SitesBLAST
Comparing PP_2213 FitnessBrowser__Putida:PP_2213 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)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
33% identity, 87% coverage: 58:547/561 of query aligns to 36:535/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
33% identity, 87% coverage: 58:547/561 of query aligns to 35:534/536 of 3c5eA
- active site: T188 (= T204), T331 (= T348), E332 (= E349), N434 (≠ T449), R439 (= R454), K524 (= K537)
- binding adenosine-5'-triphosphate: T188 (= T204), S189 (= S205), G190 (= G206), T191 (= T207), S192 (≠ T208), G305 (= G322), E306 (= E323), S307 (≠ P324), G329 (= G346), Q330 (= Q347), T331 (= T348), D413 (= D428), F425 (= F440), R428 (= R443), K524 (= K537)
- binding magnesium ion: M450 (≠ I465), H452 (= H467), V455 (= V470)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
33% identity, 87% coverage: 58:547/561 of query aligns to 32:531/533 of 3eq6A
- active site: T185 (= T204), T328 (= T348), E329 (= E349), N431 (≠ T449), R436 (= R454), K521 (= K537)
- binding adenosine monophosphate: G302 (= G322), E303 (= E323), S304 (≠ P324), E323 (≠ D343), S324 (≠ H344), Y325 (= Y345), G326 (= G346), Q327 (= Q347), T328 (= T348), D410 (= D428), F422 (= F440), R425 (= R443), R436 (= R454)
- binding Butyryl Coenzyme A: W229 (= W248), F255 (= F273), I277 (≠ T295), V301 (≠ A321), S433 (= S451), G434 (= G452), Y435 (= Y453), P501 (≠ A517), Y502 (≠ H518), Y504 (= Y520), R506 (= R522)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
33% identity, 87% coverage: 58:547/561 of query aligns to 32:531/533 of 2wd9A
- active site: T185 (= T204), T328 (= T348), E329 (= E349), N431 (≠ T449), R436 (= R454), K521 (= K537)
- binding ibuprofen: I230 (≠ A249), L231 (≠ Y250), G326 (= G346), Q327 (= Q347), T328 (= T348), R436 (= R454)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
33% identity, 87% coverage: 58:547/561 of query aligns to 32:531/533 of 2vzeA
- active site: T185 (= T204), T328 (= T348), E329 (= E349), N431 (≠ T449), R436 (= R454), K521 (= K537)
- binding adenosine monophosphate: W229 (= W248), G302 (= G322), E303 (= E323), S304 (≠ P324), E323 (≠ D343), Y325 (= Y345), G326 (= G346), Q327 (= Q347), T328 (= T348), D410 (= D428), F422 (= F440), R425 (= R443), R436 (= R454)
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)
33% identity, 87% coverage: 58:547/561 of query aligns to 68:567/577 of Q08AH3
- Q139 (≠ A128) binding
- 221:229 (vs. 204:212, 67% identical) binding
- ESYGQT 359:364 (≠ DHYGQT 343:348) binding
- T364 (= T348) binding
- D446 (= D428) binding
- R461 (= R443) binding
- SGY 469:471 (= SGY 451:453) binding
- R472 (= R454) binding
- R501 (= R483) binding
- S513 (= S495) to L: in dbSNP:rs1133607
- K532 (≠ R512) binding
- YPR 540:542 (= YPR 520:522) binding
- K557 (= K537) binding
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
33% identity, 87% coverage: 58:547/561 of query aligns to 36:533/535 of 3dayA
- active site: T189 (= T204), T332 (= T348), E333 (= E349), N435 (≠ T449), R440 (= R454), K523 (= K537)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T204), S190 (= S205), G191 (= G206), T192 (= T207), S193 (≠ T208), K197 (= K212), G306 (= G322), E307 (= E323), S308 (≠ P324), Y329 (= Y345), G330 (= G346), Q331 (= Q347), T332 (= T348), D414 (= D428), F426 (= F440), R429 (= R443), K523 (= K537)
- binding magnesium ion: M451 (≠ I465), H453 (= H467), V456 (= V470)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
33% identity, 87% coverage: 58:547/561 of query aligns to 33:530/532 of 3gpcA
- active site: T186 (= T204), T327 (= T348), E328 (= E349), N430 (≠ T449), R435 (= R454), K520 (= K537)
- binding coenzyme a: G301 (= G322), E302 (= E323), S303 (≠ P324), E322 (≠ D343), Y324 (= Y345), G325 (= G346), Q326 (= Q347), T327 (= T348), D409 (= D428), F421 (= F440), R424 (= R443), T516 (= T533), K520 (= K537), Q522 (= Q539)
- binding magnesium ion: H448 (= H467), V451 (= V470)
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)
32% identity, 90% coverage: 41:545/561 of query aligns to 75:617/652 of P27550
- K609 (= K537) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
32% identity, 93% coverage: 41:561/561 of query aligns to 70:628/637 of 2p2fA
- active site: T259 (= T204), T411 (= T348), E412 (= E349), N516 (≠ T449), R521 (= R454), K604 (= K537)
- binding adenosine monophosphate: G382 (= G322), E383 (= E323), P384 (= P324), T407 (≠ H344), W408 (≠ Y345), W409 (≠ G346), Q410 (= Q347), T411 (= T348), D495 (= D428), I507 (≠ F440), R510 (= R443), N516 (≠ T449), R521 (= R454)
- binding coenzyme a: F158 (= F126), R186 (= R153), W304 (= W248), T306 (≠ Y250), P329 (vs. gap), A352 (≠ S293), A355 (= A296), S518 (= S451), R579 (= R512), P584 (≠ A517)
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)
33% identity, 90% coverage: 40:545/561 of query aligns to 84:626/662 of P78773
