SitesBLAST
Comparing Synpcc7942_0315 FitnessBrowser__SynE:Synpcc7942_0315 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
54% identity, 100% coverage: 1:431/431 of query aligns to 1:430/431 of P12047
- H89 (= H89) mutation to Q: Abolishes enzyme activity.
- H141 (= H141) mutation to Q: Abolishes enzyme activity.
- Q212 (= Q212) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N270) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R301) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
50% identity, 99% coverage: 2:428/431 of query aligns to 1:423/427 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)
48% identity, 100% coverage: 1:429/431 of query aligns to 1:428/431 of Q9X0I0
- H141 (= H141) active site, Proton donor/acceptor
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
36% identity, 88% coverage: 1:379/431 of query aligns to 1:367/423 of 4eeiB
- active site: H67 (= H68), S140 (= S140), H141 (= H141), K256 (= K268), E263 (= E275)
- binding adenosine monophosphate: K66 (≠ R67), H67 (= H68), D68 (= D69), Q212 (= Q212), R289 (= R301), I291 (= I303), S294 (= S306), R298 (= R310)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
36% identity, 87% coverage: 1:376/431 of query aligns to 1:364/419 of 5hw2A
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
29% identity, 90% coverage: 1:389/431 of query aligns to 17:420/484 of P30566
- M26 (= M10) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (≠ F54) to V: in ADSLD; severe
- P100 (≠ G82) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D96) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ A123) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (= H141) active site, Proton donor/acceptor
- R190 (= R172) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ A176) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ D217) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (≠ E239) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S262) active site, Proton donor/acceptor
- R303 (= R276) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ I284) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ A291) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V336) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ N346) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (= S367) to R: in ADSLD; severe
- R396 (= R368) 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
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
- 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
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
29% identity, 90% coverage: 1:389/431 of query aligns to 10:413/477 of 5nx9D
- active site: H79 (= H68), T151 (≠ S140), H152 (= H141), S283 (= S263), K288 (= K268), E295 (= E275)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (≠ S140), H152 (= H141)
- binding adenosine monophosphate: R13 (= R4), Y14 (= Y5), R78 (= R67), H79 (= H68), D80 (= D69), S105 (= S94), Q234 (= Q212), R296 (= R276), L324 (≠ I303), S327 (= S306), A328 (≠ S307), R331 (= R310)
- binding fumaric acid: H79 (= H68), S105 (= S94), Q234 (= Q212), S282 (= S262), S283 (= S263), K288 (= K268)
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
27% identity, 90% coverage: 1:389/431 of query aligns to 11:410/469 of 5vkwB
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)
27% identity, 90% coverage: 1:388/431 of query aligns to 11:416/482 of Q05911
- K196 (≠ S181) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
27% identity, 90% coverage: 1:389/431 of query aligns to 10:400/464 of 5nxaA
- active site: H79 (= H68), T151 (≠ S140), H152 (= H141), K275 (= K268), E282 (= E275)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: R13 (= R4), Y14 (= Y5), R78 (= R67), H79 (= H68), D80 (= D69), T104 (= T93), S105 (= S94), Q234 (= Q212), K275 (= K268), R283 (= R276), L311 (≠ I303), S314 (= S306), A315 (≠ S307), R318 (= R310)
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
27% identity, 89% coverage: 1:382/431 of query aligns to 9:398/472 of 5eytA
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
31% identity, 87% coverage: 13:387/431 of query aligns to 35:425/476 of A0A0K2JL82
- N93 (vs. gap) mutation to A: Slight decrease in activity.
- D125 (= D96) mutation D->N,V: Almost loss of activity.
- R137 (≠ A108) binding
- R140 (≠ D111) binding
- R201 (= R172) binding
- H253 (vs. gap) mutation to A: Loss of activity.
- S302 (= S262) mutation to A: Loss of activity.
- K308 (= K268) binding ; mutation to A: Loss of activity.
- N310 (= N270) binding ; mutation to A: Loss of activity.
- R341 (= R301) mutation to A: Loss of activity.
