SitesBLAST
Comparing WP_084076515.1 NCBI__GCF_900129305.1:WP_084076515.1 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)
2y27B Crystal structure of paak1 in complex with atp from burkholderia cenocepacia (see paper)
57% identity, 98% coverage: 6:430/432 of query aligns to 7:427/427 of 2y27B
- binding adenosine-5'-triphosphate: K65 (= K64), S90 (= S89), S91 (= S90), G92 (= G91), T93 (= T92), T94 (= T93), F138 (= F137), A211 (= A210), E212 (= E211), P213 (= P212), D232 (= D231), I233 (= I232), Y234 (= Y233), G235 (= G234), L236 (= L235), S237 (= S236), D302 (= D301), I320 (≠ V322), R323 (= R325), K419 (= K422)
- binding magnesium ion: V200 (≠ K199), S202 (≠ L201), L204 (≠ F203), M226 (≠ L225), G227 (≠ N226), Q347 (≠ I349), L350 (≠ V352)
2y4nA Paak1 in complex with phenylacetyl adenylate (see paper)
57% identity, 99% coverage: 6:431/432 of query aligns to 7:426/426 of 2y4nA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: Y131 (= Y132), F136 (= F137), G138 (= G139), G208 (= G209), A209 (= A210), E210 (= E211), P211 (= P212), I231 (= I232), Y232 (= Y233), G233 (= G234), L234 (= L235), S235 (= S236), P240 (= P241), D300 (= D301), R321 (= R325), K417 (= K422)
- binding magnesium ion: V198 (≠ K199), S200 (≠ L201), Q345 (≠ I349), L348 (≠ V352)
2y4oA Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
55% identity, 99% coverage: 6:431/432 of query aligns to 9:433/433 of 2y4oA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ Y132), F140 (= F137), A213 (= A210), E214 (= E211), P215 (= P212), I235 (= I232), G237 (= G234), L238 (= L235), S239 (= S236), P244 (= P241), D304 (= D301), R325 (= R325), I331 (= I331), N336 (= N336)
2y4oB Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
55% identity, 98% coverage: 6:430/432 of query aligns to 9:432/432 of 2y4oB
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ Y132), F140 (= F137), G212 (= G209), A213 (= A210), E214 (= E211), P215 (= P212), I235 (= I232), G237 (= G234), L238 (= L235), S239 (= S236), P244 (= P241), D304 (= D301), R325 (= R325), I331 (= I331), N336 (= N336)
- binding magnesium ion: S204 (≠ L201), V228 (≠ L225)
4r1mA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.48 a resolution
47% identity, 99% coverage: 5:430/432 of query aligns to 10:433/435 of 4r1mA
- binding adenosine monophosphate: A215 (= A210), E216 (= E211), P217 (= P212), N236 (≠ D231), S237 (≠ I232), F238 (≠ Y233), G239 (= G234), M240 (≠ L235), T241 (≠ S236), D305 (= D301), R329 (= R325), I335 (= I331), N340 (= N336)
- binding zinc ion: C252 (= C247), H259 (= H255), C314 (= C310), C316 (= C312)
4r1lA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.42 a resolution
46% identity, 99% coverage: 5:430/432 of query aligns to 10:431/433 of 4r1lA
- binding adenosine-5'-diphosphate: A215 (= A210), E216 (= E211), P217 (= P212), S237 (≠ I232), F238 (≠ Y233), G239 (= G234), M240 (≠ L235), T241 (≠ S236), D305 (= D301), R329 (= R325), N340 (= N336)
- binding adenosine monophosphate: A215 (= A210), E216 (= E211), P217 (= P212), S237 (≠ I232), F238 (≠ Y233), G239 (= G234), M240 (≠ L235), T241 (≠ S236), D305 (= D301), R329 (= R325), N340 (= N336)
- binding coenzyme a: S136 (≠ A131), A164 (≠ G159), G165 (= G160), N166 (= N161), S167 (≠ T162), I185 (≠ T180), Y188 (= Y183), K337 (≠ R333), T408 (≠ S405)
- binding zinc ion: C252 (= C247), H259 (= H255), C314 (= C310), C316 (= C312)
6he0A Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in complex with 2-hib-amp and coa in the thioesterfication state (see paper)
34% identity, 99% coverage: 7:432/432 of query aligns to 30:466/477 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 (≠ G209), G242 (≠ A210), E243 (= E211), P244 (= P212), G267 (≠ Y233), S268 (≠ G234), M269 (≠ L235), A270 (≠ S236), D335 (= D301), I357 (≠ V322), N371 (= N336)
