SitesBLAST
Comparing BPHYT_RS21425 FitnessBrowser__BFirm:BPHYT_RS21425 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)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
44% identity, 94% coverage: 17:446/459 of query aligns to 31:469/476 of A0A0K2JL82
- N93 (= N79) mutation to A: Slight decrease in activity.
- D125 (= D111) mutation D->N,V: Almost loss of activity.
- R137 (≠ D123) binding
- R140 (≠ D126) binding
- R201 (= R187) binding
- H253 (= H230) mutation to A: Loss of activity.
- S302 (= S279) mutation to A: Loss of activity.
- K308 (= K285) binding ; mutation to A: Loss of activity.
- N310 (= N287) binding ; mutation to A: Loss of activity.
- R341 (= R318) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
43% identity, 94% coverage: 17:446/459 of query aligns to 17:438/439 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)
27% identity, 92% coverage: 17:437/459 of query aligns to 9:421/431 of Q9X0I0
- H141 (≠ W156) active site, Proton donor/acceptor
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
28% identity, 93% coverage: 16:444/459 of query aligns to 7:424/427 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)
30% identity, 90% coverage: 18:429/459 of query aligns to 10:413/431 of P12047
- H89 (= H104) mutation to Q: Abolishes enzyme activity.
- H141 (≠ W156) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ H230) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N287) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R318) mutation R->K,Q: Abolishes enzyme activity.
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
27% identity, 69% coverage: 18:332/459 of query aligns to 10:303/423 of 4eeiB
- active site: H67 (≠ L76), S140 (≠ T155), H141 (≠ W156), K256 (= K285), E263 (≠ A292)
- binding adenosine monophosphate: K66 (≠ A75), H67 (≠ L76), D68 (≠ G77), Q212 (= Q232), R289 (= R318), I291 (≠ L320), S294 (≠ W323), R298 (≠ W327)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
27% identity, 69% coverage: 18:332/459 of query aligns to 10:303/419 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)
25% identity, 74% coverage: 103:442/459 of query aligns to 103:455/482 of Q05911
- K196 (≠ G196) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5vkwB Crystal structure of adenylosuccinate lyase ade13 from candida albicans
26% identity, 73% coverage: 103:437/459 of query aligns to 103:443/469 of 5vkwB
Sites not aligning to the query:
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
27% identity, 76% coverage: 98:445/459 of query aligns to 93:449/472 of 5eytA
Sites not aligning to the query:
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
25% identity, 76% coverage: 98:445/459 of query aligns to 94:454/477 of 5nx9D
- active site: T151 (= T155), H152 (≠ W156), S283 (= S280), K288 (= K285), E295 (≠ A292)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T155), H152 (≠ W156)
- binding adenosine monophosphate: S105 (= S109), Q234 (≠ P228), R296 (≠ A293), L324 (= L320), S327 (≠ W323), A328 (≠ Q324), R331 (≠ W327)
- binding fumaric acid: S105 (= S109), Q234 (≠ P228), S282 (= S279), S283 (= S280), K288 (= K285)
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)
25% identity, 76% coverage: 98:445/459 of query aligns to 101:461/484 of P30566
- Y114 (≠ D111) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ A138) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ W156) active site, Proton donor/acceptor
- R190 (= R187) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ L191) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ R233) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D256) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S279) active site, Proton donor/acceptor
- R303 (≠ A293) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ A301) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ V308) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V353) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ D363) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (vs. gap) to R: in ADSLD; severe
- R396 (= R384) 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 (≠ T404) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L405) to V: in ADSLD; moderate
- R426 (≠ V408) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (= D412) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (vs. gap) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ A431) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ V434) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ Q436) 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
- 26 M → L: in ADSLD; severe; dbSNP:rs1311171245
- 72 I → V: in ADSLD; severe
- 100 P → A: in ADSLD; moderate; dbSNP:rs119450942
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
26% identity, 74% coverage: 106:445/459 of query aligns to 40:392/415 of 5nxaB
- active site: T89 (= T155), H90 (≠ W156), S221 (= S280), K226 (= K285), E233 (≠ A292)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V289), R234 (≠ A293)
- binding fumaric acid: S220 (= S279), S221 (= S280), M223 (= M282), K226 (= K285), N228 (= N287)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S109), T89 (= T155), H90 (≠ W156), Q172 (≠ P228), L262 (= L320), S265 (≠ W323), A266 (≠ Q324), R269 (≠ W327)
Sites not aligning to the query:
4efcA Crystal structure of adenylosuccinate lyase from trypanosoma brucei, tb427tmp.160.5560
30% identity, 42% coverage: 97:289/459 of query aligns to 115:309/452 of 4efcA
Sites not aligning to the query:
- active site: 96, 312
- binding adenosine monophosphate: 18, 19, 95, 96, 97, 313, 339, 341, 344, 345, 348
P08417 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
25% identity, 69% coverage: 85:399/459 of query aligns to 141:458/488 of P08417
- H154 (≠ E98) mutation to R: Abolished fumarate hydratase activity and ability to participate in DNA repair.
