SitesBLAST
Comparing WP_015799889.1 NCBI__GCF_000022745.1:WP_015799889.1 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)
34% identity, 91% coverage: 21:343/354 of query aligns to 32:374/476 of A0A0K2JL82
- N93 (≠ V82) mutation to A: Slight decrease in activity.
- D125 (= D111) mutation D->N,V: Almost loss of activity.
- R137 (= R123) binding fumarate
- R140 (≠ D126) binding fumarate
- R201 (≠ Q187) binding fumarate
- H253 (= H226) mutation to A: Loss of activity.
- S302 (= S271) mutation to A: Loss of activity.
- K308 (= K277) binding fumarate; mutation to A: Loss of activity.
- N310 (= N279) binding fumarate; mutation to A: Loss of activity.
- R341 (= R310) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
34% identity, 91% coverage: 21:343/354 of query aligns to 18:343/439 of 5xnzA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
26% identity, 89% coverage: 19:334/354 of query aligns to 7:324/427 of 2x75A
Sites not aligning to the query:
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
26% identity, 92% coverage: 20:345/354 of query aligns to 9:343/431 of P12047
- H89 (= H104) mutation to Q: Abolishes enzyme activity.
- H141 (≠ R156) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ W225) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N279) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R310) mutation R->K,Q: Abolishes enzyme activity.
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)
25% identity, 93% coverage: 21:348/354 of query aligns to 10:335/431 of Q9X0I0
- H141 (≠ R156) active site, Proton donor/acceptor
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
28% identity, 71% coverage: 41:291/354 of query aligns to 39:302/477 of 5nx9D
- active site: H79 (≠ D80), T151 (= T155), H152 (≠ R156), S283 (= S272), K288 (= K277), E295 (= E284)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T155), H152 (≠ R156)
- binding adenosine monophosphate: R78 (= R79), H79 (≠ D80), D80 (≠ G81), S105 (= S109), Q234 (= Q224), R296 (≠ L285)
- binding fumaric acid: H79 (≠ D80), S105 (= S109), Q234 (= Q224), S282 (= S271), S283 (= S272), K288 (= K277)
Sites not aligning to the query:
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
28% identity, 71% coverage: 41:291/354 of query aligns to 46:309/484 of P30566
- I72 (≠ M66) to V: in ADSLD; severe
- P100 (≠ G96) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D111) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (= R138) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ R156) active site, Proton donor/acceptor
- R190 (≠ Q187) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ Q191) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ R229) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D252) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S271) active site, Proton donor/acceptor
- R303 (≠ L285) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
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
- 26 M → L: in ADSLD; severe; dbSNP:rs1311171245
- 311 L → V: in ADSLD; severe; slightly reduced enzyme activity; dbSNP:rs2044791112
- 318 P → L: in ADSLD; severe; dbSNP:rs202064195
- 364 V → M: in ADSLD; severe; dbSNP:rs370851726
- 374 R → W: in ADSLD; severe; dbSNP:rs376533026
- 395 S → R: in ADSLD; severe
- 396 R → C: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs755492501; R → H: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs763542069
- 422 D → Y: in ADSLD; moderate; dbSNP:rs119450943
- 423 L → V: in ADSLD; moderate
- 426 R → H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- 430 D → N: in ADSLD; mild; dbSNP:rs554254383
- 438 S → P: in ADSLD; severe; dbSNP:rs119450940
- 447 S → P: in ADSLD; severe; dbSNP:rs777821034
- 450 T → S: in ADSLD; moderate; dbSNP:rs372895468
- 452 R → P: in ADSLD; severe; dbSNP:rs775671027
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, 77% coverage: 19:291/354 of query aligns to 18:306/482 of Q05911
- K196 (≠ A196) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
G4VQX9 Adenylosuccinate lyase; ADSL; Adenylosuccinase; SmADSL; EC 4.3.2.2 from Schistosoma mansoni (Blood fluke) (see paper)
26% identity, 68% coverage: 103:344/354 of query aligns to 100:358/480 of G4VQX9
- Q236 (= Q228) binding AMP
- R298 (≠ L285) binding AMP
- S329 (≠ W315) binding AMP
- R333 (≠ W319) binding AMP
Sites not aligning to the query:
- 14 binding AMP
- 15 binding AMP
- 79 binding AMP
- 80 binding AMP
- 81 binding AMP
2qgaC Plasmodium vivax adenylosuccinate lyase pv003765 with amp bound
25% identity, 63% coverage: 62:284/354 of query aligns to 66:301/455 of 2qgaC
Sites not aligning to the query:
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
29% identity, 53% coverage: 105:291/354 of query aligns to 39:240/415 of 5nxaB
- active site: T89 (= T155), H90 (≠ R156), S221 (= S272), K226 (= K277), E233 (= E284)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V281), R234 (≠ L285)
