SitesBLAST
Comparing WP_009141067.1 NCBI__GCF_000225705.1:WP_009141067.1 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)
8zpfB Sfx reaction state structure (0-20min) of alanine racemase (see paper)
35% identity, 98% coverage: 10:383/383 of query aligns to 6:379/386 of 8zpfB
- binding alanine: Y272 (= Y270), T319 (≠ C318), M320 (= M319)
- binding pyridoxal-5'-phosphate: K39 (= K43), Y43 (= Y47), R139 (= R141), H169 (= H170), T210 (= T211), R225 (= R226), G227 (= G228), I228 (= I229), Y364 (= Y368)
6q70A Crystal structure of the alanine racemase bsu17640 from bacillus subtilis in the presence of hepes (see paper)
35% identity, 98% coverage: 10:383/383 of query aligns to 6:379/386 of 6q70A
- active site: K39 (= K43), R139 (= R141), H169 (= H170), R225 (= R226), Y272 (= Y270), T319 (≠ C318), D321 (= D320)
- binding pyridoxal-5'-phosphate: V37 (= V41), K39 (= K43), Y43 (= Y47), L85 (= L89), R139 (= R141), H169 (= H170), T210 (= T211), R225 (= R226), G227 (= G228), I228 (= I229), Y364 (= Y368)
5irpA Crystal structure of the alanine racemase bsu17640 from bacillus subtilis (see paper)
35% identity, 98% coverage: 10:383/383 of query aligns to 6:379/386 of 5irpA
- active site: K39 (= K43), R139 (= R141), H169 (= H170), R225 (= R226), Y272 (= Y270), T319 (≠ C318), D321 (= D320)
- binding magnesium ion: L155 (≠ I156), K156 (≠ D157), S158 (≠ H159), L161 (≠ I162)
- binding 2-amino-2-hydroxymethyl-propane-1,3-diol: D174 (= D175), P235 (= P236), Y364 (= Y368)
- binding (5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: Y43 (= Y47), L85 (= L89), R139 (= R141), H169 (= H170), N209 (= N210), T210 (= T211), R225 (= R226), G227 (= G228), I228 (= I229), Y364 (= Y368)
2vd9A The crystal structure of alanine racemase from bacillus anthracis (ba0252) with bound l-ala-p (see paper)
33% identity, 98% coverage: 7:383/383 of query aligns to 2:371/386 of 2vd9A
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R221 (= R226), Y267 (= Y270), T313 (≠ C318), D315 (= D320)
- binding (1s)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]ethylphosphonic acid: K38 (= K43), Y42 (= Y47), R135 (= R141), H165 (= H170), N205 (= N210), S206 (≠ T211), G223 (= G228), I224 (= I229), Y267 (= Y270), T313 (≠ C318), M314 (= M319), Y356 (= Y368)
- binding {1-[(3-hydroxy-methyl-5-phosphonooxy-methyl-pyridin-4-ylmethyl)-amino]-ethyl}-phosphonic acid: K38 (= K43), Y42 (= Y47), R135 (= R141), H165 (= H170), S206 (≠ T211), R221 (= R226), G223 (= G228), I224 (= I229), Y267 (= Y270), T313 (≠ C318), M314 (= M319), Y356 (= Y368)
- binding magnesium ion: T329 (≠ D341), K330 (≠ L342)
2vd8A The crystal structure of alanine racemase from bacillus anthracis (ba0252) (see paper)
33% identity, 98% coverage: 7:383/383 of query aligns to 3:372/387 of 2vd8A
- active site: K39 (= K43), R136 (= R141), H166 (= H170), R222 (= R226), Y268 (= Y270), T314 (≠ C318), D316 (= D320)
- binding pyridoxal-5'-phosphate: K39 (= K43), Y43 (= Y47), R136 (= R141), H166 (= H170), S207 (≠ T211), R222 (= R226), G224 (= G228), I225 (= I229), Y357 (= Y368)
5yycA Crystal structure of alanine racemase from bacillus pseudofirmus (of4) (see paper)
34% identity, 99% coverage: 5:382/383 of query aligns to 2:366/368 of 5yycA
- active site: K41 (= K43), R139 (= R141), H169 (= H170), R225 (= R226), Y269 (= Y270), C316 (= C318), D318 (= D320)
- binding pyridoxal-5'-phosphate: K41 (= K43), Y45 (= Y47), R139 (= R141), H169 (= H170), N209 (= N210), S210 (≠ T211), R225 (= R226), G227 (= G228), I228 (= I229), Y352 (= Y368)
3e6eA Crystal structure of alanine racemase from e.Faecalis complex with cycloserine (see paper)
35% identity, 96% coverage: 14:382/383 of query aligns to 10:369/370 of 3e6eA
- active site: K39 (= K43), R138 (= R141), H168 (= H170), R221 (= R226), Y266 (= Y270), C312 (= C318), D314 (= D320)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: K39 (= K43), Y43 (= Y47), L85 (= L89), R138 (= R141), H168 (= H170), S206 (≠ T211), R221 (= R226), G223 (= G228), V224 (≠ I229), Y266 (= Y270), Y285 (= Y290), M313 (= M319), Y355 (= Y368)
