SitesBLAST
Comparing AO356_01575 AO356_01575 AMP-binding protein 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: 4:563/565 of query aligns to 17:580/590 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, 94% coverage: 24:554/565 of query aligns to 23:551/561 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.
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, 94% coverage: 24:554/565 of query aligns to 2:495/503 of P9WQ37
- R9 (≠ D31) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E39) 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 (≠ G248) 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.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% 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)
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)
28% identity, 89% coverage: 53:556/565 of query aligns to 59:540/546 of Q84P21
- K530 (= K546) mutation to N: Lossed enzymatic activity.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 94% coverage: 24:554/565 of query aligns to 5:495/502 of 3r44A
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 94% coverage: 25:555/565 of query aligns to 19:536/539 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 (≠ G266), 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)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 94% coverage: 25:555/565 of query aligns to 19:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H259), F245 (= F261), T249 (≠ G266), G314 (= G332), A315 (= A333), P316 (≠ T334), G337 (≠ A355), Y338 (= Y356), G339 (= G357), L340 (≠ M358), T341 (= T359), A346 (≠ V364), D420 (= D440), I432 (= I452), K527 (= 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)
28% identity, 90% coverage: 40:549/565 of query aligns to 16:497/512 of O74976
- S283 (≠ T334) modified: Phosphoserine
- S284 (≠ C335) modified: Phosphoserine
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
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
30% identity, 93% coverage: 27:553/565 of query aligns to 21:529/537 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)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
30% identity, 86% coverage: 53:540/565 of query aligns to 32:493/504 of 6qjzA
- active site: T169 (= T215), S189 (≠ N235), H213 (= H259), T314 (= T359), E315 (= E360), N414 (≠ I461), K419 (≠ N466)
- binding adenosine monophosphate: H213 (= H259), S288 (≠ A331), A289 (≠ G332), S290 (≠ A333), A312 (≠ G357), M313 (= M358), T314 (= T359), D393 (= D440), L405 (≠ I452), K410 (= K457), K419 (≠ N466)
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
28% identity, 89% coverage: 52:555/565 of query aligns to 47:534/539 of 2d1sA
- active site: S194 (≠ T215), R214 (≠ N235), H241 (= H259), T339 (= T359), E340 (= E360), K439 (≠ I461), Q444 (≠ N466), K525 (= K546)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T215), S195 (= S216), H241 (= H259), F243 (= F261), T247 (≠ M265), I282 (≠ Y302), G312 (= G332), A313 (= A333), P314 (≠ T334), Q334 (≠ I354), G335 (≠ A355), Y336 (= Y356), G337 (= G357), L338 (≠ M358), T339 (= T359), S343 (≠ P363), A344 (≠ V364), D418 (= D440), R433 (= R455), K525 (= K546)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
28% identity, 89% coverage: 52:555/565 of query aligns to 47:534/539 of 2d1rA
- active site: S194 (≠ T215), R214 (≠ N235), H241 (= H259), T339 (= T359), E340 (= E360), K439 (≠ I461), Q444 (≠ N466), K525 (= K546)
