SitesBLAST
Comparing WP_010531824.1 NCBI__GCF_000224785.1:WP_010531824.1 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)
A0A0P0ZBS7 o-succinylbenzoate synthase; OSB synthase; OSBS; 4-(2'-carboxyphenyl)-4-oxybutyric acid synthase; N-acylamino acid racemase; NAAAR; N-succinylamino acid racemase; NSAAR; NSAR; o-succinylbenzoic acid synthase; EC 4.2.1.113; EC 5.1.1.- from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
62% identity, 99% coverage: 4:368/370 of query aligns to 5:369/375 of A0A0P0ZBS7
- K166 (= K165) mutation to A: Almost loss of activity with N-formyl-D/L-methionine.
- D191 (= D190) mutation to A: Almost loss of activity with N-formyl-D/L-methionine.
- E216 (= E215) mutation to A: Almost loss of activity with N-formyl-D/L-methionine.
- D241 (= D240) mutation to A: Almost loss of activity with N-formyl-D/L-methionine.
- K265 (= K264) mutation to A: Almost loss of activity with N-formyl-D/L-methionine.
1wufA Crystal structure of protein gi:16801725, member of enolase superfamily from listeria innocua clip11262 (see paper)
44% identity, 97% coverage: 5:362/370 of query aligns to 5:362/371 of 1wufA
- active site: F20 (= F20), L54 (≠ Y54), K163 (= K163), K165 (= K165), D190 (= D190), E215 (= E215), D240 (= D240), K264 (= K264), G291 (= G291), D317 (= D317), I318 (≠ T318)
- binding magnesium ion: E215 (= E215), D240 (= D240), E241 (= E241)
Q9RYA6 N-succinylamino acid racemase; NSAAR; NSAR; N-acylamino acid racemase; NAAAR; o-succinylbenzoate synthase; OSB synthase; OSBS; EC 5.1.1.-; EC 5.1.1.-; EC 4.2.1.113 from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) (see 2 papers)
45% identity, 95% coverage: 13:362/370 of query aligns to 19:367/375 of Q9RYA6
- V48 (≠ N43) mutation to C: Loss of activity; when associated with C-120.
- M56 (≠ A51) mutation to C: Loss of activity; when associated with C-65.
- P60 (= P55) mutation to C: Loss of activity; when associated with C-100.
- E65 (= E60) mutation to C: Loss of activity; when associated with C-56.
- A68 (≠ G63) mutation to C: No change in activity; when associated with C-72.
- D72 (≠ H67) mutation to C: No change in activity; when associated with C-68.
- Y100 (≠ I95) mutation to C: Loss of activity; when associated with C-60.
- R120 (≠ K115) mutation to C: Loss of activity; when associated with C-48.
- G127 (≠ A122) mutation to C: Retains 93% of wild-type activity; when associated with C-313.
- S142 (= S137) binding N-acetyl-L-glutamine
- E149 (≠ V144) mutation to C: Retains 88% of wild-type activity; when associated with C-182.
- G163 (= G158) mutation to C: Loss of activity; when associated with C-343.
- KLK 168:170 (≠ KIK 163:165) binding N-acetyl-L-glutamine
- A182 (≠ N177) mutation to C: Retains 88% of wild-type activity; when associated with C-149.
- D195 (= D190) binding Mg(2+)
- Y218 (≠ M213) mutation to C: Retains 35% of wild-type activity.
- E220 (= E215) binding Mg(2+)
- D245 (= D240) binding Mg(2+)
- V265 (≠ I260) mutation to C: Retains 39% of wild-type activity.
- K269 (= K264) binding N-acetyl-L-glutamine
- L299 (= L294) binding N-acetyl-L-glutamine
- T313 (= T308) mutation to C: Retains 93% of wild-type activity; when associated with C-127.
- D343 (≠ N338) mutation to C: Loss of activity; when associated with C-163.
