SitesBLAST
Comparing 349956 FitnessBrowser__Btheta:349956 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 16 hits to proteins with known functional sites (download)
4r1mA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.48 a resolution
100% identity, 100% coverage: 1:434/435 of query aligns to 2:435/435 of 4r1mA
- binding adenosine monophosphate: A215 (= A214), E216 (= E215), P217 (= P216), N236 (= N235), S237 (= S236), F238 (= F237), G239 (= G238), M240 (= M239), T241 (= T240), D305 (= D304), R329 (= R328), I335 (= I334), N340 (= N339)
- binding zinc ion: C252 (= C251), H259 (= H258), C314 (= C313), C316 (= C315)
4r1lA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.42 a resolution
100% identity, 100% coverage: 1:434/435 of query aligns to 2:433/433 of 4r1lA
- binding adenosine-5'-diphosphate: A215 (= A214), E216 (= E215), P217 (= P216), S237 (= S236), F238 (= F237), G239 (= G238), M240 (= M239), T241 (= T240), D305 (= D304), R329 (= R328), N340 (= N339)
- binding adenosine monophosphate: A215 (= A214), E216 (= E215), P217 (= P216), S237 (= S236), F238 (= F237), G239 (= G238), M240 (= M239), T241 (= T240), D305 (= D304), R329 (= R328), N340 (= N339)
- binding coenzyme a: S136 (= S135), A164 (= A163), G165 (= G164), N166 (= N165), S167 (= S166), I185 (= I184), Y188 (= Y187), K337 (= K336), T408 (= T407)
- binding zinc ion: C252 (= C251), H259 (= H258), C314 (= C313), C316 (= C315)
2y4oB Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
44% identity, 98% coverage: 8:432/435 of query aligns to 7:432/432 of 2y4oB
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ S136), F140 (= F141), G212 (= G213), A213 (= A214), E214 (= E215), P215 (= P216), I235 (≠ S236), G237 (= G238), L238 (≠ M239), S239 (≠ T240), P244 (= P245), D304 (= D304), R325 (= R328), I331 (= I334), N336 (= N339)
- binding magnesium ion: S204 (≠ T205), V228 (≠ L229)
2y4oA Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
44% identity, 98% coverage: 8:432/435 of query aligns to 7:432/433 of 2y4oA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ S136), F140 (= F141), A213 (= A214), E214 (= E215), P215 (= P216), I235 (≠ S236), G237 (= G238), L238 (≠ M239), S239 (≠ T240), P244 (= P245), D304 (= D304), R325 (= R328), I331 (= I334), N336 (= N339)
2y27B Crystal structure of paak1 in complex with atp from burkholderia cenocepacia (see paper)
43% identity, 98% coverage: 8:432/435 of query aligns to 5:427/427 of 2y27B
- binding adenosine-5'-triphosphate: K65 (= K67), S90 (= S93), S91 (= S94), G92 (= G95), T93 (= T96), T94 (= T97), F138 (= F141), A211 (= A214), E212 (= E215), P213 (= P216), D232 (≠ N235), I233 (≠ S236), Y234 (≠ F237), G235 (= G238), L236 (≠ M239), S237 (≠ T240), D302 (= D304), I320 (= I325), R323 (= R328), K419 (= K424)
- binding magnesium ion: V200 (≠ R203), S202 (≠ T205), L204 (= L207), M226 (≠ L229), G227 (≠ N230), Q347 (≠ F352), L350 (= L355)
2y4nA Paak1 in complex with phenylacetyl adenylate (see paper)
42% identity, 98% coverage: 8:432/435 of query aligns to 5:425/426 of 2y4nA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: Y131 (≠ S136), F136 (= F141), G138 (= G143), G208 (= G213), A209 (= A214), E210 (= E215), P211 (= P216), I231 (≠ S236), Y232 (≠ F237), G233 (= G238), L234 (≠ M239), S235 (≠ T240), P240 (= P245), D300 (= D304), R321 (= R328), K417 (= K424)