- binding adenosine monophosphate: G242 (≠ A210), E243 (= E211), P244 (= P212), C266 (≠ I232), G267 (≠ Y233), S268 (≠ G234), A270 (≠ S236), E271 (= E237), D335 (= D301), N371 (= N336)
- binding coenzyme a: Y166 (≠ F137), A188 (≠ G159), G189 (= G160), P191 (vs. gap), S194 (≠ T162), Y210 (≠ T178), G211 (≠ C179), T212 (= T180), Y215 (= Y183), H218 (= H186), R368 (= R333), G369 (= G334), M401 (≠ L366), V439 (= V404), R440 (≠ S405)
6hdyA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with s3-hb-amp (see paper)
33% identity, 99% coverage: 7:432/432 of query aligns to 30:463/474 of 6hdyA
- binding (3s)-3-hydroxybutanoic acid: Y162 (≠ F137), S237 (≠ G209), G263 (≠ Y233), S264 (≠ G234), M265 (≠ L235), A266 (≠ S236), F271 (≠ G242)
- 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 (≠ F137), G164 (= G139), S237 (≠ G209), G238 (≠ A210), E239 (= E211), P240 (= P212), C262 (≠ I232), G263 (≠ Y233), S264 (≠ G234), A266 (≠ S236), F271 (≠ G242), D331 (= D301), I353 (≠ V322), R356 (= R325), K453 (= K422)
6hdxA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with r3-hib-amp (see paper)
33% identity, 99% coverage: 7:432/432 of query aligns to 30:463/474 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 (≠ F137), G164 (= G139), S237 (≠ G209), G238 (≠ A210), E239 (= E211), P240 (= P212), C262 (≠ I232), G263 (≠ Y233), S264 (≠ G234), A266 (≠ S236), F271 (≠ G242), D331 (= D301), I353 (≠ V322), R356 (= R325), K453 (= K422)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: Y162 (≠ F137), G164 (= G139), S237 (≠ G209), G263 (≠ Y233), S264 (≠ G234), A266 (≠ S236), F271 (≠ G242)
6sixB Paak family amp-ligase with anp (see paper)
32% identity, 69% coverage: 15:313/432 of query aligns to 17:312/437 of 6sixB
- binding phosphoaminophosphonic acid-adenylate ester: S88 (= S89), S89 (= S90), A213 (= A210), E214 (= E211), P215 (= P212), E236 (≠ I232), Y237 (= Y233), G238 (= G234), S239 (≠ L235), T240 (≠ S236), E241 (= E237), D300 (= D301)
- binding magnesium ion: R79 (≠ M80), E80 (≠ D81), P121 (≠ A122), T150 (≠ S153)
- binding zinc ion: C249 (= C247), H255 (= H255), C309 (= C310), C311 (= C312)
Sites not aligning to the query:
6siwA Paak family amp-ligase with amp (see paper)
32% identity, 69% coverage: 15:313/432 of query aligns to 12:307/432 of 6siwA
- binding adenosine monophosphate: S84 (= S90), A208 (= A210), E209 (= E211), P210 (= P212), E231 (≠ I232), Y232 (= Y233), G233 (= G234), S234 (≠ L235), T235 (≠ S236), D295 (= D301)
- binding magnesium ion: E75 (≠ D81), L77 (≠ V83), S83 (= S89), P116 (≠ A122), G143 (= G151), T145 (≠ S153), E236 (= E237)
- binding zinc ion: C244 (= C247), H250 (= H255), C304 (= C310), C306 (= C312)
Sites not aligning to the query:
6siyA Paak family amp-ligase with amp and substrate (see paper)
32% identity, 69% coverage: 15:313/432 of query aligns to 13:308/433 of 6siyA
- binding 3-hydroxyanthranilic acid: T125 (≠ N130), P126 (≠ A131), T132 (= T138), L135 (= L141), R153 (≠ G160), N177 (≠ T180), A209 (= A210), E232 (≠ I232), G234 (= G234), S235 (≠ L235)
- binding adenosine monophosphate: S85 (= S90), A209 (= A210), E210 (= E211), P211 (= P212), E232 (≠ I232), Y233 (= Y233), G234 (= G234), S235 (≠ L235), T236 (≠ S236), D296 (= D301)
- binding magnesium ion: R75 (≠ M80), E76 (≠ D81), L78 (≠ V83), P117 (≠ A122), G144 (= G151), A145 (= A152), T146 (≠ S153)
Sites not aligning to the query:
3cw8X 4-chlorobenzoyl-coa ligase/synthetase, bound to 4cba-adenylate (see paper)
23% identity, 66% coverage: 67:352/432 of query aligns to 133:427/501 of 3cw8X