- binding fumaric acid: S220 (= S271), S221 (= S272), M223 (= M274), K226 (= K277), N228 (= N279)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S109), T89 (= T155), H90 (≠ R156), Q172 (= Q224)
Sites not aligning to the query:
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
27% identity, 80% coverage: 19:301/354 of query aligns to 18:315/469 of 5vkwB
Sites not aligning to the query:
4efcA Crystal structure of adenylosuccinate lyase from trypanosoma brucei, tb427tmp.160.5560
29% identity, 61% coverage: 69:284/354 of query aligns to 86:312/452 of 4efcA
- active site: H96 (≠ R79), T173 (= T155), H174 (≠ R156), S300 (= S272), K305 (= K277), E312 (= E284)
- binding adenosine monophosphate: N95 (≠ A78), H96 (≠ R79), D97 (= D80), S127 (= S109), Q128 (= Q110), I309 (≠ V281)
- binding magnesium ion: D274 (≠ A254), D278 (≠ E258)
Sites not aligning to the query:
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
23% identity, 77% coverage: 11:284/354 of query aligns to 12:308/456 of P0AB89
- RY 15:16 (≠ LF 14:15) binding AMP; binding N(6)-(1,2-dicarboxyethyl)-AMP
- NHD 90:92 (≠ ARD 78:80) binding AMP; binding N(6)-(1,2-dicarboxyethyl)-AMP
- H91 (≠ R79) binding fumarate
- K94 (≠ P85) modified: N6-acetyllysine
- TS 122:123 (= TS 108:109) binding fumarate; binding N(6)-(1,2-dicarboxyethyl)-AMP
- H171 (≠ R156) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (= Q228) binding AMP; binding fumarate; binding N(6)-(1,2-dicarboxyethyl)-AMP
- S295 (= S271) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S272) binding fumarate; binding N(6)-(1,2-dicarboxyethyl)-AMP
- KVN 301:303 (≠ KQN 277:279) binding fumarate; binding N(6)-(1,2-dicarboxyethyl)-AMP
Sites not aligning to the query:
- 309 binding AMP; binding N(6)-(1,2-dicarboxyethyl)-AMP
- 335 binding AMP; binding N(6)-(1,2-dicarboxyethyl)-AMP
- 340:344 binding AMP; binding N(6)-(1,2-dicarboxyethyl)-AMP
- 366 modified: N6-acetyllysine
2ptqA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171n with bound amp and fumarate (see paper)
23% identity, 77% coverage: 11:284/354 of query aligns to 12:308/459 of 2ptqA
- active site: H91 (≠ R79), T170 (= T155), N171 (≠ R156), S296 (= S272), K301 (= K277), E308 (= E284)
- binding adenosine monophosphate: R15 (≠ L14), Y16 (≠ F15), N90 (≠ A78), H91 (≠ R79), Q247 (= Q228)
- binding fumaric acid: H91 (≠ R79), T122 (= T108), S123 (= S109), Q247 (= Q228), S295 (= S271), S296 (= S272), M298 (= M274), K301 (= K277), N303 (= N279)
Sites not aligning to the query:
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
23% identity, 77% coverage: 11:284/354 of query aligns to 12:308/454 of 2ptrA
- active site: H91 (≠ R79), T170 (= T155), A171 (≠ R156), K301 (= K277), E308 (= E284)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: R15 (≠ L14), Y16 (≠ F15), H91 (≠ R79), D92 (= D80), T122 (= T108), S123 (= S109), Q247 (= Q228), S295 (= S271), S296 (= S272), M298 (= M274), K301 (= K277), N303 (= N279)
Sites not aligning to the query:
3gzhA Crystal structure of phosphate-bound adenylosuccinate lyase from e. Coli (see paper)
23% identity, 77% coverage: 11:284/354 of query aligns to 25:321/469 of 3gzhA
Sites not aligning to the query:
5nx9C Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
26% identity, 71% coverage: 41:291/354 of query aligns to 38:287/441 of 5nx9C
- active site: H78 (≠ D80), T150 (= T155), H151 (≠ R156), E280 (= E284)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: R77 (= R79), H78 (≠ D80), D79 (≠ G81), T103 (= T108), S104 (= S109), Q233 (= Q224), M277 (≠ V281), R281 (≠ L285)
- binding fumaric acid: T150 (= T155), H151 (≠ R156)
Sites not aligning to the query:
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
26% identity, 71% coverage: 41:291/354 of query aligns to 39:289/464 of 5nxaA
- active site: H79 (≠ D80), T151 (= T155), H152 (≠ R156), K275 (= K277), E282 (= E284)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: R78 (= R79), H79 (≠ D80), D80 (≠ G81), T104 (= T108), S105 (= S109), Q234 (= Q224), K275 (= K277), R283 (≠ L285)
Sites not aligning to the query:
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
26% identity, 71% coverage: 41:291/354 of query aligns to 38:290/418 of 5nxaC
- active site: H78 (≠ D80), T150 (= T155), H151 (≠ R156), K276 (= K277), E283 (= E284)
- binding aminoimidazole 4-carboxamide ribonucleotide: R77 (= R79), H78 (≠ D80), D79 (≠ G81), Q233 (= Q224)
- binding fumaric acid: H78 (≠ D80), T103 (= T108), S104 (= S109), Q233 (= Q224)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: T150 (= T155), H151 (≠ R156), K276 (= K277), R284 (≠ L285)
Sites not aligning to the query:
Query Sequence
>WP_015799889.1 NCBI__GCF_000022745.1:WP_015799889.1
MSISVFEHPFLTGLFGDDEEISSLFTAYADIAAMLKFEAALAGAQADLGIIPAHAAERIM
SATETMEPDLAQLEHGTARDGVVVPALVRNLRKTVGEDVAAHVHFGATSQDVIDTSLMLR
LARVRDILVARIEQLSERFNWLETTFGQNDLTAYTRMQPAISTTVADRVESWRAPFSDYA
QRLAALQFPLQFGGAAGTLEKFVGKGAKLRAELAKRLGLEDRPQWHSQRAFIADFGHLLS
LVTGSLGKFGQDIALMAELRDEISLSGGGGSSAMPHKQNPVRAELLVTLARFNAVQVSGL
HQAMVHEQERSGTAWMLEWMILPPVVAATGAALKAALVLSENIVRMGKDRLPET
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