SitesBLAST
Comparing WP_093395010.1 NCBI__GCF_900114975.1:WP_093395010.1 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 13 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
57% identity, 97% coverage: 7:434/442 of query aligns to 7:433/435 of 4r1mA
- binding adenosine monophosphate: A215 (= A215), E216 (= E216), P217 (= P217), N236 (= N236), S237 (= S237), F238 (≠ Y238), G239 (= G239), M240 (≠ L240), T241 (≠ S241), D305 (= D305), R329 (= R329), I335 (= I335), N340 (= N340)
- binding zinc ion: C252 (= C252), H259 (= H259), C314 (= C314), C316 (= C316)
4r1lA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.42 a resolution
56% identity, 97% coverage: 7:434/442 of query aligns to 7:431/433 of 4r1lA
- binding adenosine-5'-diphosphate: A215 (= A215), E216 (= E216), P217 (= P217), S237 (= S237), F238 (≠ Y238), G239 (= G239), M240 (≠ L240), T241 (≠ S241), D305 (= D305), R329 (= R329), N340 (= N340)
- binding adenosine monophosphate: A215 (= A215), E216 (= E216), P217 (= P217), S237 (= S237), F238 (≠ Y238), G239 (= G239), M240 (≠ L240), T241 (≠ S241), D305 (= D305), R329 (= R329), N340 (= N340)
- binding coenzyme a: S136 (≠ M135), A164 (= A163), G165 (= G164), N166 (= N165), S167 (= S166), I185 (= I184), Y188 (= Y187), K337 (= K337), T408 (= T409)
- binding zinc ion: C252 (= C252), H259 (= H259), C314 (= C314), C316 (= C316)
2y27B Crystal structure of paak1 in complex with atp from burkholderia cenocepacia (see paper)
47% identity, 96% coverage: 12:434/442 of query aligns to 8:427/427 of 2y27B
- binding adenosine-5'-triphosphate: K65 (= K68), S90 (= S93), S91 (= S94), G92 (= G95), T93 (= T96), T94 (= T97), F138 (= F141), A211 (= A215), E212 (= E216), P213 (= P217), D232 (≠ N236), I233 (≠ S237), Y234 (= Y238), G235 (= G239), L236 (= L240), S237 (= S241), D302 (= D305), I320 (= I326), R323 (= R329), K419 (= K426)
- binding magnesium ion: V200 (≠ R203), S202 (≠ D205), L204 (= L208), M226 (≠ Y230), G227 (= G231), Q347 (≠ I353), L350 (≠ V356)
2y4nA Paak1 in complex with phenylacetyl adenylate (see paper)
46% identity, 96% coverage: 12:434/442 of query aligns to 8:425/426 of 2y4nA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: Y131 (≠ S136), F136 (= F141), G138 (= G143), G208 (= G214), A209 (= A215), E210 (= E216), P211 (= P217), I231 (≠ S237), Y232 (= Y238), G233 (= G239), L234 (= L240), S235 (= S241), P240 (= P246), D300 (= D305), R321 (= R329), K417 (= K426)
- binding magnesium ion: V198 (≠ R203), S200 (≠ D205), Q345 (≠ I353), L348 (≠ V356)
2y4oB Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
44% identity, 96% coverage: 12:434/442 of query aligns to 10:432/432 of 2y4oB
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ S136), F140 (= F141), G212 (= G214), A213 (= A215), E214 (= E216), P215 (= P217), I235 (≠ S237), G237 (= G239), L238 (= L240), S239 (= S241), P244 (= P246), D304 (= D305), R325 (= R329), I331 (= I335), N336 (= N340)
- binding magnesium ion: S204 (≠ D205), V228 (≠ Y230)
2y4oA Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
44% identity, 96% coverage: 12:434/442 of query aligns to 10:432/433 of 2y4oA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ S136), F140 (= F141), A213 (= A215), E214 (= E216), P215 (= P217), I235 (≠ S237), G237 (= G239), L238 (= L240), S239 (= S241), P244 (= P246), D304 (= D305), R325 (= R329), I331 (= I335), N336 (= N340)
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, 98% coverage: 2:434/442 of query aligns to 20:464/477 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 (≠ G214), G242 (≠ A215), E243 (= E216), P244 (= P217), G267 (≠ Y238), S268 (≠ G239), M269 (≠ L240), A270 (≠ S241), D335 (= D305), I357 (= I326), N371 (= N340)
- binding adenosine monophosphate: G242 (≠ A215), E243 (= E216), P244 (= P217), C266 (≠ S237), G267 (≠ Y238), S268 (≠ G239), A270 (≠ S241), E271 (= E242), D335 (= D305), N371 (= N340)
