SitesBLAST
Comparing 209425 MicrobesOnline__882:209425 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 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
42% identity, 97% coverage: 11:428/432 of query aligns to 14:433/435 of 4r1mA
- binding adenosine monophosphate: A215 (= A211), E216 (= E212), P217 (≠ A213), N236 (≠ D233), S237 (≠ I234), F238 (≠ A235), G239 (= G236), M240 (= M237), T241 (= T238), D305 (= D302), R329 (= R326), I335 (= I332), N340 (= N337)
- binding zinc ion: C252 (= C249), H259 (= H256), C314 (= C311), C316 (= C313)
4r1lA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.42 a resolution
42% identity, 97% coverage: 11:428/432 of query aligns to 14:431/433 of 4r1lA
- binding adenosine-5'-diphosphate: A215 (= A211), E216 (= E212), P217 (≠ A213), S237 (≠ I234), F238 (≠ A235), G239 (= G236), M240 (= M237), T241 (= T238), D305 (= D302), R329 (= R326), N340 (= N337)
- binding adenosine monophosphate: A215 (= A211), E216 (= E212), P217 (≠ A213), S237 (≠ I234), F238 (≠ A235), G239 (= G236), M240 (= M237), T241 (= T238), D305 (= D302), R329 (= R326), N340 (= N337)
- binding coenzyme a: S136 (≠ A133), A164 (≠ P161), G165 (= G162), N166 (= N163), S167 (≠ L164), I185 (≠ T182), Y188 (≠ M185), K337 (≠ R334), T408 (≠ R403)
- binding zinc ion: C252 (= C249), H259 (= H256), C314 (= C311), C316 (= C313)
2y27B Crystal structure of paak1 in complex with atp from burkholderia cenocepacia (see paper)
43% identity, 98% coverage: 4:428/432 of query aligns to 3:427/427 of 2y27B
- binding adenosine-5'-triphosphate: K65 (≠ V66), S90 (= S91), S91 (= S92), G92 (= G93), T93 (= T94), T94 (= T95), F138 (≠ W139), A211 (= A211), E212 (= E212), P213 (≠ A213), D232 (= D233), I233 (= I234), Y234 (≠ A235), G235 (= G236), L236 (≠ M237), S237 (≠ T238), D302 (= D302), I320 (= I323), R323 (= R326), K419 (= K420)
- binding magnesium ion: V200 (vs. gap), S202 (≠ I202), L204 (= L204), M226 (≠ L226), G227 (= G227), Q347 (≠ F350), L350 (≠ V353)
2y4nA Paak1 in complex with phenylacetyl adenylate (see paper)
43% identity, 98% coverage: 4:428/432 of query aligns to 3:425/426 of 2y4nA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: Y131 (≠ V134), F136 (≠ W139), G138 (≠ A141), G208 (= G210), A209 (= A211), E210 (= E212), P211 (≠ A213), I231 (= I234), Y232 (≠ A235), G233 (= G236), L234 (≠ M237), S235 (≠ T238), P240 (= P243), D300 (= D302), R321 (= R326), K417 (= K420)
- binding magnesium ion: V198 (vs. gap), S200 (≠ I202), Q345 (≠ F350), L348 (≠ V353)
2y4oA Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
43% identity, 96% coverage: 14:428/432 of query aligns to 15:432/433 of 2y4oA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ V134), F140 (≠ W139), A213 (= A211), E214 (= E212), P215 (≠ A213), I235 (= I234), G237 (= G236), L238 (≠ M237), S239 (≠ T238), P244 (= P243), D304 (= D302), R325 (= R326), I331 (= I332), N336 (= N337)
2y4oB Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
43% identity, 96% coverage: 14:428/432 of query aligns to 15:432/432 of 2y4oB
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ V134), F140 (≠ W139), G212 (= G210), A213 (= A211), E214 (= E212), P215 (≠ A213), I235 (= I234), G237 (= G236), L238 (≠ M237), S239 (≠ T238), P244 (= P243), D304 (= D302), R325 (= R326), I331 (= I332), N336 (= N337)
