SitesBLAST
Comparing PP_3279 FitnessBrowser__Putida:PP_3279 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
2y27B Crystal structure of paak1 in complex with atp from burkholderia cenocepacia (see paper)
70% identity, 97% coverage: 12:436/439 of query aligns to 4:427/427 of 2y27B
- binding adenosine-5'-triphosphate: K65 (= K73), S90 (= S98), S91 (= S99), G92 (= G100), T93 (= T101), T94 (= T102), F138 (= F146), A211 (= A219), E212 (= E220), P213 (= P221), D232 (= D240), I233 (= I241), Y234 (= Y242), G235 (= G243), L236 (= L244), S237 (= S245), D302 (= D310), I320 (= I328), R323 (= R331), K419 (= K428)
- binding magnesium ion: V200 (≠ H208), S202 (≠ L210), L204 (= L212), M226 (= M234), G227 (= G235), Q347 (≠ I355), L350 (= L358)
2y4oB Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
69% identity, 97% coverage: 10:436/439 of query aligns to 4:432/432 of 2y4oB
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ Y141), F140 (= F146), G212 (= G218), A213 (= A219), E214 (= E220), P215 (= P221), I235 (= I241), G237 (= G243), L238 (= L244), S239 (= S245), P244 (= P250), D304 (= D310), R325 (= R331), I331 (= I337), N336 (= N342)
- binding magnesium ion: S204 (≠ L210), V228 (≠ M234)
2y4oA Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
69% identity, 97% coverage: 10:436/439 of query aligns to 4:432/433 of 2y4oA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ Y141), F140 (= F146), A213 (= A219), E214 (= E220), P215 (= P221), I235 (= I241), G237 (= G243), L238 (= L244), S239 (= S245), P244 (= P250), D304 (= D310), R325 (= R331), I331 (= I337), N336 (= N342)
2y4nA Paak1 in complex with phenylacetyl adenylate (see paper)
70% identity, 97% coverage: 12:436/439 of query aligns to 4:425/426 of 2y4nA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: Y131 (= Y141), F136 (= F146), G138 (= G148), G208 (= G218), A209 (= A219), E210 (= E220), P211 (= P221), I231 (= I241), Y232 (= Y242), G233 (= G243), L234 (= L244), S235 (= S245), P240 (= P250), D300 (= D310), R321 (= R331), K417 (= K428)
- binding magnesium ion: V198 (≠ H208), S200 (≠ L210), Q345 (≠ I355), L348 (= L358)
4r1mA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.48 a resolution
44% identity, 97% coverage: 13:436/439 of query aligns to 9:433/435 of 4r1mA
- binding adenosine monophosphate: A215 (= A219), E216 (= E220), P217 (= P221), N236 (≠ D240), S237 (≠ I241), F238 (≠ Y242), G239 (= G243), M240 (≠ L244), T241 (≠ S245), D305 (= D310), R329 (= R331), I335 (= I337), N340 (= N342)
- binding zinc ion: C252 (= C256), H259 (≠ T264), C314 (vs. gap), C316 (≠ T318)
4r1lA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.42 a resolution
43% identity, 97% coverage: 13:436/439 of query aligns to 9:431/433 of 4r1lA
- binding adenosine-5'-diphosphate: A215 (= A219), E216 (= E220), P217 (= P221), S237 (≠ I241), F238 (≠ Y242), G239 (= G243), M240 (≠ L244), T241 (≠ S245), D305 (= D310), R329 (= R331), N340 (= N342)
- binding adenosine monophosphate: A215 (= A219), E216 (= E220), P217 (= P221), S237 (≠ I241), F238 (≠ Y242), G239 (= G243), M240 (≠ L244), T241 (≠ S245), D305 (= D310), R329 (= R331), N340 (= N342)
- binding coenzyme a: S136 (= S140), A164 (≠ G168), G165 (= G169), N166 (≠ Q170), S167 (≠ T171), I185 (≠ T189), Y188 (= Y192), K337 (≠ R339), T408 (≠ S411)