- binding coenzyme a: Y166 (≠ F141), A188 (= A163), G189 (= G164), P191 (vs. gap), S194 (= S166), Y210 (≠ H182), G211 (≠ V183), T212 (≠ I184), Y215 (= Y187), H218 (≠ R190), R368 (≠ K337), G369 (= G338), M401 (≠ L370), V439 (= V408), R440 (≠ T409)
6hdyA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with s3-hb-amp (see paper)
33% identity, 98% coverage: 2:434/442 of query aligns to 20:461/474 of 6hdyA
- binding (3s)-3-hydroxybutanoic acid: Y162 (≠ F141), S237 (≠ G214), G263 (≠ Y238), S264 (≠ G239), M265 (≠ L240), A266 (≠ S241), F271 (≠ G247)
- 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 (≠ G214), G238 (≠ A215), E239 (= E216), P240 (= P217), C262 (≠ S237), G263 (≠ Y238), S264 (≠ G239), A266 (≠ S241), F271 (≠ G247), D331 (= D305), I353 (= I326), R356 (= R329), K453 (= K426)
6hdxA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with r3-hib-amp (see paper)
33% identity, 98% coverage: 2:434/442 of query aligns to 20:461/474 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 (≠ F141), G164 (= G143), S237 (≠ G214), G238 (≠ A215), E239 (= E216), P240 (= P217), C262 (≠ S237), G263 (≠ Y238), S264 (≠ G239), A266 (≠ S241), F271 (≠ G247), D331 (= D305), I353 (= I326), R356 (= R329), K453 (= K426)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: Y162 (≠ F141), G164 (= G143), S237 (≠ G214), G263 (≠ Y238), S264 (≠ G239), A266 (≠ S241), F271 (≠ G247)
6siyA Paak family amp-ligase with amp and substrate (see paper)
29% identity, 88% coverage: 18:406/442 of query aligns to 13:383/433 of 6siyA
- binding 3-hydroxyanthranilic acid: T125 (≠ S136), P126 (≠ G137), T132 (≠ G143), L135 (≠ G146), R153 (vs. gap), N177 (≠ I184), A209 (= A215), E232 (≠ S237), G234 (= G239), S235 (≠ L240)
- binding adenosine monophosphate: S85 (= S94), A209 (= A215), E210 (= E216), P211 (= P217), E232 (≠ S237), Y233 (= Y238), G234 (= G239), S235 (≠ L240), T236 (≠ S241), D296 (= D305), V316 (≠ I326)
- binding magnesium ion: R75 (= R84), E76 (≠ D85), L78 (= L87), P117 (= P128), G144 (= G155), A145 (≠ I156), T146 (≠ L157)
6siwA Paak family amp-ligase with amp (see paper)
29% identity, 88% coverage: 18:406/442 of query aligns to 12:382/432 of 6siwA
- binding adenosine monophosphate: S84 (= S94), A208 (= A215), E209 (= E216), P210 (= P217), E231 (≠ S237), Y232 (= Y238), G233 (= G239), S234 (≠ L240), T235 (≠ S241), D295 (= D305), V315 (≠ I326)
- binding magnesium ion: E75 (≠ D85), L77 (= L87), S83 (= S93), P116 (= P128), G143 (= G155), T145 (≠ L157), E236 (= E242)
- binding zinc ion: C244 (= C252), H250 (= H259), C304 (= C314), C306 (= C316)
6sixB Paak family amp-ligase with anp (see paper)
29% identity, 88% coverage: 18:406/442 of query aligns to 17:387/437 of 6sixB
- binding phosphoaminophosphonic acid-adenylate ester: S88 (= S93), S89 (= S94), A213 (= A215), E214 (= E216), P215 (= P217), E236 (≠ S237), Y237 (= Y238), G238 (= G239), S239 (≠ L240), T240 (≠ S241), E241 (= E242), D300 (= D305), V320 (≠ I326), R323 (= R329)
- binding magnesium ion: R79 (= R84), E80 (≠ D85), P121 (= P128), T150 (≠ L157)
- binding zinc ion: C249 (= C252), H255 (= H259), C309 (= C314), C311 (= C316)
3pbkA Structural and functional studies of fatty acyl-adenylate ligases from e. Coli and l. Pneumophila (see paper)
29% identity, 24% coverage: 326:429/442 of query aligns to 443:541/555 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
>WP_093395010.1 NCBI__GCF_900114975.1:WP_093395010.1
MAQIKAWNPEREFLTRDELINLQEERFLKTVARAWESPFYRKKFSELGLSPSDIKGLSDL
SRLPFTTKDDLRSAYPYGFLTVSRDRLVRLHVSSGTTGRATAVFYTRRDIDSWAELMARC
FCMTGAGPGDVFQNMSGYGLFTGGLGFHYGAEKVGILTIPSGAGNSKRQIQLMKDFGTTV
IHVIPSYALRLMDVCQEMGVNPREDLNLRIGYLGAEPYSEEVRQRVQNFYGIRVYNSYGL
SEMNGPGVAFECLYQSGLHLWEDAYLMEVIDPDTLEPVPDGTIGELVLTTLDREGMPLIR
YRTRDLTRIIPGQCPCGRPHRRIDRIQGRSDDMFIIKGVNIFPIQVEQVLMAIPEVGSNY
RIVLTREDNLDQMTVQVEVTDRVFIEDMRHLHKLREKIAKELKSELLVTPRVELVEPNGL
PGGEGKAVRLIDLRGKSGEGGV
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