3e5pB Crystal structure of alanine racemase from e.Faecalis (see paper)
35% identity, 96% coverage: 14:382/383 of query aligns to 11:370/371 of 3e5pB
- active site: K40 (= K43), R139 (= R141), H169 (= H170), R222 (= R226), Y267 (= Y270), C313 (= C318), D315 (= D320)
- binding pyridoxal-5'-phosphate: K40 (= K43), Y44 (= Y47), R139 (= R141), H169 (= H170), S207 (≠ T211), G224 (= G228), V225 (≠ I229), Y356 (= Y368)
1sftA Alanine racemase (see paper)
36% identity, 98% coverage: 10:383/383 of query aligns to 5:368/382 of 1sftA
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R218 (= R226), Y264 (= Y270), C310 (= C318), D312 (= D320)
- binding pyridoxal-5'-phosphate: K38 (= K43), Y42 (= Y47), L84 (= L89), R135 (= R141), H165 (= H170), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), Y353 (= Y368)
1ftxA Crystal structure of alanine racemase in complex with d-alanine phosphonate
36% identity, 98% coverage: 10:383/383 of query aligns to 5:368/380 of 1ftxA
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R218 (= R226), Y264 (= Y270), C310 (= C318), D312 (= D320)
- binding (1s)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]ethylphosphonic acid: K38 (= K43), Y42 (= Y47), R135 (= R141), H165 (= H170), N202 (= N210), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), Y264 (= Y270), C310 (= C318), M311 (= M319), Y353 (= Y368)
4lusB Alanine racemase [clostridium difficile 630] (see paper)
34% identity, 97% coverage: 12:383/383 of query aligns to 6:361/374 of 4lusB
- active site: K37 (= K43), H160 (= H170), R213 (= R226), Y258 (= Y270), C304 (= C318), D306 (= D320)
- binding 3,3',3''-phosphanetriyltripropanoic acid: T77 (≠ K83), P79 (= P85), K98 (≠ Q104), C124 (≠ K130)
P10724 Alanine racemase; EC 5.1.1.1 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 8 papers)
36% identity, 98% coverage: 10:383/383 of query aligns to 6:369/388 of P10724
- K39 (= K43) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of activity.
- K129 (≠ A134) modified: N6-carboxylysine
- R136 (= R141) binding substrate
- H166 (= H170) mutation to A: 6.5-fold decrease in activity.
- R219 (= R226) 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 (= Y270) mutation to A: 5000-fold decrease in activity.; mutation to F: Loss of activity.; mutation to S: 2000-fold decrease in activity.
- M312 (= M319) binding substrate
- 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.
4y2wA Crystal structure of a thermostable alanine racemase from thermoanaerobacter tengcongensis mb4 (see paper)
32% identity, 97% coverage: 10:382/383 of query aligns to 7:374/388 of 4y2wA
- active site: K40 (= K43), R138 (= R141), H168 (= H170), R224 (= R226), Y268 (= Y270), C315 (= C318), D317 (= D320)
- binding alanine: Y268 (= Y270), Y287 (= Y290), C315 (= C318), M316 (= M319)
- binding phosphate ion: N208 (= N210), A209 (≠ T211), I227 (= I229)
1l6gA Alanine racemase bound with n-(5'-phosphopyridoxyl)-d-alanine (see paper)
36% identity, 98% coverage: 10:383/383 of query aligns to 5:368/382 of 1l6gA
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R218 (= R226), Y264 (= Y270), C310 (= C318), D312 (= D320)
- binding n-(5'-phosphopyridoxyl)-d-alanine: K38 (= K43), Y42 (= Y47), R135 (= R141), H165 (= H170), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), Y264 (= Y270), C310 (= C318), M311 (= M319), Y353 (= Y368)
1l6fA Alanine racemase bound with n-(5'-phosphopyridoxyl)-l-alanine (see paper)
36% identity, 98% coverage: 10:383/383 of query aligns to 5:368/382 of 1l6fA
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R218 (= R226), Y264 (= Y270), C310 (= C318), D312 (= D320)