- binding zinc ion: C252 (= C256), H259 (≠ T264), C314 (vs. gap), C316 (≠ T318)
6he0A Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in complex with 2-hib-amp and coa in the thioesterfication state (see paper)
31% identity, 93% coverage: 28:436/439 of query aligns to 42:464/477 of 6he0A
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] 2-methyl-2-oxidanyl-propanoate: S241 (≠ G218), G242 (≠ A219), E243 (= E220), P244 (= P221), G267 (≠ Y242), S268 (≠ G243), M269 (≠ L244), A270 (≠ S245), D335 (= D310), I357 (= I328), N371 (= N342)
- binding adenosine monophosphate: G242 (≠ A219), E243 (= E220), P244 (= P221), C266 (≠ I241), G267 (≠ Y242), S268 (≠ G243), A270 (≠ S245), E271 (= E246), D335 (= D310), N371 (= N342)
- binding coenzyme a: Y166 (≠ F146), A188 (≠ G168), G189 (vs. gap), P191 (vs. gap), S194 (≠ T171), Y210 (≠ M187), G211 (≠ V188), T212 (= T189), Y215 (= Y192), H218 (≠ N195), R368 (= R339), G369 (= G340), M401 (≠ L372), V439 (≠ I410), R440 (≠ S411)
6hdyA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with s3-hb-amp (see paper)
30% identity, 93% coverage: 28:436/439 of query aligns to 42:461/474 of 6hdyA
- binding (3s)-3-hydroxybutanoic acid: Y162 (≠ F146), S237 (≠ G218), G263 (≠ Y242), S264 (≠ G243), M265 (≠ L244), A266 (≠ S245), F271 (≠ G251)
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (3~{S})-3-oxidanylbutanoate: Y162 (≠ F146), G164 (= G148), S237 (≠ G218), G238 (≠ A219), E239 (= E220), P240 (= P221), C262 (≠ I241), G263 (≠ Y242), S264 (≠ G243), A266 (≠ S245), F271 (≠ G251), D331 (= D310), I353 (= I328), R356 (= R331), K453 (= K428)
6hdxA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with r3-hib-amp (see paper)
30% identity, 93% coverage: 28:436/439 of query aligns to 42:461/474 of 6hdxA
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (2~{R})-2-methyl-3-oxidanyl-propanoate: Y162 (≠ F146), G164 (= G148), S237 (≠ G218), G238 (≠ A219), E239 (= E220), P240 (= P221), C262 (≠ I241), G263 (≠ Y242), S264 (≠ G243), A266 (≠ S245), F271 (≠ G251), D331 (= D310), I353 (= I328), R356 (= R331), K453 (= K428)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: Y162 (≠ F146), G164 (= G148), S237 (≠ G218), G263 (≠ Y242), S264 (≠ G243), A266 (≠ S245), F271 (≠ G251)
6sixB Paak family amp-ligase with anp (see paper)
28% identity, 93% coverage: 18:427/439 of query aligns to 16:410/437 of 6sixB
- binding phosphoaminophosphonic acid-adenylate ester: S88 (= S98), S89 (= S99), A213 (= A219), E214 (= E220), P215 (= P221), E236 (≠ I241), Y237 (= Y242), G238 (= G243), S239 (≠ L244), T240 (≠ S245), E241 (= E246), D300 (= D310), V320 (≠ I328), R323 (= R331)
- binding magnesium ion: R79 (≠ Q89), E80 (= E90), P121 (≠ K133), T150 (= T162)
- binding zinc ion: C249 (= C256), H255 (≠ G262), C309 (≠ G317), C311 (≠ A319)
6siyA Paak family amp-ligase with amp and substrate (see paper)
28% identity, 93% coverage: 18:427/439 of query aligns to 12:406/433 of 6siyA
- binding 3-hydroxyanthranilic acid: T125 (≠ Y141), P126 (≠ G142), T132 (≠ G148), L135 (≠ G151), R153 (≠ G169), N177 (≠ T189), A209 (= A219), E232 (≠ I241), G234 (= G243), S235 (≠ L244)
- binding adenosine monophosphate: S85 (= S99), A209 (= A219), E210 (= E220), P211 (= P221), E232 (≠ I241), Y233 (= Y242), G234 (= G243), S235 (≠ L244), T236 (≠ S245), D296 (= D310), V316 (≠ I328)
