SitesBLAST
Comparing PfGW456L13_2593 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2593 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)
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)
41% identity, 99% coverage: 3:563/565 of query aligns to 15:580/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
32% identity, 93% coverage: 30:554/565 of query aligns to 29:551/561 of P69451
- Y213 (= Y214) mutation to A: Loss of activity.
- T214 (= T215) mutation to A: 10% of wild-type activity.
- G216 (= G217) mutation to A: Decreases activity.
- T217 (= T218) mutation to A: Decreases activity.
- G219 (= G220) mutation to A: Decreases activity.
- K222 (= K223) mutation to A: Decreases activity.
- E361 (= E360) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 89% coverage: 51:554/565 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H259), T303 (= T359), E304 (= E360), I403 (= I461), N408 (= N466), A491 (≠ K546)
- binding adenosine-5'-triphosphate: T163 (= T215), S164 (= S216), G165 (= G217), T166 (= T218), T167 (= T219), H207 (= H259), S277 (≠ G332), A278 (= A333), P279 (≠ T334), E298 (≠ Q353), M302 (= M358), T303 (= T359), D382 (= D440), R397 (= R455)
- binding carbonate ion: H207 (= H259), S277 (≠ G332), R299 (≠ A355), G301 (= G357)
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)
29% identity, 92% coverage: 38:554/565 of query aligns to 16:495/503 of P9WQ37
- R17 (≠ D39) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K223) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T246) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A248) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C260) 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 (≠ G262) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M265) 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 (≠ K297) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G357) 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 (= W435) 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 (= D440) 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 (= R455) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R462) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G464) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K546) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 92% coverage: 38:554/565 of query aligns to 19:495/502 of 3r44A
Sites not aligning to the query:
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 92% coverage: 35:555/565 of query aligns to 32:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H259), F245 (= F261), T249 (≠ M265), G314 (= G332), A315 (= A333), P316 (≠ T334), G337 (≠ A355), Y338 (= Y356), G339 (= G357), L340 (≠ M358), T341 (= T359), A346 (≠ V364), D420 (= D440), I432 (= I452), K527 (= K546)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 92% coverage: 35:555/565 of query aligns to 32:536/539 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 (= H259), F245 (= F261), T249 (≠ M265), G314 (= G332), A315 (= A333), P316 (≠ T334), G337 (≠ A355), Y338 (= Y356), G339 (= G357), L340 (≠ M358), T341 (= T359), S345 (≠ P363), A346 (≠ V364), D420 (= D440), I432 (= I452), K527 (= K546)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F261), R335 (≠ Q353), G337 (≠ A355), G339 (= G357), L340 (≠ M358), A346 (≠ V364)
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)
25% identity, 89% coverage: 53:556/565 of query aligns to 59:540/546 of Q84P21
- K530 (= K546) mutation to N: Lossed enzymatic activity.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
29% identity, 89% coverage: 53:553/565 of query aligns to 37:509/518 of 4wv3B
- active site: S175 (≠ T215), T320 (= T359), E321 (= E360), K418 (≠ I461), W423 (≠ N466), K502 (= K546)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H259), T221 (≠ C260), F222 (= F261), A293 (= A331), S294 (≠ G332), E295 (≠ A333), A296 (≠ T334), G316 (≠ A355), I317 (≠ Y356), G318 (= G357), C319 (≠ M358), T320 (= T359), D397 (= D440), H409 (≠ I452), R412 (= R455), K502 (= K546)
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)
27% identity, 90% coverage: 40:549/565 of query aligns to 16:497/512 of O74976
- S283 (≠ T334) modified: Phosphoserine
- S284 (≠ C335) modified: Phosphoserine
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 93% coverage: 25:549/565 of query aligns to 5:498/506 of 5ie2A
- active site: T165 (= T215), S185 (≠ N235), H209 (= H259), T310 (= T359), E311 (= E360), N410 (≠ I461), K415 (≠ N466), K495 (= K546)
- binding adenosine-5'-triphosphate: T165 (= T215), S166 (= S216), G167 (= G217), T168 (= T218), T169 (= T219), S284 (≠ A331), A285 (≠ G332), S286 (≠ A333), Y307 (= Y356), A308 (≠ G357), M309 (= M358), T310 (= T359), D389 (= D440), L401 (≠ I452), R404 (= R455), K495 (= K546)
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)
27% identity, 93% coverage: 25:549/565 of query aligns to 5:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 215:219) binding
- H214 (= H259) binding ; mutation to A: Abolished activity.
- S289 (≠ A331) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ AGA 331:333) binding
- EA 310:311 (≠ IA 354:355) binding
- M314 (= M358) binding
- T315 (= T359) binding
- H319 (≠ P363) binding ; mutation to A: Abolished activity.
- D394 (= D440) binding
- R409 (= R455) binding ; mutation to A: Abolished activity.
- K500 (= K546) binding ; binding ; mutation to A: Abolished activity.
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)
27% identity, 89% coverage: 52:553/565 of query aligns to 64:547/556 of Q9S725
- K211 (= K223) mutation to S: Drastically reduces the activity.
- M293 (≠ Y302) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I329) mutation K->L,A: Affects the substrate specificity.
- E401 (= E407) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C409) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R455) mutation to Q: Drastically reduces the activity.
- K457 (≠ G463) mutation to S: Drastically reduces the activity.
- K540 (= K546) mutation to N: Abolishes the activity.