5nx9C Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
27% identity, 90% coverage: 1:389/431 of query aligns to 9:389/441 of 5nx9C
- active site: H78 (= H68), T150 (≠ S140), H151 (= H141), E280 (= E275)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: R12 (= R4), Y13 (= Y5), R77 (= R67), H78 (= H68), D79 (= D69), T103 (= T93), S104 (= S94), Q233 (= Q212), M277 (≠ I272), R281 (= R276), L309 (≠ I303), S312 (= S306), A313 (≠ S307), R316 (= R310)
- binding fumaric acid: T150 (≠ S140), H151 (= H141)
5nxaC Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
27% identity, 84% coverage: 1:362/431 of query aligns to 9:371/418 of 5nxaC
- active site: H78 (= H68), T150 (≠ S140), H151 (= H141), K276 (= K268), E283 (= E275)
- binding aminoimidazole 4-carboxamide ribonucleotide: R77 (= R67), H78 (= H68), D79 (= D69), Q233 (= Q212), L312 (≠ I303), S315 (= S306), A316 (≠ S307), R319 (= R310)
- binding fumaric acid: H78 (= H68), T103 (= T93), S104 (= S94), Q233 (= Q212)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: R12 (= R4), Y13 (= Y5), T150 (≠ S140), H151 (= H141), K276 (= K268), R284 (= R276)
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
28% identity, 70% coverage: 87:389/431 of query aligns to 36:351/415 of 5nxaB
- active site: T89 (≠ S140), H90 (= H141), S221 (= S263), K226 (= K268), E233 (= E275)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ I272), R234 (= R276)
- binding fumaric acid: S220 (= S262), S221 (= S263), M223 (= M265), K226 (= K268), N228 (= N270)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S94), T89 (≠ S140), H90 (= H141), Q172 (= Q212), L262 (≠ I303), S265 (= S306), A266 (≠ S307), R269 (= R310)
Sites not aligning to the query:
5xnzA Crystal structure of cred complex with fumarate (see paper)
30% identity, 87% coverage: 13:387/431 of query aligns to 21:394/439 of 5xnzA
3gzhA Crystal structure of phosphate-bound adenylosuccinate lyase from e. Coli (see paper)
31% identity, 71% coverage: 9:312/431 of query aligns to 35:359/469 of 3gzhA
- active site: H104 (= H68), T183 (≠ S140), H184 (= H141), S309 (= S263), K314 (= K268), E321 (vs. gap)
- binding phosphate ion: H104 (= H68), T135 (= T93), S136 (= S94), S353 (= S306), T354 (≠ S307), R357 (= R310)
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
31% identity, 71% coverage: 9:312/431 of query aligns to 22:346/456 of P0AB89
- NHD 90:92 (≠ RHD 67:69) binding ; binding
- H91 (= H68) binding
- K94 (≠ I71) modified: N6-acetyllysine
- TS 122:123 (= TS 93:94) binding ; binding
- H171 (= H141) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (= Q212) binding ; binding ; binding
- S295 (= S262) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S263) binding ; binding
- KVN 301:303 (≠ KRN 268:270) binding ; binding
- N309 (≠ R273) binding ; binding
- R335 (= R301) binding ; binding
- STVLR 340:344 (≠ SSVER 306:310) 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)
30% identity, 71% coverage: 9:312/431 of query aligns to 22:346/459 of 2ptqA
- active site: H91 (= H68), T170 (≠ S140), N171 (≠ H141), S296 (= S263), K301 (= K268), E308 (vs. gap)
- binding adenosine monophosphate: N90 (≠ R67), H91 (= H68), Q247 (= Q212), N309 (≠ R273), R335 (= R301), L337 (≠ I303), S340 (= S306), T341 (≠ S307), R344 (= R310)
- binding fumaric acid: H91 (= H68), T122 (= T93), S123 (= S94), Q247 (= Q212), S295 (= S262), S296 (= S263), M298 (= M265), K301 (= K268), N303 (= N270)
Sites not aligning to the query:
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
30% identity, 71% coverage: 9:312/431 of query aligns to 22:346/454 of 2ptrA
- active site: H91 (= H68), T170 (≠ S140), A171 (≠ H141), K301 (= K268), E308 (vs. gap)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: H91 (= H68), D92 (= D69), T122 (= T93), S123 (= S94), Q247 (= Q212), S295 (= S262), S296 (= S263), M298 (= M265), K301 (= K268), N303 (= N270), N309 (≠ R273), R335 (= R301), L337 (≠ I303), S340 (= S306), T341 (≠ S307), R344 (= R310)
Sites not aligning to the query:
Query Sequence
>Synpcc7942_0315 FitnessBrowser__SynE:Synpcc7942_0315
LIERYTLPAMGGLWTDTYKLKTWLQVEIAVCEAQAELGYIPADAVETIKAKANFDPARVL
EIEQEVRHDVIAFLTNVNEYVGDAGRYIHLGMTSSDVLDTGLALQMVASVDLLLAETENL
IQAIRWQAQQHRETVMIGRSHGIHAEPITFGFKLAGWLAEMLRNRDRLVQVRQSVAVGKI
SGAVGTYANIEPRVEALTCQKLGLEPDTASTQVVSRDRHAEYVQVLALVAASLERFSVEI
RNLQRSDVLEVEEFFAKGQKGSSAMPHKRNPIRSERISGLARVIRGYAVAALENVALWHE
RDISHSSVERMMLPDCSATLHFMLVEMTELVKTLQVYPENMTRNLNRYGGVVFSQRVLLA
LVDKGLSREEAYRIVQSNAHSAWNHEGGNFRALIEADPTVQAHLSAAEIEDCFAAQHHLR
HLDDVYQRLNI
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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