SitesBLAST
Comparing BPHYT_RS21775 FitnessBrowser__BFirm:BPHYT_RS21775 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)
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 91% coverage: 43:547/553 of query aligns to 28:497/512 of O74976
- S283 (= S330) modified: Phosphoserine
- S284 (≠ A331) modified: Phosphoserine
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
33% identity, 90% coverage: 43:539/553 of query aligns to 31:494/504 of 6qjzA
- active site: T169 (= T214), S189 (≠ N234), H213 (= H258), T314 (= T356), E315 (= E357), N414 (≠ I456), K419 (≠ N461)
- binding adenosine monophosphate: H213 (= H258), S288 (= S330), A289 (= A331), S290 (≠ A332), A312 (≠ G354), M313 (= M355), T314 (= T356), D393 (= D435), L405 (≠ I447), K410 (= K452), K419 (≠ N461)
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 95% coverage: 20:547/553 of query aligns to 2:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 214:218) binding
- H214 (= H258) binding ; mutation to A: Abolished activity.
- S289 (= S330) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAA 330:332) binding
- EA 310:311 (≠ ET 351:352) binding
- M314 (= M355) binding
- T315 (= T356) binding
- H319 (≠ A360) binding ; mutation to A: Abolished activity.
- D394 (= D435) binding
- R409 (= R450) binding ; mutation to A: Abolished activity.
- K500 (= K544) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
33% identity, 95% coverage: 20:547/553 of query aligns to 2:496/504 of 5ie3A
- active site: T163 (= T214), S183 (≠ N234), H207 (= H258), T308 (= T356), E309 (= E357), N408 (≠ I456), K413 (≠ N461), K493 (= K544)
- binding adenosine monophosphate: S164 (= S215), S282 (= S330), A283 (= A331), S284 (≠ A332), Y305 (≠ M353), A306 (≠ G354), M307 (= M355), T308 (= T356), D387 (= D435), L399 (≠ I447), R402 (= R450), K493 (= K544)
- binding oxalic acid: V208 (≠ I259), S282 (= S330), A306 (≠ G354), M307 (= M355), H312 (≠ A360), K493 (= K544)
5ie2A Crystal structure of a plant enzyme (see paper)
33% identity, 95% coverage: 20:547/553 of query aligns to 2:498/506 of 5ie2A
- active site: T165 (= T214), S185 (≠ N234), H209 (= H258), T310 (= T356), E311 (= E357), N410 (≠ I456), K415 (≠ N461), K495 (= K544)
- binding adenosine-5'-triphosphate: T165 (= T214), S166 (= S215), G167 (= G216), T168 (= T217), T169 (= T218), S284 (= S330), A285 (= A331), S286 (≠ A332), Y307 (≠ M353), A308 (≠ G354), M309 (= M355), T310 (= T356), D389 (= D435), L401 (≠ I447), R404 (= R450), K495 (= K544)
P38137 Oxalate--CoA ligase; Acyl-activating enzyme 3; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
37% identity, 62% coverage: 205:547/553 of query aligns to 188:526/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
30% identity, 99% coverage: 6:550/553 of query aligns to 24:549/561 of P69451
- Y213 (= Y213) mutation to A: Loss of activity.
- T214 (= T214) mutation to A: 10% of wild-type activity.
- G216 (= G216) mutation to A: Decreases activity.
- T217 (= T217) mutation to A: Decreases activity.
- G219 (= G219) mutation to A: Decreases activity.
- K222 (= K222) mutation to A: Decreases activity.
- E361 (= E357) mutation to A: Loss of activity.