- binding magnesium ion: S204 (≠ I202), V228 (≠ L226)
6he0A Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in complex with 2-hib-amp and coa in the thioesterfication state (see paper)
30% identity, 94% coverage: 24:430/432 of query aligns to 45:466/477 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 (≠ G210), G242 (≠ A211), E243 (= E212), P244 (vs. gap), G267 (≠ A235), S268 (≠ G236), M269 (= M237), A270 (≠ T238), D335 (= D302), I357 (= I323), N371 (= N337)
- binding adenosine monophosphate: G242 (≠ A211), E243 (= E212), P244 (vs. gap), C266 (≠ I234), G267 (≠ A235), S268 (≠ G236), A270 (≠ T238), E271 (= E239), D335 (= D302), N371 (= N337)
- binding coenzyme a: Y166 (≠ W139), A188 (≠ P161), G189 (= G162), P191 (≠ L164), S194 (≠ Q167), Y210 (≠ C180), G211 (≠ S181), T212 (= T182), Y215 (≠ M185), H218 (≠ L188), R368 (= R334), G369 (= G335), M401 (≠ R367), V439 (≠ A402), R440 (= R403)
6hdyA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with s3-hb-amp (see paper)
29% identity, 94% coverage: 24:430/432 of query aligns to 45:463/474 of 6hdyA
- binding (3s)-3-hydroxybutanoic acid: Y162 (≠ W139), S237 (≠ G210), G263 (≠ A235), S264 (≠ G236), M265 (= M237), A266 (≠ T238), F271 (≠ Y241)
- 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 (≠ W139), G164 (≠ A141), S237 (≠ G210), G238 (≠ A211), E239 (= E212), P240 (vs. gap), C262 (≠ I234), G263 (≠ A235), S264 (≠ G236), A266 (≠ T238), F271 (≠ Y241), D331 (= D302), I353 (= I323), R356 (= R326), K453 (= K420)
6hdxA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with r3-hib-amp (see paper)
29% identity, 94% coverage: 24:430/432 of query aligns to 45:463/474 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 (≠ W139), G164 (≠ A141), S237 (≠ G210), G238 (≠ A211), E239 (= E212), P240 (vs. gap), C262 (≠ I234), G263 (≠ A235), S264 (≠ G236), A266 (≠ T238), F271 (≠ Y241), D331 (= D302), I353 (= I323), R356 (= R326), K453 (= K420)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: Y162 (≠ W139), G164 (≠ A141), S237 (≠ G210), G263 (≠ A235), S264 (≠ G236), A266 (≠ T238), F271 (≠ Y241)
6siyA Paak family amp-ligase with amp and substrate (see paper)
32% identity, 68% coverage: 35:327/432 of query aligns to 32:320/433 of 6siyA
- binding 3-hydroxyanthranilic acid: T125 (≠ V134), P126 (≠ G135), T132 (≠ A141), L135 (≠ G144), R153 (≠ G162), N177 (≠ T182), A209 (= A211), E232 (≠ I234), G234 (= G236), S235 (≠ M237)
- binding adenosine monophosphate: S85 (= S92), A209 (= A211), E210 (= E212), P211 (≠ A213), E232 (≠ I234), Y233 (≠ A235), G234 (= G236), S235 (≠ M237), T236 (= T238), D296 (= D302), V316 (≠ I323)
- binding magnesium ion: R75 (≠ E82), E76 (≠ K83), L78 (≠ V85), P117 (≠ Q126), G144 (= G153), A145 (= A154), T146 (≠ L155)
6siwA Paak family amp-ligase with amp (see paper)
32% identity, 68% coverage: 35:327/432 of query aligns to 31:319/432 of 6siwA
- binding adenosine monophosphate: S84 (= S92), A208 (= A211), E209 (= E212), P210 (≠ A213), E231 (≠ I234), Y232 (≠ A235), G233 (= G236), S234 (≠ M237), T235 (= T238), D295 (= D302), V315 (≠ I323)