- binding magnesium ion: R75 (≠ Q89), E76 (= E90), L78 (≠ V92), P117 (≠ K133), G144 (= G160), A145 (≠ C161), T146 (= T162)
6siwA Paak family amp-ligase with amp (see paper)
28% identity, 93% coverage: 18:427/439 of query aligns to 11:405/432 of 6siwA
- binding adenosine monophosphate: S84 (= S99), A208 (= A219), E209 (= E220), P210 (= P221), E231 (≠ I241), Y232 (= Y242), G233 (= G243), S234 (≠ L244), T235 (≠ S245), D295 (= D310), V315 (≠ I328)
- binding magnesium ion: E75 (= E90), L77 (≠ V92), S83 (= S98), P116 (≠ K133), G143 (= G160), T145 (= T162), E236 (= E246)
- binding zinc ion: C244 (= C256), H250 (≠ G262), C304 (≠ G317), C306 (≠ A319)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
22% identity, 62% coverage: 89:360/439 of query aligns to 166:441/518 of 4wv3B
- active site: S175 (= S98), T320 (≠ S245), E321 (= E246), K418 (≠ I337), W423 (≠ N342)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F146), T221 (= T147), F222 (≠ G148), A293 (≠ G218), S294 (≠ A219), E295 (= E220), A296 (≠ P221), G316 (≠ I241), I317 (≠ Y242), G318 (= G243), C319 (≠ L244), T320 (≠ S245), D397 (≠ T318), H409 (vs. gap), R412 (= R331)
Sites not aligning to the query:
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
25% identity, 47% coverage: 87:291/439 of query aligns to 186:392/546 of Q84P21
Sites not aligning to the query:
- 530 K→N: Lossed enzymatic activity.
3cw8X 4-chlorobenzoyl-coa ligase/synthetase, bound to 4cba-adenylate (see paper)
24% identity, 69% coverage: 66:366/439 of query aligns to 124:435/501 of 3cw8X
- binding 5'-O-[(S)-{[(4-chlorophenyl)carbonyl]oxy}(hydroxy)phosphoryl]adenosine: H207 (≠ G144), V208 (≠ L145), V209 (≠ T147), G281 (≠ A219), A282 (≠ E220), T283 (≠ P221), I303 (= I241), Y304 (= Y242), G305 (= G243), T306 (≠ L244), T307 (≠ S245), M310 (= M248), N311 (≠ G249), M324 (≠ W266), D385 (= D310)
3cw9A 4-chlorobenzoyl-coa ligase/synthetase in the thioester-forming conformation, bound to 4-chlorophenacyl-coa (see paper)
24% identity, 69% coverage: 66:366/439 of query aligns to 124:435/503 of 3cw9A
- active site: T161 (≠ S98), R181 (≠ W118), H207 (≠ G144), T307 (≠ S245), E308 (= E246), I406 (= I337), N411 (= N342)
- binding 4-Chlorophenacyl-coenzyme A: M203 (≠ S140), P204 (≠ Y141), H207 (≠ G144), V208 (≠ L145), V209 (≠ T147), A280 (≠ G218), G305 (= G243), T306 (≠ L244), M310 (= M248), N311 (≠ G249), S407 (≠ I338), G408 (≠ R339), G409 (= G340), E410 (≠ V341)
- binding adenosine monophosphate: T161 (≠ S98), G281 (≠ A219), A282 (≠ E220), T283 (≠ P221), I303 (= I241), Y304 (= Y242), G305 (= G243), T306 (≠ L244), T307 (≠ S245), D385 (= D310), R400 (= R331), I406 (= I337), N411 (= N342)
Sites not aligning to the query:
Query Sequence
>PP_3279 FitnessBrowser__Putida:PP_3279
MNMYHDADRALLDPMETASVDALRQHQLERLRWSLKHAYDNVPLYRQRFAEYGIHPDDLK
CLEDLAKFPFTGKNDLRDNYPYGMFAVPQEEVVRLHASSGTTGKPTVVGYTQNDIDTWAN
VVARSIRAAGGRKGDKVHVSYGYGLFTGGLGAHYGAERLGCTVIPMSGGQTEKQVQLIRD
FHPDIIMVTPSYMLNLADEIERQGIDPHDLKLRLGIFGAEPWTDELRRSIEQRMGINALD
IYGLSEIMGPGVAMECIETKDGPTIWEDHFYPEIIDPATGEVLPDGQLGELVFTSLSKEA
LPMVRYRTRDLTRLLPGTARPMRRIGKITGRSDDMLIIRGVNVFPTQIEEQVLKIKQLSE
LYEIHLYRNGNLDSVQVHVELRAECQHLDEGQRKLVVGELSKQIKTYIGISTQVHLQPCG
TLKRSEGKACHVFDRRLAS
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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