2gghC The mutant a68c-d72c-nlq of deinococcus radiodurans nacylamino acid racemase (see paper)
45% identity, 95% coverage: 13:362/370 of query aligns to 14:362/370 of 2gghC
- active site: F21 (= F20), Y95 (≠ I95), S137 (= S137), K163 (= K163), K165 (= K165), R186 (≠ P186), T188 (≠ M188), D190 (= D190), N192 (= N192), E215 (= E215), D240 (= D240), E241 (= E241), S242 (= S242), K264 (= K264), C290 (= C290), G291 (= G291), G292 (= G292), M293 (= M293), G316 (= G316), D317 (= D317), T318 (= T318)
- binding magnesium ion: D190 (= D190), E215 (= E215)
- binding n~2~-acetyl-l-glutamine: F21 (= F20), G292 (= G292), M293 (= M293), L294 (= L294)
Q44244 N-succinylamino acid racemase; NSAR; N-acylamino acid racemase; AAR; NAAAR; o-succinylbenzoate synthase; OSB synthase; OSBS; EC 5.1.1.-; EC 5.1.1.-; EC 4.2.1.113 from Amycolatopsis sp. (see 5 papers)
43% identity, 97% coverage: 4:362/370 of query aligns to 3:360/368 of Q44244
- P18 (= P19) mutation to A: Small increase in OSBS catalytic efficiency and 2-fold decrease in NSAR catalytic efficiency.
- F19 (= F20) mutation to A: 200-fold decrease in OSBS catalytic efficiency and 120-fold decrease in NSAR catalytic efficiency. 2100-fold decrease in OSBS catalytic efficiency and 180-fold decrease in NSAR catalytic efficiency; when associated with A-23.
- R20 (≠ T21) mutation to E: 32-fold decrease in OSBS catalytic efficiency and 8-fold decrease in NSAR catalytic efficiency.
- T21 (= T22) mutation to A: 4-fold decrease in OSBS and NSAR catalytic efficiencies.
- S22 (= S23) mutation to R: 3-fold increase in OSBS catalytic efficiency and 4-fold decrease in NSAR catalytic efficiency.
- F23 (= F24) mutation to A: 2100-fold decrease in OSBS catalytic efficiency and 180-fold decrease in NSAR catalytic efficiency; when associated with A-19.
- G24 (= G25) mutation to A: Small decrease in OSBS catalytic efficiency and 4-fold decrease in NSAR catalytic efficiency.
- S135 (= S137) binding 2-succinylbenzoate
- D140 (≠ P142) mutation to R: 3-fold decrease in OSBS and NSAR catalytic efficiencies.
- KLK 161:163 (≠ KIK 163:165) binding 2-succinylbenzoate
- K163 (= K165) mutation K->A,R,S: Significantly impairs both NAAAR and OSBS activities.
- D189 (= D190) binding Mg(2+)
- N191 (= N192) binding 2-succinylbenzoate
- E214 (= E215) binding Mg(2+)
- D239 (= D240) binding Mg(2+)
- K263 (= K264) mutation K->R,S: Significantly impairs both NAAAR and OSBS activities.
- G291 (= G292) mutation to D: Shows up to 6-fold higher activity than the wild-type on a range of N-acetylated amino acids; when associated with Y-323.
- I293 (≠ L294) binding 2-succinylbenzoate
- F323 (≠ Y324) mutation to Y: Shows up to 6-fold higher activity than the wild-type on a range of N-acetylated amino acids; when associated with D-291.
1sjdA X-ray structure of o-succinylbenzoate synthase complexed with n- succinyl phenylglycine (see paper)
43% identity, 97% coverage: 4:362/370 of query aligns to 3:360/367 of 1sjdA
- active site: F19 (= F20), S135 (= S137), K161 (= K163), K163 (= K165), D189 (= D190), N191 (= N192), E214 (= E215), D239 (= D240), E240 (= E241), S241 (= S242), K263 (= K264), G290 (= G291), G291 (= G292), M292 (= M293), G315 (= G316), D316 (= D317), T317 (= T318)
- binding n-succinyl phenylglycine: F23 (= F24), M50 (≠ F52), D61 (≠ G63), G62 (≠ T64), H65 (= H67), S135 (= S137), K163 (= K165), N191 (= N192), K263 (= K264), G291 (= G292), M292 (= M293), I293 (≠ L294), F323 (≠ Y324)
1sjcA X-ray structure of o-succinylbenzoate synthase complexed with n- succinyl methionine (see paper)
43% identity, 97% coverage: 4:362/370 of query aligns to 3:360/367 of 1sjcA