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 24 M→S: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.; mutation M->V,I: Abolishes processing by the mitochondrial processing peptidase. Mainly localizes in the cytosol, with a small fraction in the mitochondrion. Reduced fumarate hydratase activity.
- 24:25 MN→SF: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.
- 29:44 mutation Missing: Does not affect subcellular location.
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
31% identity, 41% coverage: 103:288/459 of query aligns to 102:285/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
31% identity, 41% coverage: 103:288/459 of query aligns to 102:285/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
31% identity, 41% coverage: 103:288/459 of query aligns to 102:285/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
31% identity, 41% coverage: 103:288/459 of query aligns to 102:285/496 of 6g3iA
Sites not aligning to the query:
P24058 Argininosuccinate lyase; ASAL; Arginosuccinase; Delta crystallin II; Delta-2 crystallin; EC 4.3.2.1 from Anas platyrhynchos (Mallard) (Anas boschas) (see 4 papers)
25% identity, 57% coverage: 91:351/459 of query aligns to 97:351/468 of P24058
- N116 (≠ Q110) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D111) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T155) binding in chain C; mutation to A: Loss of activity.; mutation to D: Loss of activity.; mutation to S: 30% decrease in catalytic efficiency.; mutation to V: Loss of activity.
- H162 (≠ W156) mutation to E: Loss of activity.
- R238 (= R233) mutation to Q: Loss of activity.
- T281 (≠ G277) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S279) mutation to A: Loss of activity.; mutation to C: Loss of activity.; mutation to D: Loss of activity.; mutation to H: Loss of activity.; mutation to T: Loss of activity.
- N291 (= N287) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ V289) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ A292) mutation to D: Loss of activity.
- Y323 (≠ H316) binding in chain A
- K325 (≠ R318) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q324) binding in chain A
- D330 (≠ E326) mutation to N: Loss of activity.
- K331 (≠ W327) binding in chain A; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 11 W→A: 98% decrease in catalytic efficiency.; W→F: 90% decrease in catalytic efficiency.; W→M: 99% decrease in catalytic efficiency.; W→R: 97% decrease in catalytic efficiency.; W→Y: 50% decrease in catalytic efficiency.
- 29 binding in chain A; S→A: 10% decrease in catalytic efficiency.
- 33 D→N: 99% decrease in catalytic efficiency.
- 89 D→N: Loss of activity.
Query Sequence
>BPHYT_RS21425 FitnessBrowser__BFirm:BPHYT_RS21425
MLDSSARLTGLLCGTQPMNDIWAPRATLQRMLDVEAALARASAAHQVIPQTAVAAIEAAC
QADQLDADALARDAALGGNLAIPLVKQLTARVKAADAEASKYVHWGATSQDIIDTATVLQ
LRDTFDLLDSSLQSTCDAVAKLAATHRTTPMIGRTWLQQALPITLGLKFAQWLDALLRHR
ERLDALRARALVLQFGGAAGTLASLRDAAPQVTQSLAKELGLTVPTLPWHTQRDRIAETA
ALFGMLIGTLGKIARDISLQMQTEIDELAEPAAAGKGGSSTMPHKRNPVGCAAVLTAATR
APGLVATVFAGMVQEHERALGGWQAEWDALPDLARLAGGALANIEQIAAGLNVNVPRLAA
NLDVTHGLILGEAVMLALGDSIGRLDAHHLVERASKAAIRDGQTLFDVLAADPAVTAHLP
LERLKQLLDPAQYVGQAHAYVDAALALHTTRSQRDHSRE
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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