SitesBLAST
Comparing WP_053767406.1 NCBI__GCF_001280255.1:WP_053767406.1 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)
3vpdA Lysx from thermus thermophilus complexed with amp-pnp (see paper)
90% identity, 100% coverage: 1:281/281 of query aligns to 1:281/281 of 3vpdA
- binding phosphoaminophosphonic acid-adenylate ester: V127 (= V127), K129 (= K129), W135 (= W135), G136 (= G136), L139 (= L139), Q169 (= Q169), V172 (= V172), K174 (= K174), D178 (= D178), R194 (= R194), W199 (= W199), T201 (= T201), F239 (= F239), E249 (= E249)
- binding butanoic acid: F256 (= F256), K257 (= K257), N258 (= N258), S259 (= S259)
1uc9A Crystal structure of a lysine biosynthesis enzyme, lysx, from thermus thermophilus hb8 (see paper)
78% identity, 100% coverage: 1:280/281 of query aligns to 1:256/256 of 1uc9A
5k2mI Bifunctional lysx/argx from thermococcus kodakarensis with lysw-gamma- aaa (see paper)
46% identity, 99% coverage: 2:279/281 of query aligns to 3:271/273 of 5k2mI
- binding adenosine-5'-diphosphate: K83 (= K89), V120 (= V127), K122 (= K129), S127 (= S134), L132 (= L139), Q162 (= Q169), V165 (= V172), K167 (= K174), D171 (= D178), W192 (= W199), I193 (= I200), T194 (= T201), N195 (= N202), F231 (= F239), N240 (= N248), E241 (= E249)
- binding 2-aminohexanedioic acid: R173 (= R180), N195 (= N202), T196 (= T203), A197 (= A204), E247 (= E255), F248 (= F256), N250 (= N258)
- binding : V51 (= V57), S52 (= S58), H53 (≠ Q59), F54 (≠ S60), F125 (≠ I132), W128 (= W135), R130 (= R137), N153 (≠ G160), Y156 (≠ H163), N245 (≠ T253)
5k2mG Bifunctional lysx/argx from thermococcus kodakarensis with lysw-gamma- aaa (see paper)
46% identity, 99% coverage: 2:279/281 of query aligns to 3:271/273 of 5k2mG
- binding adenosine-5'-diphosphate: K83 (= K89), V120 (= V127), K122 (= K129), S127 (= S134), G129 (= G136), Q162 (= Q169), V165 (= V172), K167 (= K174), D171 (= D178), W192 (= W199), T194 (= T201), N195 (= N202), F231 (= F239), N240 (= N248), E241 (= E249)
- binding magnesium ion: D229 (= D237), E241 (= E249)
- binding : V51 (= V57), S52 (= S58), H53 (≠ Q59), F54 (≠ S60), F125 (≠ I132), S127 (= S134), W128 (= W135), R130 (= R137), Y156 (≠ H163), R173 (= R180), R187 (= R194), T196 (= T203), A197 (= A204), N243 (= N251), P244 (≠ H252), N245 (≠ T253), E247 (= E255), F248 (= F256), N250 (= N258), A251 (≠ S259)
Q4JAP9 Alpha-aminoadipate--LysW ligase LysX; AAA--LysW ligase LysX; EC 6.3.2.43 from Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) (see paper)
34% identity, 94% coverage: 9:273/281 of query aligns to 1:268/276 of Q4JAP9
- NT 253:254 (≠ NS 258:259) mutation to GF: Alters substrate specificity, so that glutamate is preferred over alpha-aminoadipate.