- binding 5'-O-[(S)-{[(4-chlorophenyl)carbonyl]oxy}(hydroxy)phosphoryl]adenosine: H207 (≠ L136), V208 (≠ F137), V209 (≠ T138), G281 (≠ A210), A282 (≠ E211), T283 (≠ P212), I303 (= I232), Y304 (= Y233), G305 (= G234), T306 (≠ L235), T307 (≠ S236), M310 (≠ I239), N311 (≠ G240), M324 (≠ I256), D385 (= D301)
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
25% identity, 63% coverage: 81:353/432 of query aligns to 156:425/503 of P9WQ37
- K172 (≠ T97) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ A120) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A122) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ Y134) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ L136) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ G139) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ G173) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G234) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (≠ R296) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D301) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R325) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ I332) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G334) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- 487 K→A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3cw9A 4-chlorobenzoyl-coa ligase/synthetase in the thioester-forming conformation, bound to 4-chlorophenacyl-coa (see paper)
23% identity, 66% coverage: 67:352/432 of query aligns to 133:427/503 of 3cw9A
- active site: T161 (≠ S89), R181 (≠ W109), H207 (≠ L136), T307 (≠ S236), E308 (= E237), I406 (= I331), N411 (= N336)
- binding 4-Chlorophenacyl-coenzyme A: M203 (≠ Y132), P204 (≠ G133), H207 (≠ L136), V208 (≠ F137), V209 (≠ T138), A280 (≠ G209), G305 (= G234), T306 (≠ L235), M310 (≠ I239), N311 (≠ G240), S407 (≠ I332), G408 (≠ R333), G409 (= G334), E410 (≠ V335)
- binding adenosine monophosphate: T161 (≠ S89), G281 (≠ A210), A282 (≠ E211), T283 (≠ P212), I303 (= I232), Y304 (= Y233), G305 (= G234), T306 (≠ L235), T307 (≠ S236), D385 (= D301), R400 (= R325), I406 (= I331), N411 (= N336)
Sites not aligning to the query:
1t5dX 4-chlorobenzoyl-coa ligase/synthetase bound to 4-chlorobenzoate (see paper)
25% identity, 43% coverage: 166:352/432 of query aligns to 235:425/502 of 1t5dX
Sites not aligning to the query:
3dlpX 4-chlorobenzoyl-coa ligase/synthetase, mutant d402p, bound to 4cb (see paper)
23% identity, 66% coverage: 67:352/432 of query aligns to 133:427/504 of 3dlpX
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 40% coverage: 181:352/432 of query aligns to 252:424/502 of 3r44A
Sites not aligning to the query:
2qvxX 4-chlorobenzoyl-coa ligase/synthetase, i303g mutation, bound to 3- chlorobenzoate (see paper)
25% identity, 43% coverage: 166:352/432 of query aligns to 235:425/500 of 2qvxX
Sites not aligning to the query:
2qvyX 4-chlorobenzoyl-coa ligase/synthetase, i303g mutation, bound to 3,4- dichlorobenzoate (see paper)
25% identity, 43% coverage: 166:352/432 of query aligns to 233:423/499 of 2qvyX
Sites not aligning to the query:
Query Sequence
>WP_084076515.1 NCBI__GCF_900129305.1:WP_084076515.1
MHDIEFETMPREALEAIQLRRLQATLQRVYATVPFYRKRFDEAGFKPADMKSLDDLRRVP
FTTKQDLRDNYPFGLFAVPMDNVVRIHASSGTTGKPTVVGYTARDVNTWAELMARSLAAA
GATRGDIIHNAYGYGLFTGGLGVHYGAERLGASVIPISGGNTKRQIMIMKDFGATILTCT
PSYALHLAEVAEEMGVDFKDLKFKAGIFGAEPWSEKMRHEIEKKLNLDAVDIYGLSEVIG
PGVAVECLEAKAGLHIFEDHFIPEIINPETGEVLPYGETGELVFTSITKEAFPVIRYRTR
DITSLNPEPCICGRTHVRMNRVSGRTDDMLIIRGVNVFPSQIESVLMEIDGVEPHYQLVV
DREGTLDMLTVMVEVGEKAFTDEIKGLQHLEKLIAKNIKEYLGVSAKVKLVEPKSIARSE
GKAVRVIDNRKL
Or try a new SitesBLAST search
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