SitesBLAST
Comparing SMc00774 FitnessBrowser__Smeli:SMc00774 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4wd1A Acetoacetyl-coa synthetase from streptomyces lividans (see paper)
44% identity, 99% coverage: 5:648/650 of query aligns to 2:641/646 of 4wd1A
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)
28% identity, 93% coverage: 36:640/650 of query aligns to 21:636/648 of Q89WV5
- G263 (= G273) mutation to I: Loss of activity.
- G266 (= G276) mutation to I: Great decrease in activity.
- K269 (= K279) mutation to G: Great decrease in activity.
- E414 (≠ I416) mutation to Q: Great decrease in activity.
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)
28% identity, 93% coverage: 34:640/650 of query aligns to 31:648/662 of P78773
- T596 (≠ G589) 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, 86% coverage: 80:640/650 of query aligns to 65:645/651 of P9WQD1
- K617 (= K612) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
26% identity, 96% coverage: 30:650/650 of query aligns to 23:641/641 of 2p20A
- active site: T260 (≠ S271), T412 (≠ S415), E413 (≠ I416), N517 (= N525), R522 (= R530), K605 (= K612)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G392), E384 (≠ S393), P385 (= P394), T408 (≠ V411), W409 (≠ Q412), W410 (≠ L413), Q411 (≠ A414), T412 (≠ S415), D496 (= D504), I508 (= I516), R511 (= R519), R522 (= R530)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
26% identity, 96% coverage: 30:650/650 of query aligns to 23:640/640 of 5jrhA
- active site: T260 (≠ S271), T412 (≠ S415), E413 (≠ I416), N517 (= N525), R522 (= R530), K605 (= K612)
- binding (r,r)-2,3-butanediol: W93 (≠ F106), E140 (= E152), G169 (≠ D181), K266 (≠ V277), P267 (= P278)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G392), E384 (≠ S393), P385 (= P394), T408 (≠ V411), W409 (≠ Q412), W410 (≠ L413), Q411 (≠ A414), T412 (≠ S415), D496 (= D504), I508 (= I516), N517 (= N525), R522 (= R530)
- binding coenzyme a: F159 (≠ S171), G160 (≠ P172), G161 (≠ D173), R187 (≠ Y199), S519 (≠ G527), R580 (= R587), P585 (= P592)
- binding magnesium ion: V533 (≠ E541), H535 (≠ M543), I538 (≠ V546)
5k8fA Crystal structure of acetyl-coa synthetase in complex with atp and acetyl-amp from cryptococcus neoformans h99
27% identity, 84% coverage: 79:626/650 of query aligns to 84:645/656 of 5k8fA
- active site: T280 (≠ S271), T432 (vs. gap), E433 (≠ S417), N539 (= N525), R544 (= R530), K631 (= K612)
- 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: W325 (= W316), I326 (≠ M317), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (vs. gap), Y429 (vs. gap), W430 (vs. gap), M431 (vs. gap), T432 (vs. gap), D518 (= D504), I530 (= I516), R533 (= R519), K631 (= K612)
- binding adenosine-5'-triphosphate: T280 (≠ S271), S281 (= S272), G282 (= G273), S283 (≠ T274), T284 (= T275), K288 (= K279), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (vs. gap), Y429 (vs. gap), M431 (vs. gap), T432 (vs. gap), D518 (= D504), I530 (= I516), R533 (= R519), K631 (= K612)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
27% identity, 86% coverage: 79:640/650 of query aligns to 84:661/668 of 7l4gB
- active site: T280 (≠ S271), T432 (vs. gap), E433 (≠ S417), N539 (= N525), R544 (= R530), K631 (= K612)
- 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: W325 (= W316), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (vs. gap), Y429 (vs. gap), W430 (vs. gap), M431 (vs. gap), T432 (vs. gap), D518 (= D504), I530 (= I516), R533 (= R519)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
27% identity, 86% coverage: 79:640/650 of query aligns to 84:661/668 of 5u29A
- active site: T280 (≠ S271), T432 (vs. gap), E433 (≠ S417), N539 (= N525), R544 (= R530), K631 (= K612)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W316), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (vs. gap), Y429 (vs. gap), W430 (vs. gap), M431 (vs. gap), T432 (vs. gap), D518 (= D504), I530 (= I516), R533 (= R519)
8w0dA Acetyl-coenzyme A synthetase 2
26% identity, 97% coverage: 12:640/650 of query aligns to 19:654/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G392), E399 (≠ S393), P400 (= P394), T423 (vs. gap), Y424 (vs. gap), W425 (vs. gap), Q426 (≠ S415), T427 (≠ I416), D513 (= D504), I525 (= I516), R528 (= R519), R539 (= R530)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
26% identity, 97% coverage: 12:640/650 of query aligns to 19:654/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G392), E399 (≠ S393), P400 (= P394), T423 (vs. gap), Y424 (vs. gap), Q426 (≠ S415), T427 (≠ I416), D513 (= D504), I525 (= I516), R528 (= R519), R539 (= R530)