- binding magnesium ion: E75 (≠ K83), L77 (≠ V85), S83 (= S91), P116 (≠ Q126), G143 (= G153), T145 (≠ L155), E236 (= E239)
- binding zinc ion: C244 (≠ A251), H250 (= H256), C304 (= C311), C306 (= C313)
6sixB Paak family amp-ligase with anp (see paper)
32% identity, 68% coverage: 35:327/432 of query aligns to 36:324/437 of 6sixB
- binding phosphoaminophosphonic acid-adenylate ester: S88 (= S91), S89 (= S92), A213 (= A211), E214 (= E212), P215 (≠ A213), E236 (≠ I234), Y237 (≠ A235), G238 (= G236), S239 (≠ M237), T240 (= T238), E241 (= E239), D300 (= D302), V320 (≠ I323), R323 (= R326)
- binding magnesium ion: R79 (≠ E82), E80 (≠ K83), P121 (≠ Q126), T150 (≠ L155)
- binding zinc ion: C249 (≠ A251), H255 (= H256), C309 (= C311), C311 (= C313)
5ja2A Entf, a terminal nonribosomal peptide synthetase module bound to the non-native mbth-like protein pa2412 (see paper)
28% identity, 78% coverage: 16:353/432 of query aligns to 499:859/1238 of 5ja2A
- active site: T580 (≠ S91), E727 (≠ D233), K838 (≠ I332), R843 (≠ N337)
- binding 5'-({[(2R,3S)-3-amino-4-hydroxy-2-{[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]sulfanyl}butyl]sulfonyl}amino)-5'-deoxyadenosine: F624 (vs. gap), D625 (≠ Q131), R650 (≠ T156), V670 (≠ T182), S699 (≠ G210), G700 (≠ A211), E701 (= E212), A702 (= A213), Y723 (≠ E229), G724 (= G230), P725 (≠ S231), T726 (≠ F232), V730 (≠ G236), D731 (≠ M237), D817 (≠ H322), Y829 (vs. gap), K838 (≠ I332), R840 (= R334), G841 (= G335), Q842 (≠ V336), R843 (≠ N337)
- binding Meso-2,3-Butanediol: S583 (≠ T94), S799 (vs. gap), R800 (= R305)
Sites not aligning to the query:
P11454 Enterobactin synthase component F; Enterochelin synthase F; Nonribosomal peptide synthetase EntF; EC 6.3.2.14; EC 6.2.1.72 from Escherichia coli (strain K12) (see 5 papers)
28% identity, 78% coverage: 16:353/432 of query aligns to 522:882/1293 of P11454
Sites not aligning to the query:
- 1006 modified: O-(pantetheine 4'-phosphoryl)serine
- 1077 F→A: Retains 2% of activity.
- 1079 W→A: Abolishes enterobactin production.
- 1080 Q→A: Retains 50% of activity.
- 1138 S→A: No enterobactin synthase activity. This mutant holo-EntF is still able to adenylate serine and to autoacylate itself with serine.; S→C: 1000-fold decrease in kcat. Releases both enterobactin an linear dimers (DHB-Ser)2.
- 1165 D→A: 20-fold decrease in kcat.; D→S: 200-fold decrease in kcat.
- 1271 H→A: 10000-fold decrease in kcat. Releases only enterobactin, but accumulates both DHB-Ser-O-TE and (DHB-Ser)2-O-TE acyl enzyme intermediates.
Query Sequence
>209425 MicrobesOnline__882:209425
MSQPYRFLPSLDEEKLHAIQLEGLRWTVRHAYEGSPRYRAKLRAAGVVPDDIVHLDDVRR
LPFTTVADLRDDYPLPLLSVPEKDVVRIHASSGTTGKRKILAYTQRDVDTFALQMARCYE
LAGLTQEDRVQIAVGYGLWTAGAGFQLGCERFGALTVPVGPGNLEMQLQLLTDLGVTCLC
STASMALLMAEEVERHGLRGDIRLRKVIFGAEAHSAKMRRTFEEKLGLEGSFDIAGMTEM
YGPGTGLECEAHDGIHYWADLFLVEILDPETLQPVEPGEVGEMVVTSLRKEASPLIRYRT
RDLTRLIPGTCSCGRNIPRHDHILGRSDDMIIFRGVNIYPGQIADVLHLFPEVGSEYHIE
LTRKEGRDHMLLKVERQPGAATGDERTLGVAIGNELHRKLMARVSVAVVAPGELPRSFAK
SKRVTDLRMVEG
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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