- binding alanyl-pyridoxal-5'-phosphate: K38 (= K43), Y42 (= Y47), R135 (= R141), H165 (= H170), N202 (= N210), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), Y264 (= Y270), C310 (= C318), M311 (= M319), Y353 (= Y368)
1epvA Alanine racemase with bound inhibitor derived from d-cycloserine (see paper)
36% identity, 98% coverage: 10:383/383 of query aligns to 5:368/382 of 1epvA
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R218 (= R226), Y264 (= Y270), C310 (= C318), D312 (= D320)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: K38 (= K43), Y42 (= Y47), L84 (= L89), R135 (= R141), H165 (= H170), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), Y264 (= Y270), C310 (= C318), M311 (= M319), Y353 (= Y368)
1bd0A Alanine racemase complexed with alanine phosphonate (see paper)
36% identity, 98% coverage: 10:383/383 of query aligns to 5:368/381 of 1bd0A
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R218 (= R226), Y264 (= Y270), C310 (= C318), D312 (= D320)
- binding {1-[(3-hydroxy-methyl-5-phosphonooxy-methyl-pyridin-4-ylmethyl)-amino]-ethyl}-phosphonic acid: K38 (= K43), Y42 (= Y47), R135 (= R141), H165 (= H170), N202 (= N210), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), Y264 (= Y270), C310 (= C318), M311 (= M319), Y353 (= Y368)
1xqlA Effect of a y265f mutant on the transamination based cycloserine inactivation of alanine racemase (see paper)
36% identity, 98% coverage: 10:383/383 of query aligns to 5:368/382 of 1xqlA
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R218 (= R226), F264 (≠ Y270), C310 (= C318), D312 (= D320)
- binding (r)-4-amino-isoxazolidin-3-one: F264 (≠ Y270), M311 (= M319)
- binding pyridoxal-5'-phosphate: K38 (= K43), Y42 (= Y47), L84 (= L89), H165 (= H170), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), Y353 (= Y368)
- binding (5-hydroxy-4-{[(3-hydroxyisoxazol-4-yl)amino]methyl}-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K38 (= K43), Y42 (= Y47), L84 (= L89), R135 (= R141), H165 (= H170), N202 (= N210), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), F264 (≠ Y270), Y283 (= Y290), M311 (= M319), Y353 (= Y368)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y42 (= Y47), R135 (= R141), H165 (= H170), N202 (= N210), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), Y353 (= Y368)
1xqkA Effect of a y265f mutant on the transamination based cycloserine inactivation of alanine racemase (see paper)
36% identity, 98% coverage: 10:383/383 of query aligns to 5:368/382 of 1xqkA
- active site: K38 (= K43), R135 (= R141), H165 (= H170), R218 (= R226), F264 (≠ Y270), C310 (= C318), D312 (= D320)
- binding (5-hydroxy-4-{[(3-hydroxyisoxazol-4-yl)amino]methyl}-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K38 (= K43), Y42 (= Y47), L84 (= L89), R135 (= R141), H165 (= H170), N202 (= N210), S203 (≠ T211), R218 (= R226), G220 (= G228), I221 (= I229), F264 (≠ Y270), M311 (= M319), Y353 (= Y368)
4lutA Alanine racemase [clostridium difficile 630] complex with cycloserine (see paper)
34% identity, 97% coverage: 12:383/383 of query aligns to 6:362/375 of 4lutA
- active site: K37 (= K43), H158 (= H170), R214 (= R226), Y259 (= Y270), C305 (= C318), D307 (= D320)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: K37 (= K43), Y41 (= Y47), L83 (= L89), H158 (= H170), S199 (≠ T211), R214 (= R226), G216 (= G228), I217 (= I229), Y259 (= Y270), Y278 (= Y290), M306 (= M319), Y347 (= Y368)
Query Sequence
>WP_009141067.1 NCBI__GCF_000225705.1:WP_009141067.1
MPSSKEPATRWAWVEIDQGALRRNTRAFKNLLGYGKRLCCVVKADAYGHGAVQCAKIMHA
TGADMFAVATVSEGVQLREGGIKSPILVLNEPPIDACDTLLEYQIMPSVYSSEFALAYGE
RAVEMGCVGKYHMAIETGMNRIGVRFTDVLEFRREIDFHRGIECDGVFTHFATADDPDGW
DYRLQCTRFSEAVAAMKDAGFECGIVHCSNTPASMLDHSMQFDMIRAGIGLYGLQPCEKS
APIMPLEPVMSVRARVTRTIHPAMGEGVGYGFTFRVPRARVQVCTIPVGYADGLPRTLSN
KMDVLYRGQRIRQVGNICMDQCMVAIQQTPARQMPEAEVGDLITIVGKDGDAVISMDEMA
RLRGTINYEVACGFGMRLEKVYI
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