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
31% identity, 92% coverage: 44:550/553 of query aligns to 66:569/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
37% identity, 62% coverage: 205:547/553 of query aligns to 154:494/506 of 4gxqA
- active site: T163 (= T214), N183 (= N234), H207 (= H258), T303 (= T356), E304 (= E357), I403 (= I456), N408 (= N461), A491 (≠ K544)
- binding adenosine-5'-triphosphate: T163 (= T214), S164 (= S215), G165 (= G216), T166 (= T217), T167 (= T218), H207 (= H258), S277 (= S330), A278 (= A331), P279 (≠ A332), E298 (= E351), M302 (= M355), T303 (= T356), D382 (= D435), R397 (= R450)
- binding carbonate ion: H207 (= H258), S277 (= S330), R299 (≠ T352), G301 (= G354)
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)
29% identity, 92% coverage: 43:551/553 of query aligns to 58:537/546 of Q84P21
- K530 (= K544) mutation to N: Lossed enzymatic activity.
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
36% identity, 62% coverage: 206:550/553 of query aligns to 143:476/485 of 5x8fB
- active site: T151 (= T214), S171 (≠ N234), H195 (= H258), T288 (= T356), E289 (= E357), I387 (= I456), N392 (= N461), K470 (= K544)
- binding magnesium ion: N178 (≠ E241), L202 (= L266), L214 (≠ M278), T296 (≠ S364), L297 (≠ N365), S298 (≠ P366)
- binding o-succinylbenzoyl-N-coenzyme A: L191 (= L254), P192 (= P255), H195 (= H258), I196 (= I259), S197 (≠ N260), A237 (≠ V301), V238 (= V302), L260 (≠ F325), G262 (≠ R327), G286 (= G354), M287 (= M355), S292 (≠ A360), Q293 (≠ P361), S388 (≠ K457), G389 (= G458), G390 (= G459), E391 (= E460), K420 (≠ A489), W421 (≠ Y490), K450 (≠ R524), Y451 (= Y525)
Sites not aligning to the query:
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
36% identity, 62% coverage: 206:550/553 of query aligns to 143:476/484 of 5gtdA
- active site: T151 (= T214), S171 (≠ N234), H195 (= H258), T288 (= T356), E289 (= E357)
- binding adenosine-5'-monophosphate: G263 (≠ S328), G264 (≠ A329), Y285 (≠ M353), G286 (= G354), M287 (= M355), T288 (= T356), D366 (= D435), V378 (≠ I447)
- binding magnesium ion: F314 (≠ G382), S315 (≠ G383)
- binding 2-succinylbenzoate: H195 (= H258), S197 (≠ N260), A237 (≠ V301), L260 (≠ F325), G262 (≠ R327), G263 (≠ S328), G286 (= G354), M287 (= M355), S292 (≠ A360), Q293 (≠ P361)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
36% identity, 62% coverage: 206:550/553 of query aligns to 142:473/475 of 5burA
- active site: T150 (= T214), S170 (≠ N234), H194 (= H258), T287 (= T356), E288 (= E357)
- binding adenosine-5'-triphosphate: T150 (= T214), S151 (= S215), T153 (= T217), T154 (= T218), K158 (= K222), G263 (≠ A329), S283 (≠ T352), T287 (= T356), D365 (= D435), V377 (≠ I447), R380 (= R450)
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
29% identity, 92% coverage: 42:550/553 of query aligns to 63:546/556 of Q9S725
- K211 (= K222) mutation to S: Drastically reduces the activity.
- M293 (≠ N300) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ R327) mutation K->L,A: Affects the substrate specificity.
- E401 (= E402) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V404) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R450) mutation to Q: Drastically reduces the activity.
- K457 (≠ G458) mutation to S: Drastically reduces the activity.
- K540 (= K544) mutation to N: Abolishes the activity.