3vpbB Argx from sulfolobus tokodaii complexed with lysw/glu/adp/mg/zn/sulfate (see paper)
33% identity, 98% coverage: 2:277/281 of query aligns to 3:278/282 of 3vpbB
- binding adenosine-5'-diphosphate: K87 (= K89), I125 (≠ V127), K127 (= K129), S132 (= S134), G134 (= G136), V137 (≠ L139), Q167 (= Q169), Y169 (= Y171), I170 (≠ V172), D176 (= D178), R200 (≠ I200), A201 (≠ T201), N202 (= N202), N249 (= N248), E250 (= E249)
- binding glutamic acid: Y190 (≠ I192), R192 (= R194), N202 (= N202), V203 (≠ T203), A204 (= A204), E256 (= E255), G259 (≠ N258)
- binding magnesium ion: D237 (= D237), E250 (= E249)
- binding zinc ion: E250 (= E249), N252 (= N251)
Q970U6 Glutamate--LysW ligase ArgX; EC 6.3.2.- from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see paper)
33% identity, 98% coverage: 2:277/281 of query aligns to 3:278/282 of Q970U6
- D237 (= D237) binding Mg(2+)
- E250 (= E249) binding Mg(2+); binding Mg(2+)
- N252 (= N251) binding Mg(2+)
7qyrD Crystal structure of rimk from pseudomonas aeruginosa pao1 (see paper)
32% identity, 89% coverage: 31:280/281 of query aligns to 44:291/293 of 7qyrD
- binding adenosine-5'-diphosphate: V139 (= V127), Y179 (= Y171), I180 (≠ V172), D187 (= D178), R211 (≠ I200), S212 (≠ T201), L250 (≠ F239), M259 (≠ N248)
- binding : R64 (= R55), R189 (= R180), N262 (= N251), S264 (≠ T253), G266 (≠ E255)
Sites not aligning to the query:
4iwxA Rimk structure at 2.85a (see paper)
32% identity, 76% coverage: 62:274/281 of query aligns to 75:287/294 of 4iwxA
- binding adenosine-5'-diphosphate: V141 (= V127), K143 (= K129), E180 (= E170), Y181 (= Y171), I182 (≠ V172), K183 (= K173), D189 (= D178), R213 (≠ I200), S214 (≠ T201), N215 (= N202), M261 (≠ N248), E262 (= E249)
- binding glutamic acid: R98 (≠ T85), R104 (≠ A91), Q107 (≠ V94), L108 (≠ A95), R111 (= R98)
5zctH The crystal structure of the poly-alpha-l-glutamate peptides synthetase rimk at 2.05 angstrom resolution. (see paper)
32% identity, 76% coverage: 62:274/281 of query aligns to 73:285/292 of 5zctH
- binding phosphoaminophosphonic acid-adenylate ester: V139 (= V127), K141 (= K129), Q177 (= Q169), Y179 (= Y171), I180 (≠ V172), D187 (= D178), F210 (≠ W199), R211 (≠ I200), S212 (≠ T201), N213 (= N202), R216 (= R205), L250 (≠ F239), M259 (≠ N248), E260 (= E249)
- binding magnesium ion: D248 (= D237), E260 (= E249)
5zctA The crystal structure of the poly-alpha-l-glutamate peptides synthetase rimk at 2.05 angstrom resolution. (see paper)
32% identity, 76% coverage: 62:274/281 of query aligns to 73:285/292 of 5zctA
- binding phosphoaminophosphonic acid-adenylate ester: K100 (= K89), K141 (= K129), T146 (≠ S134), Q147 (≠ W135), G148 (= G136), Q177 (= Q169), Y179 (= Y171), I180 (≠ V172), R211 (≠ I200), S212 (≠ T201), N213 (= N202), L250 (≠ F239), M259 (≠ N248)
7lgmA Cyanophycin synthetase from a. Baylyi dsm587 with atp (see paper)
31% identity, 43% coverage: 83:202/281 of query aligns to 212:326/719 of 7lgmA
Sites not aligning to the query:
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
26% identity, 70% coverage: 79:275/281 of query aligns to 106:314/444 of 2vr1A
- active site: K116 (= K89), K159 (= K129), D194 (≠ Q164), H207 (≠ D178), R233 (≠ A204), T272 (≠ V233), E274 (≠ A235), E286 (= E249), N288 (= N251), R290 (≠ T253), E294 (≠ K257)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K129), R165 (≠ W135), M167 (≠ R137), Y201 (= Y171), L202 (≠ V172), E274 (≠ A235), L276 (= L238), E286 (= E249), N288 (= N251)
Sites not aligning to the query:
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
26% identity, 58% coverage: 104:267/281 of query aligns to 139:313/1144 of 5vyzA
- binding adenosine-5'-diphosphate: M162 (≠ V127), K164 (= K129), G168 (= G133), G170 (≠ W135), G171 (= G136), M174 (≠ L138), Y208 (= Y171), I209 (≠ V172), H214 (≠ D178), Q238 (≠ Y193), N241 (≠ S196), L283 (= L238), E293 (= E249)
- binding magnesium ion: E281 (≠ A235), E293 (= E249)
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 719, 722, 752, 753, 756
- binding adenosine-5'-diphosphate: 123, 449
- binding manganese (ii) ion: 541, 710, 739, 741
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
26% identity, 58% coverage: 104:267/281 of query aligns to 133:307/1056 of 7zyyA
- binding adenosine-5'-diphosphate: K158 (= K129), G163 (≠ S134), G164 (≠ W135), M168 (≠ L138), E200 (≠ Q169), K201 (≠ E170), Y202 (= Y171), I203 (≠ V172), H208 (≠ D178), Q232 (vs. gap), N235 (≠ S196), E275 (≠ A235), L277 (= L238), E287 (= E249)
- binding bicarbonate ion: R291 (≠ T253), Q293 (≠ E255), V294 (≠ F256), E295 (≠ K257)
- binding magnesium ion: E275 (≠ A235), E287 (= E249)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 19, 22, 43, 44, 45, 363, 414, 416, 418, 459, 460, 461, 1016, 1017, 1018, 1041, 1045
- binding adenosine-5'-diphosphate: 443
- binding magnesium ion: 520, 523, 754
- binding manganese (ii) ion: 535, 704, 733, 735
- binding pyruvic acid: 538, 572, 605, 607, 704, 868
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
26% identity, 58% coverage: 104:267/281 of query aligns to 133:307/1138 of 7zz3A
- binding adenosine-5'-triphosphate: M156 (≠ V127), K158 (= K129), G163 (≠ S134), G164 (≠ W135), G165 (= G136), M168 (≠ L138), E200 (≠ Q169), Y202 (= Y171), I203 (≠ V172), H208 (≠ D178), Q232 (≠ Y193), N235 (≠ S196), L277 (= L238), E287 (= E249), N289 (= N251)
- binding bicarbonate ion: K237 (≠ H198), R291 (≠ T253), Q293 (≠ E255), E295 (≠ K257)
- binding biotin: V294 (≠ F256)
- binding magnesium ion: E275 (≠ A235), E287 (= E249)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 22, 43, 44, 45, 46, 48, 363, 413, 414, 416, 418, 459, 461, 1016, 1017, 1018, 1045
- binding adenosine-5'-triphosphate: 117, 443
- binding biotin: 84, 342, 1104
- binding magnesium ion: 520, 523, 754
- binding manganese (ii) ion: 535, 704, 733, 735
- binding pyruvic acid: 534, 538, 605, 704, 868
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
25% identity, 70% coverage: 79:275/281 of query aligns to 106:316/449 of P24182
- K116 (= K89) binding ATP
- K159 (= K129) binding ATP
- GG 165:166 (≠ SW 134:135) binding ATP
- EKYL 201:204 (≠ QEYV 169:172) binding ATP
- H209 (≠ D178) binding ATP
- H236 (≠ R205) binding ATP
- K238 (≠ G207) binding hydrogencarbonate
- E276 (≠ A235) binding ATP; binding Mg(2+)
- E288 (= E249) binding ATP; binding Mg(2+)
- R292 (≠ T253) active site; binding hydrogencarbonate
- V295 (≠ F256) binding hydrogencarbonate
- E296 (≠ K257) mutation to A: Severe reduction in catalytic activity.
Sites not aligning to the query:
- 19 R→E: Loss of homodimerization. No effect on ATP binding.
- 23 E→R: Loss of homodimerization. No effect on ATP binding.
- 338 binding biotin; binding hydrogencarbonate; R→A: Severe reduction in catalytic activity.
- 363 F→A: Loss of homodimerization. No effect on ATP binding.
- 366 R→E: Loss of homodimerization. No effect on ATP binding.
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
25% identity, 70% coverage: 79:275/281 of query aligns to 106:316/445 of 3jziA