SitesBLAST
Comparing H281DRAFT_02594 FitnessBrowser__Burk376:H281DRAFT_02594 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)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
38% identity, 96% coverage: 12:451/456 of query aligns to 17:469/476 of A0A0K2JL82
- N93 (≠ Y88) mutation to A: Slight decrease in activity.
- D125 (= D116) mutation D->N,V: Almost loss of activity.
- R137 (≠ D128) binding
- R140 (≠ D131) binding
- R201 (= R192) binding
- H253 (= H235) mutation to A: Loss of activity.
- S302 (= S284) mutation to A: Loss of activity.
- K308 (= K290) binding ; mutation to A: Loss of activity.
- N310 (= N292) binding ; mutation to A: Loss of activity.
- R341 (= R323) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
36% identity, 96% coverage: 12:451/456 of query aligns to 3:438/439 of 5xnzA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
28% identity, 94% coverage: 20:449/456 of query aligns to 2:424/427 of 2x75A
Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
27% identity, 94% coverage: 20:448/456 of query aligns to 3:427/431 of Q9X0I0
- H141 (= H161) active site, Proton donor/acceptor
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
29% identity, 90% coverage: 20:429/456 of query aligns to 3:408/431 of P12047
- H89 (= H109) mutation to Q: Abolishes enzyme activity.
- H141 (= H161) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ W234) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N292) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R323) mutation R->K,Q: Abolishes enzyme activity.
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
27% identity, 94% coverage: 22:448/456 of query aligns to 21:459/484 of P30566
- M26 (= M27) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (= I74) to V: in ADSLD; severe
- P100 (≠ G102) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D116) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ I143) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (= H161) active site, Proton donor/acceptor
- R190 (= R192) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ A196) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ D239) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D261) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S284) active site, Proton donor/acceptor
- R303 (≠ L298) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ Q309) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (vs. gap) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V358) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ G368) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (vs. gap) to R: in ADSLD; severe
- R396 (= R389) to C: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs755492501; to H: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs763542069
- D422 (≠ A413) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L414) to V: in ADSLD; moderate
- R426 (≠ L417) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (≠ T421) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (≠ D427) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ A436) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ L439) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ L441) to P: in ADSLD; severe
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine; A → V: in ADSLD; severe; dbSNP:rs143083947
- 3 A → V: in ADSLD; severe
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
26% identity, 94% coverage: 22:448/456 of query aligns to 14:452/477 of 5nx9D
- active site: H79 (≠ Y88), T151 (= T160), H152 (= H161), S283 (= S285), K288 (= K290), E295 (= E297)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T160), H152 (= H161)
- binding adenosine monophosphate: Y14 (≠ F22), R78 (≠ G87), H79 (≠ Y88), D80 (≠ P89), S105 (≠ T114), Q234 (≠ W234), R296 (≠ L298), L324 (≠ T325), S327 (≠ W328), A328 (≠ H329), R331 (≠ W332)
- binding fumaric acid: H79 (≠ Y88), S105 (≠ T114), Q234 (≠ W234), S282 (= S284), S283 (= S285), K288 (= K290)
Sites not aligning to the query:
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 98% coverage: 5:450/456 of query aligns to 8:458/482 of Q05911
- K196 (≠ A201) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
26% identity, 75% coverage: 22:361/456 of query aligns to 5:327/419 of 5hw2A
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
26% identity, 75% coverage: 22:361/456 of query aligns to 5:327/423 of 4eeiB
- active site: H67 (≠ T83), S140 (≠ T160), H141 (= H161), K256 (= K290), E263 (= E297)
- binding adenosine monophosphate: K66 (≠ E82), H67 (≠ T83), D68 (= D84), Q212 (≠ W234), R289 (= R323), I291 (≠ T325), S294 (≠ W328), R298 (≠ W332)
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
25% identity, 98% coverage: 5:450/456 of query aligns to 8:451/469 of 5vkwB
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
24% identity, 94% coverage: 22:448/456 of query aligns to 14:439/464 of 5nxaA
- active site: H79 (≠ Y88), T151 (= T160), H152 (= H161), K275 (= K290), E282 (= E297)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: Y14 (≠ F22), R78 (≠ G87), H79 (≠ Y88), D80 (≠ P89), T104 (= T113), S105 (≠ T114), Q234 (≠ W234), K275 (= K290), R283 (≠ L298), L311 (≠ T325), S314 (≠ W328), A315 (≠ H329), R318 (≠ W332)
Sites not aligning to the query:
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
26% identity, 82% coverage: 22:394/456 of query aligns to 13:389/472 of 5eytA
Sites not aligning to the query:
