SitesBLAST
Comparing AZOBR_RS28125 FitnessBrowser__azobra:AZOBR_RS28125 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, 99% coverage: 5:452/453 of query aligns to 17:476/476 of A0A0K2JL82
- N93 (≠ Y81) mutation to A: Slight decrease in activity.
- D125 (= D110) mutation D->N,V: Almost loss of activity.
- R137 (≠ E122) binding
- R140 (≠ N125) binding
- R201 (= R186) binding
- H253 (= H229) mutation to A: Loss of activity.
- S302 (= S278) mutation to A: Loss of activity.
- K308 (= K284) binding ; mutation to A: Loss of activity.
- N310 (= N286) binding ; mutation to A: Loss of activity.
- R341 (= R317) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
37% identity, 98% coverage: 5:446/453 of query aligns to 3:439/439 of 5xnzA
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)
29% identity, 96% coverage: 15:449/453 of query aligns to 5:430/431 of Q9X0I0
- H141 (≠ N155) 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, 95% coverage: 15:443/453 of query aligns to 5:428/431 of P12047
- H89 (= H103) mutation to Q: Abolishes enzyme activity.
- H141 (≠ N155) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ H229) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N286) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R317) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
29% identity, 94% coverage: 15:442/453 of query aligns to 4:423/427 of 2x75A
Sites not aligning to the query:
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
26% identity, 79% coverage: 15:370/453 of query aligns to 5:342/423 of 4eeiB
- active site: H67 (≠ T76), S140 (= S154), H141 (≠ N155), K256 (= K284), E263 (≠ C291)
- binding adenosine monophosphate: K66 (≠ Q75), H67 (≠ T76), D68 (≠ E77), Q212 (≠ H229), R289 (= R317), I291 (≠ T319), S294 (≠ W322), R298 (≠ W326)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
26% identity, 79% coverage: 15:370/453 of query aligns to 5:342/419 of 5hw2A
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
25% identity, 96% coverage: 15:451/453 of query aligns to 21:468/484 of P30566
- M26 (= M20) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (= I67) to V: in ADSLD; severe
- P100 (≠ R95) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D110) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ A137) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ N155) active site, Proton donor/acceptor
- R190 (= R186) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ L190) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ D233) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D255) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S278) active site, Proton donor/acceptor
- R303 (≠ A295) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ H303) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (vs. gap) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V352) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ E362) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (vs. gap) to R: in ADSLD; severe
- R396 (= R383) 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 (= D406) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L407) to V: in ADSLD; moderate
- R426 (≠ T411) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (≠ S415) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (≠ A421) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ A430) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ L433) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ Q435) 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)
25% identity, 96% coverage: 15:451/453 of query aligns to 14:461/477 of 5nx9D
- active site: H79 (≠ Y81), T151 (≠ S154), H152 (≠ N155), S283 (= S279), K288 (= K284), E295 (≠ H294)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (≠ S154), H152 (≠ N155)
- binding adenosine monophosphate: Y14 (≠ F15), R78 (≠ G80), H79 (≠ Y81), D80 (≠ P82), S105 (≠ T108), Q234 (≠ W228), R296 (≠ A295), L324 (≠ T319), S327 (≠ W322), A328 (≠ E323), R331 (≠ W326)
- binding fumaric acid: H79 (≠ Y81), S105 (≠ T108), Q234 (≠ W228), S282 (= S278), S283 (= S279), K288 (= K284)
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)
24% identity, 96% coverage: 15:449/453 of query aligns to 15:463/482 of Q05911
- K196 (≠ A195) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
23% identity, 97% coverage: 13:451/453 of query aligns to 5:455/469 of 5vkwB
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
24% identity, 96% coverage: 15:451/453 of query aligns to 14:448/464 of 5nxaA
- active site: H79 (≠ Y81), T151 (≠ S154), H152 (≠ N155), K275 (= K284), E282 (≠ H294)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: Y14 (≠ F15), R78 (≠ G80), H79 (≠ Y81), D80 (≠ P82), T104 (= T107), S105 (≠ T108), Q234 (≠ W228), K275 (= K284), R283 (≠ A295), L311 (≠ T319), S314 (≠ W322), A315 (≠ E323), R318 (≠ W326)