- binding magnesium ion: V198 (≠ R203), S200 (≠ T205), Q345 (≠ F352), L348 (= L355)
6he0A Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in complex with 2-hib-amp and coa in the thioesterfication state (see paper)
33% identity, 99% coverage: 3:433/435 of query aligns to 22:465/477 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 (≠ G213), G242 (≠ A214), E243 (= E215), P244 (= P216), G267 (≠ F237), S268 (≠ G238), M269 (= M239), A270 (≠ T240), D335 (= D304), I357 (= I325), N371 (= N339)
- binding adenosine monophosphate: G242 (≠ A214), E243 (= E215), P244 (= P216), C266 (≠ S236), G267 (≠ F237), S268 (≠ G238), A270 (≠ T240), E271 (= E241), D335 (= D304), N371 (= N339)
- binding coenzyme a: Y166 (≠ F141), A188 (vs. gap), G189 (≠ A161), P191 (≠ A163), S194 (= S166), Y210 (≠ H182), G211 (≠ A183), T212 (≠ I184), Y215 (= Y187), H218 (≠ R190), R368 (≠ K336), G369 (= G337), M401 (≠ Q369), V439 (= V406), R440 (≠ T407)
6hdyA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with s3-hb-amp (see paper)
32% identity, 99% coverage: 3:433/435 of query aligns to 22:462/474 of 6hdyA
- binding (3s)-3-hydroxybutanoic acid: Y162 (≠ F141), S237 (≠ G213), G263 (≠ F237), S264 (≠ G238), M265 (= M239), A266 (≠ T240), F271 (vs. gap)
- 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 (≠ F141), G164 (= G143), S237 (≠ G213), G238 (≠ A214), E239 (= E215), P240 (= P216), C262 (≠ S236), G263 (≠ F237), S264 (≠ G238), A266 (≠ T240), F271 (vs. gap), D331 (= D304), I353 (= I325), R356 (= R328), K453 (= K424)
6hdxA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with r3-hib-amp (see paper)
32% identity, 99% coverage: 3:433/435 of query aligns to 22:462/474 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 (≠ F141), G164 (= G143), S237 (≠ G213), G238 (≠ A214), E239 (= E215), P240 (= P216), C262 (≠ S236), G263 (≠ F237), S264 (≠ G238), A266 (≠ T240), F271 (vs. gap), D331 (= D304), I353 (= I325), R356 (= R328), K453 (= K424)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: Y162 (≠ F141), G164 (= G143), S237 (≠ G213), G263 (≠ F237), S264 (≠ G238), A266 (≠ T240), F271 (vs. gap)
6sixB Paak family amp-ligase with anp (see paper)
28% identity, 78% coverage: 14:353/435 of query aligns to 14:348/437 of 6sixB
- binding phosphoaminophosphonic acid-adenylate ester: S88 (= S93), S89 (= S94), A213 (= A214), E214 (= E215), P215 (= P216), E236 (≠ S236), Y237 (≠ F237), G238 (= G238), S239 (≠ M239), T240 (= T240), E241 (= E241), D300 (= D304), V320 (≠ I325), R323 (= R328)
- binding magnesium ion: R79 (= R85), E80 (≠ D86), P121 (≠ K128), T150 (≠ L157)
- binding zinc ion: C249 (= C251), H255 (= H258), C309 (= C313), C311 (= C315)
6siwA Paak family amp-ligase with amp (see paper)
28% identity, 78% coverage: 14:353/435 of query aligns to 9:343/432 of 6siwA
- binding adenosine monophosphate: S84 (= S94), A208 (= A214), E209 (= E215), P210 (= P216), E231 (≠ S236), Y232 (≠ F237), G233 (= G238), S234 (≠ M239), T235 (= T240), D295 (= D304), V315 (≠ I325)
- binding magnesium ion: E75 (≠ D86), L77 (≠ V88), S83 (= S93), P116 (≠ K128), G143 (= G155), T145 (≠ L157), E236 (= E241)
