SitesBLAST
Comparing Ga0059261_3173 FitnessBrowser__Korea:Ga0059261_3173 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)
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
51% identity, 99% coverage: 1:434/437 of query aligns to 1:428/431 of P12047
- H89 (= H93) mutation to Q: Abolishes enzyme activity.
- H141 (= H145) mutation to Q: Abolishes enzyme activity.
- Q212 (= Q216) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N274) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R305) 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)
50% identity, 99% coverage: 1:433/437 of query aligns to 1:427/431 of Q9X0I0
- H141 (= H145) active site, Proton donor/acceptor
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
47% identity, 99% coverage: 2:433/437 of query aligns to 1:423/427 of 2x75A
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
39% identity, 96% coverage: 1:419/437 of query aligns to 1:412/423 of 4eeiB
- active site: H67 (= H72), S140 (= S144), H141 (= H145), K256 (= K272), E263 (= E279)
- binding adenosine monophosphate: K66 (= K71), H67 (= H72), D68 (= D73), Q212 (= Q216), R289 (= R305), I291 (= I307), S294 (= S310), R298 (= R314)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
39% identity, 96% coverage: 1:419/437 of query aligns to 1:408/419 of 5hw2A
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 91% coverage: 4:402/437 of query aligns to 14:427/482 of Q05911
- K196 (≠ S185) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
26% identity, 92% coverage: 1:402/437 of query aligns to 10:423/477 of 5nx9D
- active site: H79 (= H72), T151 (≠ S144), H152 (= H145), S283 (= S267), K288 (= K272), E295 (= E279)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (≠ S144), H152 (= H145)
- binding adenosine monophosphate: R13 (= R4), Y14 (= Y5), R78 (≠ K71), H79 (= H72), D80 (= D73), S105 (= S98), Q234 (= Q216), R296 (≠ N280), L324 (≠ I307), S327 (= S310), A328 (≠ S311), R331 (= R314)
- binding fumaric acid: H79 (= H72), S105 (= S98), Q234 (= Q216), S282 (= S266), S283 (= S267), K288 (= K272)
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
26% identity, 92% coverage: 1:402/437 of query aligns to 17:430/484 of P30566
- M26 (= M10) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (= I58) to V: in ADSLD; severe
- P100 (≠ G86) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D100) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ V127) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (= H145) active site, Proton donor/acceptor
- R190 (= R176) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ A180) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ D221) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (≠ E243) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S266) active site, Proton donor/acceptor
- R303 (≠ N280) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ V288) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ A295) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V340) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ D350) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (= S371) to R: in ADSLD; severe
- R396 (= R372) 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 (≠ S394) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L395) to V: in ADSLD; moderate
- R426 (≠ L398) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (= D402) to N: in ADSLD; mild; dbSNP:rs554254383
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
- 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
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
26% identity, 91% coverage: 4:401/437 of query aligns to 14:419/469 of 5vkwB
Sites not aligning to the query:
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
28% identity, 70% coverage: 95:402/437 of query aligns to 40:361/415 of 5nxaB
- active site: T89 (≠ S144), H90 (= H145), S221 (= S267), K226 (= K272), E233 (= E279)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V276), R234 (≠ N280)
- binding fumaric acid: S220 (= S266), S221 (= S267), M223 (= M269), K226 (= K272), N228 (= N274)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S98), T89 (≠ S144), H90 (= H145), Q172 (= Q216), L262 (≠ I307), S265 (= S310), A266 (≠ S311), R269 (= R314)
Sites not aligning to the query:
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
33% identity, 76% coverage: 89:419/437 of query aligns to 114:452/476 of A0A0K2JL82
- D125 (= D100) mutation D->N,V: Almost loss of activity.
- R137 (= R112) binding
- R140 (≠ D115) binding
- R201 (≠ Q173) binding
- H253 (≠ V217) mutation to A: Loss of activity.
- S302 (= S266) mutation to A: Loss of activity.
- K308 (= K272) binding ; mutation to A: Loss of activity.
- N310 (= N274) binding ; mutation to A: Loss of activity.
- R341 (≠ E297) mutation to A: Loss of activity.
Sites not aligning to the query:
- 93 N→A: Slight decrease in activity.