- binding coenzyme a: F175 (≠ S171), R203 (= R203), R206 (≠ V206), G316 (≠ T312), H538 (≠ V529), R599 (= R587), F605 (≠ R593)
8w0cA Acetyl-coenzyme A synthetase 2
26% identity, 97% coverage: 12:640/650 of query aligns to 20:655/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G392), E400 (≠ S393), P401 (= P394), T424 (vs. gap), Y425 (vs. gap), W426 (vs. gap), Q427 (≠ S415), T428 (≠ I416), D514 (= D504), R529 (= R519), R540 (= R530)
8w0bA Acetyl-coenzyme A synthetase 2
26% identity, 97% coverage: 12:640/650 of query aligns to 20:655/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ T391), G399 (= G392), E400 (≠ S393), P401 (= P394), T424 (vs. gap), Y425 (vs. gap), W426 (vs. gap), Q427 (≠ S415), T428 (≠ I416), D514 (= D504), I526 (= I516), R529 (= R519), R540 (= R530)
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
26% identity, 97% coverage: 12:640/650 of query aligns to 19:644/654 of 7kdsA
- active site: T275 (≠ S271), T427 (≠ I416), E428 (≠ S417), N534 (= N525), R539 (= R530), K620 (= K612)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ M317), G398 (= G392), E399 (≠ S393), P400 (= P394), D422 (vs. gap), T423 (vs. gap), Y424 (vs. gap), W425 (vs. gap), Q426 (≠ S415), T427 (≠ I416), D513 (= D504), R528 (= R519), N534 (= N525), R539 (= R530)
8w0jA Acetyl-coenzyme A synthetase 2
26% identity, 97% coverage: 12:640/650 of query aligns to 20:650/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G392), E400 (≠ S393), P401 (= P394), T424 (vs. gap), Y425 (vs. gap), W426 (vs. gap), Q427 (≠ S415), T428 (≠ I416), D514 (= D504), I526 (= I516), R529 (= R519), R540 (= R530)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
26% identity, 97% coverage: 12:640/650 of query aligns to 19:649/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P148), A176 (≠ P172), G177 (≠ D173), R203 (= R203), T208 (≠ S208), D317 (≠ T313), E342 (≠ D336), G343 (= G337), P345 (= P339), G398 (= G392), E399 (≠ S393), P400 (= P394), T423 (vs. gap), W425 (vs. gap), Q426 (≠ S415), T427 (≠ I416), D513 (= D504), I525 (= I516), R528 (= R519), R539 (= R530)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
26% identity, 97% coverage: 12:640/650 of query aligns to 19:649/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G392), E399 (≠ S393), P400 (= P394), T423 (vs. gap), Y424 (vs. gap), W425 (vs. gap), Q426 (≠ S415), T427 (≠ I416), D513 (= D504), I525 (= I516), R528 (= R519), R539 (= R530)
Q9NR19 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see paper)
25% identity, 93% coverage: 34:639/650 of query aligns to 43:689/701 of Q9NR19
- T363 (≠ M318) mutation to A: Loss of catlytic activity but no effect on its nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- 656:668 (vs. 607:619, 46% identical) Nuclear localization signal
- S659 (= S610) modified: Phosphoserine; by AMPK; mutation to A: No effect on catalytic activity. Loss of AMPK-mediated phosphorylation, interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- RR 664:665 (≠ EL 615:616) mutation to AA: No effect on catalytic activity. Loss of interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
Sites not aligning to the query:
- 1:107 Interaction with TFEB
8v5gA Crystal structure of acetyl-coa synthetase from cryptococcus neoformans h99 in complex with an ethylsulfamide amp inhibitor
27% identity, 84% coverage: 79:624/650 of query aligns to 83:640/655 of 8v5gA
- binding 5'-deoxy-5'-(ethylsulfamamido)adenosine: V401 (≠ T391), G402 (= G392), E403 (≠ S393), P404 (= P394), T427 (vs. gap), Y428 (vs. gap), W429 (vs. gap), M430 (vs. gap), D517 (= D504), I529 (= I516), K628 (= K612)
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
27% identity, 86% coverage: 79:640/650 of query aligns to 84:659/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W316), I324 (≠ M317), V400 (≠ T391), G401 (= G392), E402 (≠ S393), P403 (= P394), T426 (vs. gap), Y427 (vs. gap), W428 (vs. gap), M429 (vs. gap), T430 (vs. gap), D516 (= D504)
Query Sequence
>SMc00774 FitnessBrowser__Smeli:SMc00774
MQAERPLWVPDREIVERSPMAEFIDWCGERFGRSFADYDAFHDWSVSERGAFWTAVWEHC
KVIGESGEKALVDGDRMLDARFFPEARLNFAENLLRKTGSGDALIFRGEDKVSYRLTWDE
LRALVSRLQQALRAQGIGAGDRVAAMMPNMPETIALMLATASVGAIWSSCSPDFGEQGVL
DRFGQIAPKLFIVCDGYWYNGKRQDVDSKVRAVAKSLGAPTVIVPYAGDSAALAPTVEGG
VTLADFIAGFQAGPLVFERLPFGHPLYILFSSGTTGVPKCIVHSAGGTLLQHLKEHRFHC
GLRDGERLFYFTTCGWMMWNWLASGLAVGATLCLYDGSPFCPDGNVLFDYAAAERFAVFG
TSAKYIDAVRKGGFTPARTHDLSSLRLMTSTGSPLSPEGFSFVYEGIKPDVQLASISGGT
DIVSCFVLGNPLKPVWRGEIQGPGLGLAVDVWNDEGKPVRGEKGELVCTRAFPSMPVMFW
NDPDGAKYRAAYFDRFDNVWCHGDFAEWTPHGGIVIHGRSDATLNPGGVRIGTAEIYNQV
EQMDEVAEALCIGQDWEDDVRVVLFVRLARGVELTEALTREIKNRIRSGASPRHVPAKII
AVADIPRTKSGKIVELAVRDVVHGRPVKNKEALANPEALDLFAGLEELKS
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