- T596 (≠ R514) modified: Phosphothreonine
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
32% identity, 90% coverage: 41:545/561 of query aligns to 71:613/640 of 5jrhA
- active site: T260 (= T204), T412 (= T348), E413 (= E349), N517 (≠ T449), R522 (= R454), K605 (= K537)
- binding (r,r)-2,3-butanediol: W93 (≠ I60), E140 (= E107), G169 (≠ H136), K266 (vs. gap), P267 (= P210)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G322), E384 (= E323), P385 (= P324), T408 (≠ H344), W409 (≠ Y345), W410 (≠ G346), Q411 (= Q347), T412 (= T348), D496 (= D428), I508 (≠ F440), N517 (≠ T449), R522 (= R454)
- binding coenzyme a: F159 (= F126), G160 (≠ T127), G161 (≠ A128), R187 (= R153), S519 (= S451), R580 (= R512), P585 (≠ A517)
- binding magnesium ion: V533 (≠ I465), H535 (= H467), I538 (≠ V470)
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)
32% identity, 90% coverage: 41:545/561 of query aligns to 75:617/652 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 (≠ Y250) binding
- N335 (vs. gap) binding
- A357 (≠ S293) 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 (= D445) 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 (= S451) binding
- G524 (= G452) 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 (= R454) 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 (= R512) 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 (= K537) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
32% identity, 90% coverage: 41:545/561 of query aligns to 71:613/641 of 2p20A
- active site: T260 (= T204), T412 (= T348), E413 (= E349), N517 (≠ T449), R522 (= R454), K605 (= K537)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G322), E384 (= E323), P385 (= P324), T408 (≠ H344), W409 (≠ Y345), W410 (≠ G346), Q411 (= Q347), T412 (= T348), D496 (= D428), I508 (≠ F440), R511 (= R443), R522 (= R454)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
32% identity, 90% coverage: 41:545/561 of query aligns to 71:613/634 of 1pg3A
- active site: T260 (= T204), T412 (= T348), E413 (= E349), N517 (≠ T449), R522 (= R454), K605 (= K537)
- binding coenzyme a: F159 (= F126), G160 (≠ T127), R187 (= R153), R190 (vs. gap), A301 (= A244), T307 (≠ Y250), P330 (vs. gap), A356 (= A296), S519 (= S451), R580 (= R512), P585 (≠ A517)
- binding magnesium ion: V533 (≠ I465), H535 (= H467), I538 (≠ V470)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G322), E384 (= E323), P385 (= P324), T408 (≠ H344), W409 (≠ Y345), W410 (≠ G346), Q411 (= Q347), T412 (= T348), D496 (= D428), R511 (= R443), R522 (= R454)
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)
31% identity, 92% coverage: 41:557/561 of query aligns to 73:637/651 of P9WQD1
- K617 (= K537) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
35% identity, 86% coverage: 56:540/561 of query aligns to 53:538/561 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 (= P324), D340 (= D343), F341 (≠ H344), Y342 (= Y345), G343 (= G346), Q344 (= Q347), T345 (= T348), D426 (= D428), F438 (= F440), K447 (≠ T449), R452 (= R454)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
35% identity, 86% coverage: 56:540/561 of query aligns to 54:539/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
35% identity, 86% coverage: 56:540/561 of query aligns to 55:540/562 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 (≠ Y253), G321 (= G322), E322 (= E323), P323 (= P324), D342 (= D343), F343 (≠ H344), Y344 (= Y345), Q346 (= Q347), T347 (= T348), D428 (= D428), F440 (= F440), K449 (≠ T449), R454 (= R454)
- binding coenzyme a: N128 (≠ A128), W247 (= W248), K249 (≠ Y250), K273 (≠ P272), L274 (≠ F273), Q300 (≠ L299), D452 (≠ G452), Y453 (= Y453), R483 (= R483), P517 (≠ A517)
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)
31% identity, 90% coverage: 41:545/561 of query aligns to 74:614/648 of Q89WV5
- G263 (= G206) mutation to I: Loss of activity.
- G266 (= G209) mutation to I: Great decrease in activity.
- K269 (≠ A211) mutation to G: Great decrease in activity.
- E414 (= E349) mutation to Q: Great decrease in activity.
Query Sequence
>PP_2213 FitnessBrowser__Putida:PP_2213
MLQLQKQETRSPMMRDYAEAARTFDHDQAVVTALHGNLEALNACVECCDRHAGDGKLALI
HEDRDGNSACYSFDQLQVQAARFANVLKAQGVGAGDRVAGLMPRTPELLVTILATWRLGA
VYQPLFTAFGPKAIEHRLEQSHARVVVTDSHNRAKLDDVHACPTIITVKARSGELDFQQC
LERAADVCEPVMRSGNDPFLLMFTSGTTGPAKPLEVPLRAIVAFQGYMRDAIELLPEDNF
WNLADPGWAYGLYYAVTGPLSLGHATTFYDGPFSVESCARVIDKLGITNLAGSPTAYRLL
IAAGKDFSAPIKGRLRVVSSAGEPLNPEVIRWFADELGVTIHDHYGQTELGMVLCNHHGL
QHPVHLGSAGYAIPGHRIVVVDEQGNELPAGQPGILAVDREQSPLCWFGGYHGLPTKAFV
GKYYLSGDTVELNPDGSISFVGRSDDVITTSGYRVGPFDVESALIEHPAVIEAAVIGKPD
PERTELIKAFVVLASGYAGSVELEETLRQHVRQRLYAHAYPREIEFVSELPKTPSGKLQR
FILRNQEVAKQQAQQATPASV
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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