- binding adenosine monophosphate: S194 (≠ T215), S195 (= S216), H241 (= H259), G312 (= G332), A313 (= A333), P314 (≠ T334), G335 (≠ A355), Y336 (= Y356), G337 (= G357), L338 (≠ M358), T339 (= T359), D418 (= D440), K525 (= K546)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H259), F243 (= F261), T247 (≠ M265), G335 (≠ A355), G337 (= G357), L338 (≠ M358), A344 (≠ V364)
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
30% identity, 93% coverage: 27:553/565 of query aligns to 21:528/536 of 6e8oA
- active site: S190 (≠ T215), S210 (≠ N235), H234 (= H259), A336 (≠ T359), E337 (= E360), N437 (≠ I461), K442 (≠ N466), K521 (= K546)
- binding adenosine monophosphate: H234 (= H259), G310 (= G332), A311 (= A333), K312 (≠ T334), V332 (≠ A355), F333 (≠ Y356), G334 (= G357), M335 (= M358), A336 (≠ T359), D416 (= D440), V428 (≠ I452), K442 (≠ N466)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
28% 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)
1md9A Crystal structure of dhbe in complex with dhb and amp (see paper)
28% identity, 95% coverage: 24:560/565 of query aligns to 25:533/536 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)
6hpsA Near-infrared dual bioluminescence imaging in vivo using infra- luciferin (see paper)
28% identity, 95% coverage: 25:558/565 of query aligns to 17:537/539 of 6hpsA
- active site: S194 (≠ T215), R214 (≠ N234), H241 (= H259), T339 (= T359), E340 (= E360), K439 (≠ I461), Q444 (≠ N466), K525 (= K546)
- binding [(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl ~{N}-[[2-[(~{E})-2-(6-oxidanyl-1,3-benzothiazol-2-yl)ethenyl]-1,3-thiazol-4-yl]carbonyl]sulfamate: H241 (= H259), G242 (≠ C260), F243 (= F261), S310 (≠ M330), G312 (= G332), A313 (= A333), P314 (≠ T334), R333 (≠ Q353), G335 (≠ A355), Y336 (= Y356), G337 (= G357), L338 (≠ M358), T339 (= T359), A344 (≠ V364), D418 (= D440), K525 (= K546)
P40871 2,3-dihydroxybenzoate-AMP ligase; Dihydroxybenzoic acid-activating enzyme; EC 6.2.1.71 from Bacillus subtilis (strain 168) (see paper)
28% identity, 95% coverage: 24:560/565 of query aligns to 25:533/539 of P40871
- G191 (≠ S216) binding
- HN 234:235 (≠ HC 259:260) binding
- S240 (≠ M265) binding
- G307 (= G332) binding
- V329 (≠ A355) binding
- D413 (= D440) binding
- R428 (= R455) binding
- K519 (= K546) binding ; binding
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
29% identity, 88% coverage: 51:549/565 of query aligns to 53:527/535 of 5wm6A
- active site: S193 (≠ T215), N213 (= N235), H237 (= H259), A336 (≠ T359), E337 (= E360), N437 (≠ I461), K442 (≠ N466), K524 (= K546)
- binding magnesium ion: S301 (= S323), L303 (= L325), G326 (≠ H348)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (= F261), G310 (= G332), S311 (≠ A333), K312 (≠ T334), V332 (≠ I354), F333 (≠ Y356), G334 (= G357), M335 (= M358), A336 (≠ T359), D416 (= D440), K433 (= K457), K442 (≠ N466)
Query Sequence
>AO356_01575 AO356_01575 AMP-binding protein
MDQPGSHSQLSYTRGSAAKALLAQTIGEVFDQTVARYPEGEALVVRHQSLRYTWQQLAEA
VDLHARALLALGLKTGDRLGVWAPNCAQWCISQFASAKLGVILVNINPAYRVSELEYVLK
QSGCQWLVCAGAFKTSDYHAMLQTLAPELAEQPIGQMQSERLPELRGVISLDSQPPAGFL
PWSQLAALGAAVTPGQLAERQSSLRFDQPVNIQYTSGTTGFPKGATLSHHNILNNGYMVG
ESLGLTAGDRLVIPVPLYHCFGMVMGNLGCMTHGSTMIYPNDAFDPLLTLKAVAEEKATA
LYGVPTMFIALLDQPQRGDFDLSSLRTGIMAGATCPIEVMRRVINEMHMAEVQIAYGMTE
TSPVSLQTGPSDELELRVTTVGRTQPQLESKIIDEAGNLVSRGAVGELCTRGYSVMLGYW
NNPKGTSDAIDPEGWMHTGDLATMDEQGYVCIVGRNKDMIIRGGENIYPRELEEFFFTHP
AVADVQVIGIPCSRYGEEIVAWIKFHPGHSASEQELQAWCKERIAHFKTPRHFKFVEEFP
MTVTGKIQKFRMREISIEELRDKQN
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