- binding zinc ion: C244 (= C251), H250 (= H258), C304 (= C313), C306 (= C315)
6siyA Paak family amp-ligase with amp and substrate (see paper)
28% identity, 78% coverage: 14:353/435 of query aligns to 10:344/433 of 6siyA
- binding 3-hydroxyanthranilic acid: T125 (≠ S136), P126 (≠ G137), T132 (≠ G143), L135 (≠ G146), R153 (vs. gap), N177 (≠ I184), A209 (= A214), E232 (≠ S236), G234 (= G238), S235 (≠ M239)
- binding adenosine monophosphate: S85 (= S94), A209 (= A214), E210 (= E215), P211 (= P216), E232 (≠ S236), Y233 (≠ F237), G234 (= G238), S235 (≠ M239), T236 (= T240), D296 (= D304), V316 (≠ I325)
- binding magnesium ion: R75 (= R85), E76 (≠ D86), L78 (≠ V88), P117 (≠ K128), G144 (= G155), A145 (≠ C156), T146 (≠ L157)
P40806 Polyketide synthase PksJ; PKS from Bacillus subtilis (strain 168) (see paper)
24% identity, 77% coverage: 93:429/435 of query aligns to 195:553/5043 of P40806
Sites not aligning to the query:
- 1689 modified: O-(pantetheine 4'-phosphoryl)serine
6m2uA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-chloro-1,3-thiazole-5-carboxylate-amp (see paper)
25% identity, 60% coverage: 93:353/435 of query aligns to 176:441/518 of 6m2uA
- active site: S176 (= S93), T196 (≠ W113), T324 (= T240), E325 (= E241), K422 (≠ I334), Y427 (≠ N339)
- binding adenosine monophosphate: G298 (≠ A214), E299 (= E215), A300 (≠ P216), D319 (≠ N235), G320 (≠ S236), I321 (≠ F237), G322 (= G238), T324 (= T240), D401 (≠ R317), R416 (= R328), K422 (≠ I334), Y427 (≠ N339)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ G143), A297 (≠ G213), G322 (= G238), S323 (≠ M239), A328 (≠ G244)
Sites not aligning to the query:
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
25% identity, 60% coverage: 93:353/435 of query aligns to 176:441/518 of 6m2tA
- active site: S176 (= S93), T196 (≠ W113), T324 (= T240), E325 (= E241), K422 (≠ I334), Y427 (≠ N339)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ G143), G322 (= G238), S323 (≠ M239), A328 (≠ G244)
- binding adenosine monophosphate: G298 (≠ A214), E299 (= E215), A300 (≠ P216), G320 (≠ S236), I321 (≠ F237), S323 (≠ M239), T324 (= T240), D401 (≠ R317), R416 (= R328), K422 (≠ I334), Y427 (≠ N339)
Sites not aligning to the query:
3pbkA Structural and functional studies of fatty acyl-adenylate ligases from e. Coli and l. Pneumophila (see paper)
30% identity, 24% coverage: 325:429/435 of query aligns to 443:543/555 of 3pbkA
Sites not aligning to the query:
- active site: 171, 191, 216, 327, 328
- binding 5'-O-[(S)-(dodecanoyloxy)(hydroxy)phosphoryl]adenosine: 217, 222, 295, 296, 297, 323, 324, 325, 326, 327, 331, 432
Query Sequence
>349956 FitnessBrowser__Btheta:349956
MSTQYWEEEIEIMSREKLQELQLQRLKKTINIAANSPYYKEVFSKNGITGDSIQSLDDIR
KIPFTTKSDMRANYPFGLVAGDMKRDGVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARC
LYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTVPAAAGNSKRQIKFISDFKTTA
LHAIPSYAIRLAEVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMT
EMNGPGVAFECQEQNGMHFWEDCYLVEIIDPETGEPVPEGEIGELVLTTLDREMMPLIRY
RTRDLTRILPGKCPCGRTHLRIDRIKGRSDDMFIIKGVNIFPMQVEKILVQFPELGSNYL
ITLETVNNQDEMIVEVELSDLSTDNYIELEKIRRDIIRQLKDEILVTPKVKLVKKGSLPQ
SEGKAVRVKDLRDNK
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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