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
24% identity, 92% coverage: 1:402/437 of query aligns to 10:410/464 of 5nxaA
- active site: H79 (= H72), T151 (≠ S144), H152 (= H145), K275 (= K272), E282 (= E279)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: R13 (= R4), Y14 (= Y5), R78 (≠ K71), H79 (= H72), D80 (= D73), T104 (= T97), S105 (= S98), Q234 (= Q216), K275 (= K272), R283 (≠ N280), L311 (≠ I307), S314 (= S310), A315 (≠ S311), R318 (= R314)
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
22% identity, 100% coverage: 1:436/437 of query aligns to 9:433/472 of 5eytA
5xnzA Crystal structure of cred complex with fumarate (see paper)
32% identity, 76% coverage: 89:419/437 of query aligns to 100:421/439 of 5xnzA
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, 92% coverage: 1:402/437 of query aligns to 9:399/441 of 5nx9C
- active site: H78 (= H72), T150 (≠ S144), H151 (= H145), E280 (= E279)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: R12 (= R4), Y13 (= Y5), R77 (≠ K71), H78 (= H72), D79 (= D73), T103 (= T97), S104 (= S98), Q233 (= Q216), M277 (≠ V276), R281 (≠ N280), L309 (≠ I307), S312 (= S310), A313 (≠ S311), R316 (= R314)
- binding fumaric acid: T150 (≠ S144), H151 (= H145)
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
23% identity, 84% coverage: 1:367/437 of query aligns to 9:372/418 of 5nxaC
- active site: H78 (= H72), T150 (≠ S144), H151 (= H145), K276 (= K272), E283 (= E279)
- binding aminoimidazole 4-carboxamide ribonucleotide: R77 (≠ K71), H78 (= H72), D79 (= D73), Q233 (= Q216), L312 (≠ I307), S315 (= S310), A316 (≠ S311), R319 (= R314)
- binding fumaric acid: H78 (= H72), T103 (= T97), S104 (= S98), Q233 (= Q216)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: R12 (= R4), Y13 (= Y5), T150 (≠ S144), H151 (= H145), K276 (= K272), R284 (≠ N280)
3gzhA Crystal structure of phosphate-bound adenylosuccinate lyase from e. Coli (see paper)
28% identity, 63% coverage: 59:334/437 of query aligns to 91:377/469 of 3gzhA
- active site: H104 (= H72), T183 (≠ S144), H184 (= H145), S309 (= S267), K314 (= K272), E321 (= E279)
- binding phosphate ion: H104 (= H72), T135 (= T97), S136 (= S98), S353 (= S310), T354 (≠ S311), R357 (= R314)
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
28% identity, 63% coverage: 59:334/437 of query aligns to 78:364/456 of P0AB89
- NHD 90:92 (≠ KHD 71:73) binding ; binding
- H91 (= H72) binding
- K94 (≠ I75) modified: N6-acetyllysine
- TS 122:123 (= TS 97:98) binding ; binding
- H171 (= H145) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (= Q216) binding ; binding ; binding
- S295 (= S266) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S267) binding ; binding
- KVN 301:303 (≠ KRN 272:274) binding ; binding
- N309 (= N280) binding ; binding
- R335 (= R305) binding ; binding
- STVLR 340:344 (≠ SSVER 310:314) binding ; binding
Sites not aligning to the query:
- 15:16 binding ; binding
- 366 modified: N6-acetyllysine
2ptqA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171n with bound amp and fumarate (see paper)
28% identity, 63% coverage: 59:334/437 of query aligns to 78:364/459 of 2ptqA
- active site: H91 (= H72), T170 (≠ S144), N171 (≠ H145), S296 (= S267), K301 (= K272), E308 (= E279)
- binding adenosine monophosphate: N90 (≠ K71), H91 (= H72), Q247 (= Q216), N309 (= N280), R335 (= R305), L337 (≠ I307), S340 (= S310), T341 (≠ S311), R344 (= R314)
- binding fumaric acid: H91 (= H72), T122 (= T97), S123 (= S98), Q247 (= Q216), S295 (= S266), S296 (= S267), M298 (= M269), K301 (= K272), N303 (= N274)
Sites not aligning to the query:
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
28% identity, 63% coverage: 59:334/437 of query aligns to 78:364/454 of 2ptrA
- active site: H91 (= H72), T170 (≠ S144), A171 (≠ H145), K301 (= K272), E308 (= E279)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: H91 (= H72), D92 (= D73), T122 (= T97), S123 (= S98), Q247 (= Q216), S295 (= S266), S296 (= S267), M298 (= M269), K301 (= K272), N303 (= N274), N309 (= N280), R335 (= R305), L337 (≠ I307), S340 (= S310), T341 (≠ S311), R344 (= R314)
Sites not aligning to the query:
Query Sequence
>Ga0059261_3173 FitnessBrowser__Korea:Ga0059261_3173
MVPRYSRPAMTAIWSPETRFGIWFEIEAHATEALADLGVVPKSAAKALWDWWATKPQIDV
AAIDAIEAVTKHDVIAFLTWVAENVGDEARFMHQGMTSSDVLDTCLSVQLVRASDILLDD
LDQLLEVLKRRAYEHKLTPTIGRSHGIHAEPVTFGLKMAEAYAEFARNKARLQAARADIA
TCAISGAVGTFANIDPRVEAHVAEKLGLAVEPVSTQVIPRDRHAMFFATLGVIASSIERL
AVEVRHLQRTEVLEAEEYFSPGQKGSSAMPHKRNPVLTENLTGLARMVRSATIPAMENVA
LWHERDISHSSVERYIGPDATITLDFALARLTGVIDKLLVYPARMQKNLDRMGGLVHSQR
VLLALTQAGVSREDSYRLVQRNAMKVWESDGELSLLELLKADPEVTAALSAQEIEEKFDL
DYHFRQVDTIFARVFND
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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