxal-5'-phosphate: K38 (= K36), Y42 (= Y40), R135 (= R135), H165 (= H165), N202 (≠ C206), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), Y264 (= Y276), C310 (≠ T323), M311 (= M324), Y353 (= Y368)
1epvA Alanine racemase with bound inhibitor derived from d- cycloserine (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 10:365/382 of 1epvA
- active site: K38 (= K36), R135 (= R135), H165 (= H165), R218 (= R222), Y264 (= Y276), C310 (≠ T323), D312 (≠ N325)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: K38 (= K36), Y42 (= Y40), L84 (≠ M83), R135 (= R135), H165 (= H165), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), Y264 (= Y276), C310 (≠ T323), M311 (= M324), Y353 (= Y368)
1bd0A Alanine racemase complexed with alanine phosphonate (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 10:365/381 of 1bd0A
- active site: K38 (= K36), R135 (= R135), H165 (= H165), R218 (= R222), Y264 (= Y276), C310 (≠ T323), D312 (≠ N325)
- binding {1-[(3-hydroxy-methyl-5-phosphonooxy-methyl-pyridin-4-ylmethyl)-amino]-ethyl}-phosphonic acid: K38 (= K36), Y42 (= Y40), R135 (= R135), H165 (= H165), N202 (≠ C206), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), Y264 (= Y276), C310 (≠ T323), M311 (= M324), Y353 (= Y368)
P10724 Alanine racemase; EC 5.1.1.1 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 8 papers)
29% identity, 97% coverage: 8:380/384 of query aligns to 11:366/388 of P10724
- K39 (= K36) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of activity.
- K129 (≠ E128) modified: N6-carboxylysine
- R136 (= R135) binding
- H166 (= H165) mutation to A: 6.5-fold decrease in activity.
- R219 (= R222) mutation to A: 100-fold decrease in activity.; mutation to E: 1000-fold decrease in activity.; mutation to K: 4-fold decrease in activity.
- Y265 (= Y276) mutation to A: 5000-fold decrease in activity.; mutation to F: Loss of activity.; mutation to S: 2000-fold decrease in activity.
- M312 (= M324) binding
- Y354 (= Y368) mutation to A: 54-fold increase in serine racemase activity.; mutation to N: 81-fold increase in serine racemase activity.; mutation to Q: 51-fold increase in serine racemase activity.
4bf5A Structure of broad spectrum racemase from aeromonas hydrophila (see paper)
29% identity, 98% coverage: 7:382/384 of query aligns to 23:385/396 of 4bf5A
- active site: K53 (= K36), R152 (= R135), H183 (= H165), R239 (= R222), Y279 (= Y276), S326 (≠ T323), N328 (= N325)
- binding pyridoxal-5'-phosphate: K53 (= K36), Y57 (= Y40), H183 (= H165), S224 (= S207), R239 (= R222), G241 (= G224), G242 (≠ I225)
1xqlA Effect of a y265f mutant on the transamination based cycloserine inactivation of alanine racemase (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 10:365/382 of 1xqlA
- active site: K38 (= K36), R135 (= R135), H165 (= H165), R218 (= R222), F264 (≠ Y276), C310 (≠ T323), D312 (≠ N325)
- binding (r)-4-amino-isoxazolidin-3-one: F264 (≠ Y276), M311 (= M324)
- binding pyridoxal-5'-phosphate: K38 (= K36), Y42 (= Y40), L84 (≠ M83), H165 (= H165), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), Y353 (= Y368)
- binding (5-hydroxy-4-{[(3-hydroxyisoxazol-4-yl)amino]methyl}-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K38 (= K36), Y42 (= Y40), L84 (≠ M83), R135 (= R135), H165 (= H165), N202 (≠ C206), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), F264 (≠ Y276), Y283 (= Y295), M311 (= M324), Y353 (= Y368)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y42 (= Y40), R135 (= R135), H165 (= H165), N202 (≠ C206), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), Y353 (= Y368)
1xqkA Effect of a y265f mutant on the transamination based cycloserine inactivation of alanine racemase (see paper)
29% identity, 97% coverage: 8:380/384 of query aligns to 10:365/382 of 1xqkA
- active site: K38 (= K36), R135 (= R135), H165 (= H165), R218 (= R222), F264 (≠ Y276), C310 (≠ T323), D312 (≠ N325)
- binding (5-hydroxy-4-{[(3-hydroxyisoxazol-4-yl)amino]methyl}-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K38 (= K36), Y42 (= Y40), L84 (≠ M83), R135 (= R135), H165 (= H165), N202 (≠ C206), S203 (= S207), R218 (= R222), G220 (= G224), I221 (= I225), F264 (≠ Y276), M311 (= M324), Y353 (= Y368)
M4GGR9 Lysine racemase; EC 5.1.1.5 from Proteus mirabilis (see paper)
31% identity, 97% coverage: 3:374/384 of query aligns to 41:393/407 of M4GGR9
- K74 (= K36) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Completely loss of racemase activity towards lysine.
- R173 (= R135) mutation R->A,K: Loss of racemase activity towards both L-lysine and L-arginine.
- N174 (≠ T136) mutation to L: Loss of racemase activity towards both L-lysine and L-arginine.
- T391 (= T372) mutation to Y: Reduces the racemization activity towards L-lysine by 2-fold. Does not affect racemase activity towards L-arginine.
Sites not aligning to the query:
- 394 mutation S->C,N,T,Y: Arginine racemization activity is increased by 1.5-1.8 fold compared to the wild-type enzyme, while activity towards L-lysine is decreased. Almost no change in affinity for L-lysine and L-arginine.
Query Sequence
>Echvi_1545 FitnessBrowser__Cola:Echvi_1545
MRHTSRIEISKSAYRRNMKFIRSQVGDDTIVSAVIKGNAYGHGIENIIKIAENVGIRHFS
AFSTDEAKRVLQASEKNSDIMIMGMVDNQDLEWIIKHRISFFVFEFDRLMAAIKMAKKLH
IPAKIHVEVETGFHRTGFEWNEKEFLADVIYEHGIHLELTGLCTHFAGAESIANYLRVQN
QIKQYRNFKNWFDRHGIKFGTYHTACSAASLSYPETIMDMVRIGILQYGFWPSQETYMSK
FKELAAHRKNPLKRLISWKSSIMSIKEVGMGDFVGYGTTFMAHRPMRIALVPVGYCHGFS
RMLSNLGKVLIQGKMVSVVGTVTMNSISVDITDLKDVKKGDEVVIIGKQKNNEITVASFS
ETTQQVNYELLTRLPHDIPRKIVY
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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