SitesBLAST
Comparing RR42_RS06210 FitnessBrowser__Cup4G11:RR42_RS06210 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)
Q08AH3 Acyl-coenzyme A synthetase ACSM2A, mitochondrial; Acyl-CoA synthetase medium-chain family member 2A; Benzoate--CoA ligase; Butyrate--CoA ligase 2A; Butyryl-coenzyme A synthetase 2A; Middle-chain acyl-CoA synthetase 2A; EC 6.2.1.2; EC 6.2.1.25 from Homo sapiens (Human) (see 4 papers)
31% identity, 96% coverage: 22:575/577 of query aligns to 37:574/577 of Q08AH3
- Q139 (≠ L120) binding
- 221:229 (vs. 202:210, 78% identical) binding
- ESYGQT 359:364 (≠ EMFGQT 343:348) binding
- T364 (= T348) binding
- D446 (= D445) binding
- R461 (= R460) binding
- SGY 469:471 (= SGY 468:470) binding
- R472 (= R471) binding
- R501 (= R500) binding
- S513 (≠ P512) to L: in dbSNP:rs1133607
- K532 (≠ R533) binding
- YPR 540:542 (≠ YPK 541:543) binding
- K557 (= K558) binding
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
31% identity, 95% coverage: 22:570/577 of query aligns to 5:537/537 of 3b7wA
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
31% identity, 95% coverage: 22:568/577 of query aligns to 1:531/533 of 3eq6A
- active site: T185 (= T202), T328 (= T348), E329 (= E349), N431 (≠ K466), R436 (= R471), K521 (= K558)
- binding adenosine monophosphate: G302 (= G322), E303 (= E323), S304 (≠ A324), E323 (= E343), S324 (≠ M344), Y325 (≠ F345), G326 (= G346), Q327 (= Q347), T328 (= T348), D410 (= D445), F422 (≠ Y457), R425 (= R460), R436 (= R471)
- binding Butyryl Coenzyme A: W229 (= W248), F255 (= F273), I277 (≠ T295), V301 (≠ A321), S433 (= S468), G434 (= G469), Y435 (= Y470), P501 (= P538), Y502 (= Y539), Y504 (= Y541), R506 (≠ K543)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
31% identity, 95% coverage: 22:568/577 of query aligns to 1:531/533 of 2wd9A
- active site: T185 (= T202), T328 (= T348), E329 (= E349), N431 (≠ K466), R436 (= R471), K521 (= K558)
- binding ibuprofen: I230 (≠ T249), L231 (≠ G250), G326 (= G346), Q327 (= Q347), T328 (= T348), R436 (= R471)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
31% identity, 95% coverage: 22:568/577 of query aligns to 1:531/533 of 2vzeA
- active site: T185 (= T202), T328 (= T348), E329 (= E349), N431 (≠ K466), R436 (= R471), K521 (= K558)
- binding adenosine monophosphate: W229 (= W248), G302 (= G322), E303 (= E323), S304 (≠ A324), E323 (= E343), Y325 (≠ F345), G326 (= G346), Q327 (= Q347), T328 (= T348), D410 (= D445), F422 (≠ Y457), R425 (= R460), R436 (= R471)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
31% identity, 95% coverage: 22:570/577 of query aligns to 4:536/536 of 3c5eA
- active site: T188 (= T202), T331 (= T348), E332 (= E349), N434 (≠ K466), R439 (= R471), K524 (= K558)
- binding adenosine-5'-triphosphate: T188 (= T202), S189 (= S203), G190 (= G204), T191 (= T205), S192 (≠ T206), G305 (= G322), E306 (= E323), S307 (≠ A324), G329 (= G346), Q330 (= Q347), T331 (= T348), D413 (= D445), F425 (≠ Y457), R428 (= R460), K524 (= K558)
- binding magnesium ion: M450 (≠ L482), H452 (= H484), V455 (= V487)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
31% identity, 95% coverage: 22:570/577 of query aligns to 5:535/535 of 3dayA
- active site: T189 (= T202), T332 (= T348), E333 (= E349), N435 (≠ K466), R440 (= R471), K523 (= K558)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T202), S190 (= S203), G191 (= G204), T192 (= T205), S193 (≠ T206), K197 (= K210), G306 (= G322), E307 (= E323), S308 (≠ A324), Y329 (≠ F345), G330 (= G346), Q331 (= Q347), T332 (= T348), D414 (= D445), F426 (≠ Y457), R429 (= R460), K523 (= K558)
- binding magnesium ion: M451 (≠ L482), H453 (= H484), V456 (= V487)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
31% identity, 95% coverage: 22:568/577 of query aligns to 2:530/532 of 3gpcA