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
36% identity, 62% coverage: 206:550/553 of query aligns to 142:473/481 of 5busA
- active site: T150 (= T214), S170 (≠ N234), H194 (= H258), T287 (= T356), E288 (= E357)
- binding adenosine monophosphate: H194 (= H258), G262 (≠ S328), G263 (≠ A329), S283 (≠ T352), M286 (= M355), T287 (= T356), D365 (= D435), V377 (≠ I447), R380 (= R450), K467 (= K544)
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
29% identity, 99% coverage: 5:550/553 of query aligns to 32:541/559 of Q67W82
- G395 (= G401) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 91% coverage: 43:547/553 of query aligns to 49:530/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H258), F245 (≠ N260), T249 (≠ V264), G314 (≠ S330), A315 (= A331), P316 (≠ A332), G337 (≠ T352), Y338 (≠ M353), G339 (= G354), L340 (≠ M355), T341 (= T356), S345 (≠ A360), A346 (≠ P361), D420 (= D435), I432 (= I447), K527 (= K544)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ N260), R335 (≠ I350), G337 (≠ T352), G339 (= G354), L340 (≠ M355), A346 (≠ P361)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 91% coverage: 43:547/553 of query aligns to 49:530/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H258), F245 (≠ N260), T249 (≠ V264), G314 (≠ S330), A315 (= A331), P316 (≠ A332), G337 (≠ T352), Y338 (≠ M353), G339 (= G354), L340 (≠ M355), T341 (= T356), A346 (≠ P361), D420 (= D435), I432 (= I447), K527 (= K544)
Q17577 Acyl-CoA synthetase 7; EC 6.2.1.- from Caenorhabditis elegans (see paper)
27% identity, 96% coverage: 19:547/553 of query aligns to 31:525/540 of Q17577
- SS 186:187 (≠ TS 214:215) mutation to AA: Loss of catalytic activity; when associated with A-339.
- E339 (= E357) mutation to A: Severe loss of catalytic activity. Loss of catalytic activity; when associated with 186-A-A-187.
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
38% identity, 63% coverage: 194:539/553 of query aligns to 115:460/460 of 3nyrA
- active site: T137 (= T214), T157 (≠ N234), H181 (= H258), T281 (= T356), E282 (= E357), K379 (≠ I456), K384 (≠ N461)
- binding adenosine monophosphate: S255 (= S330), A256 (= A331), A257 (= A332), R277 (≠ T352), Y278 (≠ M353), G279 (= G354), M280 (= M355), T281 (= T356), D357 (= D435), K379 (≠ I456), K384 (≠ N461)
- binding malonyl-coenzyme a: P178 (= P255), H181 (= H258), T226 (= T304), R230 (vs. gap), S255 (= S330), R277 (≠ T352), G279 (= G354), G381 (= G458), G382 (= G459), Y383 (≠ E460)
Query Sequence
>BPHYT_RS21775 FitnessBrowser__BFirm:BPHYT_RS21775
MNTPVTLRALIDERAAQHPDKPFLLAALDDDETPVPDRRATVLTFRELRDDCRALEARFR
EAGLQPGEVISVFMGNGIQTARLLLAAMYSGLVANPLNLLCQPSQVRYIVDHSDTRMIFA
ASDTHAVIGAAVAELRAAGLTREIALIQTEPDDAEPPSLAKHEPALVEAAAHGASGATAP
APALAKRSVAPRPVTSRATAYEPTADDVALLMYTSGTTGTPKGVLLTHRNLVANARNISA
EHRLASDDRVLASLPLYHINGLVVTLLAPLFHGGSAVMTSRFSARTFWRDVALHACTWIN
VVPTIVAYLLNADEACTYDLSALKFCRSASAALPADHHRAFEARFGIGVIETMGMTETAA
PVFSNPYEMERRRVGSIGLPSGGEAKVIDREGRECAANECGELVLRGEQVMGGYYKRPEE
TAAAFTSDGWLRTGDLGYRDADGYFYINGRAKELIIKGGENIAPREIDEALLRHPDVLDA
AAVGVPDPAYGQDIVAFVVPRMSDGRGAPDPADLREHCLRELGRYKTPKEFRFVDELPRG
PSGKVQRLKLVPT
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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