Sites not aligning to the query:
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
24% identity, 81% coverage: 15:380/453 of query aligns to 13:373/418 of 5nxaC
- active site: H78 (≠ Y81), T150 (≠ S154), H151 (≠ N155), K276 (= K284), E283 (≠ H294)
- binding aminoimidazole 4-carboxamide ribonucleotide: R77 (≠ G80), H78 (≠ Y81), D79 (≠ P82), Q233 (≠ W228), L312 (≠ T319), S315 (≠ W322), A316 (≠ E323), R319 (≠ W326)
- binding fumaric acid: H78 (≠ Y81), T103 (= T107), S104 (≠ T108), Q233 (≠ W228)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: Y13 (≠ F15), T150 (≠ S154), H151 (≠ N155), K276 (= K284), R284 (≠ A295)
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, 77% coverage: 105:451/453 of query aligns to 40:399/415 of 5nxaB
- active site: T89 (≠ S154), H90 (≠ N155), S221 (= S279), K226 (= K284), E233 (≠ H294)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ I288), R234 (≠ A295)
- binding fumaric acid: S220 (= S278), S221 (= S279), M223 (= M281), K226 (= K284), N228 (= N286)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (≠ T108), T89 (≠ S154), H90 (≠ N155), Q172 (≠ W228), L262 (≠ T319), S265 (≠ W322), A266 (≠ E323), R269 (≠ W326)
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, 96% coverage: 15:451/453 of query aligns to 13:437/441 of 5nx9C
- active site: H78 (≠ Y81), T150 (≠ S154), H151 (≠ N155), E280 (≠ H294)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: Y13 (≠ F15), R77 (≠ G80), H78 (≠ Y81), D79 (≠ P82), T103 (= T107), S104 (≠ T108), Q233 (≠ W228), M277 (≠ I288), R281 (≠ A295), L309 (≠ T319), S312 (≠ W322), A313 (≠ E323), R316 (≠ W326)
- binding fumaric acid: T150 (≠ S154), H151 (≠ N155)
Sites not aligning to the query:
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
26% identity, 75% coverage: 40:377/453 of query aligns to 38:376/472 of 5eytA
Sites not aligning to the query:
2ptqA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171n with bound amp and fumarate (see paper)
27% identity, 76% coverage: 98:443/453 of query aligns to 113:455/459 of 2ptqA
- active site: T170 (≠ S154), N171 (= N155), S296 (= S279), K301 (= K284), E308 (vs. gap)
- binding adenosine monophosphate: Q247 (vs. gap), N309 (vs. gap), R335 (= R317), L337 (vs. gap), S340 (≠ P321), T341 (≠ W322), R344 (≠ E325)
- binding fumaric acid: T122 (= T107), S123 (≠ T108), Q247 (vs. gap), S295 (= S278), S296 (= S279), M298 (= M281), K301 (= K284), N303 (= N286)
Sites not aligning to the query:
3gzhA Crystal structure of phosphate-bound adenylosuccinate lyase from e. Coli (see paper)
26% identity, 96% coverage: 11:443/453 of query aligns to 29:468/469 of 3gzhA
- active site: H104 (≠ Y81), T183 (≠ S154), H184 (≠ N155), S309 (= S279), K314 (= K284), E321 (vs. gap)
- binding phosphate ion: H104 (≠ Y81), T135 (= T107), S136 (≠ T108), S353 (≠ P321), T354 (≠ W322), R357 (≠ E325)
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
26% identity, 76% coverage: 98:443/453 of query aligns to 113:455/456 of P0AB89
- TS 122:123 (≠ TT 107:108) binding ; binding
- H171 (≠ N155) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (vs. gap) binding ; binding ; binding
- S295 (= S278) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S279) binding ; binding
- KVN 301:303 (≠ KRN 284:286) binding ; binding
- N309 (vs. gap) binding ; binding
- R335 (= R317) binding ; binding
- STVLR 340:344 (≠ PWEIE 321:325) binding ; binding
- K366 (≠ G349) modified: N6-acetyllysine
Sites not aligning to the query:
- 15:16 binding ; binding
- 90:92 binding ; binding
- 91 binding
- 94 modified: N6-acetyllysine
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
26% identity, 76% coverage: 98:443/453 of query aligns to 113:450/454 of 2ptrA
- active site: T170 (≠ S154), A171 (≠ N155), K301 (= K284), E308 (vs. gap)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T122 (= T107), S123 (≠ T108), Q247 (vs. gap), S295 (= S278), S296 (= S279), M298 (= M281), K301 (= K284), N303 (= N286), N309 (vs. gap), R335 (= R317), L337 (vs. gap), S340 (≠ P321), T341 (≠ W322), R344 (≠ E325)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS28125 FitnessBrowser__azobra:AZOBR_RS28125
MPSTIIDSAIFGDIFSTPAMRAVWSDENRTRKYLDIEAALARVQGRLGIIPQEAADEIVA
NCSLDRIDMATLKAQTERIGYPVLGVVSQLNALCRDRLGEYCHWGATTQDITDTATVLQM
REALNLVDEDLAGLSAALATLAKRHRDTPMIGRSNLQQAVPVTFGYKMAGLLSAVERHRE
RLAQLRPRVLMGEFAGASGTLASLEHGAMETQAGLMEELDLAQPVIAWHTIRDTIAEVGC
FLGLVGGTLGKLSMDVKLMMQTEVGEVYEPFAHGRGSSSTMPQKRNPISSCYIHASISVL
RQHTAALLDAMVADHERSTGPWEIEWIVLPEAFCLLAGALKQARFVVSGLEVDAERMRAN
LEMTNGLVASEAVMMGLGRHIGREYAHDLVYDLCREAVRQNRPLLDLLAETPEISACLSR
AELAKLCDPANYLGQSGVMVDRVLDRVKNPVRG
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