- active site: T186 (= T202), T327 (= T348), E328 (= E349), N430 (≠ K466), R435 (= R471), K520 (= K558)
- binding coenzyme a: G301 (= G322), E302 (= E323), S303 (≠ A324), E322 (= E343), Y324 (≠ F345), G325 (= G346), Q326 (= Q347), T327 (= T348), D409 (= D445), F421 (≠ Y457), R424 (= R460), T516 (= T554), K520 (= K558), Q522 (= Q560)
- binding magnesium ion: H448 (= H484), V451 (= V487)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
29% identity, 87% coverage: 58:561/577 of query aligns to 66:540/562 of 8bitA
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: W252 (= W253), G321 (= G322), E322 (= E323), P323 (≠ A324), D342 (≠ E343), F343 (≠ M344), Y344 (≠ F345), Q346 (= Q347), T347 (= T348), D428 (= D445), F440 (≠ Y457), K449 (= K466), R454 (= R471)
- binding coenzyme a: N128 (≠ L120), W247 (= W248), K249 (≠ G250), K273 (≠ R272), L274 (≠ F273), Q300 (= Q299), D452 (≠ G469), Y453 (= Y470), R483 (= R500), P517 (= P538)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
29% identity, 87% coverage: 58:561/577 of query aligns to 64:538/561 of 8biqB
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: G319 (= G322), E320 (= E323), P321 (≠ A324), D340 (≠ E343), F341 (≠ M344), Y342 (≠ F345), G343 (= G346), Q344 (= Q347), T345 (= T348), D426 (= D445), F438 (≠ Y457), K447 (= K466), R452 (= R471)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
29% identity, 87% coverage: 58:561/577 of query aligns to 65:539/562 of 8biqA
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
32% identity, 86% coverage: 68:565/577 of query aligns to 41:509/518 of 4wv3B
- active site: S175 (≠ T202), T320 (= T348), E321 (= E349), K418 (= K466), W423 (≠ R471), K502 (= K558)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W248), T221 (= T249), F222 (≠ G250), A293 (= A321), S294 (≠ G322), E295 (= E323), A296 (= A324), G316 (≠ M344), I317 (≠ F345), G318 (= G346), C319 (≠ Q347), T320 (= T348), D397 (= D445), H409 (≠ Y457), R412 (= R460), K502 (= K558)
P78773 Probable acetyl-coenzyme A synthetase; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 91% coverage: 47:569/577 of query aligns to 101:629/662 of P78773
- T596 (≠ Q535) modified: Phosphothreonine
P9WQD1 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 95% coverage: 23:571/577 of query aligns to 67:630/651 of P9WQD1
- K617 (= K558) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
P27550 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Escherichia coli (strain K12) (see paper)
27% identity, 95% coverage: 21:569/577 of query aligns to 67:620/652 of P27550
- K609 (= K558) modified: N6-acetyllysine; by autocatalysis
Q8ZKF6 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
28% identity, 95% coverage: 21:569/577 of query aligns to 67:620/652 of Q8ZKF6
- R194 (vs. gap) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 3-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 2-fold reduction for CoA.
- T311 (≠ G250) binding
- N335 (≠ S274) binding
- A357 (≠ F293) mutation to V: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 3-fold reduction for CoA.
- D517 (= D462) mutation to G: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 10-fold reduction for CoA.; mutation to P: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold reduction in the affinity for ATP and 4.5-fold reduction for CoA.
- S523 (= S468) binding
- G524 (= G469) mutation to L: No acetyl-coenzyme A synthetase activity.; mutation to S: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. Almost the same affinity as the wild-type for ATP, but 9-fold reduction in the affinity for CoA.
- R526 (= R471) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 4-fold reduction for CoA.
- R584 (= R533) binding ; mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 7-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 8-fold reduction for CoA.