- active site: F19 (= F20), S135 (= S137), K161 (= K163), K163 (= K165), D189 (= D190), N191 (= N192), E214 (= E215), D239 (= D240), E240 (= E241), S241 (= S242), K263 (= K264), G290 (= G291), G291 (= G292), M292 (= M293), G315 (= G316), D316 (= D317), T317 (= T318)
- binding magnesium ion: D189 (= D190), E214 (= E215), D239 (= D240)
- binding n-succinyl methionine: F19 (= F20), F23 (= F24), M50 (≠ F52), S135 (= S137), K161 (= K163), K163 (= K165), D189 (= D190), N191 (= N192), D239 (= D240), K263 (= K264), G291 (= G292), M292 (= M293), I293 (≠ L294), F323 (≠ Y324)
1sjbA X-ray structure of o-succinylbenzoate synthase complexed with o- succinylbenzoic acid (see paper)
43% identity, 97% coverage: 4:362/370 of query aligns to 3:360/367 of 1sjbA
- active site: F19 (= F20), S135 (= S137), K161 (= K163), K163 (= K165), D189 (= D190), N191 (= N192), E214 (= E215), D239 (= D240), E240 (= E241), S241 (= S242), K263 (= K264), G290 (= G291), G291 (= G292), M292 (= M293), G315 (= G316), D316 (= D317), T317 (= T318)
- binding magnesium ion: D189 (= D190), E214 (= E215), D239 (= D240)
- binding 2-succinylbenzoate: F23 (= F24), Y55 (= Y57), K161 (= K163), K163 (= K165), D189 (= D190), N191 (= N192), D239 (= D240), K263 (= K264), G291 (= G292), M292 (= M293), I293 (≠ L294), F323 (≠ Y324)
5fjtA N-acyl amino acid racemase from amycolatopsis sp. Ts-1-60: g291d f323 mutant in complex with n-acetyl phenylalanine
43% identity, 97% coverage: 4:362/370 of query aligns to 3:360/367 of 5fjtA
- active site: F19 (= F20), S135 (= S137), K161 (= K163), K163 (= K165), D189 (= D190), N191 (= N192), E214 (= E215), D239 (= D240), E240 (= E241), S241 (= S242), K263 (= K264), G290 (= G291), D291 (≠ G292), M292 (= M293), G315 (= G316), D316 (= D317), T317 (= T318)
- binding N-acetyl-L-phenylalanine: F19 (= F20), M50 (≠ F52), S135 (= S137), K163 (= K165), N191 (= N192), K263 (= K264), D291 (≠ G292), M292 (= M293), I293 (≠ L294)
- binding magnesium ion: D189 (= D190), E214 (= E215), D239 (= D240)
5fjoA N-acyl amino acid racemase from amycolatopsis sp. Ts-1-60: g291d- f323y mutant in complex with n-acetyl naphthylalanine
43% identity, 97% coverage: 4:362/370 of query aligns to 3:360/367 of 5fjoA
- active site: F19 (= F20), S135 (= S137), K161 (= K163), K163 (= K165), D189 (= D190), N191 (= N192), E214 (= E215), D239 (= D240), E240 (= E241), S241 (= S242), K263 (= K264), G290 (= G291), D291 (≠ G292), M292 (= M293), G315 (= G316), D316 (= D317), T317 (= T318)
- binding magnesium ion: D189 (= D190), E214 (= E215), D239 (= D240)
- binding N-acetyl naphthylalanine: F19 (= F20), Q26 (≠ M27), R29 (≠ K30), M50 (≠ F52), S135 (= S137), K161 (= K163), K163 (= K165), N191 (= N192), K263 (= K264), D291 (≠ G292), I293 (≠ L294)
4a6gA N-acyl amino acid racemase from amycalotopsis sp. Ts-1-60: g291d- f323y mutant in complex with n-acetyl methionine (see paper)
43% identity, 97% coverage: 4:362/370 of query aligns to 3:360/368 of 4a6gA
- active site: F19 (= F20), S135 (= S137), K161 (= K163), K163 (= K165), D189 (= D190), N191 (= N192), E214 (= E215), D239 (= D240), E240 (= E241), S241 (= S242), K263 (= K264), G290 (= G291), D291 (≠ G292), M292 (= M293), G315 (= G316), D316 (= D317), T317 (= T318)
- binding n-acetylmethionine: F19 (= F20), F23 (= F24), S135 (= S137), K163 (= K165), K263 (= K264), D291 (≠ G292)
- binding magnesium ion: D189 (= D190), E214 (= E215), D239 (= D240)
7s8wA Amycolatopsis sp. T-1-60 n-succinylamino acid racemase/o- succinylbenzoate synthase r266q mutant in complex with n- succinylphenylglycine (see paper)
43% identity, 97% coverage: 4:362/370 of query aligns to 3:360/367 of 7s8wA