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
25% identity, 80% coverage: 22:387/456 of query aligns to 13:374/418 of 5nxaC
- active site: H78 (≠ Y88), T150 (= T160), H151 (= H161), K276 (= K290), E283 (= E297)
- binding aminoimidazole 4-carboxamide ribonucleotide: R77 (≠ G87), H78 (≠ Y88), D79 (≠ P89), Q233 (≠ W234), L312 (≠ T325), S315 (≠ W328), A316 (≠ H329), R319 (≠ W332)
- binding fumaric acid: H78 (≠ Y88), T103 (= T113), S104 (≠ T114), Q233 (≠ W234)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: Y13 (≠ F22), T150 (= T160), H151 (= H161), K276 (= K290), R284 (≠ L298)
Sites not aligning to the query:
5nx9C Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
23% identity, 94% coverage: 22:448/456 of query aligns to 13:428/441 of 5nx9C
- active site: H78 (≠ Y88), T150 (= T160), H151 (= H161), E280 (= E297)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: Y13 (≠ F22), R77 (≠ G87), H78 (≠ Y88), D79 (≠ P89), T103 (= T113), S104 (≠ T114), Q233 (≠ W234), M277 (≠ I294), R281 (≠ L298), L309 (≠ T325), S312 (≠ W328), A313 (≠ H329), R316 (≠ W332)
- binding fumaric acid: T150 (= T160), H151 (= H161)
Sites not aligning to the query:
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
25% identity, 75% coverage: 107:448/456 of query aligns to 36:390/415 of 5nxaB
- active site: T89 (= T160), H90 (= H161), S221 (= S285), K226 (= K290), E233 (= E297)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ I294), R234 (≠ L298)
- binding fumaric acid: S220 (= S284), S221 (= S285), M223 (= M287), K226 (= K290), N228 (= N292)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (≠ T114), T89 (= T160), H90 (= H161), Q172 (≠ W234), L262 (≠ T325), S265 (≠ W328), A266 (≠ H329), R269 (≠ W332)
Sites not aligning to the query:
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
25% identity, 93% coverage: 29:453/456 of query aligns to 16:446/451 of 1tj7B
3gzhA Crystal structure of phosphate-bound adenylosuccinate lyase from e. Coli (see paper)
25% identity, 92% coverage: 27:447/456 of query aligns to 36:466/469 of 3gzhA
- active site: H104 (≠ E81), T183 (= T160), H184 (= H161), S309 (= S285), K314 (= K290), E321 (vs. gap)
- binding phosphate ion: H104 (≠ E81), T135 (= T113), S136 (≠ T114), S353 (≠ A324), T354 (= T325), R357 (≠ W328)
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
25% identity, 92% coverage: 27:447/456 of query aligns to 23:453/456 of P0AB89
- NHD 90:92 (≠ REE 80:82) binding ; binding
- H91 (≠ E81) binding
- K94 (≠ D84) modified: N6-acetyllysine
- TS 122:123 (≠ TT 113:114) binding ; binding
- H171 (= H161) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (≠ W234) binding ; binding ; binding
- S295 (= S284) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S285) binding ; binding
- KVN 301:303 (≠ KRN 290:292) binding ; binding
- N309 (≠ S295) binding ; binding
- R335 (≠ Q319) binding ; binding
- STVLR 340:344 (≠ ATGPW 324:328) binding ; binding
- K366 (≠ G355) modified: N6-acetyllysine
Sites not aligning to the query:
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
27% identity, 48% coverage: 96:314/456 of query aligns to 95:312/464 of P04424
- R95 (≠ Q96) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (≠ T114) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ A121) to E: in ARGINSA; severe
- V178 (≠ A179) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ D182) to S: in a breast cancer sample; somatic mutation
- R182 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R187) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (≠ A201) to V: in a breast cancer sample; somatic mutation
- R236 (= R238) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D239) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q289) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R291) modified: N6-acetyllysine; mutation to R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.
- R297 (≠ L300) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ Q308) to W: in ARGINSA; severe; dbSNP:rs868834862
Sites not aligning to the query:
- 12 R → Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- 31 D → N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- 51 K→N: 2-fold reduction in activity.
- 69 modified: N6-acetyllysine
- 73 E → K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- 87 D → G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- 89 H→Q: 10-fold reduction in activity.
- 94 R → C: in ARGINSA; severe; dbSNP:rs374304304
- 326 Q → L: in ARGINSA; severe
- 335 V → L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- 360 M → T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- 382 M → R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- 385 R → L: in ARGINSA; severe
- 388 H → Q: in ARGINSA; severe
- 398 A → D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- 456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
Query Sequence
>H281DRAFT_02594 FitnessBrowser__Burk376:H281DRAFT_02594
MTTRTTPLSSTVFDSILFRDAFGTAKMRALFSDYALVQRYIDVEVALAKAEARVGVIPTD
AADVIARESQIERIDFDHMREETDIVGYPILPLVHQLVGMCGEAGRYVHWGATTQDIMDT
AVALQVRDALDSIDADIRELRGILVDLSKKHRDTPMAGRTHLQQALPVTFGYKTAIWLAM
FDRHQQRIAQLRPRVAVVEFAGAAGTLASLGDKGFDVQKALAAELQLGVPATTWHVARDG
FAEAVNLLALVTGSLGKIATDIMIMASNEFGEVYEPFVKGRGASSTMPQKRNPISSELML
AAAKAVRQQAGLMVDAMIQDFERATGPWHAEWIAIPESFILASGALHQAKFALGGLIVDT
DRMKHNLGISKGLIVAEAVMMQMAPYTGRQQAHDIVYDACRTVNESGGTLAEALAALPEV
TRHFDRDAINAMTDPANYLGLAPQMVDRAIALSSEI
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