- K609 (= K558) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
28% identity, 95% coverage: 21:569/577 of query aligns to 63:616/640 of 5jrhA
- active site: T260 (= T202), T412 (= T348), E413 (= E349), N517 (≠ K466), R522 (= R471), K605 (= K558)
- binding (r,r)-2,3-butanediol: W93 (≠ T53), E140 (= E99), G169 (≠ Y128), K266 (≠ P208), P267 (= P209)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G322), E384 (= E323), P385 (≠ A324), T408 (≠ M344), W409 (≠ F345), W410 (≠ G346), Q411 (= Q347), T412 (= T348), D496 (= D445), I508 (≠ Y457), N517 (≠ K466), R522 (= R471)
- binding coenzyme a: F159 (≠ S118), G160 (≠ M119), G161 (≠ L120), R187 (vs. gap), S519 (= S468), R580 (= R533), P585 (= P538)
- binding magnesium ion: V533 (≠ L482), H535 (= H484), I538 (≠ V487)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
27% identity, 95% coverage: 21:569/577 of query aligns to 62:615/637 of 2p2fA
- active site: T259 (= T202), T411 (= T348), E412 (= E349), N516 (≠ K466), R521 (= R471), K604 (= K558)
- binding adenosine monophosphate: G382 (= G322), E383 (= E323), P384 (≠ A324), T407 (≠ M344), W408 (≠ F345), W409 (≠ G346), Q410 (= Q347), T411 (= T348), D495 (= D445), I507 (≠ Y457), R510 (= R460), N516 (≠ K466), R521 (= R471)
- binding coenzyme a: F158 (≠ S118), R186 (vs. gap), W304 (= W248), T306 (≠ G250), P329 (≠ F273), A352 (≠ F293), A355 (= A296), S518 (= S468), R579 (= R533), P584 (= P538)
Q89WV5 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) (see paper)
27% identity, 95% coverage: 20:567/577 of query aligns to 65:615/648 of Q89WV5
- G263 (= G204) mutation to I: Loss of activity.
- G266 (= G207) mutation to I: Great decrease in activity.
- K269 (= K210) mutation to G: Great decrease in activity.
- E414 (= E349) mutation to Q: Great decrease in activity.
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
29% identity, 90% coverage: 47:567/577 of query aligns to 67:596/627 of 5gxdA
- active site: T238 (= T202), T390 (= T348), E391 (= E349), N498 (≠ K466), R503 (= R471), K587 (= K558)
- binding adenosine monophosphate: G364 (= G322), E365 (= E323), R366 (≠ A324), H386 (≠ M344), W387 (≠ F345), W388 (≠ G346), Q389 (= Q347), T390 (= T348), D477 (= D445), I489 (≠ Y457), R492 (= R460), N498 (≠ K466), R503 (= R471)
- binding coenzyme a: F139 (≠ S118), G140 (≠ M119), G141 (≠ L120), E167 (vs. gap), R170 (vs. gap), S279 (≠ A244), K307 (≠ R272), P308 (≠ F273), A332 (≠ F293), T334 (= T295), A363 (= A321), A500 (≠ S468), H502 (≠ Y470), K532 (≠ R500), R562 (= R533), P567 (= P538), V568 (≠ Y539)
Query Sequence
>RR42_RS06210 FitnessBrowser__Cup4G11:RR42_RS06210
MAAPALPASRRDDYPALHSQFHWHVPEFFNLAEACCGRWARDPATMDRIAVHTEHEDGRR
ASYSYAFIQAEADRLCRALRTLGVARGDRVGIVMPQRIETVIAHMAIYQLGAIAMPLSML
FGPEALAYRLQHSEACVAIADESSIDNVLAARAECPALATVIGAGAAVGRAEHDWDALLA
AELPAFTAVVTKADEAAVLIYTSGTTGPPKGALIPHRALIGNLPGFVCSQNWFPHADDVF
WSPADWAWTGGLWDALMPTLYFGKTIVGYQGRFSAQTAFELMARYRVTNTFLFPTALKQM
MKTCPAPRAHYQLHLRALMSAGEAVGETVFAWCRDALGVVVNEMFGQTEINYIVGNCTAQ
NDDGQPGWPARPGSMGRPYPGHRVAVVDDEGRPCAAGEDGEVAVCSTDVHGHPDPVFFLG
YWRNDDATAGKYLARDGLHWCRTGDLARIDEDGYLWYQGRADDVFKSSGYRIGPSEIENC
LLKHPAVSNCAVVPSPDPERGAVVKAFIVLVPSIVRSAQADAALVAELQQHVRGQLAPYE
YPKVIEFIAQLPMTTTGKIQRRVLREIEARRGAPAHP
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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