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
30% identity, 89% coverage: 51:554/565 of query aligns to 47:530/537 of 6e97B
- active site: S190 (≠ T215), S210 (≠ N235), H234 (= H259), A336 (≠ T359), E337 (= E360), N437 (≠ I461), K442 (≠ N466), K522 (= K546)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H259), N235 (≠ C260), F236 (= F261), S240 (≠ M265), G310 (= G332), A311 (= A333), K312 (≠ T334), V332 (≠ A355), F333 (≠ Y356), G334 (= G357), M335 (= M358), A336 (≠ T359), D416 (= D440), K433 (= K457), K442 (≠ N466)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
28% identity, 89% coverage: 51:554/565 of query aligns to 47:532/541 of Q5SKN9
- T184 (= T215) binding
- G302 (= G332) binding
- Q322 (≠ I354) binding
- G323 (≠ A355) binding
- T327 (= T359) binding
- E328 (= E360) binding
- D418 (= D440) binding
- K435 (= K457) binding
- K439 (≠ I461) binding
5ie3A Crystal structure of a plant enzyme (see paper)
27% identity, 93% coverage: 25:549/565 of query aligns to 5:496/504 of 5ie3A
- active site: T163 (= T215), S183 (≠ N235), H207 (= H259), T308 (= T359), E309 (= E360), N408 (≠ I461), K413 (≠ N466), K493 (= K546)
- binding adenosine monophosphate: S164 (= S216), S282 (≠ A331), A283 (≠ G332), S284 (≠ A333), Y305 (= Y356), A306 (≠ G357), M307 (= M358), T308 (= T359), D387 (= D440), L399 (≠ I452), R402 (= R455), K493 (= K546)
- binding oxalic acid: V208 (≠ C260), S282 (≠ A331), A306 (≠ G357), M307 (= M358), H312 (≠ P363), K493 (= K546)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 89% coverage: 52:554/565 of query aligns to 46:527/528 of 3ni2A
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H259), T329 (= T359), E330 (= E360), K434 (≠ I461), Q439 (≠ N466), K519 (= K546)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F261), S236 (≠ M265), G302 (= G332), A303 (= A333), P304 (≠ T334), G325 (≠ A355), G327 (= G357), T329 (= T359), P333 (= P363), V334 (= V364), D413 (= D440), K430 (= K457), K434 (≠ I461), Q439 (≠ N466)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 89% coverage: 52:554/565 of query aligns to 46:527/528 of 3a9vA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H259), T329 (= T359), E330 (= E360), K434 (≠ I461), Q439 (≠ N466), K519 (= K546)
- binding adenosine monophosphate: H230 (= H259), G302 (= G332), A303 (= A333), P304 (≠ T334), Y326 (= Y356), G327 (= G357), M328 (= M358), T329 (= T359), D413 (= D440), K430 (= K457), K434 (≠ I461), Q439 (≠ N466)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
28% identity, 89% coverage: 51:554/565 of query aligns to 39:531/539 of P0DX84
- H231 (= H259) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ M263) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A331) mutation to P: Almost completely abolishes the activity.
- G303 (= G332) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y356) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P363) mutation to A: Retains 69% of wild-type activity.
- R432 (= R455) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K457) mutation to A: Retains 36% of wild-type activity.
- D435 (= D458) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I461) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G463) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G464) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E465) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N466) mutation to A: Retains 60% of wild-type activity.
- E474 (= E497) mutation to A: Retains 33% of wild-type activity.
- K523 (= K546) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K549) mutation to A: Retains 48% of wild-type activity.
1md9A Crystal structure of dhbe in complex with dhb and amp (see paper)
27% identity, 95% coverage: 25:560/565 of query aligns to 26:533/536 of 1md9A
- active site: S190 (≠ T215), S210 (≠ N235), H234 (= H259), A333 (≠ T359), E334 (= E360), N434 (≠ I461), K439 (≠ N466), K519 (= K546)
- binding adenosine monophosphate: G191 (≠ S216), G307 (= G332), A308 (= A333), K309 (≠ T334), V329 (≠ A355), F330 (≠ Y356), G331 (= G357), M332 (= M358), D413 (= D440), V425 (≠ I452), R428 (= R455), K519 (= K546)
- binding 2,3-dihydroxy-benzoic acid: H234 (= H259), N235 (≠ C260), Y236 (≠ F261), S240 (≠ M265), G307 (= G332), V329 (≠ A355), G331 (= G357), M332 (= M358), K519 (= K546)
Query Sequence
>PfGW456L13_2593 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2593
MDQPSASPQRSYTRGSQDKALLAMTIGQAFDNTVAQYPDGEALVVRHQQLRYTWQQLAEA
ADLHARALLALGLQAGDRLGIWAPNCAQWCISQIATAKIGVILVNINPAYRSSELEYVLK
QSGCQWLVCAGAFKTSNYHAMVQGLVPELAEQSIGKLLSERLPELRGVISLDVQPPSGFL
PWSQLTDLAGGVSTEQLRERQESLHFDQAVNIQYTSGTTGFPKGATLSHYNILNNGYMVG
ESLGLTAADRLVIPVPLYHCFGMVMGNLGCITHGSTMIYPNDAFDPLLTLGTVAEEKATA
LYGVPTMFIAMLDQPQRAGFDLSSLRTGIMAGATCPIEVMRRVISEMHMSEVQIAYGMTE
TSPVSLQTGPSDDLELRVTTVGRTQPQLESKIIDEAGNLVPRGTIGELCTRGYSVMLGYW
NNPEGTADAIDQAGWMHTGDLASMNDEGYVCIAGRNKDMIIRGGENIYPRELEEFFFTHP
AVADVQVIGIPCSRYGEEIVAWIKFHPGHGATEQELQAWCKERIAHFKTPRYFKFVEEFP
MTVTGKIQKFRMREISIEELREKQE
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